Datasets:

Synthyra

/

SwissProtNLP

like 0

Follow

Synthyra 5

P27695

MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGDEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL

Cofactor: Probably binds two magnesium or manganese ions per subunit. Function: Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression. Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Acts also as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA. Binds DNA and RNA. PTM: Phosphorylated. Phosphorylation by kinase PKC or casein kinase CK2 results in enhanced redox activity that stimulates binding of the FOS/JUN AP-1 complex to its cognate binding site. AP-endodeoxyribonuclease activity is not affected by CK2-mediated phosphorylation. Phosphorylation of Thr-233 by CDK5 reduces AP-endodeoxyribonuclease activity resulting in accumulation of DNA damage and contributing to neuronal death. Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates. Sequence Mass (Da): 35555 Sequence Length: 318 Domain: The N-terminus contains the redox activity while the C-terminus exerts the DNA AP-endodeoxyribonuclease activity; both function are independent in their actions. An unconventional mitochondrial targeting sequence (MTS) is harbored within the C-terminus, that appears to be masked by the N-terminal sequence containing the nuclear localization signal (NLS), that probably blocks the interaction between the MTS and Tom proteins. Subcellular Location: Nucleus EC: 3.1.11.2

Q9UBZ4

MLRVVSWNINGIRRPLQGVANQEPSNCAAVAVGRILDELDADIVCLQETKVTRDALTEPLAIVEGYNSYFSFSRNRSGYSGVATFCKDNATPVAAEEGLSGLFATQNGDVGCYGNMDEFTQEELRALDSEGRALLTQHKIRTWEGKEKTLTLINVYCPHADPGRPERLVFKMRFYRLLQIRAEALLAAGSHVIILGDLNTAHRPIDHWDAVNLECFEEDPGRKWMDSLLSNLGCQSASHVGPFIDSYRCFQPKQEGAFTCWSAVTGARHLNYGSRLDYVLGDRTLVIDTFQASFLLPEVMGSDHCPVGAVLSVSSVPAKQCPPLCTRFLPEFAGTQLKILRFLVPLEQSPVLEQSTLQHNNQTRVQTCQNKAQVRSTRPQPSQVGSSRGQKNLKSYFQPSPSCPQASPDIELPSLPLMSALMTPKTPEEKAVAKVVKGQAKTSEAKDEKELRTSFWKSVLAGPLRTPLCGGHREPCVMRTVKKPGPNLGRRFYMCARPRGPPTDPSSRCNFFLWSRPS

Cofactor: Probably binds two magnesium or manganese ions per subunit. Function: Functions as a weak apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents . Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Also displays double-stranded DNA 3'-5' exonuclease, 3'-phosphodiesterase activities . Shows robust 3'-5' exonuclease activity on 3'-recessed heteroduplex DNA and is able to remove mismatched nucleotides preferentially . Also exhibits 3'-5' exonuclease activity on a single nucleotide gap containing heteroduplex DNA and on blunt-ended substrates . Shows fairly strong 3'-phosphodiesterase activity involved in the removal of 3'-damaged termini formed in DNA by oxidative agents . In the nucleus functions in the PCNA-dependent BER pathway . Plays a role in reversing blocked 3' DNA ends, problematic lesions that preclude DNA synthesis . Required for somatic hypermutation (SHM) and DNA cleavage step of class switch recombination (CSR) of immunoglobulin genes (By similarity). Required for proper cell cycle progression during proliferation of peripheral lymphocytes (By similarity). Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates. Sequence Mass (Da): 57401 Sequence Length: 518 Domain: The PCNA interacting protein (PIP) box mediates interaction with PCNA and recruitment to DNA single-strand breaks. Subcellular Location: Nucleus EC: 3.1.11.2

Q6DDT4

MKIVSWNINGIRATRVGLKETLDSLDADIICLQETKVTRDLLDEPSAIVEGYNSYFSFSRVRSGYSGVATFCKSSTTPQAAEEGLSGVFCNRTGSVGCYGNTEQFLEEELQSLDQEGRAVLTQHRILNCEDKEETLTVINVYCPRADPEKPERKTYKLRFYHLLQTRAEAILQNGGHVIILGDVNTSHRPLDHCDPTDLETFEENPGRQWLNQFLGDPIPSQKGDSETVMPPSAGSGLFYDSFRYFHPTQKNAFTCWCSASGARQTNYGTRIDYILGNRELVESEFLDSVIMPEVEGSDHCPVKAFMKCQPIAANKCPPLCTKYLPEFAGRQQKLLQFLVKKENTLGNTTEESSELTGTPSFTEGADISTVRKRPSDKLNSTSKKKSKIVTKNGQGNLLSFFKPERQKLTMATECNPIEVPICKKEKTVQKDLQPATPAVKYNKPQTAFWKSLLKGPPPPPNCKGHSEPCVLRTVKKAGPNCGRQFYVCARPEGHSSNPQARCNFFLWLTKKAGCED

Cofactor: Probably binds two magnesium or manganese ions per subunit. Function: Functions as a weak apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents . Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends . Exhibits 3'-5' exonuclease activity on a 3' DNA substrate; nuclease activity is stimulated by interaction with pcna . Has a preference for the 3' recessed ends over blunt-ended substrates, in both the presence and the absence of pcna . Generates single-stranded DNA (ssDNA) via 3'-5' single-strand break (SSB) end resection, thereby promoting a DNA damage response via replication protein A (rpa2)-binding to ssDNA and the recruitment of a checkpoint protein complex, including atr, atr-interacting protein atrip, and rad9, to damage sites following oxidative stress . Plays a role in reversing blocked 3' DNA ends, problematic lesions that preclude DNA synthesis . Required for chek1 phosphorylation induced by hydrogen peroxide but not by stalled replication forks . Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates. Sequence Mass (Da): 57726 Sequence Length: 517 Domain: The PCNA interacting protein (PIP) box mediates interaction with pcna and recruitment of pcna to DNA single-strand breaks. Subcellular Location: Nucleus EC: 3.1.11.2

P27916

MDARSLLLLWLLLPLLLLLGCEVQGAHLTQQDEPTSPDLLETLSTYWDSAKAAAQGLYNNTYLPAVDETIRDIYSKGSAAISTYTGILTDQILTMLQGKQ

Function: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. Both proapolipoprotein C-II and apolipoprotein C-II can activate lipoprotein lipase. PTM: Proapolipoprotein C-II is synthesized as a sialic acid containing glycoprotein which is subsequently desialylated prior to its proteolytic processing. Sequence Mass (Da): 10985 Sequence Length: 100 Subcellular Location: Secreted

P0DUX7

MGSRFLLALFLVLLVLGCEVQAAQQLQQDDPGSPALLDKVQESISSYWDTAKAAAQDLYQKTYLTSVDEKLRDMYSKSSAAMTTYASIFTDQILTLLKGE

Function: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. PTM: Proapolipoprotein C-II is synthesized as a sialic acid containing glycoprotein which is subsequently desialylated prior to its proteolytic processing. Sequence Mass (Da): 11059 Sequence Length: 100 Subcellular Location: Secreted

P02655

MGTRLLPALFLVLLVLGFEVQGTQQPQQDEMPSPTFLTQVKESLSSYWESAKTAAQNLYEKTYLPAVDEKLRDLYSKSTAAMSTYTGIFTDQVLSVLKGEE

Function: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. Both proapolipoprotein C-II and apolipoprotein C-II can activate lipoprotein lipase. In normolipidemic individuals, it is mainly distributed in the HDL, whereas in hypertriglyceridemic individuals, predominantly found in the VLDL and LDL. PTM: Proapolipoprotein C-II is synthesized as a sialic acid containing glycoprotein which is subsequently desialylated prior to its proteolytic processing. Sequence Mass (Da): 11284 Sequence Length: 101 Subcellular Location: Secreted

P0DMN9

MGTRFLLALFLVLLVLGFEVQGAQLPQQDEPSSPTLLTQMQESLSSYWDSAKEAARGLYEKTYLPTVDEKLRDMYSKSTAAVSTYAGIFTDQLLTLLKGD

Function: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. Both proapolipoprotein C-II and apolipoprotein C-II can activate lipoprotein lipase. PTM: Proapolipoprotein C-II is synthesized as a sialic acid containing glycoprotein which is subsequently desialylated prior to its proteolytic processing. Sequence Mass (Da): 11113 Sequence Length: 100 Subcellular Location: Secreted

T1W425

MGTRCLLVLLLVLLVLKCEVQGDDMARQDEATGPTLLSQMQESLYGYWGSAKAAAQDLYEKTYLTAMDEKIRDMYSTSTAAVRIYTGILTDQILSMLTGDP

Function: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase, the enzyme which hydrolyzes the triacylglycerols on chylomicrons and VLDL. PTM: Proapolipoprotein C-II is synthesized as a sialic acid containing glycoprotein which is subsequently desialylated prior to its proteolytic processing. Sequence Mass (Da): 11175 Sequence Length: 101 Subcellular Location: Secreted

Q9LKL2

MDLNGECKGGDGFIDRSRVRILLCDNDSTSLGEVFTLLSECSYQVTAVKSARQVIDALNAEGPDIDIILAEIDLPMAKGMKMLRYITRDKDLRRIPVIMMSRQDEVPVVVKCLKLGAADYLVKPLRTNELLNLWTHMWRRRRMLGLAEKNMLSYDFDLVGSDQSDPNTNSTNLFSDDTDDRSLRSTNPQRGNLSHQENEWSVATAPVHARDGGLGADGTATSSLAVTAIEPPLDHLAGSHHEPMKRNSNPAQFSSAPKKSRLKIGESSAFFTYVKSTVLRTNGQDPPLVDGNGSLHLHRGLAEKFQVVASEGINNTKQARRATPKSTVLRTNGQDPPLVNGNGSHHLHRGAAEKFQVVASEGINNTKQAHRSRGTEQYHSQGETLQNGASYPHSLERSRTLPTSMESHGRNYQEGNMNIPQVAMNRSKDSSQVDGSGFSAPNAYPYYMHGVMNQVMMQSAAMMPQYGHQIPHCQPNHPNGMTGYPYYHHPMNTSLQHSQMSLQNGQMSMVHHSWSPAGNPPSNEVRVNKLDRREEALLKFRRKRNQRCFDKKIRYVNRKRLAERRPRVKGQFVRKMNGVNVDLNGQPDSADYDDEEEEEEEEEEENRDSSPQDDALGT

Function: Controls photoperiodic flowering response. Component of the circadian clock. Expression of several members of the ARR-like family is controlled by circadian rhythm. The particular coordinated sequential expression of APRR9, APRR7, APRR5, APRR3 and APPR1 result to circadian waves that may be at the basis of the endogenous circadian clock. Positive regulator of CCA1 and LHY expression. PTM: Phosphorylated; during the day. Phosphorylation is required for optimal interaction with APRR3. Sequence Mass (Da): 69195 Sequence Length: 618 Domain: The N-terminus (1-243) is required for interactions with ADO1/ZTL and APRR3. Subcellular Location: Nucleus

Q9LVG4

MCFNNIETGDEVETERQVFGSSEEDEFRVEDTARNTNNVQISQQQQQPLAHVVKWERYLPVRSLKVLLVENDDSTRHIVTALLKNCSYEVTAVPDVLEAWRILEDEKSCIDLVLTEVDMPVHSGTGLLSKIMSHKTLKNIPVIMMSSHDSMVLVFKCLSNGAVDFLVKPIRKNELKNLWQHVWRRCHSSSGSGSESGIHDKKSVKPESTQGSENDASISDEHRNESGSSGGLSNQDGGSDNGSGTQSSWTKRASDTKSTSPSNQFPDAPNKKGTYENGCAHVNRLKEAEDQKEQIGTGSQTGMSMSKKAEEPGDLEKNAKYSVQALERNNDDTLNRSSGNSQVESKAPSSNREDLQSLEQTLKKTREDRDYKVGDRSVLRHSNLSAFSKYNNGATSAKKAPEENVESCSPHDSPIAKLLGSSSSSDNPLKQQSSGSDRWAQREAALMKFRLKRKERCFEKKVRYHSRKKLAEQRPHVKGQFIRKRDDHKSGSEDN

Function: Controls photoperiodic flowering response. Component of the circadian clock. Controls the degradation of APRR1/TOC1 by the SCF(ZTL) complex. Expression of several members of the ARR-like family is controlled by circadian rhythm. The particular coordinated sequential expression of APRR9, APRR7, APRR5, APRR3 and APPR1 result to circadian waves that may be at the basis of the endogenous circadian clock. PTM: Phosphorylated by WNK1; during the night. Phosphorylation is required for optimal interaction with APRR1/TOC1. Sequence Mass (Da): 55286 Sequence Length: 495 Subcellular Location: Nucleus

Q6LA42

MTSSEEVVEVTVVKAPEAGGGKLSRRKIRKKDAGVDGLVKWERFLPKIALRVLLVEADDSTRQIIAALLRKCSYRVAAVPDGLKAWEMLKGKPESVDLILTEVDLPSISGYALLTLIMEHDICKNIPVIMMSTQDSVNTVYKCMLKGAADYLVKPLRRNELRNLWQHVWRRQTSLAPDSFPWNESVGQQKAEGASANNSNGKRDDHVVSGNGGDAQSSCTRPEMEGESADVEVSARDAVQMECAKSQFNETRLLANELQSKQAEAIDFMGASFRRTGRRNREESVAQYESRIELDLSLRRPNASENQSSGDRPSLHPSSASAFTRYVHRPLQTQCSASPVVTDQRKNVAASQDDNIVLMNQYNTSEPPPNAPRRNDTSFYTGADSPGPPFSNQLNSWPGQSSYPTPTPINNIQFRDPNTAYTSAMAPASLSPSPSSVSPHEYSSMFHPFNSKPEGLQDRDCSMDVDERRYVSSATEHSAIGNHIDQLIEKKNEDGYSLSVGKIQQSLQREAALTKFRMKRKDRCYEKKVRYESRKKLAEQRPRIKGQFVRQVQSTQAP

