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Synthyra 5

D3KU66

MHRGRSASARQERDFRALMDLAHGFMASQVLFAGCALRVFDAAALGPVDAAALARSSGLSPRGTRLLLDACAGLGLLRRRRGAGPRGPAYTNSPLASTFLVAGSPLSQRSLLLYLAGTTYLCWGHLADGVREGRSQYARAVGVDADDPFTAIYRSEAERLLFMRGLQETWSLCGGRVLTAFDLSPFRVICDLGGGSGALARMAARLYPGSEVTVFETPDVVAAARAHFPPPADEDGAEPRVRFLSGDFFRSPLPPADLYVLARVLHDWADAACVELLRRVRGALRPGGAVLLVESVLSPGGAGPTRTLLLSLTMLLQARGRERTEAEYRALTARAGFSRLRLRRPRGPYHAMMAARGGGAGARSDGGGGDATSQTGSGTGSEVGAQD

Function: Catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine). Catalytic Activity: N-acetylserotonin + S-adenosyl-L-methionine = H(+) + melatonin + S-adenosyl-L-homocysteine Sequence Mass (Da): 40925 Sequence Length: 387 Pathway: Aromatic compound metabolism; melatonin biosynthesis; melatonin from serotonin: step 1/2. EC: 2.1.1.4

P17405

MPRYGASLRQSCPRSGREQGQDGTAGAPGLLWMGLVLALALALALALALSDSRVLWAPAEAHPLSPQGHPARLHRIVPRLRDVFGWGNLTCPICKGLFTAINLGLKKEPNVARVGSVAIKLCNLLKIAPPAVCQSIVHLFEDDMVEVWRRSVLSPSEACGLLLGSTCGHWDIFSSWNISLPTVPKPPPKPPSPPAPGAPVSRILFLTDLHWDHDYLEGTDPDCADPLCCRRGSGLPPASRPGAGYWGEYSKCDLPLRTLESLLSGLGPAGPFDMVYWTGDIPAHDVWHQTRQDQLRALTTVTALVRKFLGPVPVYPAVGNHESTPVNSFPPPFIEGNHSSRWLYEAMAKAWEPWLPAEALRTLRIGGFYALSPYPGLRLISLNMNFCSRENFWLLINSTDPAGQLQWLVGELQAAEDRGDKVHIIGHIPPGHCLKSWSWNYYRIVARYENTLAAQFFGHTHVDEFEVFYDEETLSRPLAVAFLAPSATTYIGLNPGYRVYQIDGNYSGSSHVVLDHETYILNLTQANIPGAIPHWQLLYRARETYGLPNTLPTAWHNLVYRMRGDMQLFQTFWFLYHKGHPPSEPCGTPCRLATLCAQLSARADSPALCRHLMPDGSLPEAQSLWPRPLFC

Cofactor: Binds 2 Zn(2+) ions per subunit . Function: Converts sphingomyelin to ceramide . Exists as two enzymatic forms that arise from alternative trafficking of a single protein precursor, one that is targeted to the endolysosomal compartment, whereas the other is released extracellularly . However, in response to various forms of stress, lysosomal exocytosis may represent a major source of the secretory form . PTM: Proteolytically processed . Mature lysosomal form arises from C-terminal proteolytic processing of pro-sphingomyelin phosphodiesterase . Catalytic Activity: a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine Sequence Mass (Da): 69936 Sequence Length: 631 Subcellular Location: Lysosome EC: 3.1.4.12

Q04519

MPHHRASSGQDHLRAGWEQRLERSLPAPRVGLLWMGLGLALVLALFDSTVLWVPARAYPLPSEGHSVKFSAIAPPLQSAFGWQNLTCPACKVLFTALNHGLKKEPNVARVGSVAIKICKMLNIAPLDVCQSAVHLFEDDVVEVWTRSVLSPSEACGLLLGSSCGHWDIFSTWNISLPSVPKPPPKPPSPPAPGAPVSRVLFLTDLHWDHEYLEGTDPYCADPLCCRRGSGWPPNSQKGAGFWGEYSKCDLPLRTLESLLKGLGPAGPFEMVYWTGDIPAHDVWQQSRQDQLRALTTITDLVRKFLGPVPVYPAVGNHESTPVNGFPPPFIKGNQSSQWLYEAMAKAWEPWLPADALHTLRIGGFYALTPRPGLRLISLNMNFCSRENFWLLINSTDPAGQLQWLVEELQAAENRGDKVHIIGHIPPGHCLKSWSWNYYKIIARYENTLAGQFFGHTHVDEFEIFYDEETLSRPLAVAFLAPSATTFINLNPGYRVYQIDGNYPGSSHVVLDHETYILNLTQANAAGGTPSWKRLYRARETYGLPDAMPASWHNLVYRMRDDEQLFQTFWFLYHKGHPPSEPCGTPCRLATLCAQLSARADSPALCRHLMPNGSLPDANRLWSRPLLC

Cofactor: Binds 2 Zn(2+) ions per subunit . Function: Converts sphingomyelin to ceramide . Exists as two enzymatic forms that arise from alternative trafficking of a single protein precursor, one that is targeted to the endolysosomal compartment, whereas the other is released extracellularly. However, in response to various forms of stress, lysosomal exocytosis may represent a major source of the secretory form (By similarity). PTM: Proteolytically processed. Mature lysosomal form arises from C-terminal proteolytic processing of pro-sphingomyelin phosphodiesterase. Catalytic Activity: a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine Sequence Mass (Da): 69927 Sequence Length: 627 Subcellular Location: Lysosome EC: 3.1.4.12

A8JGB0

MALASGNRLGSARGQTCADASGRVAPRLLSRACSGSPLALGVLACLGAASSVKPHPRLPATTSAASAPLPARGPAPCAAVPTVVTPDNATGVFEELAAGQQRKYIMISGKGGVGKTSLSASLAVKLAAAGHTTLVVSTDPAHSLSDSLAQDVSGGRPVLLQGTDLPLWGLEIDPEEAKREFFEGSGAGQDGEAGGPSAASQVSDFMNRMGMGFVIDQLKELKLGELLNTPPPGLDEAVAIAKVVQFVQAAEYARFSRIVFDTAPTGHTLRLLALPDFVDASLAKVIRLRKKLNGATSVVRGLFGAGESQDEAVEKLELLQQRVRMVKALFRDKTQTEFIIATIPTYLGVNESSRLLQALRAEQIPCKRIIVNQIVGPQQGDAYLRMKMKDQIAALEMVANDPGLRPLRKVIAPMVDVEVRGVPALSYFGNVVWKDVYDQMNQGADRKFFLLGGKGGVGKTSCSSSLAVHFANDGLPTLVVSTDPAHSLSDAFDQDLSGGSPVKITSPLGDELPLWGLQLDPEQAKAELRAVLADDGGKKLNETLDGLGLGVISDQLKDLQLGELLDTPPPGVDEAIAIAKVVQFLKAPEYSHFKRIVFDTAPTGHTLRLLSLPDFLDASIGKLVRLRQKLSAATSAVKNLFSGGQPGEEDVAVKRLEALQASMEDAKAMFRNQQTTEFIIVTIPTVMATAESCRLASALQHEGIPLKTIIVNQVVQANATDKFLTARRADQARALHHLEEDTGPDGLASLQLIKAPLCDLEVRGVPALSYFGNVVWK

Function: ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the chloroplast. Required for the accumulation of TOC34, an essential component of the outer chloroplast membrane translocon (TOC) complex . Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to chloroplast, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis . Sequence Mass (Da): 82383 Sequence Length: 777 Subcellular Location: Cytoplasm EC: 3.6.-.-

A8IXB8

MAADMPDPTLQNVVDQKELKWIFVGGKGGVGKTTTSSSLAVALAESGTRNRVLIISTDPAHNLSDAFRQKFTKTPTLVNGFTNLFAMEVDPQPDIGEMEQLEWAQDSFLTELAGSIPGIDEAMSFAEVMKQVQTMDYDTIVFDTAPTGHTLRLLNFPTILEKGLSKLVALKGAMGGMMGQVTRMLGGMAGGGEGAADLPDQLLGKVEGMLDVVRKVSAQFKDPLLTTFVAVCIPEFLSLYETERLVQELAKFEIDCRNIVINQIIFPESVGGSRLLDARVRMQQKYLDQFYELYEDFHILQLPLLEEEVRGPEALKAFAVNLLKPYVPAPPTDAAARQAALVSEVAALKKRVAELEAALAKK

Function: ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis . ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting (By similarity). Sequence Mass (Da): 39538 Sequence Length: 362 Subcellular Location: Cytoplasm EC: 3.6.-.-

Q16MG9

MDTDFEPLAPSLENIIDQETLKWVFVGGKGGVGKTTCSCSLAVQLAKVRESVLIISTDPAHNISDAFDQKFTKVPTKVNGFNNLFAMEIDPNVGLNELPDEYFEGENSAMKLSKGVFQEIIGALPGIDEAMSYAEVMKLVKAMNFSVVVFDTAPTGHTLRLLSFPQVVEKGLGKLLMLKMKLAPFISQMGSLFGMQDFNADTLTGKLEEMLTIIRQVNEQFRNPDQTTFVCVCIAEFLSLYETERLVQELTKCGIDTHNIIVNQLLFRREGQAPCAMCSARYKVQGKYLDQIADLYEDFYVVKLPLLDKEVRGVENVKKFSEYLIKPYCPNGTNETQEQDK

Function: ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting. Sequence Mass (Da): 38192 Sequence Length: 341 Subcellular Location: Cytoplasm EC: 3.6.-.-

O28440

MLVGLIGYGAIGKFLAEWLERNGFEIAAILDVRGEHEKMVRGIDEFLQREMDVAVEAASQQAVKDYAEKILKAGIDLIVLSTGAFADRDFLSRVREVCRKTGRRVYIASGAIGGLDAIFSASELIEEIVLTTRKNWRQFGRKGVIFEGSASEAAQKFPKNLNVAATLSIASGKDVKVRLVADEVEENIHEILVRGEFGEMEIRVRNRPMRENPKTSYLAALSVTRILRNLKEGLVV

Function: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate. Catalytic Activity: H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate Sequence Mass (Da): 26208 Sequence Length: 236 Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1. EC: 1.4.1.21

Q89FY1

MDRRWKVMTDQTASSELRVAIAGLGSIGTKIAAALDQGEGLTLSAVAVRDPAKHQAFLNGLRRPPQVLPIDQLGEAADIVVECAPSSQLRAIVEPAVKRGKAAVVVSVGGLLDNFDLVDLARANGGRIIVPTGALIGLDAVNAAVIGTIHSVKMVTRKPIDGLKGAPFIVHNNIDIDTLREPLKLFEGTAREAAKGFPANLNVAVALSLAGVGPDRTSVQIWADPTVTRNVHRIEVEADSARFSMSIENIPSENPKTGLITALSVIALLRKQRATLCVGT

Function: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate. Catalytic Activity: H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate Sequence Mass (Da): 29472 Sequence Length: 280 Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1. EC: 1.4.1.21

A6X792

MSVSETIVLVGWGAIGKRVADLLAERKSSVRIGAVAVRDRSASRDRLPAGAVLIENPAELAASGASLVVEAAGRPSVLPWGEAALSTGMDFAVSSTSAFVDDALFQRLKDAAAASGAKLIIPPGALGGIDALSAASRLSIESVEHRIIKPAKAWAGTQAAQLVPLDEISEATVFFTDTARKAADAFPQNANVAVITSLAGIGLDRTRVTLVADPAARLNTHEIIAEGDFGRMHLRFENGPLATNPKSSEMTALNLVRAIENRVATTVI

Function: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate. Catalytic Activity: H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate Sequence Mass (Da): 27854 Sequence Length: 268 Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1. EC: 1.4.1.21

Q63LV9

MLNAHAPVDVAMIGFGAIGAAVYRAVEHDAALRVAHVIVPEHQCDAVRGALGERVDVVSSVDALACRPQFALECAGHGALVDHVVPLLKAGTDCAVASIGALSDLALLDALSNAADAGGATLTLLSGAIGGIDALAAARQGGLDEVRYIGRKPPLGWLGTPAEAICDLRAMAAEQTIFEGSARDAAQLYPRNANVAATVALAGVGLDATRVCLIADPAVTRNVHRIVARGAFGEMSIEMSGKPLPDNPKTSALTAFSAIRALRNRASHCVI

Function: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate. Catalytic Activity: H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate Sequence Mass (Da): 27704 Sequence Length: 271 Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1. EC: 1.4.1.21

O58478

MPFLPFSYYPFSLEVILMEYPKIVVKPPGPRAKELIEREKKVLSTGIGVKLFPLVPKRGFGPFIEDVDGNVFIDFLAGAAAASTGYAHPKLVKAVKEQVELIQHSMIGYTHSERAIRVAEKLVEISPIENSKVIFGLSGSDAVDMAIKVSKFSTRRPWILAFIGAYHGQTLGATSVASFQVSQKRGYSPLMPNVFWIPYPNPFRNIWGINGYEEPDELINRVLDYLEYYVFSHVVPPDEVAALFAEPIQGDAGIVVPPENFFKELKKLLEEYGILLVMDEVQTGIGRTGKWFASEWFNVKPDMIIFGKGVASGMGLSGVIGRKEIMDITSGSALLTPAANPVISAAAEATLEIIEEENLLKNALEVGEFIMGRLKEIKERFEIIGDVRGKGLMIGVEIVKENGRPDPEMTGKICWRAFELGLILPSYGMFGNVIRITPPLVLTKEVAEKALEIIERAIKDTLTGKVERKVVTWH

Function: Catalyzes the interconversion of L-alanine and D-alanine, and L-serine and D-serine. Has weak activity with valine and threonine. Catalytic Activity: L-alanine = D-alanine Sequence Mass (Da): 52570 Sequence Length: 474 EC: 5.1.1.-

P26474

MAIKITPDEFSLLIQRLNKKWRVFAPSAEFRGGRFSDTDNIIYQRISGWRDLIWHEKSHMSPNTIIAPITETLFYFDKDTIQIAETDTSPIIIFARACDINAMSRLDYMYLSNGNNSDYSYQLLREHIRFVLIECEESFENCFCVSMGTNKTDCYSAAMRFSDEGALVSIRDPFIEAAIQGLGQEADYTPSFVSENRETVVTPDSVCHDPQKIRDILTHHPLWDAYDSRCISCGRCTTGCPTCTCYSVFDVAYDENPQRGERRRQWASCMVPGFSDMAGGHGFREKPGERLRYRALHKVNDYKARNGIEHMCVGCGRCDDRCPQYIKFSLIINKMTAAVRQALAEEA

Cofactor: Binds 2 [4Fe-4S] clusters. Function: Electron transfer protein for anaerobic sulfite reductase subunit A. Sequence Mass (Da): 39680 Sequence Length: 347 Pathway: Sulfur metabolism; sulfite reduction. Subcellular Location: Cytoplasm

P26475

MSHCSCHDKPQHSLLPAAYRILSITRHTPLEWNFRVAVDFPAHWGQFVEVSLPRVGEAPISVSDYGDGWIDLLIRNVGKVTSALFTLKEGDNVWLRGCYGNGYPVDTLRHKPLLVVAGGTGVAPVKGLMRYFVENPQEIGQLDMILGYKNRDCVLYKEEMATWRGKHNLVLTLDEGEADDRYQIGRVTDRLADMTLSDIDTMQAIVVGPPIMITFTVKMLLQKGLKPEQIWVDYERRMACSVGKCGHCRMGEVYVCTDGPIFNYAVAQRFAD

Cofactor: Binds 1 [2Fe-2S] cluster per subunit. Function: This enzyme catalyzes the hydrogen sulfide production from sulfite. It is strictly anaerobic. It is regulated by electron acceptors rather than by cysteine. Sequence Mass (Da): 30609 Sequence Length: 272 Pathway: Sulfur metabolism; sulfite reduction. Subcellular Location: Cytoplasm

P0A1Y3

MSIDIDIIKARAKNEYRLSKVRGEAMISVRIPGGILPAHLLTVARDIAETWGNGQIHLTTRQKLAMPGIRYEDIDNVNAALEPFLREIEIELCDVQVEDTKAGYLAIGGRNIVACQGNRICQKANTDTTGLSRRLEKLVYPSPYHLKTVIVGCPNDCAKASMADLGIIGVAKMRFTADRCIGCGACVKACSHHAVGCLALKNGKAVKEESACIGCGECVLACPTLAWQRKPDQLWQVRLGGRTSKKTPRVGKLFLNWVTEDVIKQVIVNLYEFEKEMLGGKPIYLHMGHLIDKGGYLRFKERVLRGVQLNPEAMVAERIYWAEDESVARMHLKPAGH

Cofactor: Binds 3 [4Fe-4S] clusters per subunit. Function: This enzyme catalyzes the hydrogen sulfide production from sulfite. It is strictly anaerobic. It is regulated by electron acceptors rather than by cysteine (By similarity). Catalytic Activity: 3 H2O + hydrogen sulfide + 3 NAD(+) = 4 H(+) + 3 NADH + sulfite Sequence Mass (Da): 37291 Sequence Length: 337 Pathway: Sulfur metabolism; sulfite reduction. Subcellular Location: Cytoplasm EC: 1.8.1.-

