ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A5DIB1 | MTEDWGGDILARLKLRDDLESRDSKYFEAFDLLRRKKVIKGTSGDPDVAAENERLIEKLNNLAIEVEKKDSQISKLKRQLSVAEKTIKSHQNKLENLALEVQEKNKNIEIVNDEVLMNQIQTAVLQKKLGELTKENETLVKRWMDRVSSEAQQMNDANQFLESMRKTSG | Function: Stabilizes the ATG5-ATG12 conjugate which is necessary for autophagy. The ATG5-ATG12/ATG16 complex is required for efficient promotion of ATG8-conjugation to phosphatidylethanolamine and ATG8 localization to the pre-autophagosomal structure (PAS). Recruits also ATG3 to the PAS. Involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19487
Sequence Length: 169
Subcellular Location: Preautophagosomal structure membrane
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O94656 | MELIKKIQDRDAAEKAYYDVIEPYSELLEFSFHKEFVSEEKVTQRTASSDSLNTIASENNDENVINLEEFRQLKRNCDLYQRNLQKLQLLFKQQSQKNTLLEKQLSLQTELNQEKDKRVKILQDELWALQLEVAALERKSPNA | Function: Stabilizes the atg5-atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The atg5-atg12/atg16 complex is required for efficient promotion of atg8-conjugation to phosphatidylethanolamine and atg8 localization to the preautophagosomal structure (PAS). Involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Required for meiotic chromosome segregation.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16892
Sequence Length: 143
Subcellular Location: Cytoplasm
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A7TIN2 | MDSLFVERLAQRDEVEGRFCELFKEVQIMVGPQLEDESMERKLIVALKSDLVEKDLRIGELEEILQLRNKDYERLNDELISLNIENNILRDKLQNMTEENSKLVKRWLNKVQQEADAMNENLH | Function: Stabilizes the ATG5-ATG12 conjugate which is necessary for autophagy. The ATG5-ATG12/ATG16 complex is required for efficient promotion of ATG8-conjugation to phosphatidylethanolamine and ATG8 localization to the pre-autophagosomal structure (PAS). Recruits also ATG3 to the PAS. Involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14616
Sequence Length: 123
Subcellular Location: Preautophagosomal structure membrane
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Q6C4Y4 | MQLNVTHRTNAERLEKHNRELETALAKKTEEHKEQAKALLLLQDDMLANQIQLNVLEQKTEALQQENETLVQRLVAKAAADADKMNDANAFLER | Function: Stabilizes the ATG5-ATG12 conjugate which is necessary for autophagy. The ATG5-ATG12/ATG16 complex is required for efficient promotion of ATG8-conjugation to phosphatidylethanolamine and ATG8 localization to the pre-autophagosomal structure (PAS). Recruits also ATG3 to the PAS. Involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 10776
Sequence Length: 94
Subcellular Location: Preautophagosomal structure membrane