Function: Transcriptional repressor of CCA1 and LHY, thereby controlling photoperiodic flowering response. Involved in the positive and negative feedback loops of the circadian clock. With RVE8, forms a negative feedback loop of the circadian clock . Expression of several members of the ARR-like family is controlled by circadian rhythm. Proteolytic substrate of the E3 ubiquitin ligase SCF(ADO1) complex. APRR9, APRR7, and APRR5 coordinately act on the upstream region of the target genes to repress their expression from noon until midnight. The particular coordinated sequential expression of APRR9, APRR7, APRR5, APRR3 and APPR1 result to circadian waves that may be at the basis of the endogenous circadian clock. Negative regulator of shade avoidance response. Involved in the inhibition of leaf expansion in shade avoidance response. PTM: Phosphorylation varies throughout the diurnal cycle and enhances ADO1 binding. Sequence Mass (Da): 62301 Sequence Length: 558 Subcellular Location: Nucleus

Q93WK5

MNANEEGEGSRYPITDRKTGETKFDRVESRTEKHSEEEKTNGITMDVRNGSSGGLQIPLSQQTAATVCWERFLHVRTIRVLLVENDDCTRYIVTALLRNCSYEVVEASNGIQAWKVLEDLNNHIDIVLTEVIMPYLSGIGLLCKILNHKSRRNIPVIMMSSHDSMGLVFKCLSKGAVDFLVKPIRKNELKILWQHVWRRCQSSSGSGSESGTHQTQKSVKSKSIKKSDQDSGSSDENENGSIGLNASDGSSDGSGAQSSWTKKAVDVDDSPRAVSLWDRVDSTCAQVVHSNPEFPSNQLVAPPAEKETQEHDDKFEDVTMGRDLEISIRRNCDLALEPKDEPLSKTTGIMRQDNSFEKSSSKWKMKVGKGPLDLSSESPSSKQMHEDGGSSFKAMSSHLQDNREPEAPNTHLKTLDTNEASVKISEELMHVEHSSKRHRGTKDDGTLVRDDRNVLRRSEGSAFSRYNPASNANKISGGNLGSTSLQDNNSQDLIKKTEAAYDCHSNMNESLPHNHRSHVGSNNFDMSSTTENNAFTKPGAPKVSSAGSSSVKHSSFQPLPCDHHNNHASYNLVHVAERKKLPPQCGSSNVYNETIEGNNNTVNYSVNGSVSGSGHGSNGPYGSSNGMNAGGMNMGSDNGAGKNGNGDGSGSGSGSGSGNLADENKISQREAALTKFRQKRKERCFRKKVRYQSRKKLAEQRPRVRGQFVRKTAAATDDNDIKNIEDS

Function: Transcriptional repressor of CCA1 and LHY, and positive regulator of LWD1 and LWD2 expression. Represses the expression of other clock proteins and master regulators of plant growth, development and response to abiotic stress. Involved in the positive and negative feedback loops of the circadian clock. Controls photoperiodic flowering response and temperature compensation. Expression of several members of the ARR-like family is controlled by circadian rhythm. APRR9, APRR7, and APRR5 coordinately act on the upstream region of the target genes to repress their expression from noon until midnight. The particular coordinated sequential expression of APRR9, APRR7, APRR5, APRR3 and APPR1 result to circadian waves that may be at the basis of the endogenous circadian clock. PTM: Phosphorylated. Phosphorylation varies throughout the diurnal cycle. Sequence Mass (Da): 79663 Sequence Length: 727 Subcellular Location: Nucleus

Q8L500

MGEIVVLSSDDGMETIKNRVKSSEVVQWEKYLPKTVLRVLLVESDYSTRQIITALLRKCCYKVVAVSDGLAAWEVLKEKSHNIDLILTELDLPSISGFALLALVMEHEACKNIPVIMMSSQDSIKMVLKCMLRGAADYLIKPMRKNELKNLWQHVWRRLTLRDDPTAHAQSLPASQHNLEDTDETCEDSRYHSDQGSGAQAINYNGHNKLMENGKSVDERDEFKETFDVTMDLIGGIDKRPDSIYKDKSRDECVGPELGLSLKRSCSVSFENQDESKHQKLSLSDASAFSRFEESKSAEKAVVALEESTSGEPKTPTESHEKLRKVTSDQGSATTSSNQENIGSSSVSFRNQVLQSTVTNQKQDSPIPVESNREKAASKEVEAGSQSTNEGIAGQSSSTEKPKEEESAKQRWSRSQREAALMKFRLKRKDRCFDKKVRYQSRKKLAEQRPRVKGQFVRTVNSDASTKS

Function: Transcriptional repressor of CCA1 and LHY, and positive regulator of LWD1 and LWD2 expression. Controls photoperiodic flowering response and temperature compensation. Involved in the positive and negative feedback loops of the circadian clock. Expression of several members of the ARR-like family is controlled by circadian rhythm. Regulated at the transcriptional level by a corepressor complex consisting of ELF4, ELF3, and LUX. APRR9, APRR7, and APRR5 coordinately act on the upstream region of the target genes to repress their expression from noon until midnight. The particular coordinated sequential expression of APRR9, APRR7, APRR5, APRR3 and APPR1 result to circadian waves that may be at the basis of the endogenous circadian clock. PTM: Phosphorylated. Phosphorylation varies throughout the diurnal cycle. Sequence Mass (Da): 52565 Sequence Length: 468 Subcellular Location: Nucleus

B0CHX9

MESGFKVTLKDAIRTIPDYPKPGVQFRDVTTLMGNAQAFRRAVDELVYPYAGNRIDKVAGIEARGFILGGAIAHQLSAGFVPIRKKGKLPRDTARIAYSLEYGVDEMEMHRDAIEKGERVVLVDDLIATGGTAEAAAKLLLQMGAEIVAACFIIDLPDLGGRKKLEALGLPVRTLVAFEGD

Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Sequence Mass (Da): 19586 Sequence Length: 181 Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Subcellular Location: Cytoplasm EC: 2.4.2.7

P07741

MADSELQLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKATHGGRIDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRGKLPGPTLWASYSLEYGKAELEIQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSLKGREKLAPVPFFSLLQYE

Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Sequence Mass (Da): 19608 Sequence Length: 180 Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Subcellular Location: Cytoplasm EC: 2.4.2.7

Q31JG9

MKQHPLAQYLEAVPDFPKEGILFQDISPLLRDHFVATIDAMSLLFSAKEWAEVDYLVGVESRGFIFASALALKHDKGFVKVRKPGKLPNVHASMEYGLEYGTDKLEMQKGNGKKVIICDDLIATGGSMQAAAKLCNEVGYEVVGMACLVDLKALNSFSHDGMTVRSVIQFDD

Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Sequence Mass (Da): 18913 Sequence Length: 172 Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Subcellular Location: Cytoplasm EC: 2.4.2.7

Q1G9R7

MSIDFKKYIASVKDFPNEGIIFRDITPILQDGEAFAAATHEIAEYAKSRQADVIVGPEARGFLVGTPVAIELGIGFVPARKPHKLPREVEAAAYDLEYGSNVLEMHKDAIKPGQRVVICDDLMATAGTMHATKELIERLGGKVVGAAFYIELTDLKGREKFPDVDIFSLVQYTGA

Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Sequence Mass (Da): 19125 Sequence Length: 175 Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Subcellular Location: Cytoplasm EC: 2.4.2.7

Q9CHT5

MELKDYIATIENYPKEGVVFRDISPLMADGNAYNYAATEIVQYARDKEIDMVVGPEARGFIIGCPVAFALGVGFAPVRKPGKLPREVIEATYEKEYGTDTLTMHSDSIKPGQRVLIVDDLLATGGTIAATIELVEKMGGIVVGCAFLIELDELKGREKIGDYDYKVLMHY

Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Sequence Mass (Da): 18713 Sequence Length: 170 Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Subcellular Location: Cytoplasm EC: 2.4.2.7

B1XL39

MDLKSLIRDIPDFPKPGILFRDITTLLNHPEGMRYTMDALVQLCLEANLKPDHVVGMESRGFIFGPTLAYNLNAGFVPVRKPGKLLAAVHTVEYELEYGTDTLEIHQDAVGSGDKIVIVDDLIATGGTAKATAELLTKIGCDIIGFVFIVELLDLKGRDRLPDAPVLSLIQY

Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Sequence Mass (Da): 18849 Sequence Length: 172 Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Subcellular Location: Cytoplasm EC: 2.4.2.7

P73935

MDLKALIRDIPDFPKPGIMFRDITTLLNSPEGLRYTIDSLVEQCESQELVPDHVVGMESRGFLFGMPLAYQMNAGFIPVRKPGKLPAPVHRVEYDLEYGKDSLEIHQDAVAPHHRVLIVDDLIATGGTAKATAELLTKLGCEVLGFAFIIELAALNGRQCLPDLPIISLVEY

Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Sequence Mass (Da): 18997 Sequence Length: 172 Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Subcellular Location: Cytoplasm EC: 2.4.2.7

Q9X1A4

MFKLDLKRFIRDIPDFPQKGIVFRDITPLLRNQEAFKEAIDRMCELVFDREFDLVVAPEARGFILGAAMAYKLGKGFVPVRKPGKLPYKTVYEEYQLEYGTEQLHIHEDAIEKGQKVLIVDDVLATGGTAEALIRLVKKLGGEVVSLAFLVELSYLEPRKRLEGYDVKTLIVY

Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Sequence Mass (Da): 19766 Sequence Length: 173 Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Subcellular Location: Cytoplasm EC: 2.4.2.7

Q73M27

MTIAKIRCRLFIMKDKIIDAAIRRVPDFPKKGILFYDITGILVNPEVFSYCLDKMTEMYKDKKVDAVAAIEARGFIFAAPFAYKMGIPLILIRKKGKLPGETYSASYDLEYGQASVEVHKTDVVKGQKVLLLDDLIATGGTLNAARSILEEGGAKVVGFCGVVGLPFLNYSKVLGDLPVKTLIEYDSEKI

Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Sequence Mass (Da): 20975 Sequence Length: 190 Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Subcellular Location: Cytoplasm EC: 2.4.2.7

Q13520

MDAVEPGGRGWASMLACRLWKAISRALFAEFLATGLYVFFGVGSVMRWPTALPSVLQIAITFNLVTAMAVQVTWKASGAHANPAVTLAFLVGSHISLPRAVAYVAAQLVGATVGAALLYGVMPGDIRETLGINVVRNSVSTGQAVAVELLLTLQLVLCVFASTDSRQTSGSPATMIGISVALGHLIGIHFTGCSMNPARSFGPAIIIGKFTVHWVFWVGPLMGALLASLIYNFVLFPDTKTLAQRLAILTGTVEVGTGAGAGAEPLKKESQPGSGAVEMESV

Function: Forms a water-specific channel that participates in distinct physiological functions such as glomerular filtration, tubular endocytosis and acid-base metabolism. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 29370 Sequence Length: 282 Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). Subcellular Location: Cytoplasmic vesicle membrane

B0DLE4

MDDKFDDDALPNSKTTPEDYGDKLAEYDYTNTFPNTWMRLREPFREYIAEFVGVAVLIIFGVGADCQVVLSANTGVAPSPKGDYLSLNCGWAIGTAMGVWISGGISGGHINPAVTLALMAWRGFPWWKVPGFIFAQLLGGIVGAGLVYVNYIHAIDIVEGGRHIRTLDTAGLFATYAADYMTNVSCFFSEFLATAVLIVVIHAMNDKRNAPPPAGLAPLVLFFLILGIGASLGMETGYAINPARDLGPRMLTAMVGYGRQVFAFRNQYWIWCPVIAPFLGAQVGTIFYDLFFYKGQDNVFGRLGSHIHISPA

Function: Water channel required to facilitate the transport of water across membranes . In addition to water, shows also strong glycerol and ammonium transport activities . May be involved in fungal nitrogen (ammonium) support of the plant host in symbiosis . Glycerol accumulation has never been observed in ectomycorrhizal (ECM) fungi, therefore, glycerol permeability of Lacbi1:391485 might be a relict of the affiliation of the protein to the group of aquaglyceroporins, and other osmotic active compounds (e.g. trehalose or mannitol) may have taken over glycerol function in ECM fungi (Probable). Catalytic Activity: H2O(in) = H2O(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 34015 Sequence Length: 312 Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). Subcellular Location: Membrane

G5CTG3

MAFMDKSEVRQRLQKVLQQCAKAPTWSPKEEVRQSIFWKSIRAELIGSLVLMVFSCSRDSIYGPVSYGCTYAILSYCFKSISAHFNPVITIAALLLRSITPFRCISLVLAQTLGTLSGASVCYYGLSNETETGSAPISPVLNVSPAKGFGYEFFGTFVIILTMSSYLDCNDYVSESGDSNLLPLIFGLSVGLSSGMARQATGGFLNPMRAFSLALFELNHWSNHYIYWIGPIFGCLLAVFTFDYTRPIIPNRDSNNRINFPTFNKNNKYEVEMQPETEITLATLA

Function: Probable water-specific aquaporin that may modulate the water content and osmolytes during anhydrobiosis . Location Topology: Multi-pass membrane protein Sequence Mass (Da): 31694 Sequence Length: 285 Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). Subcellular Location: Cell membrane

Q9WTY0

MEPGLCNRAYLLVGGLWTAISKALFAEFLATGLYVFFGVGSVLPWPVALPSVLQVAITFNLATATAVQISWKTSGAHANPAVTLAYLVGSHISLPRAVAYIAAQLAGATVGAALLYGVTPGGVRETLGVNVVHNSTSTGQAVAVELVLTLQLVLCVFASMDSRQTLGSPAAMIGTSVALGHLIGIYFTGCSMNPARSFGPAVIVGKFAVHWIFWVGPLTGAVLASLIYNFILFPDTKTVAQRLAILVGTTKVEKVVDLEPQKKESQTNSEDTEVSV