A7MLT4

MKKVLALVVAATMGLSAAAFAADNTAAPAPAAAATTTTTAAPAKAPAAKTHHKKSHKKAVEQKAQAAKKHHKKAAEQKPAAEQKAQAAKKHHKKAAAQKPAVEQKAQAAKKHHKKAVKHDAAKPAAQPAA

Function: Required for growth and/or survival at acidic conditions. PTM: Proteolytic processing gives rise to the active protein. Sequence Mass (Da): 13294 Sequence Length: 130 Subcellular Location: Periplasm

B7MV44

MKKVLALVVAAAMGLSSAAFAAETAITPAPTATTTKAAPAKTTHHKKQHKAAPAQKAQAAKKHHKNAKAEQKAPEQKAQAAKKHAKKHSHQQPAKPAAQPAA

Function: Required for growth and/or survival at acidic conditions. PTM: Proteolytic processing gives rise to the active protein. Sequence Mass (Da): 10543 Sequence Length: 102 Subcellular Location: Periplasm

Q7VTJ9

MTTILPNLPTGQKVGIAFSGGLDTSAALLWMRQKGAVPYAYTANLGQPDEPDYDEIPRRAMQYGAEAARLVDCRAQLVAEGIAALQAGAFHISTAGLTYFNTTPIGRAVTGTMLVAAMKEDGVNIWGDGSTFKGNDIERFYRYGLLTNPDLKIYKPWLDQTFIDELGGRAEMSEYMRQAGFDYKMSAEKAYSTDSNMLGATHEAKDLELLSAGIRIVQPIMGVAFWQDSVQIKAEEVTVRFEEGQPVALNGVEYADPVELLLEANRIGGRHGLGMSDQIENRIIEAKSRGIYEAPGLALLFIAYERLVTGIHNEDTIEQYRENGRKLGRLLYQGRWFDPQAIMLRETAQRWVARAITGEVTLELRRGNDYSLLNTESANLTYAPERLSMEKVENAPFTPADRIGQLTMRNLDIVDTREKLFTYVKTGLLAPSAGSALPQIKDGKK

Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+) Sequence Mass (Da): 49323 Sequence Length: 445 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. Subcellular Location: Cytoplasm EC: 6.3.4.5

P14568

MSGKGSVVLAYSGGLDTSCILVWLKEQGYDVIAYLANIGQKEDFEEARKKALKLGAKKVFIEDISKEFVEEFIWPAIQSSALYEDRYLLGTSLARPCIARKQVEIAQREGAKYVSHGATGKGNDQIRFELTCYSLAPQIKVIAPWRMPEFYNRFQGRNDLMEYAKQHGIPVPVTPKNPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNSPDMLEIEFKKGVPVKVTNVGDGTTHSTALELFLYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAELVYTGFWHSPECEFVRHCIAKSQERVEGKVQVSVFKGQVYILGRESPLSLYNEELVSMNVQGDYEPVDATGFININSLRLKEYHRLQNKVTAK

Function: One of the enzymes of the urea cycle, the metabolic pathway transforming neurotoxic amonia produced by protein catabolism into inocuous urea in the liver of ureotelic animals. Catalyzes the formation of arginosuccinate from aspartate, citrulline and ATP and together with ASL it is responsible for the biosynthesis of arginine in most body tissues. PTM: Acetylated by CLOCK in a circadian manner which negatively regulates its enzyme activity. Deacetylated by histone deacetylases. Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+) Sequence Mass (Da): 46417 Sequence Length: 412 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. Subcellular Location: Cytoplasm EC: 6.3.4.5

C0R1H5

MKKKLVLAYSGGLDTTVIIPWLKENYDYDVIAVCVDVGQGTETDGLEEKALKTGAVKYRLVKCEDEFVTDYIYPIVKAEATYEDKYLLGTSAARPLIAKKLVEVALEEGATAIAHGATGKGNDQVRFELTVKALAPNFEIIAPWREWNISSREEEIKYLEDRNIEVPMKKDDSYSRDKNLWHLSHEGLELEDPANMPNYERLLKLSNTIENAPNEGQFVELEFEKGIPTKVDGKTFSPSDLVKYLNEIGGKHAVGIVDLLENRVVGIKCRGVYETPGGTILYAAHREIEHLCLDRETLYFKHVVSHKLTDLVYSGRWFTPLREALCAFIDSTQQTVTGKVKLKLYKGNIIPAGVTSPYSLYNQSLASFTTGELYDHHDAQGFITLFGLPLKVNALMKEQAKKMGLK

Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+) Sequence Mass (Da): 45587 Sequence Length: 406 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. Subcellular Location: Cytoplasm EC: 6.3.4.5

A4YJX9

MTTILKGLPTGEKVGIAFSGGLDTSAALLWMKQKGARCFAYTANLGQPDESDYDEIPRKAMSFGAEKARLVDCRTQLVHEGIAAIQSGAFHISTGGATYFNTTPLGRAVTGTMLVAAMKEDGVNIWGDGSTYKGNDIERFYRYGLLTNPNLKIYKPWLDQQFIDELGGRAEMSAFLTAHGFNYKMSAEKAYSTDSNLLGATHEAKDLESLSSGIRIVNPIMGVPFWREDCAVRPETVVVRFEEGQPVALNGQTFTDPVALFLEANAIGGRHGLGMCDQIENRIIEAKSRGIYEAPGMALLHIAYERLVTGIHNEDTIEQYRMSGMKLGRLLYQGRWFDSQALMLRETAQRWVASAITGEVTLELRRGNDYSLLNTESPNLTYQPERLSMEKVEDAAFTPADRIGQLTMRNLDITDTRTKLKLYSDTGLLSGAEGAQIFQLGHDKGDKS

Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+) Sequence Mass (Da): 49427 Sequence Length: 448 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. Subcellular Location: Cytoplasm EC: 6.3.4.5

A6WV13

MSKWKDVKKVVLAYSGGLDTSIILKWLQTELGAEVVTFTADLGQGEELEPARKKAEMLGIKEIFIEDVREEFVRDFVFPMFRANAVYEGVYLLGTSIARPLISKHLIEIARKTGADAIAHGATGKGNDQVRFELSAYALNPDIKIIAPWRDWSFKSRTHLLEFAEQHQIPVAKDKKGEAPFSVDANLLHSSSEGKVLEDPAVEAPEYVHMRTISPETAPDKATIIKIGFEKGDAVSINGERLSPATLLAKLNDYGRDNGIGRLDLVENRFVGMKSRGVYETPGGTILLAAHRAIESITLDRGAAHLKDELMPRYAELIYYGFWFSPEREMLQAAIDHSQRHVEGEVTLKLYKGNVMVIGRESDKSLYSDKLVTFEDDQGAYDQKDAAGFIKLNALRLRTLAARDRK

Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+) Sequence Mass (Da): 45323 Sequence Length: 406 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. Subcellular Location: Cytoplasm EC: 6.3.4.5

Q7UFW4

MKSCVLAYSGGLDTSVILGWLQDQGYEVHCVYVDLGQPCEDRDAIMEKARTCGAKSSRLVDVREELCRDFAFPVLAWQAKYEQIYLLGTSIARPLISKVCLEVAREVGATAYAHGATGKGNDQCRFQLAAEALDPNIEMIAPWRIKSFRDAFPGRTELIEYCDVKRIPVKASTAKPYSSDENVLHISYEAGKLEELDVNGVELVEFGMGVSPQDAPDKPEEVTIGFESGVPKTLNGKAVNALEMVEQLNDIAGRNGVGRIDMVENRFVGMKSRGVYESPGMTVLYDALMYVEQLTMDRDLMHLRDRMAPEVAEMVYYGFWYTPKMDALMSFIETAQRPVTGEVTLQLYKGNIMVSSRTSPNSLYDEEIATMEGGGSYNQDDAEGFLRIQGLPSRVQGRVSPRKF

Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+) Sequence Mass (Da): 44949 Sequence Length: 404 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. Subcellular Location: Cytoplasm EC: 6.3.4.5

Q2RMV0

MKKGDVKKVVLAYSGGLDTSIILRWLQDEYDCEVVTFTADIGQGEELEPARQKAEMMGIKEIYIEDLREEFVRDYVFPMFRANTLYEGVYLLGTSIARPLIGKRLVEIAEATGADAVSHGATGKGNDQVRFELTAYALKPDIKIIAPWRTWDLHSRTKLIEYAMRHQIPVPKDKHGEAPYSMDANLLHISYEGKALENPWTEPSEDMFRLTVSPEAAPDKAQYIEVDFERGDAVAIDGEKLTPAALLAKLNEIGGRHGVGRLDLVENRYVGMKSRGVYETPGGTILQVAHRAVESLTLDREVMHLRDELMPRYAKLIYNGFWFAPERLMLQAAIDQTQQTVTGTARLKLYKGNVSVVGRKAAKSLYRMDYVTFEEDTVYDQHDAEGFIKLNALRLRLGKMARDS

Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+) Sequence Mass (Da): 45609 Sequence Length: 404 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. Subcellular Location: Cytoplasm EC: 6.3.4.5

A7NPB0

MSSRVHKVVLAYSGGLDTSIIVPWLKQNYGNPEVICYCANIGQDDELSGLEAKAIATGASKCYVEDLREEFVRDFLFPLLQSGAVYERTYLLGTSVARPLIARRQAEIALQEGADALAHGCTGKGNDQVRFELTYMAFAPHLKVIAPWREWNIRSREDALDYAAEHNVPVTATLKSIYSRDRNIWHMSHEGGILEDPWQEPEEAMYTLTTAPEAAPDEPEYVTVGFDQGVPVSVNGERLGPVDLLLALNNIGAKHGIGRVDLVENRLVGMKSHGVYETPGGTILRVAHQGLEQLALDRDTLHYKDVIAHRYAELVYYGQWYTPLREALDAFVRVTQRNVTGEARLKLYKGNAMLVGRRAAKSLYNPDIASFTMSDSYNQKDAEGFIKIFGLPVKVQALLEGR

Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+) Sequence Mass (Da): 44770 Sequence Length: 402 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. Subcellular Location: Cytoplasm EC: 6.3.4.5

P22768

MSKGKVCLAYSGGLDTSVILAWLLDQGYEVVAFMANVGQEEDFDAAKEKALKIGACKFVCVDCREDFVKDILFPAVQVNAVYEDVYLLGTSLARPVIAKAQIDVAKQEGCFAVSHGCTGKGNDQIRFELSFYALKPDVKCITPWRMPEFFERFAGRKDLLDYAAQKGIPVAQTKAKPWSTDENQAHISYEAGILEDPDTTPPKDMWKLIVDPMDAPDQPQDLTIDFERGLPVKLTYTDNKTSKEVSVTKPLDVFLAASNLARANGVGRIDIVEDRYINLKSRGCYEQAPLTVLRKAHVDLEGLTLDKEVRQLRDSFVTPNYSRLIYNGSYFTPECEYIRSMIQPSQNSVNGTVRVRLYKGNVIILGRSTKTEKLYDPTESSMDELTGFLPTDTTGFIAIQAIRIKKYGESKKTKGEELTL

Function: Catalyzes the eighth step in arginine biosynthesis. Also has a catabolic function as the first enzyme of citrulline utilization as nitrogen source via arginine and the reactions involved in the arginase pathway. Catalytic Activity: ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+) Sequence Mass (Da): 46928 Sequence Length: 420 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. Subcellular Location: Cytoplasm EC: 6.3.4.5

P35183

MAKDILKNQDPKLQAMIVEHSAPAPKEIPMDAPVLKRVARPLRHVKFIPIKSLIFHTKTGPMDFSYEKKIKTPIPKNKIVVRVSNVGLNPVDMKIRNGYTSSIYGEIGLGREYSGVITEVGENLNYAWHVGDEVYGIYYHPHLAVGCLQSSILVDPKVDPILLRPESVSAEEAAGSLFCLATGYNILNKLSKNKYLKQDSNVLINGGTSSVGMFVIQLLKRHYKLQKKLVIVTSANGPQVLQEKFPDLADEMIFIDYLTCRGKSSKPLRKMLEEKKISQYDPVEDKETILNYNEGKFDVVLDFVGGYDILSHSSSLIHGGGAYVTTVGDYVANYKEDIFDSWDNPSANARKMFGSIIWSYNYTHYYFDPNAKTASANNDWIEQCGDFLKNGTVKCVVDKVYDWKDHKEAFSYMATQRAQGKLIMNVEKF

Function: Lipid raft-associated protein involved in the targeting of PMA1 from Golgi to the plasma membrane . May induce clustering of PMA1, which facilitates partition of PMA1 into lipid rafts after leaving the ER and its transport to the cell surface . Location Topology: Peripheral membrane protein Sequence Mass (Da): 48349 Sequence Length: 429 Subcellular Location: Cell membrane

Q32G87

MRNAWEVNFDGLVGLTHNYAGLLFGNEASTRHRFQVSNPRLAAKQGLLKMKNLADAGFPQAVIPPHERPFIPVLRQLGFSGSDEQVLEKVARQAPHWLSSVSSASPMWVANAATIAPSVDTLDGKVHRTVANLNNKFHRSLEAPVTESLLKAIFNDEEKFSVHSALPQVALLGDEGAANHNRLGGHYGEPGMQLFVYGREKGNDTRPSRYPARQTREASEAVARLNQVNPQQVIFAQQNPDVIDQGVFHNDVIAVSNRQVLFCHQQAFARQSQLLANLRARVNGFMAIEVPATQVSVSDAVSTYLFNSQLLSRDDGSMMLVLPQECREHAGVWCYLNELLAADNPISELKVFDLRESMANGGGPACLRLRVVLTEEERRAVNPAVMMNDTLFNALNDWGDRYYRDRLTDADLADPQLLREGREALDVLSQLLNLGSVYPFQREGGGNG

Function: Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2). Catalytic Activity: 2 H(+) + 2 H2O + N(2)-succinyl-L-arginine = CO2 + N(2)-succinyl-L-ornithine + 2 NH4(+) Sequence Mass (Da): 49589 Sequence Length: 448 Pathway: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 2/5. EC: 3.5.3.23

A0A3S9NM20

MIDSLSFTTMPVVLLVGLVLYQLLAFTYRLFFSPLAKFPGQKIAGMTHWYEFYHDVIRRGQYTFHIRDMHKKYGPILRINPYELHISDPSFYNEIYAVQNRRRDRWEWSTRPGGFGGSVGGTNPHELHRRRRAALNPFFSRANIRKLQHEIDQKAVQLVERLEKETDRVIKVNHAFAALTNDIVMQYSFGRDDNRAAHKDRAARALPMEMLSKISSVVAMFWQEKQSITEEVRQILNGTNKAYKERPNRTIYHGILESKLPPEEKELNRLAEEAQITIGAGTLATAWVMSVGMYHLLAPGSVSMLKTLREELQRAIPDPSEPIDLAALEKLPYLTGVVKECLRLGNGTTTRLQRIAPDETLIYTDPNTGKVWDIPPGTPVSLSSLHIHHDETIFADPESFRPERWIENPDLERYLLTFSKGSRQCLGIHLAYAEMYIVLARVFRLYGRKEEGPSKGPSDKLGNLELFETELRDTLCVADLVVPAVWEGSQGIRIKVTE

Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the asperterpenoids, sesterterpenes that exhibit anti-tuberculosis activity . The first step of the pathway is performed by the sesterterpene synthase astC that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylfarnesyl diphosphate (GFPP) and further converting GFPP into preasperterpenoid A, respectively . The cytochrome P450 monooxygenase astB then dually oxidizes preasperterpenoid A to produce asperterpenoid A along with a minor product, asperterpenoid B . Finally, the cytochrome P450 monooxygenase astA converts asperterpenoid A into asperterpenoid C . Catalytic Activity: 4 O2 + preasperterpenoid A + 4 reduced [NADPH--hemoprotein reductase] = asperterpenoid A + 5 H(+) + 5 H2O + 4 oxidized [NADPH--hemoprotein reductase] Location Topology: Single-pass membrane protein Sequence Mass (Da): 57028 Sequence Length: 498 Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis. Subcellular Location: Membrane EC: 1.-.-.-

Q5NNB4

MIVSEVNFDGLIGPTHNYAGLSRGNVASALHAGQPSYPRQAALQGLEKMKHLMDMGLTQGVFLPPLRPVTHLLHHLGYKGDDKTILKQAAKDDRLLFNNLCSASSMWAANAATVISEFDSHDGRVHFITANLATMLHRHLEAQTTYAQLNQIFSNSCFFAMHHPLPCGQHFSDEGAANHMRITSAHGRTGINIFVYGEKNDIYPARQKLRASQAVARLGEVKPDLAWFIPQKKEAIAKGAFHNDVVAVANEYVLLAHAEAFEDQGEWIKRIAEKIDGFIPIIIDNITLEQAVKSYLFNSQIVTLKDRTMALILPQEVKSDPAVWETVNRIISGNNPIKKAVVVDVRESMANGGGPACLRLRVPLSKAALEAVDQRFILTPKRWEKLYQLVENFWPEKITPDDLVLPELWKTAVRAHWALTSWLG