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A6ZML8 | MGNFIITERKKAKEERSNPQTDSMDDLLIRRLTDRNDKEAHLNELFQDNSGAIGGNIVSHDDALLNTLAILQKELKSKEQEIRRLKEVIALKNKNTERLNDELISGTIENNVLQQKLSDLKKEHSQLVARWLKKTEKETEAMNSEIDGTK | Function: Stabilizes the ATG5-ATG12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The ATG5-ATG12/ATG16 complex is required for efficient promotion of ATG8-conjugation to phosphatidylethanolamine and ATG8 localization to the pre-autophagosomal structure (PAS). Recruits also ATG3 to the PAS. Involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17222
Sequence Length: 150
Subcellular Location: Preautophagosomal structure membrane
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Q757A7 | MSSSNQVKGFYFNAQRRLSRAQALCQNSQDTLHNMQLLLVRWQRTVSKLQFTIHCICNQTVFLAECILKKTVGQQLIETEWKRMLLDELQGEMQRSQEEITGKIDALRRTKNELDGSGATLADFISMENIFLLGDKLKDVPVVQEQVEHIKVQYESLVDKVVEQLQNNRVRKLEADFAAAFRSGKNDFNAFSMKYLQKIRQLETDLADILKSLTDHYDKCSLLKAGDLPAAEQAELFEVVKNDDQELDSIMGVLEVIVRDIKSLAKNVSIRLRQKERDKQQLKNAMGKAHSELLKYEEHLTVFQGIDDLIRNFKASCLHNVSKVRELCEFYDNFLNSYQVLLREVERRRRVAKQMEDILQACEGQLMALSDTDLKQRQQFLMRHGDYLPENIWPGNIDDLSPLYDLEYRIKKV | 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): 47998
Sequence Length: 413
Subcellular Location: Cytoplasm
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Q6BYP8 | MSNRDSSEHGDSSNKIASNECNEATKLGFNFTQLWSQITTTYSLIDRNDSNMFNRDERVESEQEKKSVVILGKKYDDISVDDGVIEQDIYSKIWLTYRTGFEPIAKCLDGPQPLSFVQSMVFNRNPISSTFNNFHGLLDNDNFTTDVGWGCMIRTSQALLANTYQLLFLGRGFSYGRDRSPRHDEIIDMFMDEPRAPFSLHNFIKVASESPLKVKPGQWFGPNAASLSIKRLCDNVYESNGTGRVKVVISESSNLYDDIITQMFTTLNPVPDAILVLLPVRLGIDKVNPLYHASVLELLALRQSVGIAGGKPSSSFYFFGYKGNDLLYLDPHYPQFVRNKTSVYDTYHTNSYQKLSVDDMDPSMMIGILIKDINDYEDFKSSCTKSSNKILHFHPTSEKADRRGSLSEFKRKNSEFVCIESKDVQRREDFITIDNVSRDDLNNMEGFIDMADEFDSEIDQNNKDDNFDDDEPVNVSQTSIGEEYTSTAGSRP | 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): 55840
Sequence Length: 492
Subcellular Location: Cytoplasm
EC: 3.4.22.-
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Q557H7 | MFTKYSHHNGYQDGSHLQPFQYQQQTYNQQSYLRQQQQAPQQISYGFNQPNSPTSSSSTPSSSTAMGNSFQNQRQINLQQQQQQEQFLQEQVFYQQQLLQQQSQIKEQQRQKEQKQKTNILNIYKEGKQKIMMSFYNLYRNYPTEPPHFSPSPIWLMGRCYTSKDNNSNNNSNNNQVPQTQPTQLQQSIGIFQNNNSNSNNNNNHNNNHNNNNNNLTTDLIYRPAIESGFLSDVASMIWFSYRKDFPPIENTNITTDIGWGCMLRTGQMILARALIKHLYKENDMVPEIERKKPHSNYSQVLAWFSDYPSKEHVYGIHQIVNKKQAMEKNNRKQQILREQVISLNRGGGGSSKGKKKKEKEEEINDNVEEWLAPTRISNILRQLIKFQHLEDLEMYVPTDGVIYKDYINNLCNNSNTHNHYQIIQQQLQHLREQQNIQQNNNKNNNNNNPTTTTTTTTTATSSNNNNNQSPPSRVPNGYNNQVFDDESLFDYNTAISSIPPKWKSLIIMIPLKLGADKLNSTYIEKLKLLLKLPQSLGFIGGKPKQSFYFIGFQDDQVIYLDPHFVQESVNPNSFDYSNTYSGCIPQKMPFTQLDPSLSIGFYCRDQASFEDLCDRLSVINNCEFPIISVCQKLPDYQIECELVDDYAESETTEMLAITIANGGNNHSCIPENIVVDDEEFIVHHHIPYNPNNNQNNNQNNNNNNNKNNNNNTNQQQTPNYPPKLNTYQPDFSSDGEIDDFTMVG | 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 PE-conjugated ATG8 proteins (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): 86136
Sequence Length: 745
Subcellular Location: Cytoplasm
EC: 3.4.22.-