Function: Forms a water-specific channel that participates in distinct physiological functions such as glomerular filtration, tubular endocytosis and acid-base metabolism. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 28860 Sequence Length: 276 Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). Subcellular Location: Cytoplasmic vesicle membrane

A0A384J409

MNINEPRDGGGFVLPFFNDSKKSRKSHAGRDSLKSNRVPFTKWVPDTVSYTTKPLKNAHRWLHLHNKTRNHFVATVAEFAGTTLFLFFAFSGTQVALLATPANDSNVVGTPSNPAQLLYVSLCFGFSLAVNAWVFFRISGGLFNPAVTMGMCIVGALPYFRGLLLIFAQIIGGIAAAAIVSALFPGPITFRTSLGGGTSIVQGLFIEMFLTAELVFTIFMLAAEKHKGTFIAPIGIGLSLFIAELTGVYFTGGSVNPARSFGPSVVSGQFTGYHWIYWVGPILGAILASAFYKFIKMLEYETANPGQDAGRVGEVIDPEAQAIKNRVSFASEGLVGRELDESGASHVHENGNHFGAPKEYGTKRRPFSDSPAPPNANDQFAGLSEGGLHTDEFANENIGGGHSGEGAMHRNKRDSEGTLVGNGKKGVLKVGAGGTGGAAVGSTNENLRDNTHNN

Function: Water channel required to facilitate the transport of water across membranes (Probable). Involved in conidiation . Catalytic Activity: H2O(in) = H2O(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 48351 Sequence Length: 454 Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). Subcellular Location: Membrane

O14520

MVQASGHRRSTRGSKMVSWSVIAKIQEILQRKMVREFLAEFMSTYVMMVFGLGSVAHMVLNKKYGSYLGVNLGFGFGVTMGVHVAGRISGAHMNAAVTFANCALGRVPWRKFPVYVLGQFLGSFLAAATIYSLFYTAILHFSGGQLMVTGPVATAGIFATYLPDHMTLWRGFLNEAWLTGMLQLCLFAITDQENNPALPGTEALVIGILVVIIGVSLGMNTGYAINPSRDLPPRIFTFIAGWGKQVFSNGENWWWVPVVAPLLGAYLGGIIYLVFIGSTIPREPLKLEDSVAYEDHGITVLPKMGSHEPTISPLTPVSVSPANRSSVHPAPPLHESMALEHF

Function: Forms a channel that mediates water and glycerol transport across cell membranes at neutral pH . The channel is also permeable to urea . Plays an important role in body energy homeostasis under conditions that promote lipid catabolism, giving rise to glycerol and free fatty acids. Mediates glycerol export from adipocytes. After release into the blood stream, glycerol is used for gluconeogenesis in the liver to maintain normal blood glucose levels and prevent fasting hypoglycemia. Required for normal glycerol reabsorption in the kidney (By similarity). Location Topology: Multi-pass membrane protein Sequence Mass (Da): 37232 Sequence Length: 342 Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro/Ala-Ala/Ser (NPA). Subcellular Location: Cell membrane

B0D4J9

MSGQHQITEQSSRNPLSRVSTLLPEKPLSPTSTYAGTQKHPEAPRQSSFLIQLQNIRNAIRKPMAEFFGVALLIIFGAGSACQVVLSTNPDVASSARGSFLSINFGWAIGIAMGVWVSGGISGGHINPAITIAMATYRGFPWRKVPSYILAQVLGGVVGAGLVYANYIHAIDIFEGGHHIRTQATASLFATYALPYMTQASCFFSEFLATAVLSMMVFALTDKRNHSPTNGLLPFALFILFVGLGASLGMETAYALNPARDFGPRLFLAMAGYGKALFNYRSQYWLWAPIIAPVLGAQAGGLLYDTFLNDGDNSPIKWRCASSQEHQLAEVV

Function: Water channel required to facilitate the transport of water across membranes . Acts as thre most efficient Laccaria water channel . In addition to water, shows also strong ammonium transport activity . May be involved in fungal nitrogen (ammonium) support of the plant host in symbiosis . Catalytic Activity: H2O(in) = H2O(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 35816 Sequence Length: 332 Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). Subcellular Location: Membrane

Q4R691

MVQTSRHRRSTRGSKMVSWSVMAKIQEILQKKMVREFLAEFMSTYVMMVFGLGSVAHMVLNKKYGSYLGVNLGFGFGVTMGVHVAGHISGAHMNAAVTFANCALGRVPWRKFPVYVLGQFLGSFLAAATIYTLFYTAILHFSGGQLMVTGPVATAGIFATYLPDHMTLWRGFLNEAWLTGMLQLCLFAITDQENNAALPGTQALVIGILVVIIGVSLGMNTGYAINPSRDLPPRVFTFIAGWGKEVFSEGENWWWVPVVAPLLGACLGGIIYLVFIGSTTPREPLKLEDSVAYEDHGITVLPKMGSHEPTISPLTPVSVSPANRSSVRPAPPLHESMALGHF

Function: Forms a channel that mediates water and glycerol transport across cell membranes at neutral pH (By similarity). The channel is also permeable to urea (By similarity). Plays an important role in body energy homeostasis under conditions that promote lipid catabolism, giving rise to glycerol and free fatty acids. Mediates glycerol export from adipocytes. After release into the blood stream, glycerol is used for gluconeogenesis in the liver to maintain normal blood glucose levels and prevent fasting hypoglycemia. Required for normal glycerol reabsorption in the kidney (By similarity). Location Topology: Multi-pass membrane protein Sequence Mass (Da): 37196 Sequence Length: 342 Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro/Ala-Ala/Ser (NPA). Subcellular Location: Cell membrane

G5CTG4

MAHNEKDPSSVEPIKRKRFSNEYVRLFLAEFLGTFILIVFGCGTVAVTILSKHQSQDFFSVNVGFFLGIAFGVFIAGGVSGGHLNPAVTLAFAVINKCKWRKVPVYMAAQYLGAWVGSAILTAIYYDALHNHDQGNRTIETAGIYASYPQEFLTWQGGLADQIFATLLLMMGILALTDERNMVGPTGRAYVPLLVGLLVLAIGLAFGFNCGYPINPARDFGPRLFTAMAGWGTQVFSEPRGTYNWWWIPIIGPHVGAIIGALAYNFFIGYHWPKERDDVQLQSPSSPIVIVKNDAYQPLRPSRSVYSEELRITTS

Function: Aquaglyceroporin that may modulate the water content and osmolytes during anhydrobiosis . Location Topology: Multi-pass membrane protein Sequence Mass (Da): 34796 Sequence Length: 315 Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). Subcellular Location: Cell membrane

O54794

MAPRSVLETIQSVLQKNMVREFLAEFLSTYVMMVFGLGSVAHMVLGENSGSYLGVNLGFGFGVTMGVHVAGGISGAHMNAAVTFTNCALGRMTWKKFPVYVLGQFLGSFSAAATTYLIFYGAINHFAGGDLLVTGSKATANIFATYLPEYMTLWRGFLDEAFVTGMLQLCLFAITDKKNSPALQGTEPLVIGILVTVLGVSLGMNSGYAINPSRDLPPRLFTFIAGWGKQVFRAGNNWWWVPVVAPLLGAYLGGIVYLGLIHPSIPQDPQRLENFTARDQKVTASYKNAASANISGSVPLEHF

Function: Forms a channel that mediates water and glycerol transport across cell membranes at neutral pH . The channel is also permeable to urea (By similarity). Plays an important role in body energy homeostasis under conditions that promote lipid catabolism, giving rise to glycerol and free fatty acids . Mediates glycerol export from adipocytes . After release into the blood stream, glycerol is used for gluconeogenesis in the liver to maintain normal blood glucose levels and prevent fasting hypoglycemia . Required for normal glycerol reabsorption in the kidney . Location Topology: Multi-pass membrane protein Sequence Mass (Da): 32667 Sequence Length: 303 Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro/Ala-Ala/Ser (NPA). Subcellular Location: Cell membrane

P56403

MAGSVLENIQSVLQKTWVREFLAEFLSTYVLMVFGLGSVAHMVLGERLGSYLGVNLGFGFGVTMGIHVAGGISGAHMNAAVTFTNCALGRMAWKKFPIYVLGQFLGSFLAAATTYLIFYGAINHYAGGELLVTGPKSTANIFATYLPEHMTLWRGFVDEVFVTGMLQLCIFAITDKLNSPALQGTEPLMIGILVCVLGVSLGMNTGYAINPSRDLPPRFFTFIAGWGKKVFSAGNNWWWVPVVAPLLGAYLGGIVYLGLIHAGIPPQGS

Function: Forms a channel that mediates water and glycerol transport across cell membranes at neutral pH . The channel is also permeable to urea . Plays an important role in body energy homeostasis under conditions that promote lipid catabolism, giving rise to glycerol and free fatty acids. Mediates glycerol export from adipocytes. After release into the blood stream, glycerol is used for gluconeogenesis in the liver to maintain normal blood glucose levels and prevent fasting hypoglycemia. Required for normal glycerol reabsorption in the kidney (By similarity). Location Topology: Multi-pass membrane protein Sequence Mass (Da): 28882 Sequence Length: 269 Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro/Ala-Ala/Ser (NPA). Subcellular Location: Cell membrane

A0A384JP03

MALRSPARDYLVSMIGELVGTFLFLFFAFAAAQTANQPNGTKPLTPNATDTSKLLYIALAFGASLAANVWVFFRVSGGQFNPAVTLALVLIRAVSPTKALILIPAQLVGGSLAAAAVKGIIPGDDILFAVSLGPGVANVQGLFIELLLTFMLVFTILMLVAEKTKSTFVAPIGIGFSLFIGHLVGIFWTGAGINPARAFSPALIQASFPSYHWIYWLGPALGSFLAAGLYLGLKEMKYELVGGDADKEKREEGLTVQQADLIIETLRGLPRAIQGSGALGQFEGTTEGHRSPVDLERGAEVRILEDDPHIRKSRYGSPDSTDLPT

Function: Plasma membrane water channel that regulates the reactive oxygen species (ROS)-signaling pathway through its capacity to act as a membrane channel for hydrogen peroxide uptake . Required for the formation of infection structures and infection, especially on host leaves where it is essential for the penetration into the host . Regulates the expression of proteins related to redox-regulation and intracellular signal transduction and plays a role in the distribution of mitochondria in the hyphae . Catalytic Activity: H2O2(out) = H2O2(in) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 34592 Sequence Length: 325 Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). Subcellular Location: Cell membrane

O94778

MSGEIAMCEPEFGNDKAREPSVGGRWRVSWYERFVQPCLVELLGSALFIFIGCLSVIENGTDTGLLQPALAHGLALGLVIATLGNISGGHFNPAVSLAAMLIGGLNLVMLLPYWVSQLLGGMLGAALAKAVSPEERFWNASGAAFVTVQEQGQVAGALVAEIILTTLLALAVCMGAINEKTKGPLAPFSIGFAVTVDILAGGPVSGGCMNPARAFGPAVVANHWNFHWIYWLGPLLAGLLVGLLIRCFIGDGKTRLILKAR

Function: Channel that allows the facilitated permeation of water and uncharged molecules, such as hydrogen peroxide and the neutral form of ammonia (NH3), through cellular membranes such as plasma membrane, inner mitochondrial membrane and endoplasmic reticulum membrane of several tissues . The transport of the ammonia neutral form induces a parallel transport of proton, at alkaline pH when the concentration of ammonia is high (By similarity). However, it is unclear whether the transport of proton takes place via the aquaporin or via an endogenous pathway (By similarity). Also, may transport ammonia analogs such as formamide and methylamine, a transport favourited at basic pH due to the increase of unprotonated (neutral) form, which is expected to favor diffusion . Does not transport urea or glycerol . The water transport mechanism is mercury- and copper-sensitive and passive in response to osmotic driving forces . At the canicular plasma membrane, mediates the osmotic transport of water toward the bile canaliculus and facilitates the cAMP-induced bile canalicular water secretion, a process involved in bile formation . In addition, mediates the hydrogen peroxide release from hepatocyte mitochondria that modulates the SREBF2-mediated cholesterol synthesis and facilitates the mitochondrial ammonia uptake which is metabolized into urea, mainly under glucagon stimulation . In B cells, transports the CYBB-generated hydrogen peroxide from the external leaflet of the plasma membrane to the cytosol to promote B cell activation and differentiation for signal amplification (By similarity). In the small intestine and colon system, mediates water transport through mitochondria and apical membrane of epithelial cells (By similarity). May play an important role in the adaptive response of proximal tubule cells to acidosis possibly by facilitating the mitochondrial ammonia transport . PTM: Sulfenylation at Cys-53(C53-SOH) when hydrogen peroxide flows through the AQP8 channel, making it susceptible to hydrogen sulfide produced by CBS. Location Topology: Multi-pass membrane protein Catalytic Activity: H2O(in) = H2O(out) Sequence Mass (Da): 27381 Sequence Length: 261 Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). Subcellular Location: Cell membrane

G5CTG5

MSTAESRNHYKEVPTIEHYSEAIGITNRKKMDWRGWLRKSTLVRSQLIRGCMAEFLAVFVLMVFIEGSAATAIFTNRRQDILFGSISSGLGVAMAVYVAGGVSGAFLNPAVALAFAVLGKLSWKNCIFYMISQYLAAFVASCTMFAYLYEALNNFDGGERQMFGPNGTAHIWSTYPQPFLSPHTAFADQVFCTAILLIVVLAMCDSKNWKPHNGFLPIAIGLLIITISCTLSYNAGAAMNPSRDLAPRFFSYLAGYGTEPFGVKGYTWFFVPVLGSHCGAIIGGAIYQLFIGGQWPDDTSDTNSVSSMSYNEDNSTLTKRKQVSNIVHDSKGAKGSSTAPVN