Function: Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2). Catalytic Activity: 2 H(+) + 2 H2O + N(2)-succinyl-L-arginine = CO2 + N(2)-succinyl-L-ornithine + 2 NH4(+) Sequence Mass (Da): 47270 Sequence Length: 424 Pathway: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 2/5. EC: 3.5.3.23

Q2UEK4

MTKINPYKGILVELKDIVFTSSSDQIKLPINTFKSILCCGATAQYQCGKINRAQYYSRLARDFALSLADVTALFDTVQATIRPEESFLAFLAELKSRFGEQLKLYAVANMSREDYAMLKSLPIDWSLFDGVFLSADLGMRKPELRFFRHVLESISMKPEDTILVDNDTDNILCALSMGLKGILFGSTSVPQALTNLLEYDHISRAEQFLRSHAKSLHSVTHTGVTIRENFAQLLILEATGDIDLVELEYHPTTWNYFIGTQSSQLLLHKHNADRMTTMTSCWLVSAFLVVS

Function: Sesquiterpene cyclase; part of the gene cluster that mediates the biosynthesis of astellolides, drimane-type sesquiterpene esters that show antimicrobial, anti-inflammatory, and anti-tumor activities . The first step in astellolide biosynthesis is performed by the sesquiterpene cyclase astC that catalyzes the formation of drimanyl pyrophosphate from farnesyl pyrophosphate . Drimanyl pyrophosphate is then dephosphorylated by the sesquiterpene phosphatase astI to produce drimanyl monophosphate which is further dephosphorylated to drim-8-ene-11-ol by atsK . Drim-8-ene-11-ol is converted to confertifolin, probably by the cytochrome P450 monooxygenase astD and/or the dehydrogenase astE . The cytochrome P450 monooxygenases astB, astF and astJ then hydroxylate confertifolin at C6, C14, or C15 to form trihydroxy confertifolin . The nonribosomal peptide synthetase astA catalyzes ester bond formation between trihydroxy contifolin and benzoic acid (BA) or 4-hydroxy benzoic acid (4HBA), leading to the formation of dideacetyl astellolides A and B, respectively . Finally, the O-acetyltransferase astG converts dideacetyl astellolides A and B into deacetyl astellolides A and B . Sequence Mass (Da): 32794 Sequence Length: 291 Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis. EC: 4.2.3.-

A8AHE0

MSLSITRENFDEWMMPVYAPAPFIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPALREALNEQASKFWHTGNGYTNEPVLRLAKMLIDATFAERVFFCNSGAEANEAALKLARKYAHDRFGTHKSGIVAFKNAFHGRTLFTVSAGGQPAYSQDFAPLPPDIRHAVYNDLNAASELIDDTTCAVIVEPMQGEGGVLPATKAFLQGLRELCDRHNALLIFDEVQTGVGRTGELYAYMHYGVTPDLLTTAKALGGGFPIGALLATEKCASVMTVGTHGTTYGGNPLASAVAGKLLEIVNTPEMLNGVKQRHDGFVERLNAINERFGLFSEIRGLGLLIGCVLEAEFAGKAKLISQEAAKAGVMVLIAGANVVRFAPALNVSKEEVATGLDRFALACERIKAGGSS

Function: Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. Catalytic Activity: 2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde Sequence Mass (Da): 43500 Sequence Length: 406 Pathway: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. EC: 2.6.1.81

Q7MH21

MTQWIAGEWVEGLGEEFTSLSPYDNQVVWRGKGATAEQVEMAVKAARQAFVGWKKLSVAEREAMVLAFAEQVKENSEEIAQVIAKETGKPLWETRTEAAAMAGKIAISIRAYHERTGESQKEAAGNQIVLRHRPLGVMAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSEQTPWTGELAMKLWQAAGLPQGVINLVQGGKETGIALAESKGIDGLLFTGSANTGHLLHRQFAGQPGKMLALEMGGNNPMVITDHYGDLDATVYTIIQSAFISAGQRCTCARRLYIPLGEKGDALITRLVEATKKLRVDQPFAEPAPFMGPQISEAAANFILAAQANLQSLGGESLIEAKAGEAAFVTPGIIDVTNIAELPDEEYFGPLLQVVRYQTLEQAVELANDTRFGLSAGLVSTDDGEWQYFVDHIRAGIVNRNRQLTGASGDAPFGGPGASGNLRPSAYYAADYCAYPMASMEGEETLLPATLSPGVEL

Function: Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate. Catalytic Activity: H2O + N-succinyl-L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + N-succinyl-L-glutamate + NADH Sequence Mass (Da): 52000 Sequence Length: 485 Pathway: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 4/5. EC: 1.2.1.71

O13978

MTNTVTIELKIGYKYAAEVVKAVLGVILFHRQFSTVPARTIDVLDITVPTLVGAELNEQLATKAAEFIDTIRNEAGANGQMILLLYERSPKKSWFGKGNTIPWEQWILHTTILEEGDSYQESSLSLEAAVEQIVQAVNLRSLSYLPPVAMDSGNYPYEIVTPTSTEGWGSLLKRMIIENVSGGD

Function: Autophagy factor required for autophagosome formation . Component of the atg1 kinase complex in which it stabilizes atg13 . Is also responsible for recruiting downstream factors to the autophagosome-formation site . Has a role in meiosis and sporulation . Location Topology: Peripheral membrane protein Sequence Mass (Da): 20318 Sequence Length: 184 Subcellular Location: Cytoplasm

Q9GKS6

MACNLCYEAESPDEAALVYAARAYQCTLQSRTPEQVMVDFAASGPLTFQLLHILPFDSVRKRMSVVVRHPLSNQVVVYTKGADSVIMELLSVASPDGAGPEKQQMIIREKTQRHLDDYAKQGLRTLCIAKKVMSDTEYAEWLRNHFLAETSIDNREELLLESAMRLENKLTLLGATGIEDRLQEGVPESIEALHKAGIKIWMLTGDKQETAVNIAYACMLMSTILKELQKKTQALPEQVSLSVDLHQPPVPQDSGLRAGLIITGKTLEFALQESLQKQFLELTSWCQTVVCCRATPLQKSEVVKLVRSHLQVMTLAIGDGANDVSMIQVADIGIGVSGQEGMQAVMASDFAVSQFKHLSKLLLVHGHWCYTRLSNMILYFFYKNVAYVNLLFWYQFFCGFSGTSMTDYWVLIFFNLLFTSAPPVIYGVLEKDVSAETLMQLPELYKSGQKSEAYLPHTFWITLLDAFYQSLVCFFVPYFTYQGSDIDIFAFGNPLNTAALFIILLHLIIESKSLTWIHMLVITGSILSYFLFAIVFGAMCVTCNPPSNPYWIMQEHVLDPVFYLVCILTTCIALLPRFVYRGAGKMNQVTSNYANQSADKSGRRPKPGPSTVFAMKSATSCAIEQGNLSLCETALDQGYSETKAFEMARPCKD

Function: Catalytic component of a P4-ATPase flippase complex, which catalyzes the hydrolysis of ATP coupled to the transport of glucosylceramide (GlcCer) from the outer to the inner leaflet of the plasma membrane. PTM: Autophosphorylated at the conserved aspartate of the P-type ATPase signature sequence. Location Topology: Multi-pass membrane protein Catalytic Activity: ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2. Sequence Mass (Da): 73060 Sequence Length: 653 Subcellular Location: Cell membrane EC: 7.6.2.1

Q0CS59

MRRVTSVYVWLTVVVKDNTIIATAIPRITDQFKALEDVGWYGSSYLLVTCMFQLIFGKLYGYFPIKWVFLAAIIIFEIGSAVCGAAPTSDAFILEMVVSTYLPEPFDHVLSAGSFYINLPIGAVVIVVLLQFLHVPNTVPVEASSKTLFQHMDPLGVVTFLPAIVCLLLALQWGGTTFPWANGRIIALFVLAGVLLIAFLAIQRKRQDNAMVPPRIITMHPVAFSSLFMTLFAGAYFTIIYYLPIWFQAIKNASAVNSGIMCLPLMLSMVIFSFVAGGGVTATGNPVPFFYIATVLAAAGAGLMTTFEVHTGHPKWIGYQVLLGSGVGMGIQLPIIAVQAVLPAADIPVGTAILTFCQTFGGAIFVSVAQAVFANRLQTGLLRAVPGVSPGLVQEVGATNLDTVIDAQHMGAVKVVYNDALVSAWYLAVALFSVAVLGAVGMSTKRKSA

Function: Efflux pump that may provide the dual role of acetylaranotin export and self-protection by allowing the fungus to evade the harmful effect of its own acetylaranotin production . Location Topology: Multi-pass membrane protein Sequence Mass (Da): 48068 Sequence Length: 449 Subcellular Location: Cell membrane

F6QV99

MVHAETFSRPLSRNEVVGLIFRLTIFGAVTYFTIKWMVDAIDPTRKQKVEAQKQAEKLMKQIGVKNVKLSEYEMSIAAHLVDPLNMHVTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDHSCQVIVMGATNRPQDLDSAIMRRMPTRFHINQPALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVNSTSEESHDEDEIRPVQQQDLHRAIEKMKKSKDAAFQNVLTHVCLD

Function: Outer mitochondrial translocase required to remove mislocalized tail-anchored transmembrane proteins on mitochondria (By similarity). Specifically recognizes and binds tail-anchored transmembrane proteins: acts as a dislocase that mediates the ATP-dependent extraction of mistargeted tail-anchored transmembrane proteins from the mitochondrion outer membrane (By similarity). Also plays a critical role in regulating the surface expression of AMPA receptors (AMPAR), thereby regulating synaptic plasticity and learning and memory. Required for NMDA-stimulated AMPAR internalization and inhibition of GRIA1 and GRIA2 recycling back to the plasma membrane; these activities are ATPase-dependent (By similarity). Catalytic Activity: [protein]-with a C-terminal TM segment(out) + ATP + H2O = [protein]-with a C-terminal TM segment(in) + ADP + H(+) + phosphate Location Topology: Single-pass membrane protein Sequence Mass (Da): 40774 Sequence Length: 361 Subcellular Location: Mitochondrion outer membrane EC: 7.4.2.-

Q8NBU5

MVHAEAFSRPLSRNEVVGLIFRLTIFGAVTYFTIKWMVDAIDPTRKQKVEAQKQAEKLMKQIGVKNVKLSEYEMSIAAHLVDPLNMHVTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDHSCQVIVMGATNRPQDLDSAIMRRMPTRFHINQPALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVNSTSEESHDEDEIRPVQQQDLHRAIEKMKKSKDAAFQNVLTHVCLD

Function: Outer mitochondrial translocase required to remove mislocalized tail-anchored transmembrane proteins on mitochondria . Specifically recognizes and binds tail-anchored transmembrane proteins: acts as a dislocase that mediates the ATP-dependent extraction of mistargeted tail-anchored transmembrane proteins from the mitochondrion outer membrane (By similarity). Also plays a critical role in regulating the surface expression of AMPA receptors (AMPAR), thereby regulating synaptic plasticity and learning and memory (By similarity). Required for NMDA-stimulated AMPAR internalization and inhibition of GRIA1 and GRIA2 recycling back to the plasma membrane; these activities are ATPase-dependent (By similarity). Catalytic Activity: [protein]-with a C-terminal TM segment(out) + ATP + H2O = [protein]-with a C-terminal TM segment(in) + ADP + H(+) + phosphate Location Topology: Single-pass membrane protein Sequence Mass (Da): 40744 Sequence Length: 361 Subcellular Location: Mitochondrion outer membrane EC: 7.4.2.-

B4F6J6

MVHGEAFSRPLSRNEVVGLIFRLTIFGAVTYFTIKWMVDAIDPTRKQKVEAQKQAEKLMRQIGVKNVKLTEYEMSIAAHLVDPLSMLVTWSDIAGLDDVITDLKDTVILPIRKRYLFENSRLLQPPKGVLLYGPPGCGKTMIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVFSLAVKLQPSIIFIDEIDSFLRSRSSSDHEATAMMKAQFMSLWDGLDTDFNCQVIVMGATNRPQDLDTAIMRRMPTRFHINQPSLKQREAILDLILRNESVDSHVDLMEIARGSDGFSGSDLKEMCRDAALLCVRDSVNNSSEESPCEEIRPIHQQDLLRAIDKMKRSKSATNQNVLMHVSLD

Function: Outer mitochondrial translocase required to remove mislocalized tail-anchored transmembrane proteins on mitochondria (By similarity). Specifically recognizes and binds tail-anchored transmembrane proteins: acts as a dislocase that mediates the ATP-dependent extraction of mistargeted tail-anchored transmembrane proteins from the mitochondrion outer membrane (By similarity). Also plays a critical role in regulating the surface expression of AMPA receptors (AMPAR), thereby regulating synaptic plasticity and learning and memory (By similarity). Catalytic Activity: [protein]-with a C-terminal TM segment(out) + ATP + H2O = [protein]-with a C-terminal TM segment(in) + ADP + H(+) + phosphate Location Topology: Single-pass membrane protein Sequence Mass (Da): 40492 Sequence Length: 360 Subcellular Location: Mitochondrion outer membrane EC: 7.4.2.-

Q925I1

MSWLFGIKGPKGEGTGPPLPLPPAQPGAEGGGDRGAGDRPSPKDKWSNFDPTGLERAAKAARELEHSRHAKEALSLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRVQAEERRKTLTEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAIRRATVEREMELRHKNEMLRVEAEARARAKADRENADIIREQIRLKAAEHRQTILESIRTAGTLLGEGFRAFVTDWDKVTATVAGLTLLAVGVYSAKNATSVAGRYIEARLGKPSLVRETSRISVLEALRHPIQVSRRLVSRPQDALEGVILSPSLEARVRDIAIATRNTKKNKSLYRNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAMHKVFDWASTSRRGLLLFVDEADAFLRKRATEKISEDLRATLNAFLHRTGQHSSKFMLVLASNQPEQFDWAINDRIDEMVCFALPQREERERLVRMYFDKYVLKPATEGKQRLKVAQFDYGKKCSEVAQLTEGMSGREIAQLAVAWQAMAYSSEDGVLTEAMMDARVQDAVQQHQQKMQWLKVERPDSQTNKPPHPSLLSC

Function: Essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organism and cellular level. May play an important role in mitochondrial protein synthesis. May also participate in mitochondrial DNA replication. May bind to mitochondrial DNA D-loops and contribute to nucleoid stability. Required for enhanced channeling of cholesterol for hormone-dependent steroidogenesis. Involved in mitochondrial-mediated antiviral innate immunity. Location Topology: Single-pass membrane protein Sequence Mass (Da): 66742 Sequence Length: 591 Domain: The transmembrane domain and a C-terminal adjacent region contain all information necessary for mitochondrial targeting. Subcellular Location: Mitochondrion inner membrane

Q3KRE0

MSWLFGIKGPKGEGTGPPLPLPPAQPGAESGGDRGAGDRPSPKDKWSNFDPTGLERAAKAARELEHSRHAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRVQAEERRKTLNEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAIRRATVEREMELRHKNEMLRVEAEARARAKADRENADIIREQIRLKAAEHRQTILESIRTAGTLFGEGFRAFVTDWDKVTATVAGLTLLAVGVYSAKNATSVAGRYIEARLGKPSLVRETSRISVLEALRHPIQVSRRLVSRPQDALEGVILSPSLEARVRDIAIATRNTKKNKSLYRNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAMHKVFDWASTSRRGLLLFVDEADAFLRKRATEKISEDLRATLNAFLHRTGQHSNKFMLVLASNQPEQFDWAINDRIDEMVCFALPQREERERLVRMYFDKYVLKPATEGKQRLKVAQFDYGKKCSEVAQLTAGMSGREIAQLAVAWQAMAYSSEDGVLTEAMMDARVQDAVQQHQQKMQWLKVERPDSEASKPPHPSLLSC

Function: Essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organism and cellular level. May play an important role in mitochondrial protein synthesis. May also participate in mitochondrial DNA replication. May bind to mitochondrial DNA D-loops and contribute to nucleoid stability. Required for enhanced channeling of cholesterol for hormone-dependent steroidogenesis. Involved in mitochondrial-mediated antiviral innate immunity. Location Topology: Single-pass membrane protein Sequence Mass (Da): 66759 Sequence Length: 591 Domain: The transmembrane domain and a C-terminal adjacent region contain all information necessary for mitochondrial targeting. Subcellular Location: Mitochondrion membrane

Q6NVR9

MSWLFGLNKGQQGPPSVPGFPEPPSPPGGSGDGGDKNKPKDKWSNFDPTGLERAAKAARELDQSRHAKEALNLAKVQEETLQLEQQSKIKEYEAAVEQLKNEQIRVQAEERRKTLNEETKQHQARAQYQDKLARQRYEDQLRQQQLQNEENLRRQEESVQKQEAMRKATVEHEMELRHKNEMLRIEAEARARAKVERENADIIRENIRLKAAEHRQTVLESIKTAGTVFGEGFRAFISDWDKVTATVAGLSLLAVGIYTAKNATGVAGRYIEARLGKPSLVRDTSRFTVAEAVKHPVKISKRLLSKIQDALEGVILSPKLEERVRDIAIATRNTKANKGLYRNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMGREGVTAMHKVFDWAGTSKRGLLLFVDEADAFLRKRSTEKISEDLRATLNAFLYRTGEQSNKFMLVLASNQPEQFDWAINDRIDEIVHFDLPGLEERERLVRLYFDKYVLQPASEGKQRLKVAQFDYGKKCSDLAQLTEGMSGREISKLGVAWQAAAYASEDGILNEAMIDARVADAIRQHQQKMEWLKAEGKENAAKESGKNPLQPLLEGTPV