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Q5B7L0 | MNATDIERCRKRIIQYIWDPEPKNDEEPGSPIWCLGTRYPPQCVEETADESRNPDHGQQQNTNTSAPGWPEAFLLDFESKIWMTYRSNFPPIPKDAGQEGSLSLTLGVRLRSQLIDAQGFTSDTGWGCMIRSGQSLLANSMAILLLGRDWRRGERLEEEGKLLSLFADSPHAPFSIHSFVKHGADFCGKHPGEWFGPTATARCIQGLAARYDQSNLQVYIADDNSDVHQDKFMSVSRDEKGTVRPTLILLGLRLGIDRITAVYWNGLKAVLQLPQSVGIAGGRPSASHYFVAVQGSHFFYLDPHNTRPALRYSESGTYTEDEVNTYHTRRLRRLNIQDMDPSMLIGFLIRDEDDWEDWKARIMSLEGKPIITILSESDAASWKGRREALDEVEAFDDLDVAL | 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): 45379
Sequence Length: 402
Subcellular Location: Cytoplasm
EC: 3.4.22.-
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W0TGM7 | MEFLTKITQQLGLVGEIDKVGSVFVLGEEYRPYIFKTQGKADDAETAFGSFLGNAQTNPQLLSDIETRIFFTYRTQFTPIPRDEEGPSPINLTLFFRDNPINTLENVLTDPDSFYSDIGWGCMIRTGQSLLANAIQRVKQTREFRVNLENIDIKEMSIIQWFQDDWKYPLSLHNFVKVEGKKSGMKPGQWFGPSSTARSIQSLINDFPDCGIDRCLISPQSADIYEDEMIRVFEENKRANVLLLFATRLGVNEINSIYWSDIFQILKSSYSVGIAGGKPSSSLYFFGYQNDYLFYLDPHQTQSSSLDMDDNSYYRSCHGHRFSKIHISETDPSMLLGMLISGKAEWDLFKDEFKNSRIIQFVASKPSDDIYEGVDLSPGSVSVHSIQSDLQDTGDYIDVGNFMSEKANSSQPSKNEEFENVKCKNQRILICENPSETEIEQVLVEDSTTDN | 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 (By similarity). 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 (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): 51288
Sequence Length: 451
Subcellular Location: Cytoplasm
EC: 3.4.22.-
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A5DSB4 | MSLMSDDSEVFVQAPTVANAELNIEAKPEANAQVNAEADSDANLGNNLGEQQTTDESAFGRNIGKFTAFVKEITGSGTEVEEQEKRNNHTISVDPSSNHENTSFEPTTYKILGRTYTSTTDASARVQELLWLSYRCGFEPIPKSDDGPQPITFFPSIVFNRLTLVNLSNLRSLLDKDHFTSDAGWGCMIRTSQNLLANALLRLFHTTGGQPQNFAVTKTEADVIELFQDTLSAPFSLHNFIKAANSLSLNIKPGQWFGPSAASLSIKKLVNDYNLIQQERRSERDSGRDSGHKVPTPNLKLHSKSADSDSDSDSDAISKRNSIPYVYVSENCDLYDDEINAIFELEQRPILFLFPIRLGIEQVNKYYYSSILQILASKFSVGIAGGKPSSSFYFIGYEGEDDLIYFDPHLPQIVQTPVNLESYHTSEYSKLKIDQLDPSMMIGILIETIDEYQEFKMSCFESDNKILHFHPLVTTAPRESSINQSWEEVQGEEEFVNLNIVKNEEDFVDLGSASTQGQNHEPS | 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): 58443
Sequence Length: 523
Subcellular Location: Cytoplasm
EC: 3.4.22.-
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Q523C3 | MDSAVAGAADIGRYGRRIVRMIWDPEPTNDPIANRPAWCLGYEYTLETNITSKTKGEDSKLSTATSSDQQRPPAQANKVPQMPSAQLPTEAAATALSGNTTPPTPEAALEPTKITSQPAAIDTPPDSVDSSFDSSMAYDDVPDDGGWPPAFLNDFESRIWMTYRSGFEPIPRSTDPTASSRMSFAMRLKTMADQQAGFTTDSGWGCMIRTGQSLLANSLLTCRLGRSWRRGQAPDEERKLLSLFADDPRAPYSIHNFVAHGAAKCGKYPGEWFGPSATARCIHALANATENSFRVYSTGDLPDVYEDSFMEVAKPDGKTFHPTLILISTRLGIDKINQVYWESLTATLQLPQSVGIAGGRPSSSHYFVGAQRSDEDQGSYLFYLDPHHTRPALPFHEDPQLYTPSDVDSCHTRRLRRLHIREMDPSMLIGFLILDEENWHAWKSSVKHVQGKSIITVSEHDPSKGSASGRPSAIDEVETLSDDDGDTVLDG | 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 (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): 53934