Function: Aquaglyceroporin that may modulate the water content and osmolytes during anhydrobiosis . Location Topology: Multi-pass membrane protein Sequence Mass (Da): 37279 Sequence Length: 342 Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). Subcellular Location: Cell membrane

Q88S84

MLSVPDYEFWFVTGSQHLYGEEQLKSVAKDAQDIADKLNASGKLPYKVVFKDVMTTAESITNFMKEVNYNDKVAGVITWMHTFSPAKNWIRGTELLQKPLLHLATQYLNNIPYADIDFDYMNLNQSAHGDREYAYINARLQKHNKIVYGYWGDEDVQEQIARWEDVAVAYNESFKVKVARFGDTMRNVAVTEGDKVEAQIKMGWTVDYYGIGDLVEEINKVSDADVDKEYADLESRYEMVQGDNDADTYKHSVRVQLAQYLGIKRFLERGGYTAFTTNFEDLWGMEQLPGLASQLLIRDGYGFGAEGDWKTAALGRVMKIMSHNKQTAFMEDYTLDLRHGHEAILGSHMLEVDPSIASDKPRVEVHPLDIGGKDDPARLVFTGSEGEAIDVTVADFRDGFKMISYAVDANKPEAETPNLPVAKQLWTPKMGLKKGALEWMQAGGGHHTMLSFSLTEEQMEDYATMVGMTKAFLK

Cofactor: Binds 1 Mn(2+) ion per subunit. Function: Catalyzes the conversion of L-arabinose to L-ribulose. Catalytic Activity: beta-L-arabinopyranose = L-ribulose Sequence Mass (Da): 53573 Sequence Length: 474 Pathway: Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): step 1/3. EC: 5.3.1.4

Q6D4W5

MDHFKQLEVWFVIGSQHLYGPETLRQVKENAEKVVAGLNQQANLPVKLVLKPLVKTPDEILALCRDANYQDNCIGLLTWLHTFSPAKMWIGGLSVLSKPLLQFHTQFNAEVPWDTMDMDFMNLNQTAHGGREFGFIGARMRQAHQVVVGHWQDKNAHVRIGKWMRVAAAIQESKQLKVARFGDNMREVAVTEGDKVGAQIQFGYSVSAWGLGDLTAVVDAVSKGDIDALIEEYETSYQLTDAVKLNGANRQNLLDAAQIELGMKRFLEQGGYHAFTTDFENLYGLKQLPGLAVQRLMQQGYGFGGEGDWKTAALLRIMKVMAGGLSGGTSFMEDYTYNFQNGNDLVVGSHMLEVCPTIAKEQKPILDAQHLGIGGKADPARLIFSTPAGPSLNASVIDMGDRFRMLVNLVDTIEQPRPLPKLPVARAIWKAQPSLEVAAEAWILAGGAHHTVFSQALDLDHMRLYAEMQNIELLVIDNETRLHEFKDALRWNEVYYKLCSR

Cofactor: Binds 1 Mn(2+) ion per subunit. Function: Catalyzes the conversion of L-arabinose to L-ribulose. Catalytic Activity: beta-L-arabinopyranose = L-ribulose Sequence Mass (Da): 55893 Sequence Length: 501 Pathway: Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): step 1/3. EC: 5.3.1.4

Q1JUP6

MSQAMQPQRTSPSPDAAIAPARARGGVWQLINRSGIVMVFLVLFATLSLTVPDFLTPRNIQGLLLSVTLIGSIAVTMMFVLALGEVDLSVASIVAFSGVVASTLITATHSVVLGIAGGVLAGGAVGLVNGVLIARWRINSLIVTLAMMEVVRGLAFITSNGDAVMISEERFFDLGGGSFLGISYPIWSNIVGFVVFGFLLRKTVFGKNVLAVGGNGEAALLAGLPVMRIKITVFVLQGLVTGFAGVMLASRMSLGDPKTSVGLELGVISACVLGGVSLTGGVATISGVLVGVLIMGSVQDAMSLLNVPTFYQYLIRGGILLLAVLFDQYRRNQRRAMKI

Function: Part of the ABC transporter complex AraFGH involved in L-arabinose import. Responsible for the translocation of the substrate across the membrane (Probable). Location Topology: Multi-pass membrane protein Sequence Mass (Da): 35372 Sequence Length: 339 Subcellular Location: Cell inner membrane

P0AE26

MSSVSTSGSGAPKSSFSFGRIWDQYGMLVVFAVLFIACAIFVPNFATFINMKGLGLAISMSGMVACGMLFCLASGDFDLSVASVIACAGVTTAVVINLTESLWIGVAAGLLLGVLCGLVNGFVIAKLKINALITTLATMQIVRGLAYIISDGKAVGIEDESFFALGYANWFGLPAPIWLTVACLIIFGLLLNKTTFGRNTLAIGGNEEAARLAGVPVVRTKIIIFVLSGLVSAIAGIILASRMTSGQPMTSIGYELIVISACVLGGVSLKGGIGKISYVVAGILILGTVENAMNLLNISPFAQYVVRGLILLAAVIFDRYKQKAKRTV

Function: Part of the binding-protein-dependent transport system for L-arabinose. Probably responsible for the translocation of the substrate across the membrane. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 34211 Sequence Length: 328 Subcellular Location: Cell inner membrane

A3KNS9

MTANVTVSSMYLFTVLLLLFNVYVNSQDTDAQLCQMCEGTIRHDSPVWSFCITKGYVKGHCCFKNNTSDVDTIIGLDLSNCSISHVEHLYNSSTALIIDLSNNPISNLSDYVFQGFSQLTQLLLPSKLECPGGRASWEKVEVKSITRICEGQKNACNQTVQMPLVCPENSLCSPYGPGFFECSCLNNFHGYKCMRQGEFPLVKVLGILTASTVVVSSVLWFTQRRKVKNT

Function: Involved in osteoblast cell differentiation. May play a role in inducing the cell cycle arrest (By similarity). Location Topology: Single-pass membrane protein Sequence Mass (Da): 25580 Sequence Length: 230 Subcellular Location: Nucleus envelope

Q6UW56

MAPHDPGSLTTLVPWAAALLLALGVERALALPEICTQCPGSVQNLSKVAFYCKTTRELMLHARCCLNQKGTILGLDLQNCSLEDPGPNFHQAHTTVIIDLQANPLKGDLANTFRGFTQLQTLILPQHVNCPGGINAWNTITSYIDNQICQGQKNLCNNTGDPEMCPENGSCVPDGPGLLQCVCADGFHGYKCMRQGSFSLLMFFGILGATTLSVSILLWATQRRKAKTS

Function: Promotes osteoblast cell differentiation and terminal mineralization. Plays a role in inducing the cell cycle arrest via inhibiting CCND1 expression in all-trans-retinoic acid (ATRA) signal pathway. In osteoclasts, forms a transporter complex with ATRAID for nitrogen-containing-bisphophonates (N-BPs) required for releasing N-BP molecules that have trafficked to lysosomes through fluid-phase endocytosis into the cytosol . Location Topology: Single-pass membrane protein Sequence Mass (Da): 24747 Sequence Length: 229 Subcellular Location: Nucleus envelope

Q6PGD0

MASRESGGSRAAALLLVLGVERALALPEICTLCPGGMHNLSRVAAYCEDTSKLMQARCCLNQKGTILGLDLQNCSLKDPGPNFLQAYTAIIIDLQANPLKDDLANTFRGFTQLQTLILPQDVPCPGGSNAWDNVTSFKDKQICQGQRDLCNSTGSPEMCPENGSCASDGPGLLQCVCADGFHGYKCMRQGSFSLLMFFGILGSTTLAISILLWGTQRRKAKAS

Function: Promotes osteoblast cell differentiation and terminal mineralization. Plays a role in inducing the cell cycle arrest via inhibiting CCND1 expression in all-trans-retinoic acid (ATRA) signal pathway (By similarity). In osteoclasts, forms a transporter complex with ATRAID for nitrogen-containing-bisphophonates (N-BPs) required for releasing N-BP molecules that have trafficked to lysosomes through fluid-phase endocytosis into the cytosol . Location Topology: Single-pass membrane protein Sequence Mass (Da): 23858 Sequence Length: 223 Subcellular Location: Nucleus envelope

P23910

MKKVILSLALGTFGLGMAEFGIMGVLTELAHNVGISIPAAGHMISYYALGVVVGAPIIALFSSRYSLKHILLFLVALCVIGNAMFTLSSSYLMLAIGRLVSGFPHGAFFGVGAIVLSKIIKPGKVTAAVAGMVSGMTVANLLGIPLGTYLSQEFSWRYTFLLIAVFNIAVMASVYFWVPDIRDEAKGNLREQFHFLRSPAPWLIFAATMFGNAGVFAWFSYVKPYMMFISGFSETAMTFIMMLVGLGMVLGNMLSGRISGRYSPLRIAAVTDFIIVLALLMLFFCGGMKTTSLIFAFICCAGLFALSAPLQILLLQNAKGGELLGAAGGQIAFNLGSAVGAYCGGMMLTLGLAYNYVALPAALLSFAAMSSLLLYGRYKRQQAADTPVLAKPLG

Function: May be involved in either the transport or processing of arabinose polymers. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 41926 Sequence Length: 394 Subcellular Location: Cell inner membrane

P83572

ANFPTVSLNTVGITRQIPQDFMNAV

Function: Toxic type II ribosome-inactivating protein (RIP). Induces apoptosis. Has cytotoxic activity against several human cancer cell lines. Is less cytotoxic to normal human cells. PTM: Glycosylated. Catalytic Activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA. Sequence Mass (Da): 2734 Sequence Length: 25 EC: 3.2.2.22

Q1JUP5

MQQIHPAGQATLLADTRNTLGEGATWCDRTRALYWVDIEGAQLWRCRADGSDLTPWPMPERLACFALTDDPDVLLVGLATHLAFFDLRSGAFTRIVEVEPELPTRLNDGRCDGSGAFVFGMKDEGAEPPRAVGGFYRLNADLTLERLALPPAAIANSIGFSPDGSKMYFCDSLVREIFVCDYRPGGEVANVRPFARLTDPDGDPDGSIVDRDGGLWNAQWGGRRVVRYGPDGVETDRVAVPTAQPSCTALDGEGRLYVTSARVGLSDDALADDPHAGGVFVAQTRHAGMATARFAGTPRG

Cofactor: Binds 1 divalent metal cation per subunit. Function: Catalyzes the cleavage of L-arabino-gamma-lactone to L-arabonate. Is involved in a degradation pathway of L-arabinose that allows A.brasilense to grow on L-arabinose as a sole carbon source. Can also use D-galactono-1,4-lactone as substrate in vitro; however, the enzyme is probably not involved in the metabolism of D-galactose in vivo. Catalytic Activity: H2O + L-arabinono-1,4-lactone = H(+) + L-arabinonate Sequence Mass (Da): 32300 Sequence Length: 300 EC: 3.1.1.15

P94526

MRIMASHDTPVSPAGILIDLDGTVFRGNELIEGAREAIKTLRRMGKKIVFLSNRGNISRAMCRKKLLGAGIETDVNDIVLSSSVTAAFLKKHYRFSKVWVLGEQGLVDELRLAGVQNASEPKEADWLVISLHETLTYDDLNQAFQAAAGGARIIATNKDRSFPNEDGNAIDVAGMIGAIETSAQAKTELVVGKPSWLMAEAACTAMGLSAHECMIIGDSIESDIAMGKLYGMKSALVLTGSAKQGEQRLYTPDYVLDSIKDVTKLAEEGILI

Function: Catalyzes the dephosphorylation of C5 and C6 carbon sugars in vitro . Catalyzes the dephosphorylation of 3'-AMP and phosphoserine in vitro . Catalytic Activity: sugar phosphate + H2O = sugar + phosphate. Sequence Mass (Da): 29315 Sequence Length: 272 EC: 3.1.3.23

P94528

MKKMTVCFLVLMMLLTLVIAGCSAEKSSGKSGETELTFWTFNGLHEQFYVEMVKEWNKKYPDRKIKLNTVVYPYGQMHDNLSISLIAGEGVPDIADVELARFSNFLKGSDIPLADLTPLIEKDRDKFVEARLTLYSKNGKLYGLDTHVGTTVMFYNMDVMKKAGVNPDDIKTWDDYHKAGQKVRKVTGKPMGTVETNDSATFLSMISQQNSGYFDKNGKLILNNDTNVKTLQYLKDMINDKTMIPAPGGGHHSEEYYGFMNQGGAASVLMPIWYMGRFIDYMPDLKGKIAIRPLPAWKEGGDRSAGLGGTATVVPKQSKHVELAKEFLAFAKGSEEGNKKLWSVLGFDPLRWDVWSSKELKEKNKYTDYFQNGTGIFSVLLDIKDEINPIYLHEDFAKASDLVNRSVLFDALKSQQKTPKQALDRAAGELKQK

Function: Part of the ABC transporter complex AraNPQ involved in the uptake of arabinooligosaccharides. Transports alpha-1,5-arabinooligosaccharides, at least up to four L-arabinosyl units . AraN captures the substrate and delivers it to the two transmembrane components (Probable). Location Topology: Lipid-anchor Sequence Mass (Da): 48674 Sequence Length: 433 Subcellular Location: Cell membrane