Function: Essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organism and cellular level. May play an important role in mitochondrial protein synthesis. May also participate in mitochondrial DNA replication. May bind to mitochondrial DNA D-loops and contribute to nucleoid stability. Required for enhanced channeling of cholesterol for hormone-dependent steroidogenesis (By similarity). Location Topology: Single-pass membrane protein Sequence Mass (Da): 66860 Sequence Length: 594 Subcellular Location: Mitochondrion inner membrane

W0T4C1

MNSGVLLSESETDTSETSERQSGLLSAQGSIKGKLEEFSAKLDRLRLDDENSEEEHALKSQSVSVNSEGNISRSASASASASASASAKLRNSQSPVQEYTSDTNPETDASFRVKIRLRPIGSIPQIQPRVCQISSHQNFSALVKFLCKRLKRNHVHCYINNAFAPSLNQTIGDLWSQFKTNDELIVSYCETVAFG

Function: Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt), autophagy vesicles formation, mitophagy, and nucleophagy . Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function (By similarity). The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 and ATG8 association to the vesicle membranes (By similarity). ATG12-ATG5 rearranges the ATG3 catalytic center and enhances its E2 activity (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 21388 Sequence Length: 195 Subcellular Location: Preautophagosomal structure membrane

A5E1F1

MSQLQDSSIRQSDPDSDLDSDSNSNSDLGSLVDQGNAQFEDEYIATEEQTNLEPKVPLSTSIVLDKLPQDQQSQLNHNPYLKSEQKSQSREGTKFRMETVLPKKTTEKNENQHSSASTTKSPEKVTIRFQPIGSTTAIHPKVFKISSVQSILTVNRFLSQKLKNNERQPLHLYIQNSFLPSPDERVGDLYALFATNHELIISYCNTIAFG

Function: Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt), autophagy vesicles formation, mitophagy, and nucleophagy. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate functions as an E3-like enzyme which is required for lipidation of ATG8 and ATG8 association to the vesicle membranes (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 23631 Sequence Length: 210 Subcellular Location: Preautophagosomal structure membrane

Q9CQY1

MSEDSEVVLQLPSAPVGAGGESLPELSPETATPEPPSSAAVSPGTEEPPGDTKKKIDILLKAVGDTPIMKTKKWAVERTRTIQGLIDFIKKFLKLVASEQLFIYVNQSFAPSPDQEVGTLYECFGSDGKLVLHYCKSQAWG

Function: Ubiquitin-like protein involved in autophagy vesicles formation. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. PTM: Acetylated by EP300. Location Topology: Peripheral membrane protein Sequence Mass (Da): 15207 Sequence Length: 141 Domain: Shares weak sequence similarity with ubiquitin family, but contains an 'ubiquitin superfold' and the C-terminal Gly is required for isopeptide linkage. Subcellular Location: Cytoplasm

Q7S083

MASSQPLHGTASPSLVHDDNNPNSSTASPVLEGRDSPNLPLTMTASTVLMTLPRDATAALAEAGTFDQEKVVIRFKPVGSAPALRREQVKVLSTHSFETVVAYLRKTLKVQETDSVFLYVNSVFAPALDEVVGNLWRCFKDSTNQLNVSYSMTPSFG

Function: Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt), autophagy vesicles formation, mitophagy, and nucleophagy. Conjugation with apg-4/atg5 through a ubiquitin-like conjugating system involving also apg-5/atg7 as an E1-like activating enzyme and atg10 as an E2-like conjugating enzyme, is essential for its function. The atg12-apg-4/atg5 conjugate functions as an E3-like enzyme which is required for lipidation of apg-6/atg8 and apg-6/atg8 association to the vesicle membranes (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 17001 Sequence Length: 157 Subcellular Location: Preautophagosomal structure membrane

A7KAM3

MNTSSPTRSPQSSPSPNPQSTLSHRPSPRQPQSSDTPPNSSANAPIPDDEHGADLPMNMTASVMLTNLPRDAHQALADVESIDSGKVTVRFQPLPSAPILKNRVFKVSASQKFETVVKFLRKKLDCKDTDSVFCYVNSVFAPGLDEGMGGLWRCFKTDDQLIVAYSMTPAFG

Function: Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt), autophagy vesicles formation, mitophagy, and nucleophagy. Conjugation with atg5 through a ubiquitin-like conjugating system involving also atg7 as an E1-like activating enzyme and atg10 as an E2-like conjugating enzyme, is essential for its function. The atg12-atg5 conjugate functions as an E3-like enzyme which is required for lipidation of atg8 and atg8 association to the vesicle membranes (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 18695 Sequence Length: 172 Subcellular Location: Preautophagosomal structure membrane

Q0UNW1

MSAQEERIPEDDDTTEAPLTMAASVVLTNLPRDASKALETAGSLNVQKITVRLHPIGSAPALTQRVFKLSTNQRFDTIVRFLRKRLGVKEHESVFCYVGSVFAPGLDEGVGGLWSGEELVVGYAMAPAFG

Function: Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt), autophagy vesicles formation, mitophagy, and nucleophagy. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate functions as an E3-like enzyme which is required for lipidation of ATG8 and ATG8 association to the vesicle membranes (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 14049 Sequence Length: 130 Subcellular Location: Preautophagosomal structure membrane

A7KAJ7

MSDKDLASSLMELNIKVGTTDIPQTIAEEQNQVTDTKEEVLDDETTIKNDPQKTKITLNQSMMLSKLPAKTTSAVLSVSKPTESKIQIRFKSIGSVDQVSPAVFKISKSSKFSSILRFLELKLGKKVYCYLNNSVSPNPDEELENLYNIFRVGDELIVSYCNIVAFG

Function: Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt), autophagy vesicles formation, mitophagy, and nucleophagy. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate functions as an E3-like enzyme which is required for lipidation of ATG8 and ATG8 association to the vesicle membranes (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 18587 Sequence Length: 167 Subcellular Location: Preautophagosomal structure membrane

A5DK05

MTPPTSNSSMVDSLSSWVAESLSSDMRNNYSTSVGKGRAKLACGFYQERWCIDALQKVVSINEILCGMSFIHSEPDSDSSTTSADSNTLSQHVDKTSVPLDTSIVVKRLPEVEQRQWHKTIKPLPATKITIRLVPIGSTRAITPKVLQVSSDQTVAVLMRFIAKKLRISTDSVYMYIHNTFQPTPDERLGDLYDQFRTNQELIFNYCNTVAFG

Function: Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt), autophagy vesicles formation, mitophagy, and nucleophagy. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate functions as an E3-like enzyme which is required for lipidation of ATG8 and ATG8 association to the vesicle membranes (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 23830 Sequence Length: 213 Subcellular Location: Preautophagosomal structure membrane

A3GI31

MFLSERVKEPSRIPLSNESEEAVGGSAENANTVDDEDAKTEVSNDRIDNENNTATASSGAVHNEYTSIDAEGPEKEPLATHGLSMELISDISTSKEVQKHLEKTEPETTSTSKYSIQSDTSSKSDSSPNSGTAPKRASSLKPGLDSDSTLKADSSPKSASEAKTTIRFVPIGSTPRINPLVFTISSNQTVSILIKFLAKKLKTKDHVYLYIQNSFQPTPDEKLSDLYNLFRTNNELIVSYCESVAFG

Function: Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt), autophagy vesicles formation, mitophagy, and nucleophagy. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate functions as an E3-like enzyme which is required for lipidation of ATG8 and ATG8 association to the vesicle membranes. ATG12-ATG5 rearranges the association to the vesicle membranes (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 26831 Sequence Length: 247 Subcellular Location: Preautophagosomal structure membrane

Q5R7W1

MAEEPQTVLQLPPSSAAGGEGLTDVSPETTTPEPPSSAAVSPGTEEPAGDTKKKIDILLKAVGDTPIMKTKKWAVERTRTIQGPIDFIKKFLKLVASEQLFIYVNQSFAPSPDQEVGTLYECFGSDGKLVLHYCKSQAWG

Function: Ubiquitin-like protein involved in autophagy vesicles formation. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. The ATG12-ATG5 conjugate also regulates negatively the innate antiviral immune response by blocking the type I IFN production pathway through direct association with RARRES3 and MAVS. Also plays a role in translation or delivery of incoming viral RNA to the translation apparatus (By similarity). PTM: Acetylated by EP300. Location Topology: Peripheral membrane protein Sequence Mass (Da): 15081 Sequence Length: 140 Domain: Shares weak sequence similarity with ubiquitin family, but contains an 'ubiquitin superfold' and the C-terminal Gly is required for isopeptide linkage. Subcellular Location: Cytoplasm

Q9US24

MTGLVDQQELEKRLATEEDSQNEDIENQLPSIETIINTYREKENRRVNLRFKAIGRTPLLRKTVFSINASQRFEKVTRFLKKELGLPMNSSLVLYVNSSFAPSPDEIVGNLYDNFAIDSHLLINYCINVAFG

Function: Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt), autophagy vesicles formation, mitophagy, and nucleophagy. Conjugation with atg5 through a ubiquitin-like conjugating system involving also atg7 as an E1-like activating enzyme and atg10 as an E2-like conjugating enzyme, is essential for its function. The atg12-atg5 conjugate functions as an E3-like enzyme which is required for lipidation of atg8 and atg8 association to the vesicle membranes (By similarity). Plays a role in meiosis and sporulation. Location Topology: Peripheral membrane protein Sequence Mass (Da): 15154 Sequence Length: 132 Subcellular Location: Cytoplasm

A7EAE5

MTSSLLLTNLPHDSSSALEHAFSFPTAKITVRFQPIGSAPILQRPVSKISSSQQRFETVVAYLRRVLKLDRKGGEGDSVFLYVNSCFAPALDEVVGNLHRCFKDSKDQLIVTYSMTPAFG

Function: Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt), autophagy vesicles formation, mitophagy, and nucleophagy. Conjugation with atg5 through a ubiquitin-like conjugating system involving also atg7 as an E1-like activating enzyme and atg10 as an E2-like conjugating enzyme, is essential for its function. The atg12-atg5 conjugate functions as an E3-like enzyme which is required for lipidation of atg8 and atg8 association to the vesicle membranes (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 13250 Sequence Length: 120 Subcellular Location: Preautophagosomal structure membrane

F7W503

MASPQPPFGGGSNSNSNTASPSNNLSPTASPLLEGRDSPNLPLTMTASTVLMTLPRDATAALAEAGKFGQEKVVIRFKPVGSAPALRREQVKVSSTERFDTVMTYIRKTLKCRESDSVFLYVNSVFAPALDEVVGNLWRCFKDSTNQLNVSYSMTPSFG

Function: Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt), autophagy vesicles formation, mitophagy, and nucleophagy (By similarity). Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function (By similarity). The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 and ATG8 association to the vesicle membranes . ATG12-ATG5 rearranges the ATG3 catalytic center and enhances its E2 activity (By similarity). Plays a role in sexual development and perithecia formation . Location Topology: Peripheral membrane protein Sequence Mass (Da): 17139 Sequence Length: 159 Subcellular Location: Preautophagosomal structure membrane

A7TJM4

MSGMLLESESDHEDSEISSGYSENGRLMSQDPLSLSTGNVMQSRLEQYSKRLSQLGLAATDGDSNGDGTDNDIIPSEYDEEEISVPKQEVPMTTSLILDKLPPTTNEFLHQLSIKEMEQDIEKTVHKIQIKFQPIGSIPLITPSVCTISSQQTFSMIILFLKKRLKVEQVFCYINNSFAPNPQQTIGSLWSQFKVNDELIVSYCGTVAFG

Function: Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt), autophagy vesicles formation, mitophagy, and nucleophagy. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate functions as an E3-like enzyme which is required for lipidation of ATG8 and ATG8 association to the vesicle membranes (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 23390 Sequence Length: 210 Subcellular Location: Preautophagosomal structure membrane

Q5AI71

MTNEINSATVTQDEVIKWSREAQSTLEKTQKICTDAQSSMQKTAQELTILIPDKLQAIEFLFKSYREQYDSILKQIETTKIYLHTNIDKVFNDIKDLLDPSLARLNNILLELKKTRVPSIVVEGTSEGKTLFDFTSIQSINLLKENIGIFKSNCSKIKNLLDLEVKEKLNIEQDRMNSRWNKSVKMYDLIAPLQLELRALIHGASNESNSFMGTILRENQALENELVSILEMQTNHFDQCMKAVELISSGNGCDMNLGVLKNDAQELPEVFKELTTIYDIILRNEERSKKFLATHMPNIEKISDIVKEELAVFRKFKTEEIPRYTFLIAECENKLKECSMPVKSDQSPSQVYTQTLQELTEHYVKFINIYKTKYLAELHHQQFTYPRKFLKKLTEFLNEDIYRIQIEESERRRQWTSRYGEFIPSEFKLPGEHELPVIVQIITEGLEYIQKEDGQEEEPNIGNEKELMDMITGSNK

Function: Autophagy-specific protein that functions in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize pre-autophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles. Plays particularly a role in pexophagy and nucleophagy (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 55407 Sequence Length: 476 Subcellular Location: Cytoplasm

Q6FPD4

MPESLAERARSTLLKAQVLCREVESRIAEVKDRLSQWEKNRHTLRFLVSCLEHQLGFLEQCALRQGIGRALIETEWSQVVLVDLVNEMKLWYDKIQLRLERLDQVENILVADNKHLSHYISQEQALVLKKRLDEVPIIRPQIENIQTQYDTMCKRVRQKLINKRLTEIKTIFDSQFGDELTETAELTEVKPRDLDSIELELVDYINSLTDHFDKCQALEKGLFNDSNEYDELLKIVSADDSQLDDIMKHLLNTIDSTNHQIDKVYEILDIKTKQKTILHGKINELIANCTKYSEYLAIFKGIATSIEKFKEGCMQDIQLTKELYKFYDEFENSYNKLLQEVQRRRALSQKMLGIIKNCENELKTLHDEDQKLRTHFLSENGAFLPETIWPGEIDDLSPLYALDYHIKEI

Function: Autophagy-specific protein that functions in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize pre-autophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles. Plays particularly a role in pexophagy and nucleophagy (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 47978 Sequence Length: 409 Subcellular Location: Cytoplasm

Q6BSK5

MSSGVDRDTVISWSEQAQTTLQEAKKMCTRAQASLQSTTYQLVTQLPERLQFVTFMVDALKQQHELLTSIVESQSRIRKESVSQFNVQVERDLTPALAELDDILARLAKAKVPSYLINNVVHELEVHIDTLVEDRNLCDFISMDDIKLLTTNIEIYKANCTKLHGLLEKTMNESVIEPYQIIALKKYHNIMKQYKELMPVQLGMNLAPDVSPYKLNNLINTILKENSSLEHELVPMLEMMTNHYDQCVQGTLFFNTKNPKDPSGDVNFEVLRNDALELPDVLKELNTVYDIIVNNEVRTKKLLSSEFSRIDSLISMIKDLLEFYTDYKATHLSKYMILVLSCDEIFGKCSIAMNSNQTPLEAYIETITSLSYHYTQFLSIYKSEYLTELFYEQYTYPRKYLAKLTDFLNNDMFHLQQEEYERRKNWLARYGEFIPNEFKLPGELNQPSIIQVVTEGLDDVQKDYNDGKFNESAEEINLSDLIKTMKL

Function: Autophagy-specific protein that functions in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize pre-autophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles. Plays particularly a role in pexophagy and nucleophagy (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 56482 Sequence Length: 487 Subcellular Location: Cytoplasm

B0G140

MDFSSKSLELCKSHSNQTDQLLKISKQTYEKYDNSLSKLHLIIRELNKQLIILKETSTQFNDRYNTFINDFTSLSNQKQSLFTSIENKLEILKKKYLDKGLVFKNNNNNNNNNNNNNNNNNNNSNKSTEDDNNENNNNNDVNKNNNNNNNNNLNTLYDFIDIESLELIKNQFLSELSGLNEICDKSKQIYKSTNESNLEMENRFLEIQKQYNKQIEESNSLSDLLTQQNNLYKTIQNQLINVASQCDFITFYKPSPSPLSPSPSPSSSSSSSSPSPSSPQQQHDFNINNKKEQIQLLLTSSLENIQLMSKNVKDIENQFKESCSIYTLVYLLNEKLSFGNDFSENWETFERFNCIFEQRLAGANYFIGELYSLGKWYDLFDESYDNLLEEVKRRQKEYLRQKTIAEQFNEELKHNYNQEIQNRLKFYDSYGKYLPVSLFSTISDQPISFQVKQIIEESVIDYSFNPLNLKRSSPINQQQQQQQPPPNS

Function: Autophagy-specific protein that functions in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize pre-autophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles. Plays particularly a role in pexophagy and nucleophagy (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 57014 Sequence Length: 488 Subcellular Location: Cytoplasm