Sequence Length: 491
Subcellular Location: Cytoplasm
EC: 3.4.22.-
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A2Q1V6 | MVLKDLCDRIVAAKCSSKSSTEIVDNTQVPASSKAGSSDSKFPKASLWSTFFTSGFSVDETYSESSSSEKKTVHSRNSGWAAAVRKVVSGGSMRRFQERVLGSCRTDVSSSDGDIWLLGVCHKISQHESTGDVDIRNVFAAFEQDFFSRILITYRKGFDAIEDSKYTSDVNWGCMLRSSQMLVAQALLFHKLGRSWRKTVDKPVDKEYIDILQLFGDSEAAAFSIHNLLQAGKGYGLAVGSWVGPYAMCRTWEVLARNQREKNEQGEQLLPMAIYVVSGDEDGERGGAPVVCIEDACKRCLEFSRGLVPWTPLLLLVPLVLGLDKVNLRYIPLLQSTFKFPQSLGILGGKPGASTYIIGVQNDKAFYLDPHEVKPVVNITGDTQEPNTSSYHCNISRHMPLDSIDPSLAIGFYCRDKDDFDDFCSRATKLAEESNGAPLFTVAQSRSLPMQVTSNSVSGDDTRFEEDDSLSMNLVNDAGNEDDWQFL | 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. In addition to the protease activity, also mediates delipidation of PE-conjugated ATG8 proteins (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): 53809
Sequence Length: 487
Subcellular Location: Cytoplasm
EC: 3.4.22.-
|
A7KAL5 | MTMDMEKCKRIVQYFWDPEPRNDVPAASIWCLGREYAPSQPPSDPASNNPRSPSRQPNASTLNDTTWPKAFLSDFGSRIWITYRSNFTPIPRTKTPEATSSMTLGVRLRSQLMDPQGFTSDTGWGCMIRSGQSLLANTFSVLLLGRDWRRGEKVEEESKLISMFADHPEAPFSIHRFVNRGAESCGKYPGEWFGPSATAKCIQLLSTQSEVPQLRVYLTNDTSDVYEDKFAHVAHDESGRIQPTLILIGTRLGIDNVTPAYWDGLRAALTYPQSVGIAGGRPSASHYFVGAQDCHLFFLDPHTTRPATLYRPDGLYTQEELDSYYTSRLRRIHIKDMDPSMLIGFLVKDEDDWADWKKRIRSTPGQPIVHIFPSQHQPDHGHGRAEALDEVEALDDSDEME | 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 (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): 45302
Sequence Length: 401
Subcellular Location: Cytoplasm
EC: 3.4.22.-
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Q0U199 | MNDFERFGRNVVRTFYDPPPCNESNEPIWLLGQRYDSRPPLPKPAPSDSSTTATATAQAERNEDESWIRTSIDDKERKEAPNGEDPTQYGNWPSAFLDDFESRVWMTYRSGFSPIQKSQDPKATSAMSFRVRMQNLASPGFTSDAGFGCMIRSGQCILANALQILRLGRDWRWQENHADKDHAEILSLFADDPQAPFSIHRFVEHGAAVCGKYPGEWFGPSAAARCIQDLANKHREAGLKVYVSGDGADVYEDKLKQVAVDEDGLWQPTLILVGTRLGIDKITPVYWEALKASLQIPQSIGIAGGRPSASHYFVGVQGNNFYYLDPHSTRPLLPFHPPSLAAATSDTPNLTASTTSVSSTTSSTTIVPPADSIPAPSDPRQSLYPPSDLSTCHTRRIRRLQIREMDPSMLLAFLVTSEADYQDWKEGVQGVQGKSVVHVQDKEPPPRGQEREGAIDEVESWDEDGLQ | 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): 51812
Sequence Length: 467
Subcellular Location: Cytoplasm
EC: 3.4.22.-
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A7KAI3 | MASHSLNTLHTVFEYIWDRELPNDDFTNTLTVLGRTYAPGPPPHQEKAPDLRTLFHKFKPDQAADTEASWPREFLRDVHSRIWLTYRSGFPLIKRAEDGPSPLSFGSLIRGTVDLATVTKGFTTDAGWGCMIRTSQSLLANSLLQLRLGRGWRYDQTRECAKHAEIVSWFVDIPTAPFSIHNFVEQGANCAGKKPGEWFGPSAAARSIQVLCEANYDKTGLKVYFTASGDIYEDELFELAQQGAELRPVLILAGIRLGVKNVNPLYWDFLKKTLGWPQSVGIAGGRPSSSHYFFGFQGDYLFYLDPHVPQKALLIASEAPHESPDPNHYVEVESGLDLDSVHTNKIRKLHLDQMDPSMLVGLLVENRASYDALKHSINSHDQGSRFLNVYDSRPVLAAKSSGGLEESEFVDLGVLSMNEYDAIDDCDVGTCSALLRKERAFSHPVLVAMDPEEPEEIDASIHFDKDASILEKDPDRANETFEEIHVSETESRFEPDEPVVVSHDSAAVM | 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 (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): 56839