Q9KEE7

MGKNILFFSFVGVMVLVLVACGGSSSSSSDADETSVIGDDIEGATELIFWTFAGQHVDLFEDAVVSWNEEFPDRPIKLVAETYPFDQMHNNLLLALQSGSGAPDLADIEVSRFPNFLQGVPQLLPMNDHVEPVIDKFVEARFNLYAKDGEYYGIPTHVGASVMYYNKEIMDEAGVDIESIETWDDYVEAGKQVVERTGKVMTTVPTDDYLPMFQMVSQRGSDFFDENGNLTLDTQENIEVLQFLYDLIYVHEIAELTPGGQPHAEEYYQYMNDGNVASMAMPIWYMGRFLDNMPDLAGKMLIQPLPAWEEGGFRSAGMGGTGTVVTNQTDHEELAKDFLAYAKISEKANEKLWTILGFDPPRWDVWDNPVFQEDNDFYQFFGENIFEVLLDVRDEINSINISQYTPSVANEFSTNIFNDVLRQQTHTPEEALKKAQETIEANMQQ

Function: Part of the ABC transporter complex AraNPQ involved in the uptake of arabinooligosaccharides (By similarity). AraN captures the substrate and delivers it to the two transmembrane components (By similarity). Location Topology: Lipid-anchor Sequence Mass (Da): 50220 Sequence Length: 445 Subcellular Location: Cell membrane

O53092

MTEEKPAKKIGLLALIALVISSSIGSGVFGLTSDLASASAPGPVLIAWVIVGFGILMLALSLNNLLMKEPELEGIFSYAEKGFGPFAGFISGWGYWLSAWLGNVTFATILMSALGYFFPIFKSRQNLPSILVASVLSWSLTYFVNRGVEGAAAINTLVTICKLIPLFVFIIFGIVLFKGHLFTQAFWNNMSSSFVAGDVMSQIKNCMMVMMWVFVGIEGASMLSARAEKKSDAGKATILGLVSLLAIYILASVLPYGYLTQDQLASIKQPAMLYIFEQMVGTWGGYFIGVGLIISILGAWLSWTMLPAETMLLMAKQNLLPAYFGRVNKKKAPTFALVVTAGLIQVFLFTLLFTTKAYNFAYSLCTASIIVCYMLVAAYQIKYSWAHLQEKGNRQQLLIGVLALLFEIAGILMAGVSYLLLCFIAYIPGIYFYGRARKNNGHQHFLSKGEWLITTIIVIGAIIGIWLVVSGKIVI

Function: Catalyzes electroneutral exchange between L-arginine and L-ornithine. Catalytic Activity: L-arginine(out) + L-ornithine(in) = L-arginine(in) + L-ornithine(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 51881 Sequence Length: 475 Subcellular Location: Cell membrane

P18275

MSQESSQKLRLGALTALVVGSMIGGGIFSLPQNMAASADVGAVLIGWAITAVGMLTLAFVFQTLANRKPELDGGVYAYAKAGFGDYMGFSSAWGYWISAWLGNVGYFVLLFSTLGYFFPIFGKGDTVAAIVCASVLLWALHFLVLRGIKEAAFINTVTTVAKVVPLFLFILICLFAFKLDIFTADIWGKSNPDLGSVMNQVRNMMLVTVWVFIGIEGASIFSSRAEKRSDVGKATVIGFITVLLLLVLVNVLSMGVMTQPELAKLQNPSMALVLEHVVGHWGAVLISVGLLISLLGALLSWVLLCAEIMFAAAKDHTMPEFLRRENANQVPANALWLTNICVQVFLVVVFFTSGDPDGMDPYTKMLLLATSMILIPYFWSAAYGLLLTLKGETYENDARERSKDLVIAGIAVAYAVWLLYAGGLKYLLLSALLYAPGAILFAKAKHEVGQPIFTGIEKLIFAAVVIGALVAAYGLYDGFLTL

Function: Catalyzes electroneutral exchange between arginine and ornithine to allow high-efficiency energy conversion in the arginine deiminase pathway . Also mediates the proton motive force-driven uptake of arginine and ornithine, but the exchange is several orders of magnitude faster than the proton motive force-driven transport . Catalytic Activity: L-arginine(out) + L-ornithine(in) = L-arginine(in) + L-ornithine(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 52027 Sequence Length: 482 Subcellular Location: Cell inner membrane

Q9UU82

MIAATPAKSKPSDVNLEQTFKGVSETSKIDLRRSRAAYRPLELSPTPSIFARNYQRNAVDFTGFFVLFWVAVSIMIFMSFLENFELTGRPVVGTIFKYFQSNLLDLAKADLAMSSMFLLAFPFQKIFALGYLRWYGLGVYLYSILILLFLSHCVLRCCLSNWSWTHRAMFILHSMVILMKLHSYNVVNGWYSYCYHSLNKLQSKKTDLDDDERSSVEFYEHCLNHHGNTYPENLTIPNALDFLFMPSLCYQLYYPRTAHVRIHYLIECALGTFGCIFLLVIISDHFMVPVLAKAIRTIIEAPEDASATYFAIRLGHTVAFLMFPFMLSFLLVFWVIFEGVCNFSAEITRFADRNFYDDWWNCWTWDQFARTWNKPVHYFLLRHVYVPLNSFMSKSLSTFFTFFVSSVLHELVMGCITLKIRGYGLFFQMTQIPYIIIQRQKFVRRHRLLGNIAFWFSIIIGIALIAALYILF

Function: Sterol O-acyltransferase that catalyzes the formation of stery esters. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 55157 Sequence Length: 472 Subcellular Location: Endoplasmic reticulum membrane EC: 2.3.1.-

O15033

MFYVIGGITVSVVAFFFTIKFLFELAARVVSFLQNEDRERRGDRTIYDYVRGNYLDPRSCKVSWDWKDPYEVGHSMAFRVHLFYKNGQPFPAHRPVGLRVHISHVELAVEIPVTQEVLQEPNSNVVKVAFTVRKAGRYEITVKLGGLNVAYSPYYKIFQPGMVVPSKTKIVCHFSTLVLTCGQPHTLQIVPRDEYDNPTNNSMSLRDEHNYTLSIHELGPQEEESTGVSFEKSVTSNRQTFQVFLRLTLHSRGCFHACISYQNQPINNGEFDIIVLSEDEKNIVERNVSTSGVSIYFEAYLYNATNCSSTPWHLPPMHMTSSQRRPSTAVDEEDEDSPSECHTPEKVKKPKKVYCYVSPKQFSVKEFYLKIIPWRLYTFRVCPGTKFSYLGPDPVHKLLTLVVDDGIQPPVELSCKERNILAATFIRSLHKNIGGSETFQDKVNFFQRELRQVHMKRPHSKVTLKVSRHALLESSLKATRNFSISDWSKNFEVVFQDEEALDWGGPRREWFELICKALFDTTNQLFTRFSDNNQALVHPNPNRPAHLRLKMYEFAGRLVGKCLYESSLGGAYKQLVRARFTRSFLAQIIGLRMHYKYFETDDPEFYKSKVCFILNNDMSEMELVFAEEKYNKSGQLDKVVELMTGGAQTPVTNANKIFYLNLLAQYRLASQVKEEVEHFLKGLNELVPENLLAIFDENELELLMCGTGDISVSDFKAHAVVVGGSWHFREKVMRWFWTVVSSLTQEELARLLQFTTGSSQLPPGGFAALCPSFQIIAAPTHSTLPTAHTCFNQLCLPTYDSYEEVHRMLQLAISEGCEGFGML

Function: E3 ubiquitin-protein ligase that catalyzes 'Lys-11'- or 'Lys-33'-linked polyubiquitin chains, with some preference for 'Lys-33' linkages . E3 ubiquitin-protein ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates . Ubiquitinates SEPTIN4, DIABLO/SMAC and HTRA2 in vitro . Modulates pulmonary inflammation by targeting SOCS2 for ubiquitination and subsequent degradation by the proteasome . PTM: Autoubiquitinated in vitro in the presence of E2 enzyme UBE2D1/UBCH5A. Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. Sequence Mass (Da): 94223 Sequence Length: 823 Pathway: Protein modification; protein ubiquitination. EC: 2.3.2.26

P0DKH9

MGLSDCLIYRLVVRCFLDYSICAPFYFYHKFMLSASEPVF

Function: Negative regulator of the auxin response. Location Topology: Single-pass membrane protein Sequence Mass (Da): 4747 Sequence Length: 40 Subcellular Location: Cytoplasm

A9B055

MPTTIQAISAEAINLPLTEPFAIASGAQAVAANVLVKVQLADGTLGLGEAAPFPAVSGETQTGTSAAIERLQSHLLGADVRGWRKLAAMLDHAEHEAAAARCGLEMAMLDALTRHYHMPLHVFFGGVSKQLETDMTITAGDEVHAAASAKAILARGIKSIKVKTAGVDVAYDLARLRAIHQAAPTAPLIVDGNCGYDVERALAFCAACKAESIPMVLFEQPLPREDWAGMAQVTAQSGFAVAADESARSAHDVLRIAREGTASVINIKLMKAGVAEGLKMIAIAQAAGLGLMIGGMVESILAMSFSANLAAGNGGFDFIDLDTPLFIAEHPFIGGFAQTGGTLQLADVAGHGVNLA

Cofactor: Binds 1 Mg(2+) ion per subunit. Function: Has epimerase activity with a variety of hydrophobic dipeptides (in vitro). Enzyme activity is highest with L-Phe-L-Tyr, but is still relatively low, suggesting that L-Phe-L-Tyr is not the physiological substrate. Sequence Mass (Da): 36784 Sequence Length: 356 EC: 5.1.1.-

B5BLW5

MPLDPEVRNFLQVYYKANIIDFTKYQFQEIRQKVNELLAKAVPKDPVGETRDMKIKLEDYELPIRIYSPIKRTNNGLVMHFHGGAWILGSIETEDAISRILSNSCECTVISVDYRLAPEYKFPTAVYDCFNAIVWARDNAGELGIDKDKIATFGISAGGNLVAATSLLARDNKLKLTAQVPVVPFVYLDLASKSMNRYRKGYFLDINLPVDYGVKMYIRDEKDLYNPLFSPLIAEDLSNLPQAIVVTAEYDPLRDQGEAYAYRLMESGVPTLSFRVNGNVHAFLGSPRTSRQVTVMIGALLKDIFK

Function: Has a broad substrate specificity. Hydrolyzes various p-nitrophenyl phosphates, aromatic esters and p-nitrophenyl fatty acids in vitro. Most active against paraoxon, phenyl acetate and p-nitrophenyl caproate (C6), respectively. Has also tributyrinase activity, but shows no hydrolytic activity toward other triacylglycerols including tricaprylin, trimyristin, tripalmitin or triolein in vitro. Catalytic Activity: a phenyl acetate + H2O = a phenol + acetate + H(+) Sequence Mass (Da): 34552 Sequence Length: 306 EC: 3.1.1.2

Q94231

MGLFFSKISSFMFPNIECRTLMLGLDGAGKTTILYKLKLNETVNTIPTIGFNVETVTFQKITLTVWDVGGQKKIRALWKYYFPNTTTLVFVVDSSDIERIPEAKEELFSLLAEPELADSHLLVFANKQDMPNARSPAELTQLLDLGSLKNREWFICGTNAHSGQGLYEGLMWVKKQMKT

Function: Small GTPase involved in protein trafficking between different compartments (By similarity). Modulates vesicle budding and uncoating within the Golgi complex (By similarity). In its GTP-bound form, triggers the recruitment of coatomer proteins to the Golgi membrane (By similarity). The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles (By similarity). Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate Location Topology: Lipid-anchor Sequence Mass (Da): 20247 Sequence Length: 179 Subcellular Location: Golgi apparatus membrane EC: 3.6.5.2

P36397

MGLSFGKLFSRLFAKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRDRVVEARDELHRMLNEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRQRHWYIQSTCATSGEGLYEGLDWLSNNIASKA

Function: GTP-binding protein involved in protein trafficking; required for the sequence-specific vacuolar sorting route to the lytic vacuole, for the ER-to-Golgi transport and for the Golgi-derived transport to the plasma membrane . Involved in the recruitment of COPI and GDAP1 to membranes. Required for recycling of PIN auxin transporters (e.g. PIN1 and PIN2) in a fungal toxin brefeldin A (BFA)-dependent manner. Involved in various auxin-dependent developmental processes . Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate Sequence Mass (Da): 20609 Sequence Length: 181 Subcellular Location: Golgi apparatus EC: 3.6.5.2

P51822

MGLSFTKLFSRLFAKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRDRVVEARDELHRMLNEDELRDAVLLVFANKQDLPNAMNAAEIIDKLGLHSLRQRHWYIQSTCATSGEGLYEGLDWLSNNIASKS

Function: GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate Sequence Mass (Da): 20681 Sequence Length: 181 Subcellular Location: Golgi apparatus EC: 3.6.5.2

O00909

MGLAFGKLFSRFFGKKDMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEFKNINFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERIQEACDELTKMLNEDELRDAVLLVFCNKQDLPNAMSVAEVTDKLNLHSLRSRKWYIQSTCATSGDGLYEGLDWLSNTLTSSSK

Function: GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate Sequence Mass (Da): 20682 Sequence Length: 182 Subcellular Location: Golgi apparatus EC: 3.6.5.2

P61209

MGNVFANLFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERIGEAREELMRMLAEDELRDAVLLIFANKQDLPNAMNAAEITDKLGLHSLRNRNWYIQATCATSGDGLYEGLDWLSNQLKNANR

Function: Small GTPase involved in protein trafficking between different compartments. Modulates vesicle budding and uncoating within the Golgi complex. In its GTP-bound form, triggers the recruitment of coatomer proteins to the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles (By similarity). Has a role in eye development . Required for cleavage furrow ingression in embryonic cells . Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate Location Topology: Lipid-anchor Sequence Mass (Da): 20688 Sequence Length: 182 Subcellular Location: Golgi apparatus membrane EC: 3.6.5.2