Q5AZC0

MSAVDSSTSSGHPEREAQHETGLPPLETLISHLVAAKRSLSAINHVWRANEIVTSARSALEESVVVSARTGFLRSGLNNQLRLLYNVRAEVEEISLRGRSEFANALKSLDAADARLKKTLGLLRETIVHASFRPEGEEPKSLHDFVDERGVEELHSTLKSSIDRTNAAQADLDASNNAFDVELQSIKQALSTYRATTKLASSRGSVSSSGSQSGSSSSLPSISSMPSMVHSLEMHAQEMANLLESLVRHFDLCVTAVKHTEGGGAAAQSITGDMPAGVMGSHPGPGHGAGTGPTIEGDFNANPNAPLDPLSASEYREMVSVIVNDAAEAEDVVMEIQDRIGEMESVLETLTAQRDSFAAIYNATKEVFSYLSSLASTRLPGYIAQAHAFTAVWNDEHDRIKGGLADLSDLNALYDGFLDAYDGLIIEVARRRHVRHRVEKILRDARNKLDALYEEDVNARETFRVEQGDYLPSDIWPGLSREPMRVEFHRISGGPLKGVLQSPDQAQSPQPNEGEQLGHQDPQNPGDADSRFGEVIPDLPQELVEQALARLKSKRQR

Function: Autophagy-specific protein that functions in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize pre-autophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles. Plays particularly a role in pexophagy and nucleophagy (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 60607 Sequence Length: 557 Subcellular Location: Cytoplasm

I1RR07

MASSSATSLRQGSSGASSGHSHPQSTSLSRHSNSNSNSSRSRSFTHQDVDPNAPSISIDTLVNHLLVAKRSLSSMTLVLRANEIANAARQSHEDVAILAAQAGFLKESILDQTTILVRVRRSLQGTYDWGKRDFKKLIRSMDLVDGGLEQTMEMLRDTSVEGVFRPEGEERRSLLDFIDEGGVHGVREAMKKSIQELQSFDGDLLRFDTDIRNLRKIITDTPALTHDDTHFPTFELLEGLVDHSANMAQLLVSLTHHFDMCVTAIRTTEGGVALARRRAAEVTQTQGNDGVSISGVIAEQESNVSDLEPNTAKDRAEMLKVVVQDAGEVNDVVQEIQERLTAMEQDYLVLQEQHDISKQAYSNMLEAYAVLGEIGDRLADYLAAEGDFKSRWDMEKESVFSKLQEMQQLKEFYERYASAYDSLIIEVERRRAVDDKVKNIWRKAQDSVDKLLDADRASRETFRQDVGEYLPTDLWAGMQGSAKKWTVVPDGEGEDVKGPALRRSVVEGARERLGRVERR

Function: Autophagy-specific protein that functions with ATG13, ATG29, and CIS1/ATG31 in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize pre-autophagosomal structure (PAS) formation (By similarity). Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles, through interacting with and regulating ATG1 kinase activity (By similarity). Plays particularly a role in pexophagy and nucleophagy (By similarity). With ATG13, is required for ATG1 activation by autophosphorylation (By similarity). Recruits ATG9 to the pre-autophagosomal structure (By similarity). Autophagy is required for proper vegetative growth, asexual/sexual reproduction, and full virulence . Autophagy is particularly involved in the biosynthesis of deoxynivalenol (DON), an important virulence determinant . Location Topology: Peripheral membrane protein Sequence Mass (Da): 58016 Sequence Length: 519 Subcellular Location: Cytoplasm

W0T3R8

MSYHYDGIPDIEIDLYWNKARNHLLKAQVECEESLKLLSTIRSEMDSCQKSRLKLQFILNCLVNQVEFFSSVILEKCIAVELLDNEWSKVVLVGVVKDLNYWQDEITNKINALKNTKYDLNAEYKSLADFICEDHVEILQQKLDEVPFIKKQVSNIRQHYKSIKEGVQYQLKAGKVKKLKKYYETHFSRDNHLFELLEGEYLTKLNSYESELTDYIRSITDHFDKCSILKADGLPPQDLKDLFEVVKNDDAELEHIRELIYESDAEITQFYKNVEGTITSIKENVADFYGLSTKIMVELEKCEEYVSIFQDIAKLVSVYKESCIRKIEQVQELCEVYDKFKKAYFNLLKERERRKSVAIQMKSILDECKGKLMALNEDDLDHRQQFLHENGDYLPENIWPGKIDDMTPLYSLEYTIYNEQK

Function: Autophagy-specific protein that functions with ATG13, ATG29, and CIS1/ATG31 in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize pre-autophagosomal structure (PAS) formation . Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles, through interacting with and regulating ATG1 kinase activity (By similarity). Plays particularly a role in pexophagy and nucleophagy (By similarity). With ATG13, is required for ATG1 activation by autophosphorylation (By similarity). Recruits ATG9 to the pre-autophagosomal structure (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 49638 Sequence Length: 421 Subcellular Location: Cytoplasm

Q51Y68

MPSSSSARSSQSLRSSAAAAVSTSSGAADQPSVPIEILVEHLLAAKRSLSSMTLVLEANDLTTQARSVHEDSVVLAARTAFLRAGIAQQIHTLERIRRGLARTYDVGRRDFEQLIKVLDDAGERLTRTMNVLHNTIVDPVFRPAGEEPRSLMFFVDEGNVDRLTKSLKESIAELKAAETSYDGDLLRFDNDIRSVKKHLLAAPGLPSPSNSVFSRPMADLVRTLTNHSHAMAENLSSLTRHFDLCVTAVRASEGGAALALRKAAEDGPSTISISGVIRGDGTDADDQDIKTMSARERDEMLRVVMQDATEVGEVVRDINSGLEEMQALGALVEQQAAHVRTAHECTLDAFRRLEEVEARLGSYVAAEREYVDRCEVEKDAIHERLAQAEDLVVFYEGYAGAYDGLVLEYERRRNVEDKIRALWRKAAAAVEKLEEQDAAARDSMRKDVGDYIPGDLWVGMDDPVRKWKVVAVDEGEGGSGEIEGSSVRLKKGTVEAARERVHGR

Function: Autophagy-specific protein that functions in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize pre-autophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles. Plays particularly a role in pexophagy and nucleophagy (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 55292 Sequence Length: 504 Subcellular Location: Cytoplasm

Q872W1

MASFHSHSPSPPAALSPDDAPQPRRPSRTSLHDAAAAAAPALSPESPGHELEDGADSSEFNADDVPVEVLVKHLLAAKQSLSSMTLVLRANDLATSARQMHQEFVILSAQTAFLRHGILQELHILHQLRRGMARAYDNGTRDFKHIIRTLDTADGRLEKIMQVLRKTTVENVFRQPGEEPKCLLDFVDPKIVEQVRDALKESIHELSAAKTSFDGDLLRFDTDLRTLTDAMAAAASLANPTTTTPDGYPPDQRSIPNLLSALSEGSHLMAEHLSSLTRHFDMCVTAVRTTEGGAALARRRAAEATSSDEDQAPVSISGVISAQESESGPSAFEPMDPLERQELLHVVMRDAAEVDDVVADIHNVLQQMEMDHASLHSLFSASRASHAATLTCFSMLEEVGARASSYVAAEAEFMQRWEDEKETIDENVSKMDELKKFYEGFLNAYGGLLLEVERRRAVEGKIDSIWRKAKEQVDKLVEADKREREHFRLEVGDYVPADLWGVVDRPLGRWAVVPLEDTREGSYEMEAHGEPENEGKVETAYERETEPSTPTPRKMPLNGPGSAGERPF

Function: Autophagy-specific protein that functions in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize pre-autophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles. Plays particularly a role in pexophagy and nucleophagy (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 62724 Sequence Length: 568 Subcellular Location: Cytoplasm

A7KAM6

MASSQSSSSSIRPQAGLNEGDHQSLPQLDTLISYLLGAKRSLSSITHVWRANEIVTASHSALEKSVVLCSRTGFLRRGLNGQLRLLYDVRSEVEQISYRGRDEFSIALKNLDAADARLKHTLDLLRGTIVHASFRPGDEEQKSLHDFVDERGVEELHASLKASIDRTNTARAELDTSNHEFDDELQAIKKSLRHYHTATKLASSRLSITSSSSSASDSGLLTLSSMPGQIQSLEAHAQEMATLLEALVRHFDLCVTAVKHTDGGGAVARSITGDMPAGVDGSNDGMPNIGAEINANLNAPLDPMTDAEYQEMVAVLIKDAPEADDVVMEIQDRINEMESIFEQVQAQRDALLSISKATIEVHSHLSSLASSRLPRYISQAHNFTRVWLEENDRINSGLVELSDLHSLYDGFLNAYDSLMLEVARRRHVRQRVEKVLRDTRHKLDQLHDEDAAARETFRAEQGDFLPSDIWPGVGLAPMQVQFTRLSGGQLDGGPIGQKPLEEPSGGEYAGAAKAGVSDGSAEGEQIPDLPRHLVEEAYARVKARNKVASQLHTV

Function: Autophagy-specific protein that functions in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize pre-autophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles. Plays particularly a role in pexophagy and nucleophagy (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 60713 Sequence Length: 554 Subcellular Location: Cytoplasm

A7KAK1

MAIPIAQWVADARANLAHAEQVCNDANMYLTSTSEKLRRREMKVPKLIYYLDALKQQLRLLEIIRDSLVLNLNGVMEKRAALQSQLLKDVDRLHQTIDTLKNTVVVFDGQTTLYEYISESGVEELFNGVSQNLKDIQTLIKGNRTDALLIRLTSDLDHLSNELNALDSKFRDMRLVDTQSSSIDPISKLLEINAELEHDMVAILTSFNNHYDQCEKGEAILKDPAVPQDEKDELVSVLQNDVEELPEAQRSLTSNAEIIKKNCKEVMKILDIFEDYFQRVETYVCELQEYGESKLRVQLKEFSDINTEVSRKLEIAQTHQDELVQYNSDFQQFVRSYYSLILELDRRMRVNEHISSAIDNFRSTISNIVEKDHEKRMEFLQKHGDFIPQNLVDSSVINSGTPQISINFDQEPLPAISKEVVQLAKKMQK

Function: Autophagy-specific protein that functions in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize pre-autophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles. Plays particularly a role in pexophagy and nucleophagy (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 49398 Sequence Length: 429 Subcellular Location: Cytoplasm

A3LX29

MHATVDRATVTAWAKQAQSTLEKAQTLCTNAQTSLHATSYQLTSHLPDLLEEANVLYESLKTQHELLAKISESLRRSIRDQLLNTLEKQQSTLLQPALNNLDDIVGHLSATIVPSFLIEKDEAENRTLADFISTDSINLLRRNIQIYTNNHEKIRQLLNNKLQDVILSPFHEIGSKKFNKTVKLYEEITPLQLKLKAITSNIAPLDSSNVVATLLKENAALENELVSILEMLTNHYDQCTQGVQILYSGGSQQVNLEILKNDAQELPDVLKELHTVYDIIVNNEARAQKFINAHSPSIEVVIATMKDQLSFYRSFKSKNIPEIMVLFTVCEEILMKSPIEDPGGPEQTPIEKFTDTVNQLVYHYTQFLNVFKSQYLRELHHEQFSYPRKFLSKLTNFLNDELYKMQIEEKERRRAWLTKYGDFIPKEFRLPGEYNQPVITQVVTEGLEDVQKEGADAERHITQEKELLELLRKMEELNRERRY

Function: Autophagy-specific protein that functions in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize pre-autophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles. Plays particularly a role in pexophagy and nucleophagy (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 55710 Sequence Length: 483 Subcellular Location: Cytoplasm

O42651

MELLQQWTQQAKAALTQARQLCGDAHKFNEDAKTDLRNSIKQHQQLKELAKLTASQCTRLDSSTALIKQLLDLVQNYPTFNQLNVLHDRLESSLKRLRDCTLDPALGSEYTNLYAFVDDTALEDLKTRLRGVTDGVWNAFEKLAGLLEEDLCANYHKRLEAVSLDFLPPAYNDTAEELADLLLQVAQHYDQCSEALNIYDTLSDAEKKDLQEVLQSDSNHVPSVLTELRSGLDQTIHYFNAVQSYKSKVDSATSILEALAEELNKNQLTNQRHEAAHELMRAQTGLEIPQLAQELVQLERHYTHFAKAYTALLQEIHRRQTYENCVRSIVDEFVGRLEKEQQAEAKCRIDFFNQYGDYLPQTLWGAVTDPPLHFEIIEHQYTELPNVKVIPDKNDKKSKQREKSSTTASKR

Function: Autophagy-specific protein that functions in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize preautophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles. Plays particularly a role in pexophagy and nucleophagy (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 47062 Sequence Length: 411 Subcellular Location: Cytoplasm

A7EM16

MASPTNAPGSQSQTSVSSANHPDPIIHGREILETLVSHLLASKRSLSSISTVWRANEIVTSAKTALEESVILNARTGFLQSGINEQMKVLMKVRNSIECVYNDGQKDFKNVLHTLDAANARLESTMDVLRSTMVDAAFRPAGEEPRSLLDFVDEQGVEGMRDGLKELIRESKETQKEFDTSLLSFDDDLRSLRSGFKNTKVSPPSYSPIPSHLATLEGHAQEMAALLSSLSSHFDLCLNAIRHTEGGYAAVRNAASNPPPGAEPVSVSGVMNTSHDDINEEPLTEHEREEMLFVLEKDAAEVEDVVMELRDRQNEMEIKHDAILDHVSHLTEQFKQTTSIYKILEGVYERLPGYIIAGQDFRARWEDTKAQICGQMDDLEGMRLFYENYLSSYDGLILEVRRRKVAEEKAKTIAKKAMEQISKIYDADMKERHDFKHDVGDYLPVDLYPGINAAAPRWEFRLMEDEEAVNSSPSLERELVEVSSKRDGEAQG

Function: Autophagy-specific protein that functions in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize pre-autophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles. Plays particularly a role in pexophagy and nucleophagy (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 55103 Sequence Length: 492 Subcellular Location: Cytoplasm

A7TM40

MKIERFVNASRKTLVEAQVLCQDANSRISNARSSFSHWERSISKIRFLLNCLKNQGSFIKNCILKVGIEENLIEKEWTQSILVDLAKELKYWNSKINEQVRVLDSIENILDEDTKSESKNLGYFVSRDNLDILEKRLKEIPNVKYHIDNIRGQYNTMFKKVSNYLINKRLKSVQEYFLTNFENDSDDIKKLTTTLPSKLVSLEHDLADYLSSITNHYDQSKLLQTLKPADPDYTDLLEVVKNDNSELDGIVTLLRETVDEVDETLKTFLGIFNEIELKQKECNKLLFGVIEEFKINHEYLLIFNDISSLIDNFKETCIEDINNTRSLCIFYQKFEIGYQNLLFEIERRKTVAQKMTDIIKNCELELSKINEEDQKNRSEFLKLNGDYLPENIWPGKIDDFSPLYSLEYSIKEI

Function: Autophagy-specific protein that functions in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize pre-autophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles. Plays particularly a role in pexophagy and nucleophagy (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 48447 Sequence Length: 413 Subcellular Location: Cytoplasm

Q6C0L6

MEQLFREAQDALAAAGPLCQESQDVLARARQNLEVAVHLGIRTQFLAKAHAHQWTLASKFYSNALTRTKKSLETVTRQQTRFQAARGALEEALGELAATPVQLRVNNGAHNLREFVDEDLISAQVQGKGWNEVHEEALNVFRVLLPEIQRHGDIVNRSKKEFEREKAEQTELLIHQTSDSGIYDLLNSAEACSEDMANLLQSLARHYDLCERGQDLSTGAIEAEDVNELGELRAVLENDAQQLPDVLDELQERLDEVKQGCQGVHNHMTQMYHSYSLEVRQLEGIQAVEKTMDATLEICETQQRDTKEYLLKVQRYVSETSAVVTHYQTFLNSYKALLHEAERRNAAEAKMKDYVTEVNAKLAQMSIQETNRRQDFVAQQGDYLPADIWDELLLPSRRFEARELDGEL

Function: Autophagy-specific protein that functions in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize pre-autophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles. Plays particularly a role in pexophagy and nucleophagy (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 46433 Sequence Length: 408 Subcellular Location: Cytoplasm

A7KAK7

MLHLITPLLLLLARFSMAIDISDEHFSAYPRMKELIGSHLVSRTEETPPSTKKITWYLKITDSGSGSPKDDTFPSECPKDSQLCGLTEISLPNRDPVITEVFSFSNKLTPQFDVNTSSFIVNLRGANWGAYTLDAEIEFVCASDDNAEGLKLVKFDYSTVSLQYKTSSACKSNETPPKDGKNKAPKDDDSNSWGVFTWLFILLVIVMASYIIAQAWINANRVGSSHEFLNELVESIVETLTKLPEFLREIANKLFTSGSRGGYSAV

Function: Regulates the cytoplasm to vacuole transport (Cvt) vesicle formation. Location Topology: Single-pass type I membrane protein Sequence Mass (Da): 29537 Sequence Length: 266 Subcellular Location: Cytoplasmic vesicle membrane