Sequence Length: 509
Subcellular Location: Cytoplasm
EC: 3.4.22.-
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A5DEF7 | MTWDTKNQFETTKTSQELPATSQDHISDNKMNSEPSHRLSQFWSSLTRSSSESITAEPVVILGHTYREGDRDREGDSEVQKQVKKRYWMSYRSGFEPIKKHEDGPSPLSFVQSMIFNKNVGNTFANIHSLVDNDNFTTDVGWGCMIRTSQSVLANAIDRAGYEVDVELFADTSSAAFSLHNFVKVASDSPLRVRPGQWFGPSAASLSIKRLCEARNSSTNVPLSVLVCESGDIYDDQIQTFPVLLLLPLRLGIDHVNNVYHSSLLQLLEVPQSAGIAGGKPSSSLYFFGYQGTSLLYLDPHYPQNVSAGVGSYHSSSYQKLDISDMDPSMMAGIVLKNNEDYTDLKRRTTGNKIIHFHEARNYNDYVEVEREDFIDLGQNNRSATAGAEADFDSESSMVIVD | 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): 44844
Sequence Length: 402
Subcellular Location: Cytoplasm
EC: 3.4.22.-
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Q8NJJ3 | MYRFLGLGTHPNDDQNKIHVLGRQYDPIKTQETEGKDLDLNSRFQQVLDSIKDGNKKSTTYSQSFIDDVYSKIWLTYRAGFPPIARDKDSPTFTLGALLRGQFDFNEIGFTSDAGWGCMIRTSQSLLANALLFLHLGRDWVFKAKDPANVEHDRIISWFVDIPDEPFSIHNFVQQGIKCCDKKPGEWFGPSAASRAIKNLCKEYPPCGLRVYFSSDCGDVYDTEVRELAYGDSDTFTPILVLLGIRLGVEKVNLYIGDLLRECLSLKQSVGISGRKTSFLALLSIGFQGDYLFYLIPTFPKKALTFGKHGEPVHRLQTKKTDENAAGQYPVFKYWIQIMKQTMMTAMKASKTTASTLKFFRVLMSNQSTHQKVTKLHLSHMDPSMLIGFLITSEDDFNDWKENIGKKDPSHKIVHITETKVSESTSNFQFNSLRSNSIADYDNCSGEDCDSAAIASDSDDFVDLAADFAVTGLEPRTHTGVDDETSSDYVQHFPIRRFSQPVIVSREDVVPTLSEDNGVIALDDKMSGISVGR | 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): 59883
Sequence Length: 533
Subcellular Location: Cytoplasm
EC: 3.4.22.-
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A3LQU0 | MAREDASVPRSHDSADASPNSTAKEIPVPQPPLLNLNLNLNMNSGFNLSNWWHQITSIEADSSDDRNNNNSNNGINAAESDSAQSQPIVVLGHSYQTTEEAHEDIIKKLCLTYRYGFERIPRAVNGPSPLSFMQSVIFSKSLLYNLQNFNNFIEKENFTTDVGWGCMIRTSQSLLANTFVRLLDKQSDIIALFNDTYLAPFSLHNFIRVASSSPLKVKPGEWFGPNAASLSIKRLCDGYYDNSTSETILPRINVLISESTDLYDSQIAQLLEPSTETKGLLVLLPVRLGIDSINSYYFSSLLHLLSLEQSVGIAGGKPSSSFYFFGYQDNSLIYMDPHSAQIFSSDIDMSTYYATRYQRVDIGKLDPSMLIGVFIRDLTSYENFKKSCLDAANKIVHFHATERSTVPESRRKNSEFVNINRSDLKDEDYINIDRVNRLDSTDDFIDLGDDYVETNTNLEEATPSAEDTVPVSTLSASESEITTSSYETPTSKDDNSSRASLDVVVLDTTGEQQE | 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): 57380
Sequence Length: 514
Subcellular Location: Cytoplasm
EC: 3.4.22.-
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Q9P373 | MELMARFLERYLHFAPTNTEPPGTLIWFLGHSYKIEDSQWPEKFLYDSFSLITITYRSGIEGLENMTSDTGWGCMIRSTQTLLANCLRICYPEKQLKEILALFADEPSAPFSIHQFVTMGKTLCDINPGQWFGPTTSCSCVARLSDQNPDVPLHVYVARNGNAIYRDQLSKVSFPVLLLIPTRLGIDSINESYYDQLLQVFEIRSFVGITGGRPRSAHYFYARQNQYFFYLDPHCTHFAHTTTQPASEETFHSATLRRVAIQDLDPCMIFGFLIRDEEEWHSFEANQKYFADIVQIFDSEPQPVETHDDFVLDENVEDHL | 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 (By similarity). 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 (By similarity). Plays a role in meiosis and sporulation .