P84077

MGNIFANLFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLRNQK

Function: Small GTPase involved in protein trafficking between different compartments . Modulates vesicle budding and uncoating within the Golgi complex . In its GTP-bound form, triggers the recruitment of coatomer proteins to the Golgi membrane . The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles . The GTP-bound form interacts with PICK1 to limit PICK1-mediated inhibition of Arp2/3 complex activity; the function is linked to AMPA receptor (AMPAR) trafficking, regulation of synaptic plasticity of excitatory synapses and spine shrinkage during long-term depression (LTD) (By similarity). PTM: (Microbial infection) Demyristoylated by S.flexneri cysteine protease IpaJ which cleaves the peptide bond between N-myristoylated Gly-2 and Asn-3. Location Topology: Lipid-anchor Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate Sequence Mass (Da): 20697 Sequence Length: 181 Subcellular Location: Golgi apparatus membrane EC: 3.6.5.2

Q6FDQ8

MPHQHKGIDKAKILTEALPYIQRFSGKTLVVKYGGNAMTDPELESSFARDIVLLKTVGLNPIVVHGGGPQVDSLLKRLGQVSDRIDGMRVTDEATMEVVEMVLGGSVNKSIVNLINQHGGRAIGLTGKDGNLIRARKLLMEKHDEQGDIKHIDLGLVGEVVGIKTDVLEMFTQSDFIPVIAPLGVDESGNTYNINADLVAGKVAEALGAEKLILLTNISGVLDENKNLLTGLSTQEVDRLIATGVIYGGMIPKVGCALDAVKGGVVSAHIVDGRVPHATLLEIFTDHGVGTLITNRLHAKSEH

Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate Sequence Mass (Da): 32305 Sequence Length: 303 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. Subcellular Location: Cytoplasm EC: 2.7.2.8

Q5HB82

MKLRNVSKNNLNKEDTKLSIEQFGGNVEWFNITKTLSESLPYIQQFSGETFIIKYGGAAMTDKKLAESFAHDVVLLKQLGINPIVVHGGGNKINEFLEKINKKSTFINGLRITDAETLEIVEMVLCGLVNKNITQLINNAGGNAIGLCGKDANLIEAKKICYTYKENQSNNVEKILDMGFVGEPHDINTDLLFFMEESDFIPVIAPVCSGENNLTYNVNADLVAGALANAMAAAKLIILTNVSGVTDSNGNLISELSVSHAENLIDNGTAHTGMIPKLQTCVRVVKEGYGSAHIIDGRIPHVLLLELFTIHGTGTMVVNSGV

Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate Sequence Mass (Da): 34878 Sequence Length: 322 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. Subcellular Location: Cytoplasm EC: 2.7.2.8

B1H0L5

MSELTVVKFGGSLTENPQAQNKFLEELTLISKRQNIILVHGGGPEINALLEKFAITSRFVNGLRFTDADTLGVVELALSGKVNRVLTTGLIKNGANAVGISGKDGKSVICRQVEYLGFVGEPVKVNRKLIDILIKSRFLPVIASIAADVEGNIMNVNADTLAASIAVAFKAQKLIFLTDVAGVFDKNNNIIKEIKIKEINSLIEDKTITGGMIPKIKGCAESVKKGLKEVWIAEGISGIQKIKGTVIKK

Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate Sequence Mass (Da): 26755 Sequence Length: 249 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. Subcellular Location: Cytoplasm EC: 2.7.2.8

Q0RFA8

MTDTAPTDITTATDITTATGAATGTGRGPAATARGHAALAKTQVLIEALPWLSRFQGATIVIKYGGNAMTEPALRAAFAADIVFLRYSGLRVVVVHGGGPQITAHLARLGVESTFVGGLRVTTPETMDVVRMVLLGQVNRDVVGLVNDHGPFAVGLSGEDANLFTARRRPAIVDGQEVDVGLVGDIVEVRAETVDALLDSGKVPVVASVARGIDGGVYNVNADTAAAELAVALGATKLVVLTDVEGLYADWPTSDEVLSELSITELEQLLPTLAAGMIPKMEACRRAVRGGVPQAHVLDGRVPHAVLLEIFTDDGIGTLITPDRDTANRVAPAAPTAYSGGRP

Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate Sequence Mass (Da): 35508 Sequence Length: 343 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. Subcellular Location: Cytoplasm EC: 2.7.2.8

Q2J862

MNAPTRTPPPSNGGHGSTGSTGSTGDAAPGGGTGRGPAATARGHAALAKTQVLIEALPWLSRFQGATIVVKYGGNAMTEPALREAFAADVVFLRHSGLRVVVVHGGGPQITAHLERLGVPSTFVGGLRVTTPQTMDVVRMVLLGQVNRDVVGLVNDHGPFAVGLSGEDANLFTARRRPAIVDGREVDVGLVGDIVEVRPETINALLGSGKVPVVASVARGVDGGVYNVNADTAAAELAVALGATKLVVLTDVEGLYADWPASDEVISELSITELEQLLPSLTAGMIPKMEACRRAVRGGVPQAHVLDGRVPHAVLLEIFTDDGIGTLIMAESGTSPEPGTPPAPAARPAGIVPAGEPTGGTP

Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate Sequence Mass (Da): 36857 Sequence Length: 362 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. Subcellular Location: Cytoplasm EC: 2.7.2.8

Q07905

MGKTVVIKCGGSVLDELSPAFFASVNAMRKQGMEVVIVHGGGPEIGQMLKTLRVPSEFVNGLRKTTKDVLAVVEMVLSGKVNKQLASMLRQHGLPAVGVSGVDGGLLEAEPIDLAKLGYVGRVKTVRSQLLRTLLAAGYIPVISPLGIDQNGQTYNINADTAAGAVAAAIGASQLAFVTNVPGILRDGALVAEATAEMIERLIEDGVITGGMIPKVQAALSALSDALPEVMIVSGKTTFYQNGTWHGTTIRKEVGVYL

Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate Sequence Mass (Da): 26935 Sequence Length: 258 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. Subcellular Location: Cytoplasm EC: 2.7.2.8

A4IL48

MENTVVIKCGGSVLDELSPAFFASVKTMREQGMNVVIVHGGGPEIGKMLKQLNVRSEFVNGLRKTTKEVLAVVEMVLSGKVNKQLVTMFKQHGLPAVGISGVDGGLLEAEPIDGIKLGYVGRVTAVRVDLLQTLLAANYIPVISPLGVGRSGQTYNINADTAAGAIAAAIGANQLAFVTNVPGLLQDGTLIGEATAETVEQLLKDGVITGGMIPKVKAALSALSDALPKVMIVSGKTPFYEQGTWHGTTIRKEVGAYL

Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate Sequence Mass (Da): 26981 Sequence Length: 258 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. Subcellular Location: Cytoplasm EC: 2.7.2.8

B0TL87

MANTRAISSGAKPVMVLKVGGALLQCEMGMARLMEAAAKIIANGQPIIMVHGGGCLVDEQLKANGMTTKKLDGLRVTPQEQIPVIVGALAGTSNKTLQAAAIKAGVTSLGMSLADAGMMSAKVKDPQLGLVGEVEPKDASYLEFVLSKGWMPIVSSIAISEQGEMLNVNADQAATALAKLVSGSLVLLSDVSGVLDGKGQLISSLNRAQVNELTKIGVIEKGMKVKVEAALDVAESMGQAVQIASWRHAQQLIALSRGETVGTQIQPQIQ

Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate Sequence Mass (Da): 27994 Sequence Length: 270 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. Subcellular Location: Cytoplasm EC: 2.7.2.8

A7GSF4

MKVAIIGATGYGGIELIRLLQQHPYFSIVSIHSFSQVGEHITSSYPHLRRFLVYTLQEIDVESIKKEADLVFLATPAGVSVKLTPLLLKAGLKVIDLSGDFRMVNPSIYEMWYKKPAASEEFLQQAVYGLSEWKRDEIQQAKLVANPGCFATATLLAIAPLMRNKIIEENSIIIDAKSGVSGAGKTPTHAAHFPELYDNLHIYKVNEHQHIPEIEQMLIGWNEQAKPITFSTHLIPVSRGIMVTLYAKIRKYVQIEELHNLYTNIYKNAYFVRIRPYGEFPSIKEVRGSNYCDIGIGYDERTKRITVVAVIDNMMKGAAGQAVQNANLVARLDEKTGLQYIPIYP

Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH Sequence Mass (Da): 38838 Sequence Length: 345 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4. Subcellular Location: Cytoplasm EC: 1.2.1.38

Q8A1A7

MIKAGIIGGAGYTAGELIRLLLNHPETEIVFINSSSNAGNRITDVHEGLYGETDLRFTDQLPLDAIDVLFFCTAHGDTKKFMESHNVPEDLKIIDLSMDYRIKSDDHDFIYGLPELNRRATCTAKHVANPGCFATCIQLGLLPLAKNLMLTGDVSVNAITGSTGAGVKPGATSHFSWRNNNISIYKAFDHQHVPEIKQSLKQLQNSFDSEIDFIPYRGDFPRGIFATLVVKTKVALEEIVRMYEEYYAKDSFVHIVDKNIDLKQVVNTNKCLIHLEKHGDKLLIISCIDNLLKGASGQAVHNMNLMFNLEETVGLRLKPSAF

Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH Sequence Mass (Da): 35838 Sequence Length: 322 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4. Subcellular Location: Cytoplasm EC: 1.2.1.38

P59305

MAKYTVAVAGATGYAGGEALRILAAHPDFDITCVAGHSSVGESMAKHMPHIPQLANLVVEDTAPEVLNGHDVIILALPHGASGKLASQLDPNAVVVDLGADHRLEEQAAWDEFYGGDFYEHWTYGMPELITGKAADGSYTRQRAALPGTKRIAGPGCNVTATTLALQPGIAEGLVESQDIVADLVVGYSGAGKNLKRTNLLAAEALQSALPYSVGGKHRHIPEILQNFAHAAGKSAAEASEFTLGFTPILAPMSRGILATVSARMTDKAKTLSDEEIRAVWSKAYEGQDFMVLLPEGTLPATGNIIGSNAAHLQVVTDRKAGRIYAFAAIDNLNRGTAGQAVQSLNIALGLPEDAGLTKIGVAP

Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH Sequence Mass (Da): 38017 Sequence Length: 364 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4. Subcellular Location: Cytoplasm EC: 1.2.1.38

C0QYU7

MIKVSVIGATGYAGAELIRLLLSHSKVELKNLSSKSFVGKNINEIYPNLNKNLDKLLLDENEIFEDTDVVFASLPAGLSDDIANKCFEKNILFIDLGADFRLDNEEDYKNWYGNEYKYKNLHKEAIYSIPEIIKYDNVYNKKELKNAKIIGNPGCYPTSIGLALAPALVNKFIIKDDIIIDSKSGATGAGRELKLNTHYTECNEAFAPYKIAEHRHTPEIEQTLSNIYGEDIKVTFVPHLLPLNRGIVSTIYAKLENKNIKLKDIHNTYKNFYKDSAFVRVLNIGEIANLKYVKYSNYCDISLHMDDRTNKLIIVSTIDNMVKGAAGQAIQNMNIALGLKEDEGLNFIPPAF

Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH Sequence Mass (Da): 39651 Sequence Length: 352 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4. Subcellular Location: Cytoplasm EC: 1.2.1.38

Q92QR7

MKPKIFIDGEHGTTGLQIRVRMAGRTDLELLSIPEAERRNAAMREDLLNSADIAILCLPDDASREAVAMVAGNNRVRIIDTSTAHRVAPDWAYGFAEMDKAQPQRIRDARHVANPGCYPTGAIALIRPLRQAGILPDGYPVTVNAVSGYTGGGKQMIAQMEDDQNPDHIGAPHFLYGLTLKHKHVPEMKMHGLLERAPVFSPSVGKFAQGMIVQVPLYLEDLAAGATLETIHRALVDHYAGQSIVEVVPLDESAKLARIDATELAGSDAMKLFVFGTKGGAHVNLVALLDNLGKGASGAAVQNMDLMLSA

Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH Sequence Mass (Da): 33298 Sequence Length: 310 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4. Subcellular Location: Cytoplasm EC: 1.2.1.38

Q7UVL4

MSSSNLRVALVGSTGYTALEVARLLLTHPGADLVVATSRQDEGKPLSEIHPMLAGRCDVTLQPLDADVIAKSADVAMCCLPHGASAESVKQLAEAGMRVIDFSADFRLSSLETYQHWYGVKHPWPERIGDVVYGMPEFFADEIRSADIVANPGCYPTSAIMPLAPLVKAGLIETDDIIVDSKSGVSGAGRSPKLGTLYCETNESISAYAVGTHRHAPEIADLVERIAGAPIEVMFTPHLTPMDRGILSTIYVKPVGKAGSVEDAVRAMMSLLRDTYSDQPCVHVVDHLPATKYVAGTNHVQISVRPSGKRAVIVCAIDNLTKGASGAAVQNMNVMFGLPETAGLLM

Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH Sequence Mass (Da): 36822 Sequence Length: 346 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4. Subcellular Location: Cytoplasm EC: 1.2.1.38

Q9LA02

MTQKIAILGASGYTGAELARIIATHPEMEITALSGDRKAGMRMGEVFPHLRHIGLPDLVKIEEIDFSGIDLAFCALPHATSQAVIAELPRDLKVVDLSADFRLRDAAEYEKWYGKPHAAMDLQAEAVYGLTEFYREELKTARLCAGTGCNAAAGQYAIRPLIEAGVIDLDEIVIDLKAGVSGAGRSLKENLLHAELAGGTMPYSAGGKHRHLGEFDQEFSKVAGRPVRVQFTPHLMPFNRGILATVYVRGTPEDIHAALASRYENEVFLEVLPFGQLASTRSVAGSNFVHLGVIGDRLPGRAVVTVALDNLTKGSSGQAIQNANLMLGLPETLGLMLAPVFP

Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH Sequence Mass (Da): 36780 Sequence Length: 342 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4. Subcellular Location: Cytoplasm EC: 1.2.1.38

Q2RRM4

MSERVNVAILGASGYTGAELVRLLARHPRVTLAALTANRKAGQAFASVFPHLGGLDLPVLSTIEAVDWSAIDFVFCALPHGTTQTIIGDLLNGPHGGRLRIADLSADFRLADPMVYQTWYGHAHEAVELQKEAVYGLTEINRAAIATARLVAVPGCYPTSAQLPLIPLLRAGLIDPDAIIIDAKSGASGAGRDAKEGSLHCEVSEGIHAYGVGTHRHGPEIEQGLSLAVGRPVAVTFTPHLMPMNRGILSTIYLRATAGNDATTLRQALSAAYADEAFVRVVPEGVSPHTRHVRGSNFVLIGVHADRVPGRVIVTCVEDNLVKGASGQAIQDMNVMLGFPETLGLDQQPLFP

Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH Sequence Mass (Da): 37298 Sequence Length: 352 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4. Subcellular Location: Cytoplasm EC: 1.2.1.38

Q1AS32

MGLSVGIYGGSGYVGVELVRLLAGHPEVGSLAVASRGHAGRRIGEVYPQVAVGGEYLDPSEVDVSSLDVAFVAYGHGESAEAVRGLLEGGVRLVVDLSADFRLPDVRVYEEWYGEHPAPELLGEAHYGLPEVFGALEGRLVANPGCYPTAAILALAPVVRRMGGEVRSVTINALSGVSGAGAKPSARTHFVSVNESVSPYGVSGGEPRHRHTPEIEIMLRRLGEAPPVTFVPHLLPISRGELETITVEAGELPGAEEVLGWYREDYGGWRFVEAREEVPHISHVANTNRARLSAAVDRRAGKLLLFAAVDNLLKGAAGEAVQNMNLALGYPEDLGLEHLR

Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH Sequence Mass (Da): 36171 Sequence Length: 340 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4. Subcellular Location: Cytoplasm EC: 1.2.1.38

P54638

MTKPVASYELDEKRFLTLLGKLIGETENLQNRPPALIPIEDNAGRHVIEALTPYLKANGGVLELEQVHCDPVNYPKRGNIIIEYPGTSKGTSSPKTISFVGSHLDVVPADKTAWDRNPFQLIIEGDKLYGRGTTDCLGHVALLTDLFIQLATEKPALKHSIFAVFIVSEENDEIPGIGVDALDHSGKMNPCKNGPVYWVDSADSQPTIGTGGAQTWNLTAHGKNMHSAMPYRTVNSVELVNEALAEIQRRFYIDFKPHPKEAEYKFDCSSTMKPTLWKPIAGSYNTIPGESTICGDIRLTPFYDMKEMRAKVEGYIKDINANITELRNRGPYSKYDVPASEGVEPVKGSVSIEWLGEASAGVACKLDSDGYKALGKATSEILGSLTPVATCGTLPLVRDLQDSGFDIQITGFGKEETYHADNEYALLSDFKNAIKILSRTIDLLEKN

Cofactor: Binds 2 Zn(2+) or Co(2+) ions per subunit. Catalytic Activity: H2O + N(2)-acetyl-L-ornithine = acetate + L-ornithine Sequence Mass (Da): 49070 Sequence Length: 447 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine from N(2)-acetyl-L-ornithine (linear): step 1/1. EC: 3.5.1.16

Q8Y6U2

MELIKGNIASPKGFYADGKHAGLKRKRNDIGWIYSEVPANAAAVYTMNQMQAAPIFVTKDSFQSNAKLQAIIVNSGNANACTGNQGMLDALAMRAQTAEKLEIPLDSVAVASTGIIGDMLPMDKINAGIEMLEKQTGNAADFEEAILTTDTFQKQISFQTEIGGRKVTMSGVAKGSGMIHPNMATMLAFITTDAAIPAELLQKLLKIKVDKTFNQITVDGDTSTNDMVVVMANGCAENPMLQEGTADFAKFADMFQAVTEHLAKSIARDGEGATKLIEVQVNGATKTEDARMIAKKIVSSSLVKTAAFGGDGNWGRIICAIGYSGGRFAPDNITIKIGGIEILNHSSQTIYNQQALDAYLEEEHIIIEVDLHIGLESGTAWGCDLSYEYVKINACYRT

Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate. Catalytic Activity: L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate Sequence Mass (Da): 42737 Sequence Length: 398 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1. Subcellular Location: Cytoplasm

C0PF72

MSPPSVLLLHSRIPLQPRPFRMNSRAAPSRVVVCSVASTEGFISAAPILLPDGPWKQVEGGVTAAKGFKAAGIYSGLRAKGEKPDLALVACDVDATVAGAFTTNVVAAAPVLYCKHVLSTSKTGRAVLINAGQANAATGDLGYQDAVDSADAVAKLLNVSTDNILIQSTGVIGQRIKKEALLNSLPRLVGSLSSSVQGANSAAVAITTTDLVSKSIAVQTEIGGVAIRIGGMAKGSGMIHPNMATMLGVLTTDAQVSSDVWREMIRMSVSRSFNQITVDGDTSTNDCVIAMASGLSGLSGIQSLDSIEAQQFQACLDAVMQSLAKSIAWDGEGATCLIEVTVSGANNEAEAAKIARSVASSSLVKAAIFGRDPNWGRIACSVGYSGIQFDANRLDISLGVIPLMKNGQPLPFDRLTASKYLKDAGDAHGTVNIDISVGSGGGNGKAWGCDLSYKYVEINAEYTT

Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate. Catalytic Activity: L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate Sequence Mass (Da): 47952 Sequence Length: 464 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1. Subcellular Location: Plastid

A8Q9M0

MWYRTFRTLGYTICRPYATCATKAERFVKTIDPSTLPRGYLVSSTYAGIKNAIRPVTSTNEPSAATTNVPHPQEAPKPDVALIVSSVPAAIAGTFTTNVFKAAPVVHATTALKAAGPNARVRAILTNSGCANAVTGQQGLEDTQTLVNRVQALLSPRNQNAIPTYEQDARSSSTDVLMMSTGVIGVRLPVAHIQRCLEHLAAPSILQSHPDAWLEAARAYMTTDTFPKIRTRQFILGNRRCSIVGIDKGAGMIHPRMTRSGGQLHATLLGVFATDAPISSATLQRCLDEAVRVSFNCISVDGDMSTNDTILALANGQAPFVDLDCTDTPNEWTETEHPDMVNKFAEELKSLCIEMSHLIVRDGEGAEKFVQVHVRNAGTYEQAHAIASSISTSALVKCAMHGEDANWGRILCSAGYASLPASTPAWTLDPSKVNVTFLPPPHQPDDLAPLPTLVNGVPQAVNETQAKKLLSYEDIYVDVDLQGGSWGSQGRSEATYWTCDFSKEYITVRW

Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate. PTM: The alpha and beta chains are autoproteolytically processed from a single precursor protein within the mitochondrion. Catalytic Activity: L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate Sequence Mass (Da): 55171 Sequence Length: 510 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1. Subcellular Location: Mitochondrion matrix

Q8TK55

MKKIEGGICAVKGVTANGIKLGKMGITVIRAEGPAAGVFTKNKVTAAPVVLSKGVIETQHQLSAIIANSGNANAFTGDDGFLDAMEMASALSESLDLEPDTVAVASTGVIGRRLDVSWIREHLPEVLEGLGSSPECSLAAAKAIMTTDKALKEVAVELDCGVRIGAIAKGSGMIEPNMGTMLCFAYTDALVPADVLDAALRIAVDKTFNMVVVDGDTSTNDMVLFTSTCKSGIKPCMECLDEFEDALIYLFTDLAKKMARDGEGATKLIEARVTGAKTYEDARLAVKAIVRSPLVKSAIFGKDPNWGRVVAAAGYSGAELEQERLSLSFSAGGETVELVKSGEISRVSDLALLNKIMANEEIIITLDFGMGKESATAWGCDLTYDYVRINAEYTT

Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate. Catalytic Activity: L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate Sequence Mass (Da): 41700 Sequence Length: 395 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1. Subcellular Location: Cytoplasm

Q607S6

MAASPEDRNLSDIRLCPIAGIRLGTAAAAIKHVGRDDVLLIEMAEGSACAAVFTQNAFCAAPVTVAREHLRQAPRWLLVNSGNANAGTGTRGLADARASCEAVAALVGGRADRVMPFSTGVIGEYLPLDKIRAALPKAFEALSEDGWEAAARAIMTTDTRPKKAVRRIEIAGRPVVVSGIAKGAGMIHPNMATMLAFVATDARIGAGLLQSVLERAVNRSFNCITVDGDTSTNDACVLMASQRSEAPLIEPGSAHVEAFQSAVDAVLAELAEAIVRDGEGATKFIRILVEEAASEDEARLVGKTIAHSPLVKTAFFASDPNWGRILAAVGRAGCKDLDISRVAIWLDEVRIVAAGARDREYTEARGITVMRRPEITVRVSLGRGQASARVMTCDLSLDYVRINAEYRT

Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate. Catalytic Activity: L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate Sequence Mass (Da): 43287 Sequence Length: 408 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1. Subcellular Location: Cytoplasm

Q57645

MRVIDGGVTAPKGFKANGYKEGKFGVAIIISEKDAVGAGTFTTNKVVAHPVVLSRELIKNRDKFRAIVANSGNANCFTKDGMEDAKEMQRLVAELFNINEDEVLVASTGVIGRKMDMNIIKDRINKVYNLIKEGNSSINAAKAIMTTDTKPKEIAVEFEVNGKTVRVGGIAKGAGMIAPNMLHATMLCFITTDIEIDKESLTNILQKVVDKTFNNISVDGDTSTNDTVFVLANGLSGVNYEECGEEFENALLYVCRELAKMIVKDGEGATKFMEVVVKGAKTEEDAVKASKAIVNSLLVKTAVFGGDPNWGRIVAAVGYSGADFNPEVVDVILSNYKDEVYLVKDGIPLADEGTEELKKAEEIMKSDEIKIVVDLKMGEFENVCYGCDLSYEYVRINAEYTT

Function: Catalyzes only the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor. Catalytic Activity: L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate Sequence Mass (Da): 43757 Sequence Length: 402 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1. Subcellular Location: Cytoplasm EC: 2.3.1.35

Q8TX15

MRAPEGFLLGGIKREGIGVGLIFSERRCAVAGTFTENTLRAAPVEHSEEVCDRGVARGVIVNSGHANAMTGEEGYQDVLRTAEAIAELMGAPEDEIVVCSTGVIGERPPVDKIVRYAREVWEDIGPTERHVREFSRAIMTTDTEEKIALYEGDGWSLLGIAKGAGMIHPNMSTMLAFLLTDVGAKPKELQMWLRDVVNDTFNMITVDGDESTNDSVVLLANGSSNLKVGSDVTITEFQRALEEVCTELAEKIVRDGEGATKLMIVCVHGASNEVEARRAARAIASSNLVKAALFGENPNWGRIGAAVGAARVDVDPDELRIAFRSSEGEIVTYEGGPVDFDEEKAKRVLSASEVEIVVDLGVGDASARAWGCDLTYEYVRINAEYRT

Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate. Catalytic Activity: L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate Sequence Mass (Da): 41840 Sequence Length: 387 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1. Subcellular Location: Cytoplasm

Q8PZL8

MKQIEGGICAVRGVSAYGIKPGKMGIAVIRAEGPAAGVFTRNKVVAAPVTLSRERIETEHRLSAVIANSGNANAFTGDDGFLDAMEMASMVAENLGLDPDNVAVASTGVIGRRLDVSFIKEHLPEVLEGLGSSPECSRAAAKAIMTTDRALKESAVELDCGVRIGAIAKGSGMIEPNMGTMLCFAYTDAKVPADVLDAALKIAVDKTFNMVVVDGDTSTNDMVLFTSTCKSGVKPCLDCLDDFEEGLVCVFTDLAKKMAKDGEGATKLIEARVTGAKKYEDARLVAKTIVRSPLVKSAIFGKDPNWGRVVAAAGYSGAELEQERLTLSFSGGGEEVELVKAGEISTASDLSLLKKIMANDEIIINLDLAMGEESATAWGCDLTYDYVRINAEYTT

Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate. Catalytic Activity: L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate Sequence Mass (Da): 41714 Sequence Length: 395 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1. Subcellular Location: Cytoplasm

O26284

MYTMELRFIRGGVCAVDGVLAAGCREGKYGVGLIINRGSTAAAVFTSNRVRAEPVKLTERVIADGSISAIVANSGNANCFTGREGMDDARRMARKVAESLSMDESEVAVASTGVIGRRMPIDKIEFLIQSAAAQLENSEAASGALAEAIMTTDTFPKEVAVEFELETGEKARIGAVAKGSGMIAPNMATMLSFITTDVDASSSELTEALRVAVDESFNMLIVDGDESTNDMVIISSTRTSGRIDSNFREALVAVCRELARMMARDGEGVTKSFQVDVVNAGTHEDAKMAARAIAGSSLVKTAIFGADPNWGRIVAAAGYSGAEFDPEEISVTLESDSESVVIVDHGDILAFEGTEELETAERVMTSKEIRIIVDLAAGDESATAYGCDLTYDYVRINAEYTT

Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate. Catalytic Activity: L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate Sequence Mass (Da): 42650 Sequence Length: 402 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1. Subcellular Location: Cytoplasm

Q6D9D2

MRNSTKQEDLVKAFKALLKEEKFSSQSEIVHALQDEGFENINQSKVSRMLTKFGAVRTRNAKMEMVYCLPAELGVPTTSSPLKNLVLDVDYNDAVVVIHTSPGAAQLIARLLDSLGKSEGILGTIAGDDTIFTTPARGFSVKQLYEAILVLFEQEL