A7TFH9

MLKMRLLLTWVLLVLPLVNALKCANNRVLRKYHIDKHSAKKSVARDTPPSKTTEKWYVNPCEEHPADDIYDGCDKSDDICGIVMVDLPVFNKDPFVIKRIEATDMASFTATEESNALVLRYTGISWGQNMVAANIRYFCDKNSNEDEITSSIWANNDISIIIKGPSGCKKDSSELEDGDVEESSGLSWFTWLFIYAIFFTVVYLVVTSYTQTRGGSIDDFRHDFVERAKQFFTSLPAFVREVVSKVLGSAPNAAERGGYSAV

Function: Regulates the cytoplasm to vacuole transport (Cvt) vesicle formation. Location Topology: Single-pass type I membrane protein Sequence Mass (Da): 29436 Sequence Length: 262 Subcellular Location: Cytoplasmic vesicle membrane

Q6CBS9

MKSAIIGYMAVAVAAASCQFTVDSKNYDLSAISGPKSVEYTIETPPSKRKMEFVLDPCASLKQDKKKPADEQCPDNTIVCGLGYILLPKEKDFVLSEVMPFGNGPAPQYQPLKTGPEGTEGLSTSYGNPWGSEKLDIDVNYICSDKEEGPKLENVGLGLNNYYEINWKTPAACINDGSKPKQPVKEPGKTPNDGDDASNGNPSWGWFTWLFIIIVLGVAVYIIGNAWINYDRYGNAGVDLLPHADSLRDVPYLIRDLIAKVVGTFTGSSRTGYSAV

Function: Effector of VPS34 phosphatidylinositol 3-phosphate kinase signaling. Regulates the cytoplasm to vacuole transport (Cvt) vesicle formation. Plays a role in ATG protein retrieval from the pre-autophagosomal structure (PAS) and is especially required for autophagy-dependent cycling of ATG9 (By similarity). Location Topology: Single-pass type I membrane protein Sequence Mass (Da): 30002 Sequence Length: 276 Subcellular Location: Cytoplasmic vesicle membrane

P46989

MVSKTWICGFISIITVVQALSCEKHDVLKKYQVGKFSSLTSTERDTPPSTTIEKWWINVCEEHNVEPPEECKKNDMLCGLTDVILPGKDAITTQIIDFDKNIGFNVEETESALTLTLKGATWGANSFDAKLEFQCNDNMKQDELTSHTWADKSIQLTLKGPSGCLKSKDDDKKNGDGDNGKDGDSEGKKPAKKAGGTSWFTWLFLYALLFTLIYLMVVSFLNTRGGSFQDFRAEFIQRSTQFLTSLPEFCKEVVSRILGRSTAQRGGYSAV

Function: Effector of VPS34 phosphatidylinositol 3-phosphate kinase signaling. Regulates the cytoplasm to vacuole transport (Cvt) vesicle formation. Plays a role in ATG protein retrieval from the pre-autophagosomal structure (PAS) and is especially required for autophagy-dependent cycling of ATG9. Location Topology: Single-pass type I membrane protein Sequence Mass (Da): 30201 Sequence Length: 271 Subcellular Location: Cytoplasmic vesicle membrane

A0A098DT87

MSSPSMFDRISSPRQRLSNPLRSPPIREVSEYDLDELEPRSDDVLFDQEPPLPRLKKNMQHVSATSTRRSSSPASWDSKHRYSNSPPHTRSKPIFAGPPPPIASSMMMNQHPSRQSTVSSHGDNGRGYGLISASRFGSNSPSQKHVDNRPRLDSIWRSLQRREKALERDIQQLLDLQASGLIAGSGEGSESNFGSDTTTGESTFYSTATSKSRMMNSLHMPTRSTPDGNVIPVRQPVSNKPRGLKSTRVGLQRSMAALSDLKAEEDLHLSTALEQRKDALAYLDKMSKRRDDIYSELHALEDDEEEPLGQELRSLEAERQELDHDIQRLEEKLAGAKKRRRWVREKMEDVKGRREAGLSGYRAAGRDVDIEVRTLMQTPPIAPLDIDALGYGENTRPKENMDILRGTEFLQLRPERRTVEMARTWWQGEIAALERRKAQISQDRQALIEGSEVWSDVTGLVAQFEAKLRELVKSSQAGDADEEPQQAAMQSQLSEMDDVVQELQKRLQLAESKHWNLLICAIGAELEAFVEAKALLSDTLGLPEPAAAVDSPELSDSTDKAEGTSQEERADSHDESDNEVPADLLVSRMEDHDHDPPDSPQQQSVVLRRGSAGNNEVPVEFLADLHGPNKIEQDTEIAAVTRLMSK

Function: Required for the autophagic degradation of peroxisomes called pexophagy, but not essential for general autophagy (By similarity). Involved in resistance to elevated pH (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 72220 Sequence Length: 646 Subcellular Location: Cytoplasm

C4R159

MICLFGNCNCQTGIFGLYDYVSFLYHSPSSCRVRLVLSLPASPNHMEEQSPKFESSFPRRTSEGPVDDVGKSPPASFYRELLANKAQQPQLSEDEEDHNPKDFLFKEDSEDELLIPDSENHNSSSTSPRKFKVENIRWGSDTLNGSILPLNSQGSNLQSLLSNVGELEHLLSKDVAKHSKYLKEQSSKVEKARANIVTNLTRLSLVLSSIFNTYQAKAQDKQAILDKIEEWEDEKKSLLDDMKEVLSTDDNADGETHKFLELASESINVENEIEALETRLKQLKIKQRTLKNECFQSQGIIESRLSNFVQAVEKIEMRERKSIEQVVQQLSENQLGYWNDNLALEVMNGLTINPGDISLVEEYEPVDILKQVESLEKPTIAADYHLPKNTNKQASRFTRQLLEFNYKCQPKLNVYPVVGLITKELKEDSAKEQEYKHRYDQVTHTLSALKDSFALIYHTEQQLQSITQSTQDLKDFQSLMNQMVESLLKTHSEADQYNLYLAKDVLAQEISIIHQALNKLNQSTEYSSVESDNVKNHDGLLFQTFSKAQERTKLPSIKSATSIRYAPSLYNSLSPTSTSKTTAKGEVNYDAGINKYTKVKEVLRSGKGNKDE

Function: Required for the autophagic degradation of peroxisomes called pexophagy, but not essential for general autophagy. Involved in resistance to elevated pH. Location Topology: Peripheral membrane protein Sequence Mass (Da): 69519 Sequence Length: 612 Subcellular Location: Cytoplasm

Q68EP9

MEASGTDDVEKLKSKFLSAWHNMKYSWVLKTKTYFKRNSPVFLLGKCYHFKYEDSSVTSDGGSNSGSESKEDLSGNVDEFRKDFISRIWLTYREEFPQIETSSWTTDCGWGCTLRTGQMLLAQGLIVHFLGRDWTWTEALDIFSSESEFWTANTARKLTPSLETSFSENNECVSSNKQPLHNCDKKSNSEDFHQKIISWFADYPLAYFGLHQLVKLGKNSGKVAGDWYGPAVVSHLLRKAIEESSDPELQGITIYVAQDCTIYSADVYDLQCNKGTEKAVVILVPVRLGGERTNMEYFEFVKGILSLEFCIGIIGGKPKQSYYFVGFQDDSLIYMDPHYCQSFVDVSVKNFPLESFHCPSPKKMSFKKMDPSCTIGFYCRNAREFEKAAEELTKVLKSSTKQNYPLFTFVNGHAQDFDFVCTPVYDQNDLFTEDEKKRLKRFSTEEFVLL

Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins. The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins to reveal a C-terminal glycine (By similarity). Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy (By similarity). In addition to the protease activity, also mediates delipidation of ATG8 family proteins. Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy (By similarity). Catalytic Activity: [protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine Sequence Mass (Da): 51544 Sequence Length: 450 Subcellular Location: Cytoplasm EC: 3.4.22.-

R4GER2

MNSVSPSAVQYIVGGGAHEDKASASSKRHLGHGAVPDGIREGSGEPDEVDRLKAKFMSAWNNVKYGWTVKSKTSFNKSSPLILLGQSFLFNNEDEVERFRQTFVSCVWLTYRREFPQLDGSSLTTDCGWGCMLRSGQMMLAQGLLLHLMPTDWRWSDCHALTDVDFEVLKPRSPSRPAGMSMPSFSSSWSSSIPQINPSPGITEAHRRAPARCPSASPDPQVDALHRKVVSCFGDHPSAPFGVHQLVELGKESGKRAGDWYGPSVVAHMLRKAVARAAEFEDLAVYVAQDCTVYKEDVMSLCESSGVGWKSVVILVPVRLGGESLNPSYIECVKNILKLKCCIGIIGGKPKHSLFFVGFQDEQLLYLDPHYCQPVVDVTQANFSLESFHCNSPRKMNFSRMDPSCTIGLYARSKTDFESLCTAVSEALSSSKEKYPIFTFVEGRGQIYGMEGPSGGSVDAPAHIFTCSRLSRNNKRGSTDEFVLL

Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins (By similarity). The protease activity is required for proteolytic activation of ATG8 family proteins to reveal a C-terminal glycine (By similarity). Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy (By similarity). In addition to the protease activity, also mediates delipidation of ATG8 family proteins. Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy (By similarity). Also involved in non-canonical autophagy, a parallel pathway involving conjugation of ATG8 proteins to single membranes at endolysosomal compartments, by catalyzing delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) (By similarity). ATG4D plays a role in the autophagy-mediated neuronal homeostasis in the central nervous system . Catalytic Activity: [protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine Sequence Mass (Da): 53363 Sequence Length: 485 Subcellular Location: Cytoplasm EC: 3.4.22.-

Q86TL0

MNSVSPAAAQYRSSSPEDARRRPEARRPRGPRGPDPNGLGPSGASGPALGSPGAGPSEPDEVDKFKAKFLTAWNNVKYGWVVKSRTSFSKISSIHLCGRRYRFEGEGDIQRFQRDFVSRLWLTYRRDFPPLPGGCLTSDCGWGCMLRSGQMMLAQGLLLHFLPRDWTWAEGMGLGPPELSGSASPSRYHGPARWMPPRWAQGAPELEQERRHRQIVSWFADHPRAPFGLHRLVELGQSSGKKAGDWYGPSLVAHILRKAVESCSDVTRLVVYVSQDCTVYKADVARLVARPDPTAEWKSVVILVPVRLGGETLNPVYVPCVKELLRCELCLGIMGGKPRHSLYFIGYQDDFLLYLDPHYCQPTVDVSQADFPLESFHCTSPRKMAFAKMDPSCTVGFYAGDRKEFETLCSELTRVLSSSSATERYPMFTLAEGHAQDHSLDDLCSQLAQPTLRLPRTGRLLRAKRPSSEDFVFL

Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins . The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins MAP1LC3 and GABARAPL2, to reveal a C-terminal glycine . Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy (By similarity). In addition to the protease activity, also mediates delipidation of ATG8 family proteins . Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy . Also involved in non-canonical autophagy, a parallel pathway involving conjugation of ATG8 proteins to single membranes at endolysosomal compartments, by catalyzing delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) . ATG4D plays a role in the autophagy-mediated neuronal homeostasis in the central nervous system (By similarity). Compared to other members of the family (ATG4A, ATG4B or ATG4C), constitutes the major protein for the delipidation activity, while it promotes weak proteolytic activation of ATG8 proteins (By similarity). Involved in phagophore growth during mitophagy independently of its protease activity and of ATG8 proteins: acts by regulating ATG9A trafficking to mitochondria and promoting phagophore-endoplasmic reticulum contacts during the lipid transfer phase of mitophagy . PTM: Cleaved by CASP3 during apoptosis which leads to increased activity . The cleavage by CASP3 reveals a cryptic mitochondrial targeting sequence immediately downstream of their canonical caspase cleavage sites which leads to mitochondrial import of the protein . Catalytic Activity: [protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine Sequence Mass (Da): 52922 Sequence Length: 474 Domain: The cryptic mitochondrial transit peptide is revealed after cleavage by caspase upon oxidative stress and cell death . It acts then as a functional transit peptide, and allows the import of the cleaved protein into the mitochondria . Subcellular Location: Cytoplasm EC: 3.4.22.-

Q75E61

MGFLIAYVFNLSPCSGDEMFETIGLAIIHFEGLNTNRVSKCNQNWHQESKQVAMELIQKVSQGLWELENCDTVNSVVVLGKEYPPVPEQRQEERHENGVNMFQHIFTRQGRWNEEFLADVHTRLHFTYRTRFVPIPRHPNGPSPMSISVMLRDNPLNVIENVLNNPDCFQTDIGWGCMIRTGQSLLANALQRACLGRDFRIDDNAANEHELRIIKWFEDDPKYPFSLHKFVQEGFSLSGKKPGEWFGPSATSRSIQALVAKFPACGIAHCVISTDSGDVYMDEVEPLFRADPSAAVLLLLCVRLGVDVVNEVYWEHIRHILSSEHSVGIAGGRPSSSLYFFGYQDEHLFYLDPHKPQLNLASYQQDLDLFRSVHTQRFNKVHMSDIDPSMLIGILLNGKDDWQLWQQHIASSQIIHLSDSKPVDLMLDHQLESAILGDRYLSEDGQGPSSKVDTGDYIDVGSFVPCTDSSCKINESEDEYQDVKCKNQRIVVVGETTTNGSPEVEVEKVLVEKETIPVRSK

Function: Cysteine protease that plays a key role in cytoplasm to vacuole transport (Cvt) and autophagy by mediating both proteolytic activation and delipidation of ATG8. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. The protease activity is required for proteolytic activation of ATG8: cleaves the C-terminal amino acid of ATG8 to reveal a C-terminal glycine. ATG8 ubiquitin-like activity requires the exposure of the glycine at the C-terminus for its conjugation to phosphatidylethanolamine (PE) and its insertion to membranes, which is necessary for autophagy. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. In addition to the protease activity, also catalyzes deconjugation of PE-conjugated forms of ATG8 during macroautophagy: ATG8 delipidation is required to release the protein from membranes, which facilitates multiple events during macroautophagy, and especially for efficient autophagosome biogenesis, the assembly of ATG9-containing tubulovesicular clusters into phagophores/autophagosomes, and for the disassembly of PAS-associated ATG components. ATG8 delipidation by ATG4 also recycles ATG8-PE generated on inappropriate membranes to maintain a reservoir of unlipidated ATG8 that is required for autophagosome formation at the PAS. Catalytic Activity: [protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine Sequence Mass (Da): 59038 Sequence Length: 521 Subcellular Location: Cytoplasm EC: 3.4.22.-

A6SDQ3

MTAADLGRYKRFVQYFWDPEPTNDTASQSPIWCLGKEYPILEKSATSAITDSPPQEGHYLPAQSLPTNEVTTPPDSTVGSLESSSGSQNCDTANADGGWPSAFLDDFEAKIWLTYRSNFPAIAKSQDPKALSAMSLSVRLRSQLVDQGGFTSDTGWGCMIRSGQSLLANALLTLRMGREWRRGVSSNEERKILSLFADDPRAPYSIHKFVEHGASACGKHPGEWFGPSATARCIQALSNSQAKSELRVYITGDGSDVYEDKFMSIAKPNHSDFTPTLILVGTRLGLDKITPVYWEALKYSLQMPQSVGIAGGRPSSSHYFIGVQESDFFYLDPHQTRPALPYKDNVEDYTTEDIDSCHTRRLRRLHIKEMDPSMLIAFLIRDENDWNEWRRAVKEVQGKGVIHVADTDPASYGLGGERDGAIDEVETFDDDDDDTILDA

Function: Cysteine protease that plays a key role in cytoplasm to vacuole transport (Cvt) and autophagy by mediating both proteolytic activation and delipidation of ATG8. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. The protease activity is required for proteolytic activation of ATG8: cleaves the C-terminal amino acid of ATG8 to reveal a C-terminal glycine. ATG8 ubiquitin-like activity requires the exposure of the glycine at the C-terminus for its conjugation to phosphatidylethanolamine (PE) and its insertion to membranes, which is necessary for autophagy. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. In addition to the protease activity, also catalyzes deconjugation of PE-conjugated forms of ATG8 during macroautophagy: ATG8 delipidation is required to release the protein from membranes, which facilitates multiple events during macroautophagy, and especially for efficient autophagosome biogenesis, the assembly of ATG9-containing tubulovesicular clusters into phagophores/autophagosomes, and for the disassembly of PAS-associated ATG components. ATG8 delipidation by ATG4 also recycles ATG8-PE generated on inappropriate membranes to maintain a reservoir of unlipidated ATG8 that is required for autophagosome formation at the PAS. Catalytic Activity: [protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine Sequence Mass (Da): 48742 Sequence Length: 439 Subcellular Location: Cytoplasm EC: 3.4.22.-