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): 36929
Sequence Length: 320
Subcellular Location: Cytoplasm
EC: 3.4.22.-
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Q6TGJ4 | MRKLCGNGSTSMISTDSYKNTTFFVIAFSTFLISCIDYTKLFSSLSTPEAVGRLEDVLIGQCITKGSFAHTLFLIILSAFFIFQVANFAMSVPRLLDMYRFYTHLLGVPDADIQTLPWPEIVRLIGDIRKHNPVTSLSNGQATALADMVGNDAKAPVKKLDAHDIANRILRQENYLIALFNKDLLDLRVRIPVPHIFTAFIPSSMLILSADPPLPSLQSEPERKFLSFGANHLTKALEWNLRFCLLGYLFDRRGQVRKEFVREKRRKDLVQGLRRRFVFMGILNAIFAPFIILYLLIYSFFRYFEEYHKNPSSIGSRQYTPYAQWKFREFNELPHLFERRLDRSYETAKEYVDQFPKERTALVMRFVAFVAGSFAAVLLVASLIDPDLFLHFEITPHRTVLFYLGVFGSVLAISRGMVPQENMVFDPEASLNEVVRWTHYLPVEWRGQLHSQMVHQEFSKLFALKIMIFFSELLSVILTPFILFFSLPPCAAAIIDFFREFTVHVDGVGYVCSFAVFDFARHGNIDSNRPETGVQGATGPDAGDSGGGGGGGGGGFAAGKSGRQTTRRAASASPSRFKQKDWRSNENKMEQSFLHFKATHPDWQPSDPSSSLFLDRLMGAGARNRPAGGISGSIYGGGGGGGGGGGRGLGIDGSVMAEMEEERLRAKSQSYERAWAKSSHLHRPDISNPLRHPHSAASEIIEEEEGGEGDKGDDSIDGWSKRMKTDGESDDEQEEHGRLWKDDGVQIDIKQ | 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): 84191
Sequence Length: 751
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
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P0CM41 | MGKGEGYLDPTILSVASGSRNSGKGKERTRRKGGHKYHSLHVQDEEEEEPPESDALRTRGKVGLNAYEKALWKWVNVDDLDGFLQEVYDYYKGKGIYCIVLARVLNLLTTFFVIAFSTFLISCIDYSKLFSSISTAEAVGRLEDVLVAQCITKFVHFKLYILNKTNSSAYDYRGSFAHTLFLIILSAFFIFQVASFAMSVPRLLDMYRFYTHLLGVPDADIQTLPWPEIVRLIGDIRKHNPVTSLSNGQATALADMVGNDAKAPAKKLDAHDIANRILRQENYLIALFNKDLLDLRVRIPVPHVLTAFIPSSILISSADAPLPSLQSEPERKFLSFGANHLTKALEWNLRFCLLGYLFDRRGQVRKEFVREKRRKDLVQGLRRRFIFMGILNAIFAPFIILYLLIYSFFRYFEWKFREFNELPHLFERRLDRSYEIAKEYVDQFPKERTALVMRFVAFIAGSFAAVLLVASLIDPDLFLHFEITPHRTVLFYLGVFGSILAISRGMVPQENMVFDPEASLNEVVRWTHYLPVEWRGQLHSQMVHQEFSKLFALKIMIFFSELLSVILTPFILFFSLPPCAAAIIDFFREFTVHVDGVGYVCSFAVFDFARYGNVDANQPETGLEGATGPDGGPAADGFAAGKPSRPTTRRTTSSSPSRLKHRDWRGNENKMEQSFLHFKATHPDWQPSDPSSSLFLDRLMGAGTRNRHGGGPVSAATGGISGSIYGGGGGGVGGRGLGVDGSVMAEMEEERLRAKRQSYERAWAKSSHLHRPDSSHSHPLRHPHSAASEIIEEEEGGEGDKGDDSIDGWSKRVKTDGETDDEEERERLWKDEGVIIIFFLTNNHITVVVMNVCRCIFRVAADEHKTAGRINKSQTRRLT | 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): 99290
Sequence Length: 879