Function: Regulates arginine biosynthesis genes. Sequence Mass (Da): 17162 Sequence Length: 156 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation]. Subcellular Location: Cytoplasm

A6KXY8

MKSKNSRLDAIKIIISSKEVGSQEELLQELAKEGFRLTQATLSRDLKQLKVAKAASMNGNYVYVLPNNTMYKRMTEQHSASEMLMHNGFISIEFSANLAVIKTRPGYASSLAYDIDNRNFDEILGTIAGDDTIMLVIREGCTRAGVKNALSLIIPNIQ

Function: Regulates arginine biosynthesis genes. Sequence Mass (Da): 17528 Sequence Length: 158 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation]. Subcellular Location: Cytoplasm

A9WQ89

MSAESAAIVQPIALIPATKTARQARIAALLTAQSVRSQAELAALLADDGVQVTQATLSRDLVELGAVRVRADGGLVYAVPQAGVDRTPHAAVSKEYLDARMTRLCAELLVTAEASANLVVLRTPPGAANFLAMAIDHSVLPDILGTIAGDDTVLVIARDPFGGAAIAERFLQFAEEPGT

Function: Regulates arginine biosynthesis genes. Sequence Mass (Da): 18566 Sequence Length: 179 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation]. Subcellular Location: Cytoplasm

Q5FWH6

MSAQSLPAATPPTLKPPRIIRPRPPSRHRAPHSPGPLHNGSSPKALPQISNDASASVCTSIFWEPPTASLKPPALLPPSVSRTSLDSQTSPDSPSSTPSPSPVSRRSISPEPAPCSPVPPPKPSGSSRTPLPSGPTPLQDGSASAPGTVRRLAGKFEWGAEGKAQSSDSLERCSQGSTEVNGEKETPEAALSGNGSQENGTPDAALACPPCCPCVCHVAKPGLELRWVPVGSSEDILRIPCRASPLRASRSRINPPVISHPPVVLTSYRSTAERKLLPPLKPPKPTKVRQDISTSEELPQPDLKLPSEDGIQTATKAWEGDRPEGAPLNAPPVALEGREEEGLDGLKGLQWELPLQDEPLYQTYRAAVLSEELWGVGEDGGPSPANPGEAPTFSRLPGPRNTLWQELPAVRGSGLLESLSPQERRMQESLFEVVTSEASYLRSLRLLTDTFVLSQALRDTLTPRDHHTLFSNVQRVQSVSERFLGTLLSRVRSSPHITDLCDVVHAHAVGPFFVYVDYVRNQQYQEETYSRLMDTNVRFSAELRRLQSLPKCERLPLPSFLLLPFQRITRLRMLLQNILSQTEEGSSRQENAQKALGAVSKIIERCSAEVGRMKQTEELIRLTQRLRFHKVKALPLVSWSRRLELQGELTELGCRRGGVLFTSRPRFTPLCLLLFSDLLLITQPKSGQRLQVLDYAHRSLVQAQQVPDPSGPPTFRLSLLSNHQGRPTHRLLQAASLSDMQRWLGAFPTPGPLPCSPDTIYEDCECSQELCSEPSTPSKTEGQSLESKAPRKHLHKNPEGWLKGLPGAFPAQLVCEVTGEHERRKHLRQHQKLLEAVGPSSGTPDTPQP

Function: Specific GEF for RhoA activation. Does not activate RAC1 or CDC42. Regulates vascular smooth muscle contractility. Negatively regulates excitatory synapse development by suppressing the synapse-promoting activity of EPHB2. PTM: Phosphorylated on tyrosine residues upon EFNA1 stimulation. EPHB2-dependent phosphorylation at Tyr-361 triggers UBE3A-mediated ubiquitination. Sequence Mass (Da): 92946 Sequence Length: 849 Subcellular Location: Cell projection

Q5VV41

MAQRHSDSSLEEKLLGHRFHSELRLDAGGNPASGLPMVRGSPRVRDDAAFQPQVPAPPQPRPPGHEEPWPIVLSTESPAALKLGTQQLIPKSLAVASKAKTPARHQSFGAAVLSREAARRDPKLLPAPSFSLDDMDVDKDPGGMLRRNLRNQSYRAAMKGLGKPGGQGDAIQLSPKLQALAEEPSQPHTRSPAKNKKTLGRKRGHKGSFKDDPQLYQEIQERGLNTSQESDDDILDESSSPEGTQKVDATIVVKSYRPAQVTWSQLPEVVELGILDQLSTEERKRQEAMFEILTSEFSYQHSLSILVEEFLQSKELRATVTQMEHHHLFSNILDVLGASQRFFEDLEQRHKAQVLVEDISDILEEHAEKHFHPYIAYCSNEVYQQRTLQKLISSNAAFREALREIERRPACGGLPMLSFLILPMQRVTRLPLLMDTLCLKTQGHSERYKAASRALKAISKLVRQCNEGAHRMERMEQMYTLHTQLDFSKVKSLPLISASRWLLKRGELFLVEETGLFRKIASRPTCYLFLFNDVLVVTKKKSEESYMVQDYAQMNHIQVEKIEPSELPLPGGGNRSSSVPHPFQVTLLRNSEGRQEQLLLSSDSASDRARWIVALTHSERQWQGLSSKGDLPQVEITKAFFAKQADEVTLQQADVVLVLQQEDGWLYGERLRDGETGWFPEDFARFITSRVAVEGNVRRMERLRVETDV

Function: Guanyl-nucleotide exchange factor of the RHOG GTPase stimulating the exchange of RHOG-associated GDP for GTP. May play a role in chemotactic cell migration by mediating the activation of RAC1 by EPHA2. May also activate CDC42 and mediate activation of CDC42 by the viral protein HPV16 E6. Sequence Mass (Da): 80105 Sequence Length: 709 Domain: The PDZ-binding motif mediates interaction with TAX1BP3. Subcellular Location: Cytoplasm

Q86VW2

MRGGHKGGRCACPRVIRKVLAKCGCCFARGGRESYSIAGSEGSISASAASGLAAPSGPSSGLSSGPCSPGPPGPVSGLRRWLDHSKHCLSVETEADSGQAGPYENWMLEPALATGEELPELTLLTTLLEGPGDKTQPPEEETLSQAPESEEEQKKKALERSMYVLSELVETEKMYVDDLGQIVEGYMATMAAQGVPESLRGRDRIVFGNIQQIYEWHRDYFLQELQRCLKDPDWLAQLFIKHERRLHMYVVYCQNKPKSEHVVSEFGDSYFEELRQQLGHRLQLNDLLIKPVQRIMKYQLLLKDFLKYYNRAGMDTADLEQAVEVMCFVPKRCNDMMTLGRLRGFEGKLTAQGKLLGQDTFWVTEPEAGGLLSSRGRERRVFLFEQIIIFSEALGGGVRGGTQPGYVYKNSIKVSCLGLEGNLQGDPCRFALTSRGPEGGIQRYVLQAADPAISQAWIKHVAQILESQRDFLNALQSPIEYQRRESQTNSLGRPRGPGVGSPGRIQLGDQAQGSTHTPINGSLPSLLLSPKGEVARALLPLDKQALGDIPQAPHDSPPVSPTPKTPPCQARLAKLDEDEL

Function: May play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. It works as a guanine nucleotide exchange factor for Rho family of small GTPases. Links specifically G alpha q/11-coupled receptors to RHOA activation. May be an important regulator of processes involved in axon and dendrite formation. In neurons seems to be an exchange factor primarily for RAC1. Involved in skeletal myogenesis (By similarity). Sequence Mass (Da): 63843 Sequence Length: 580 Domain: The guanine nucleotide exchange activity is autoinhibited by the PH domain. Subcellular Location: Cell membrane

C1F4E8

MKMWSGRFREPLDPAFDHWQRSLQFDWQLLPEEVAASKAHALALEAAGVLTAGEREALHNALDLVTSRFHAPDGSGPSWVMSNQEAEDIHHFVELQLVATVGDLGLKLHTGRSRNEQIATDLRLFVRSRAQMLQAYLGTWAEILVARAQQMGNAAMPAYTHLQRAEPVLVAHWLLAYAEMLLRDASRLEDCVRRLNYCPLGSGAVAGATLALDRGIASQALNFAAPTANSMDATSDRDFVLEFLQALTGIALHASRFAEEITLYATAEFGFVDLPEAYSTGSSAMPQKKNPDLTELVRAKVGRINGAAQAVTLLLKGLPLAYNKDMQETQEPLFQATIATHQMLHLLAKFTHALQFRTDHMQAACESGFLNAMAAATYLVHKGIPFRKAHEIVGHAVRLGLDKGCELAGLSLDELRSLSPEFGADFYDAVTLESTLDCHDVLGGTARAQVQASLEAMQRRTGDLVNARGRIDLGLSTVAEVSHADS

Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Sequence Mass (Da): 53046 Sequence Length: 486 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Subcellular Location: Cytoplasm EC: 4.3.2.1

Q46104

MKNEMWSGRFSGASDELLKEFNASLNVDKTLFNEDIQGSIAHATMLESCGILKKEELDAIIKGLEQVRSEIEQGKFIFDIKDEDIHMAVEKRLSEIIGSEIGGRLHTARSRNDQVATDFKLFVKKSHIELIKLLKELIQTMLEHAKVHKKTIMPSFTHLQHAQPVSFSFYILAYAFMLMRDIKRLQNSLELADFSPLGSCACAGTSYAINRELSAKILGFKDIMPNAMDGVSDRDFALDLLYDIAVIFTHTSRLCEEMILFSSSEFSFITISDSFSTGSSIMPQKKNPDVCELIRGKTGRVYGNLISLLTIMKALPLAYNKDMQEDKEGIFDSVKTAKDSLIILNAMLKEIQINKENMLNACKKGHLLATDLADYLVREKNIPFRKAHFIVGNVVAQAEAQGIDISEIKDLSKIDPVFDEKAMELLNFEFSLNSKQSEGSSSIASVEKQIQILEGFIQNL

Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Sequence Mass (Da): 51660 Sequence Length: 460 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Subcellular Location: Cytoplasm EC: 4.3.2.1

A9WJR8

MEHRLWGGRFSEPTAAEMRRFNDSFHFDVRLAEVDIAGSIAWAGALLQAGLINETEHADLVRGLELVRAEFANGSFVAAAGDEDIHTAVERRLRELIGDAALKLHTGRSRNDQVATDMRLYTIGIARQLDRRLRDLQLALLAQAEQHTATVMPGYTHLQRAQPITFGHWCLAYVEMFARDRSRLNDAIRRMRVLPLGAGALAGNSLGVERERLTELLDEFDELSANSLDAVSDRDFVAEVLFACALIGVHLSRLAEDVILYASAEFGFLELADAYSTGSSLMPQKKNPDSMELLRGKSGRLLGNLVALLTVLKGLPLTYNKDMQEDKEPLFDSFDTLDLGLQVAAAAIATMTVRPERMAAALDDAMLATDLADELVRRGVPFRVAHSKVGQLVQRALTRGVSLRQLPLADYQAVEPSLDASIYDVFDMQRSVAQKASYGGTAPQRVREQCARWRDSLLNDE

Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Sequence Mass (Da): 51005 Sequence Length: 461 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Subcellular Location: Cytoplasm EC: 4.3.2.1

P51464

MASEGDKLWGGRFVGSIDPIMEMFNSSVSYDQRMWSADIRGSQAYVKALEKAGLVSPTEMEHILTGLDQIHEEWSKGTFVLTKADEDIHTANERRLKELIGEPAGKLHTGRSRNDQVVTDMRLWLRDSCSALHLHLTRLIRTMVDRAAIEIDILFPGYTHMQRAQPIRWSHWILSHAVALCRDAERLGELRKRINVLPLGSGAIAGNPLGVDRELLRKELEFDSVSLNSMDATSERDFIAEFLFWASLCMTHLSKMSEDLIIYSTKEFSFVTLSDSYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCSGFLMTLKGLPSTYNKDLQEDKEAMFDVYDTVCAVLQVASGVISTLQINKEGMEKALSPDMLATDIAYYLVRKGMPFRQAHGLSGKVVQLAETKGIALNKLSLEDLKSISPLFSNDVSKVWNYTNSVEQYTAAGGTAKSCVVAQVEQLRTWLKKTQESVI

Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Sequence Mass (Da): 52258 Sequence Length: 467 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. EC: 4.3.2.1

Q8TR65

MSNILRRGRLEAAPDEEILRYASSMETDRWIFSADIAVDLAHTVMLKEQGIISAEDCSKILAGLLKIREEGMEKLDFSYEDIHISLESRLIDMVGEDVGGRMHSGRSRNDEVATCIRLTLREELLGLLEEIFALRKTLVSLAEKHTETLMPGFTHLQHAQPTTLAHHLCAHEAALGRDFDRVQDAFSRVNLCPLGAAAFASTGFNLNRKRTQELLGFEGLLENSMDAVSSRDFLIECASVFSNLMINLSRMAEELVIWSSSEFNFIELDDTYASTSSIMPQKKNPDTAELMRGKTGVAVGALMSLLTICKGLPLSYNRDLQEATPNIWRSVETVRASVRVMEGMVRTMKIHPEVLSAQSVTGFTTATELADTFVREAGIPFRTAHQIVGMLAREGEKPTIEKIDSVAEIVLGESLSSRGLTEKMIKEALNPVSNIKRRKIEGGPAPEEMQHYIGRQQTELELNEQEIATIKDSIDSAFEALLEVVDEYRKV

Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine Sequence Mass (Da): 54705 Sequence Length: 491 Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. Subcellular Location: Cytoplasm EC: 4.3.2.1