Q6FP20

METIHNISNRLQEVLATNKSVNVDTDNDSLSSNQEDNEVEKVRHLVVILGEKYSYAVDRNTGINALMQWFTTNSEIPEEILNAIRSKLNFTYRTNFEPIERAPDGPSPINPLIMLRINPIDAIENVFNNRECFFTDVGWGCMIRTGQSLLGNALQRVKSTVKDQPYIYEMDDTKEITDLFKDNTKSAFSLQNFVKCGRIYNKIAPGEWFGPATTATCIRYLIQENPCYGIEACYISVSSGDIFKENIQGMIDRYPNGNILILLGIKLGLDSVHERYWGEIKTMLESPFSVGIAGGRPSSSLYFFGYFDDTLLFFDPHNSQTALIDDFDESCHTENFGKLNFSDLDPSMLLGFLLPCSKWDEFQEFTSLLTIVNVLDGMDQYRDPDLNSNDIGNVELSPQLKLSQTPDAITDDDYVDIGALIQGNSMNINDRDNGYQEVQCKNQQIVIMDSLNETKPLEIEKVLVGQGTNLVNATTPCREAFPK

Function: Cysteine protease that plays a key role in cytoplasm to vacuole transport (Cvt) and autophagy by mediating both proteolytic activation and delipidation of ATG8. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. The protease activity is required for proteolytic activation of ATG8: cleaves the C-terminal amino acid of ATG8 to reveal a C-terminal glycine. ATG8 ubiquitin-like activity requires the exposure of the glycine at the C-terminus for its conjugation to phosphatidylethanolamine (PE) and its insertion to membranes, which is necessary for autophagy. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. In addition to the protease activity, also catalyzes deconjugation of PE-conjugated forms of ATG8 during macroautophagy: ATG8 delipidation is required to release the protein from membranes, which facilitates multiple events during macroautophagy, and especially for efficient autophagosome biogenesis, the assembly of ATG9-containing tubulovesicular clusters into phagophores/autophagosomes, and for the disassembly of PAS-associated ATG components. ATG8 delipidation by ATG4 also recycles ATG8-PE generated on inappropriate membranes to maintain a reservoir of unlipidated ATG8 that is required for autophagosome formation at the PAS. Catalytic Activity: [protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine Sequence Mass (Da): 54515 Sequence Length: 483 Subcellular Location: Cytoplasm EC: 3.4.22.-

Q6C794

MRSKFKDEHPFEKRRAEAERIRKKYDDRVPVICEKVEKSDIPVIDKKKYLVPADLTVGQFVYVIRKRIKLSSERAIFIFVDDVLPPTAALMSSIYEEHKDEDGFLYVTYSGENTFGDLEQYRLE

Function: Ubiquitin-like modifier involved in autophagosomes formation. With ATG4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. PTM: The C-terminal 8 residues are removed to expose Gly-116 at the C-terminus. The C-terminal Gly is then amidated with phosphatidylethanolamine by an activating system similar to that for ubiquitin. Location Topology: Lipid-anchor Sequence Mass (Da): 14639 Sequence Length: 124 Subcellular Location: Cytoplasmic vesicle

Q3T904

MAQFDTEYQRLEASYSDSPPGEEDLLVHVPEGSKSPWHHIENLDLFFSRVYNLHQKNGFTCMLIGEIFELMQFLFVVAFTTFLVSCVDYDILFANKMVNHSLHPTEPVKVTLPDAFLPAQVCSARIQENGSLITILVIAGVFWVHRLIKFIYNICCYWEIHSFYLHALRIPMSALPYCTWQEVQARIVQTQKEHQICIHKRELTELDIYHRILRFQNYMVALVNKSLLPLRFRLPGLGEVVFFTRGLKYNFELILFWGPGSLFLNEWSLKAEYKRGGQRLELAQRLSNRILWIGIANFLLCPLILIWQILYAFFSYAEVLKREPGALGARCWSLYGRCYLRHFNELEHELQSRLNRGYKPASKYMNCFLSPLLTLLAKNCAFFAGSILAVLIALTIYDEDVLAVEHVLTTVTLLGVTVTVCRSFIPDQHMVFCPEQLLRVILAHIHYMPDHWQGNAHRSQTRDEFAQLFQYKAVFILEELLSPIVTPLILIFCLRPRALEIIDFFRNFTVEVVGVGDTCSFAQMDVRQHGHPQWLSGGQTEASVYQQAEDGKTELSLMHFAITNPGWQPPRESTAFLGFLKEQVQRDGAAAGLAQGGLLPENALFTSIQSLQSESEPLSLIANVVAGSSCRGPPLPRDLQGSRHRAEVASALRSFSPLQPGQAPTGRAPSTMTGSGVDARTASSGSSVWEGQLQSLVLSEYASTEMSLHALYMHQLHKQQAQAEPERHVWHRRESDESGESAPEEGGEGARATQPIPRSASYPCAAPRPGAPETTALQGGFQRRYGGITDPGTVPRAPSHFSRLPLGGWAEDGQSASRHPEPVPEEGSEDELPPQVHKV

Function: Phospholipid scramblase involved in autophagy by mediating autophagosomal membrane expansion. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 (ATG2A or ATG2B) from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion. Also required to supply phosphatidylinositol 4-phosphate to the autophagosome initiation site by recruiting the phosphatidylinositol 4-kinase beta (PI4KB) in a process dependent on ARFIP2, but not ARFIP1 (By similarity). In addition to autophagy, also plays a role in necrotic cell death (By similarity). Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 94440 Sequence Length: 839 Domain: Forms a homotrimer with a solvated central pore, which is connected laterally to the cytosol through the cavity within each protomer. Acts as a lipid scramblase that uses its central pore to function: the central pore opens laterally to accommodate lipid headgroups, thereby enabling lipid flipping and redistribution of lipids added to the outer leaflet of ATG9A-containing vesicles, thereby enabling growth into autophagosomes. Subcellular Location: Preautophagosomal structure membrane

Q7Z3C6

MAQFDTEYQRLEASYSDSPPGEEDLLVHVAEGSKSPWHHIENLDLFFSRVYNLHQKNGFTCMLIGEIFELMQFLFVVAFTTFLVSCVDYDILFANKMVNHSLHPTEPVKVTLPDAFLPAQVCSARIQENGSLITILVIAGVFWIHRLIKFIYNICCYWEIHSFYLHALRIPMSALPYCTWQEVQARIVQTQKEHQICIHKRELTELDIYHRILRFQNYMVALVNKSLLPLRFRLPGLGEAVFFTRGLKYNFELILFWGPGSLFLNEWSLKAEYKRGGQRLELAQRLSNRILWIGIANFLLCPLILIWQILYAFFSYAEVLKREPGALGARCWSLYGRCYLRHFNELEHELQSRLNRGYKPASKYMNCFLSPLLTLLAKNGAFFAGSILAVLIALTIYDEDVLAVEHVLTTVTLLGVTVTVCRSFIPDQHMVFCPEQLLRVILAHIHYMPDHWQGNAHRSQTRDEFAQLFQYKAVFILEELLSPIVTPLILIFCLRPRALEIIDFFRNFTVEVVGVGDTCSFAQMDVRQHGHPQWLSAGQTEASVYQQAEDGKTELSLMHFAITNPGWQPPRESTAFLGFLKEQVQRDGAAASLAQGGLLPENALFTSIQSLQSESEPLSLIANVVAGSSCRGPPLPRDLQGSRHRAEVASALRSFSPLQPGQAPTGRAHSTMTGSGVDARTASSGSSVWEGQLQSLVLSEYASTEMSLHALYMHQLHKQQAQAEPERHVWHRRESDESGESAPDEGGEGARAPQSIPRSASYPCAAPRPGAPETTALHGGFQRRYGGITDPGTVPRVPSHFSRLPLGGWAEDGQSASRHPEPVPEEGSEDELPPQVHKV

Function: Phospholipid scramblase involved in autophagy by mediating autophagosomal membrane expansion . Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome . Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 (ATG2A or ATG2B) from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion . Also required to supply phosphatidylinositol 4-phosphate to the autophagosome initiation site by recruiting the phosphatidylinositol 4-kinase beta (PI4KB) in a process dependent on ARFIP2, but not ARFIP1 . In addition to autophagy, also plays a role in necrotic cell death (By similarity). Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 94447 Sequence Length: 839 Domain: Forms a homotrimer with a solvated central pore, which is connected laterally to the cytosol through the cavity within each protomer . Acts as a lipid scramblase that uses its central pore to function: the central pore opens laterally to accommodate lipid headgroups, thereby enabling lipid flipping and redistribution of lipids added to the outer leaflet of ATG9A-containing vesicles, thereby enabling growth into autophagosomes . Subcellular Location: Preautophagosomal structure membrane

Q674R7

MVSRMGWGGRRRRLGRWGDLGPGSVPLLPMPLPPPPPPSCRGPGGGRISIFSLSPAPHTRSSPSSFSPPTAGPPCSVLQGTGASQSCHSALPIPATPPTQAQPAMTPASASPSWGSHSTPPLAPATPTPSQQCPQDSPGLRVGPLIPEQDYERLEDCDPEGSQDSPIHGEEQQPLLHVPEGLRGSWHHIQNLDSFFTKIYSYHQRNGFACILLEDVFQLGQFIFIVTFTTFLLRCVDYNVLFANQPSNHTRPGPFHSKVTLSDAILPSAQCAERIRSSPLLVLLLVLAAGFWLVQLLRSVCNLFSYWDIQVFYREALHIPPEELSSVPWAEVQSRLLALQRSGGLCVQPRPLTELDIHHRILRYTNYQVALANKGLLPARCPLPWGGSAAFLSRGLALNVDLLLFRGPFSLFRGGWELPHAYKRSDQRGALAARWGRTVLLLAALNLALSPLVLAWQVLHVFYSHVELLRREPGALGARGWSRLARLQLRHFNELPHELRARLARAYRPAAAFLRTAAPPAPLRTLLARQLVFFAGALFAALLVLTVYDEDVLAVEHVLTAMTALGVTATVARSFIPEEQCQGRAPQLLLQTALAHMHYLPEEPGPGGRDRAYRQMAQLLQYRAVSLLEELLSPLLTPLFLLFWFRPRALEIIDFFHHFTVDVAGVGDICSFALMDVKRHGHPQWLSAGQTEASLSQRAEDGKTELSLMRFSLAHPLWRPPGHSSKFLGHLWGRVQQDAAAWGATSARGPSTPGVLSNCTSPLPEAFLANLFVHPLLPPRDLSPTAPCPAAATASLLASISRIAQDPSSVSPGGTGGQKLAQLPELASAEMSLHVIYLHQLHQQQQQQEPWGEAAASILSRPCSSPSQPPSPDEEKPSWSSDGSSPASSPRQQWGTQKARNLFPGGFQVTTDTQKEPDRASCTD

Function: Phospholipid scramblase involved in autophagy by mediating autophagosomal membrane expansion. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 (ATG2A or ATG2B) from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion (By similarity). In addition to autophagy, also plays a role in necrotic cell death (By similarity). Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 101019 Sequence Length: 924 Domain: Forms a homotrimer with a solvated central pore, which is connected laterally to the cytosol through the cavity within each protomer. Acts as a lipid scramblase that uses its central pore to function: the central pore opens laterally to accommodate lipid headgroups, thereby enabling lipid flipping and redistribution of lipids added to the outer leaflet of ATG9B-containing vesicles, thereby enabling growth into autophagosomes. Subcellular Location: Preautophagosomal structure membrane

Q8RUS5

MMSSGHKGPNVRNFFKWQRGESSSSLTTGLLHNESHEIELSNYGGIPSPGSESPSGLLNGESLNVQPIADLDLFVERLYSYYRDKGLWCIIVKWAVELLSLGFIICFSGFFLLYVDWNGLQNAKCGMDAVESGTKPCDLVKEAIHPHPLSPFTLTTAIIVGYLALFSVYWLFCFLRFFAQLKDTLDFRHFYYNNLHVTDNEILTMPWATVLEKVVQLQSSQCLCVVKDLSAHDMVMRLMRKENYLIGMLNKGLLSFPISHWIPGAGPAVKSAPDGTQYHLVLTKTLEWTLNWCILQSMFDCNFRVRRDFVSNPTTLKKRLFVVGLAMLLLSPFLVIFMLVYLFLRHAEQFYNHPSTASSRRWSNLSKWLFREFNEVDHLFKHRINSSVVHASEYLKQFPSPIISIIAKFVSFVSGGFAAVLIIIAFLEESLLEGHIFGRNLFWYAAVFGTITAISRAAISDELLVLDPVGTMSLVVQNTHYMPKRWRGKENKDDVRLELETLFQYTGMMLLEEIASIFITPFLLMFVVPKRVDDILQFIKDFTVDIEGVGHVCSFSAFYFENHGNIKYGSPHNATRREQRSSQGKMEKSFLSFQSSYPSWESDSLGKQFLSNLRTFRDRKLHEINTRHSSPSRAWRESTNTPALYRDIPRNPLASGNHTDSMWLIDPDQRNHPYLLDWYYTSQAHNRTDHPIERANEILTANQNATDCWPPDLGIRGEDSRDLLNMEASTSGQFFRESILRHDQPEGEDSYGSQHPLDGRNQWWGRGNHSQISTAHPATTNSFIEPPDFINRYTAGNLLDNSWSRRSIEEEDEEEEELDWEENARRNLSRTTFMDDNDIEAGIDLHFDDVYSSRPQETSTSSTTLR

Function: Phospholipid scramblase involved in autophagy by mediating autophagosomal membrane expansion . Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion (By similarity). In addition to autophagy, also plays a role in necrotic cell death (By similarity). Plays an essential role in plant nutrient recycling . Location Topology: Multi-pass membrane protein Sequence Mass (Da): 99467 Sequence Length: 866 Domain: Forms a homotrimer with a solvated central pore, which is connected laterally to the cytosol through the cavity within each protomer. Acts as a lipid scramblase that uses its central pore to function: the central pore opens laterally to accommodate lipid headgroups, thereby enabling lipid flipping and redistribution of lipids added to the outer leaflet of ATG9-containing vesicles, thereby enabling growth into autophagosomes. Subcellular Location: Preautophagosomal structure membrane

Q75A48

MEQSEDTIQHERKNTFLSRVFGVHSSEVGDSIETAELSQYPIQIARSGSNAIDESRVIESDQASSSEEEDTDGHDLSVAENMTSYNGAQGSGSEDSDVPFSDQELETIETYTIAKVGQGSSSEDDRLQADSAEEEDALLFQHRLQDGSKGRNKVSSQPLGLKRILGSKGKSILGKEPASQEDSFIFRKGPTWDEENQLRPESKRPGLLSGKSNARLSSPSRPSPLSARERALWKWANVENLDGFLQDVYSYYLGNGFYCIMIEKILNLLTLLFIVFISTYMSHCIDYSKLPNGHKFSDVRVDQCYETQITGTTKLLFWIFGVFVVLKVVQMYFDFRRIHEIHNFYTYLLNISDKELQTIPWQSVIHQIMRLKDQNAVTANVVEVKAKNHIDAHDVANRIMRKENYLIALYNKDILHLSLPIPLYRTSTLTKTLEWNIHLCIIGFAFNEAGFLKQSFLNPAQREFLSEELKKRFILAGFLNIILAPFLVVYFVLLYFFRYFNEYKTSPGSLSTRQYTPIAEWKFREYNELYHLFKKRMGLSYEVANTYINQFPNALGDYFFKFVKFISGSFVAILALMTVLDPENFLNFELTADRTVLFYMTVLGTIWAVCHSAVNDNCSVFDPEDSLKELITYIHYAPKEWDGRYHTDEVKQEFCKLYNLRVILLLRELASLIMTPFILWFSLPNSAESIVDFFREVTVYGDGLGYVCKYAMFDENCKKGLRTNKHLQGTQTKYGHSLGDDHDSSDEETDKGMNKMIQSYMYFVDDYQNSVNAVGKYQIPKTQNLSHESKYNMKSHQHYSWKKQFKLGSKPEDFKIGSVTPRALSSSILANKPKSNLRARLDPEISHSNVQFDDLGESFINSIPVADYDPIERSDAMGGNGVLGLLNQYYRKSDVGR

Function: Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion. Required for mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Different machineries are required for anterograde trafficking to the PAS during either the Cvt pathway or bulk autophagy and for retrograde trafficking. PTM: Phosphorylated by ATG1. ATG1 phosphorylation is required for preautophagosome elongation. Location Topology: Multi-pass membrane protein Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out) Sequence Mass (Da): 102811 Sequence Length: 897 Domain: Forms a homotrimer with a solvated central pore, which is connected laterally to the cytosol through the cavity within each protomer. Acts as a lipid scramblase that uses its central pore to function: the central pore opens laterally to accommodate lipid headgroups, thereby enabling lipid flipping and redistribution of lipids added to the outer leaflet of ATG9-containing vesicles, thereby enabling growth into autophagosomes. Subcellular Location: Preautophagosomal structure membrane