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
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Q54NA3 | MSHEDRGGDYYPMMDDPEDRNFIQAKYPNSTGHMSSGGGSNHMSFDDNHGIEMLRDDEHSLLHESPVSIPAIHNLDSFLTDVYNYFRGKGFMCIFFNDLFELVSSLFVVLFFTFLVCFVDYSKLFSEQMPPPALRESVNFSAPIPIWLMVFLVIFSLYWLSKLFSFFSSIKTNWEISSFYKNTLKINEDDIQTIEWREVVSKIVLVPRLCIVKENMNALDIANRIMRKENYIIGLINQRILNLSIPFPFLRNLTFITKTLEWSLMYSLFNYIFDENGIIKSEFQDPTQRKRLSRGLSRRFMTIGILGLFTTPFIFFFLLINFFFEYAEELKNRPGSLFSREWSPLARWEFRELNELPHYFQNRLNLSYSHANQYVESFPSQMLSTIAKFISFLFGSVLAVFIVLGIVSDHFIMNYQIFDRTPIWYIGILGTIVAITRSLIVDENQVFQPAKHMARTVQNTHYLPMSWVGKTHTHKVRDEFLVLFEYRIVDFVRDIFSVLFTPFILIFSLPKSSQAIIDFFGNNTVVLEGVGPICQLGDFSNIRKLGDNSFGSLNHSQNKISLTNNAKLEKSIINFKCLNPEWNTDNNELLQNLNEFSKIKNNNNNNNNNGSNNHIGNHSQLPTTSVDDFQFIHDSHYIPHEIIDAVLGTHHHSQQSNNNAPRFKTGRVDQNILNAVNDLHQSFYESQYKHKNDNFVNSI | 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). Required for lipopolysaccharide (LPS)-enhanced bacterial clearance through the autophagic pathway .
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): 81314
Sequence Length: 699
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
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Q5B6U6 | MMASNVLSRLLPQTGQSVYETIRQHDNDSDASDVEERAGLVYDDDVNLGNRFSDRELEEAMADATREGSSSPSDTFLTPQIAQRGERSASSGPRMRKPNNPRFMRSVTPRPEFVEDDLDDDHDDDVPASLLMEGQHDDEYLRTRLPPPPSHHFSDPQPSRSARSPRREHIRTFAFVVGFTTFLTNCIDYRLVRTSKSLDQILISKCTSRMSASSTFLLWLLCLFWIGKIFQLILDIRRLKNMHDFYHYLLGVSDAEIQTISWQEVVSRLMTLRDANPATAGAVSAFNRRLLGSQSKQRMDAHDIANRLMRKENYLIALINKDILDLTLPIPFLRNRQLFSRILEWNINLCIMDYVFNEQGQLSSRQYTPLAEWKFREFNELWHLFEKRINLSYPYATRYVDQFPKDKTVQVAGFVAFISGALASVLALASILDPELFLGFELTHDRTTLFYLGVFGSVWAFARGMVPEETLVFDPEYALLEVIQFTHYFPSHWKGKLHSDDVRREFAVLYQMKIIIFMEEILSMIFTPFILWFSLPKCSERVIDFFREFTVHVDGMGYLCSFAVFDFKKGTNVIPQGHINQRDARQDPRVDYFSTKDGKMLASYYGFLDNYGGNPRATNANKRAFHPPPTFPSLGSPPFVGASNIGNRQDPIQARVNTASAALGQQSMLGATRLGALGVGDTQSPAPSLLLDPQHQPSASGFRATNHIAPHHRQRLGRPPPAPVSESIIDDNEPSIAAARRPAPRRKSGQLHTNSGSSEALGAGDSNVEDSWGMKSGGEVNDEDAEENVDDVVGGAGVLGLIQQFQKVNKDNRPRAAVGL | 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): 92456
Sequence Length: 820
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