A1CU77

MMTSNILSRFLPPNNSPSVYEAIRQNDADSDSSDVEERAGLTLEDGHGGHYTDHELQDAMVDADQSELPSPDDAFLARESHHRVPSEGPSKSTSRRRKNSRPRWMQAASPGQDFEYGDDDDVPASLLVEGHHDDEDLKSRLPPPPRPLSPHEIQPSLPGPSSQGDQARWRAARDQQPLHNASRRRPPGVKWSLGQPNLNTVDPKEKAMWMWANVDNLDNFLKEVYSYFLGNGIWSILLTRVLSLLTFAFVVGFSTFLTNCVNYHKVRGSKTLDDILVDRCTTKMSLSSTFLLWLLTFFWIGKAFQCLLGIRRLKHMHDFYHYLLGVSDTDIQTISWQEVVSRLMTLRDANPATAGAVSARHRKFMGSQSKQRMDAHDIANRLMRKENYLIALVNKDILDLTLPIPFLRNRPLFSQTLEWNLNLCIMDYVFNEQGQVRTLFLKDTHRKALSEGLRRRFIFAGFMNIFVAPFIVVYFMMHYFFRYFNEYKKNPSQIGSRQYTPLAEWKFREFNELWHLFERRINMSYPFASRYVDQFPKDKTVQVAGFVAFVSGALASVLALASVVDPELFLGFEITHDRTVLFYLGVFGSVWAVARGMVPEETNVFDPEYALLEVINYTHYFPSQWKGRLHSDEVRREFAELYQMKIVIFLEEILSMIFTPFILWFSLPRCSDRLIDFFREFTVHVDGMGYLCSFAVFDFKKGTNVITQGDRREPARQDLRADYFATKDGKMLASYYGFLDNYGANPRGAHPSTKRQFHPPPAFPTLGSPSAMDLGHLGDRADPPQARPFAGQQSTFGPSRFGPTGLADHGSPAPSMLLDPHHQPSASGFRTAHRTAFSRYRSSRAAPPISGAILDDDESPSAPNRNGSARSAAGAPAPPGGSSGGGVGASDSNLEDSWRMNLTGDTDDEDAGAGGENADAIAGGAGVLGLIQQFQRVNQDGRGRTAVGL

Function: Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through atg2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion. Required for mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Different machineries are required for anterograde trafficking to the PAS during either the Cvt pathway or bulk autophagy and for retrograde trafficking. PTM: Phosphorylated by atg1. Atg1 phosphorylation is required for preautophagosome elongation. Location Topology: Multi-pass membrane protein Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out) Sequence Mass (Da): 106768 Sequence Length: 949 Domain: Forms a homotrimer with a solvated central pore, which is connected laterally to the cytosol through the cavity within each protomer. Acts as a lipid scramblase that uses its central pore to function: the central pore opens laterally to accommodate lipid headgroups, thereby enabling lipid flipping and redistribution of lipids added to the outer leaflet of atg9-containing vesicles, thereby enabling growth into autophagosomes. Subcellular Location: Preautophagosomal structure membrane

Q4WLT9

MMTSNILSRFLPPNGSPSVYETIRNHDATSDSSDVEERAGLTLEDGPGEHYSDRELEDAMADAGRSRLLDRDDAFISRRSPRKASVAGPSKSNSRRRHFSRPRWAHDASPSHDFEDGDDDVPASLLVEGHHDDDELKSRLPPPPTSHITPDDRQPSRPGPSTRGVRGRGRAAKEQQPLHHADRRRAPAVRWSLGQPNLNTVDPKEKAMWMWANVENLDNFLKEVYTYFLGNGIWSILLNRVLSLLTFAFVVGFSTFLTNCIDYHKVRGSKSLNDILIKQCTTKMSLSSTFLLWLLTLFWIGKAFQCLLDIRRLKHMHDFYYYLLGVSDTDIQTISWQEIVSRLMTLRDANPATAGAVSARHRKFMGSQSKQRMDAHDIANRLMRKENYLIALINKDILDLTLPIPFLRNKQLFSRTLEWNINLCIMDYVFNEQGQVRTLFLKDTHRKALSEGLRRRFIFAGIMNIFVAPFIVVYFMMHYFFRYFNEYKKNPSQIGSRQYTPLAEWKFREFNELWHLFERRINMSYPFASRYVDQFPKDKTVQVAGFVAFVSGALASVLALASIVDPELFLGFEITHDRTVLFYLGVFGSVWAVARGLVPEETTVFDPEYALLEVINYTHYAPSHWKGRLHSDEVRREFTELYQMKIVIFLEEILSMIFTPFILWFNLPKCSDRLIDFFREFTVHVDGMGYLCSFAVFDFKKGTNVINQGDRRDPARQDLRADYFSTKDGKMLASYYGFLDNYGANHRGSHPATRRQFYPPPAFPTLGSPPAGEMGTIGDRLDQTQTRHGLAGPFMGQQSVFGPSRYGLTGLGDHASPAPSILLDPHHQPSTSGFRGTSRAAGVQRYRSSRAHPPISGTIADGDESPVATGRSDPSRPAANAAGASSAGGVGTSDSNLGDSWRMNLVEDGDDDNTEGGENVDAIAGGAGVLGLIQQFQRVNKDSRGRTAVGL

Function: Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through atg2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion. Required for mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Different machineries are required for anterograde trafficking to the PAS during either the Cvt pathway or bulk autophagy and for retrograde trafficking. PTM: Phosphorylated by atg1. Atg1 phosphorylation is required for preautophagosome elongation. Location Topology: Multi-pass membrane protein Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out) Sequence Mass (Da): 107356 Sequence Length: 951 Domain: Forms a homotrimer with a solvated central pore, which is connected laterally to the cytosol through the cavity within each protomer. Acts as a lipid scramblase that uses its central pore to function: the central pore opens laterally to accommodate lipid headgroups, thereby enabling lipid flipping and redistribution of lipids added to the outer leaflet of atg9-containing vesicles, thereby enabling growth into autophagosomes. Subcellular Location: Preautophagosomal structure membrane

Q5ANC9

MSSSSYNPYKNNVNDRLINNSTDSFQDNDQGIPNNNDTFLSRIFGLNSIYNQLQDNYQYYDPEFDSSLNQQLQQSIQENDEAEDESLLPQHQQQQQQAAPMDLSIQDKSAKQKSKSSSLLNSDSDSDLSSSEDSYVRPNIPQIPSTPIETENQGSSSKIKFSIPQRAKNFVGKLHPHHEPTLPVYQTPQEFRRNLPQQQRASATVNTNYQRTRNNNRRFIIPPKERALYLWANITNMDEFLSDVYYYYRGRGLLNIVLSRGFDLIILIFILIFTVFLKWGIDYSIFFDNLHQEESKHITLNDMIIPNYFATIPLSIKFILFGFSVYILLRSVQLYLDYNYKLKELKNFYHYLLDVTDDELMTISWKTIVEKLMLLKDYNSLTSTTKSNNFSENHYVNDLSSKVRLNAHDIANRIMRRENYMIALINKDILDLSVLFMNEKSLLTKTLEWNLKLCIDNFIYNQQGQINGKILKEYNRNQLARELTSRFKLAAIINLILSPFIVIYFVLLYFFRYFNEYKSNPASILGLRQYTPYAEWKLREYNELSHLFNKRLIMSMGPANTYIDQFPKGFLVVNLMRLINFISGSILAVLVIMGILLEDENHSFWSFEITDGRSALFYISIFGTIWAITASSATGTSHESTISTTSQSSNSNSNSNAASTFVYDPEASLRYVAQFTHYLPSSWNKKLHTIQVKNEFCQLYCLKIIIIINEILSSVLTPFILWFKISHNSGNIIDFYREYSIHVDGLGYVCYFAMFNFEEKDKNMMSDLNKSKKRRKRMKNKMNKYGKTKMVNPISGKTVNSEIEMTKISKSESERSSDDESGNEQDYDNDEELDYLSYKKDDKMIKSYMYFLESYGGSKQPQPQPPQQQQHPQNQNQTVGGLRNRNPIQSIDPAIMTGNYYDQQSLNSSIYNINYKFDDSGLLQDETMNSSSRKKGGVLGMLNQFYKQDINR

Function: Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation . Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through atg2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion. Required for mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Different machineries are required for anterograde trafficking to the PAS during either the Cvt pathway or bulk autophagy and for retrograde trafficking (By similarity). PTM: Phosphorylated by ATG1. ATG1 phosphorylation is required for preautophagosome elongation. Location Topology: Multi-pass membrane protein Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out) Sequence Mass (Da): 110751 Sequence Length: 952 Domain: Forms a homotrimer with a solvated central pore, which is connected laterally to the cytosol through the cavity within each protomer. Acts as a lipid scramblase that uses its central pore to function: the central pore opens laterally to accommodate lipid headgroups, thereby enabling lipid flipping and redistribution of lipids added to the outer leaflet of ATG9-containing vesicles, thereby enabling growth into autophagosomes. Subcellular Location: Preautophagosomal structure membrane

Q6FQT7

MEQSGHEPGKNTFLSRVFGLQSDDVSTSIHTQELSTIPLDEDESNHGALVESEDDEDHNDGVRLLESDPGTSTQDSLESDTSEEDERINGINSDSQVIDTSRPLLSKKETMELHPFGSQNGRIMESSIKLGQPSSDEEDLINVNESLQPDLENRINPIYHEDKLDKALGNSSKNIRTSTFLDRVLKPNDVKKNSTKKRQNSHNYNPTSTYTNSSSNTFLNTVKGEKSSKKYKLKRPNILNALSVVNNMPERRLNTLSPKERALWKWANVDNLDLFLQDAYNYYLGNGFHCIILQKVLNILTLLFVVFVSSFMGYCVDYSKLPTSTRFSEIKIDHCYSQNITGFTKFLLFLFYGFVILKVIQLYFDINNIREMKLFYHYLLNISDDELQTIPWQNIIQQLMYLKDQNALTANVVAVKAKNKLNAHGIANRIMRKENYLIALYNNDILDLRFPIPFFGSQPLTKTLEWNINLCVMGYVFNEAGFIKQGFLKATQKEYFANELRKRFMLAGFLNIILSPFLVSYFVLLYFFRYFNEYKTSPENIGARQYTPMAEWKFREYNELYHIFRKRIGLSNPLASKYVDQFPKEKTNILLKFVSFISGSFVAILAILALWDPENFLNFEVTHDKTVLFYITVLGAIWSISQGSVSTEYHVFDPEETLRELAEYTHYLPDSWKDRYHTEGVKQEFCELYNLRITVLLRELASLITTPFILWFSLPNSAGKMVDFFRESSVYVDGLGYVCKYAVYDGDADAVKKHFGTDGNETTEQDAATEEQDIDSEPDEATKKMMQSYMYFLDDYENDDNLLGKYQIPKKRRESFDNTQYDVSNSNQKNQDDDSDMILANRYTWRKQFKPGQKPELFRIGNHVLNDKTFTQQGSNHLGIDESYARSQISNTAEESNRSSLYNSKYKSPTKGVLGLVKEYYKKSDVGR

Function: Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion. Required for mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Different machineries are required for anterograde trafficking to the PAS during either the Cvt pathway or bulk autophagy and for retrograde trafficking. PTM: Phosphorylated by ATG1. ATG1 phosphorylation is required for preautophagosome elongation. Location Topology: Multi-pass membrane protein Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out) Sequence Mass (Da): 107241 Sequence Length: 928 Domain: Forms a homotrimer with a solvated central pore, which is connected laterally to the cytosol through the cavity within each protomer. Acts as a lipid scramblase that uses its central pore to function: the central pore opens laterally to accommodate lipid headgroups, thereby enabling lipid flipping and redistribution of lipids added to the outer leaflet of ATG9-containing vesicles, thereby enabling growth into autophagosomes. Subcellular Location: Preautophagosomal structure membrane

Q06067

MHYMKWIYPRRLRNQMILMAILMVIVPTLTIGYIVETEGRSAVLSEKEKKLSAVVNLLNQALGDRYDLYIDLPREERIRALNAELAPITENITHAFPGIGAGYYNKMLDAIITYAPSALYQNNVGVTIAADHPGREVMRTNTPLVYSGRQVRGDILNSMLPIERNGEILGYIWANELTEDIRRQAWKMDVRIIIVLTAGLLISLLLIVLFSRRLSANIDIITDGLSTLAQNIPTRLPQLPGEMGQISQSVNNLAQALRETRTLNDLIIENAADGVIAIDRQGDVTTMNPAAEVITGYQRHELVGQPYSMLFDNTQFYSPVLDTLEHGTEHVALEISFPGRDRTIELSVTTSRIHNTHGEMIGALVIFSDLTARKETQRRMAQAERLATLGELMAGVAHEVRNPLTAIRGYVQILRQQTSDPIHQEYLSVVLKEIDSINKVIQQLLEFSRPRHSQWQQVSLNALVEETLVLVQTAGVQARVDFISELDNELSPINADRELLKQVLLNILINAVQAISARGKIRIQTWQYSDSQQAISIEDNGCGIDLSLQKKIFDPFFTTKASGTGLGLALSQRIINAHQGDIRVASLPGYGATFTLILPINPQGNQTV

Function: Member of the two-component regulatory system AtoS/AtoC. In the presence of acetoacetate, AtoS/AtoC stimulates the expression of the atoDAEB operon, leading to short chain fatty acid catabolism and activation of the poly-(R)-3-hydroxybutyrate (cPHB) biosynthetic pathway. Also induces the operon in response to spermidine . Involved in the regulation of motility and chemotaxis, via transcriptional induction of the flagellar regulon . AtoS is a membrane-associated kinase that phosphorylates and activates AtoC in response to environmental signals . PTM: Autophosphorylated . Each AtoS molecule may phosphorylate its partner within the dimer rather than phosphorylating itself . Location Topology: Multi-pass membrane protein Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. Sequence Mass (Da): 67790 Sequence Length: 608 Subcellular Location: Cell inner membrane EC: 2.7.13.3

Q94BT9

MSQTVVLRVAMTCEGCVGAVKRVLGKMEGVESFDVDIKEQKVTVKGNVQPDAVLQTVTKTGKKTAFWEAEGETAKA

Cofactor: Binds 1 copper ion per subunit. Function: Plays an important role in copper homeostasis by conferring tolerance to excess of copper and subclinical copper deficiency during vegetative stage. Can complement the yeast mutants atx1 and sod1. Sequence Mass (Da): 8158 Sequence Length: 76 Subcellular Location: Cytoplasm

B1WXB4

MDITPDSIIYWQWQWINLNATIVFSWLVMLILVLGSWLITRNLSIEPPLSRWQVALEIIVEQIRQQIRDASQQKADQFLPFIGTLFLFITMANLLTIFPVYQSPAGSLSTTAALALCVFVAVPIYGIKNVGITNYLRHYIQPTPVMLPFNLISEISRTVSLAIRLFGNIMSTSLLVAILISIVPLFFPAVMTLFGLLVGVIQAYVFTILAMVYIASGMNLQQRKTGNHHA

Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 25828 Sequence Length: 230 Subcellular Location: Cellular thylakoid membrane

Q2SNG4

MNDGVSTPVWLHIGPLEIHETVVTTWLIMLVLVVASILLTRRLSLQPGRLQAMLEGVVLTLESAIANADSRNARRLLPLIGTFWIFLPVANLLGVIPGMHSPTRDLSVTAALALVVFFAVHAYGVRQSGLGYFKHYLSPSPILLPFHIISEFTRTVALAIRLFGNIMSLEMAALLILLVAGFLAPVPILMLHIIEALVQAYIFGMLALIYVAGAMQQTTESPITSSSRSTSGAP

Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 25332 Sequence Length: 234 Subcellular Location: Cell inner membrane

B4S798

MHLSGDDVIVWQYGVVKLNQTIVMTWVIMVFLAGGSAFLTRRLSSGIRISRWQSFLEMIVTMAMQQIREIGLRQPEKYLSYLATLFLFVATAVLFTIIPGYEPPTGSLSTTAALALSVFVAVPLYGIERVGFGAYLKSYMKPTFIMLPFNIISEFSRTLALAVRLFGNMMSGVMIIGILLGIAPLFFPVLMSVLGLLTGMVQAYIFSMLATVYIAAATKSRDE

Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 24637 Sequence Length: 223 Subcellular Location: Cell inner membrane

P92547

MERLTRLNHFLVNMRWDFYEGVIQAGYIRNLQRELDHTPAELLGSKLDLIFFRESLNLSTYVNNWYMQNLGVPGPVNFIEKYHDACFSNYMKLMEIPSPLDQFEIVPLIPMHIGNFYFSFTNSSLFMLLTLSFFLLLIHFVTKKGGGNLVPNAWQSLVELLYDFVLNLVKEQIGGLSGNVKQMFFPCILVTFLFLLFCNLQGMIPYSFTVTSHFLITLALSFSIFIGITIVGFQRHGLHFFSFLLPAGVPLPLAPFLVLLELISYCFRALSLGIRLFANMMAGHSLVKILSGFAWTMLCMNDIFYFIGALGPLFIVLALTGLELGVAILQAYVFTILICIYLNDAINLH

Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane (By similarity). Location Topology: Multi-pass membrane protein Sequence Mass (Da): 39729 Sequence Length: 349 Subcellular Location: Mitochondrion inner membrane

A5EBW8

MQSSPLTSTLLFHIGPVAITRPVVTTWVIMAALALVCRFVTRRLAILPDGRQALLEGIVTSVAGQIEDVIRKDARPFLPLLGTLIIFLVVANLSGVLPGVEAPTSKIETPAALALIVFFSVHYFGVRERGLRGYLASFAEPKLIMLPLNILSEITRTFSLMVRLFGNIMSGEFIIGLVVALAGLFVPIPLMALEILVGLVQAYIFTVLATVFIGAAVGSVAKG

Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 23854 Sequence Length: 223 Subcellular Location: Cell inner membrane