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I1S9X9 | MASNIFSRIKSPSGGSQSFYQQLRSGEDPEYDPGLDEENLGHRFDDFQAEGMDIGDSSMTVESVAPGSKGKGKATFRPTAHARSSGITSPRWQQDDDGDNEVPASLLMEPKDLDPPASPPNKRATNPGSSRTPASVGPSSARTRAQWEAATAQQQLHQDHPYTTPMGPQPIPVARGTMSNNPREKALWRWVNTSNLDSFMRDVYDYFEGGGLWCILCANALWLFQCIDYSRVPDSRSLHEVIVPQCTRKMSGLWNFAIWLYTFFFIWKCVQYFVEIRRLTYIRDFYIYLLDIPEQDMQTISWQDVVARIMALREENPKTATNISPRLRQFMGSQSKERLDALDIANRLMRKENYLIAMINKDILDLSLPVPFLRGRQMFSKTMEWYLQYCILDMAFNELGQVQQDFLRPDRRRLLSQKLRQRFLFAGFLNLLFAPVVLAYVVIVYFFTYYYEYQKDPKQAAARKYTSLAEWKFRQFNELPHIFYERLHMSYPFATRYIDQFPKRITEAVARTIAFMSGAITAILAIGSVLDSELFLNFEITKDRPVIFYLGVFAAIWATTRGMVSEETLVFNPEYALRNVIEYTRYVPDHWKNKLHSSEVKQEFSELYKMKVVIFLEEMMGIVTTPMLLLFSLPRCSDQIVDFFREFTIHVDGLGYVCSFAVFDFQKGPGNTGPQGPRPDVREDYYSTKHGKMAASYYGFLDNYAANPKTGIPGHLPPGPKPSFHPPPSFPGIGSPTLAADMQGSHIGRTGTETGRARSRAPGGRGPRIGVMPQPSPMASMLLDQHHQPPGGNMVARSLHASRYPRGYRGESQIIEETEASSIRRNGEDDELYEPGGALGESVWETSPARGVTRENSAANTEDPEAGVLGLIYQLQQTQRPRRGGGMV | 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). 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 . Required for aerial hyphae development and lipid droplet degradation in response to starvation .
PTM: Phosphorylated by ATG1 (By similarity). ATG1 phosphorylation is required for ATG18 interaction and preautophagosome elongation (By similarity).
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): 100819
Sequence Length: 888
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
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Q51WZ9 | MASNIFSRLVPQDRGRSFYEDLRQTDPDADLESRAGIDIDEENLNRSYHDYDLDEAERLAGDESHISHSRGDVAGANTVHRRGQKANTARWLGAGVEDDVDNDVPESLLVETPRAPQHLLLSPSRAGPSHPRPTAVPGPSTRQNQAQWEATRHQQRLHNDDTMPHGPFSGRAGQGRPEPPPVGLMAGDPYEQAMWRWVNVSNLDNFIKDVYAYYRAAGFWCIIVQRILELVNAAFVAVFLTFLSQCVDYHKLPHSKKMEDIIIPKCTQNMSLVWNVGLWLFAIYFICRCFGLIIQLRQLKHLRDFYTHLLKIPEADMQSVSWQDVVGRIMALRDSHPRTAGNLTRVQRAWIGSQSKERLDAHDIANRIMRRENFMIAMLNKDVLDLTIPLPFFRNKQHMSECVVLAISFSILDFVFDNQGQVNPEFLKASRRRQLSQKLKSRFFFAGLMIFVMSPFIALYLILVYFLTYFHEFRNDPGALGARTYNSLAKWKFREFNELDHLFNDRMNMSHPFAKRYIDMFPKRKTEQVARTVSFITGSIVAVLGLATIFDSEAFLTFEITPDRSVLFYVSILATLWAVARGNISDDNEVYDPEFAMKSIIEFTHYEPDHWRGRLHSTEVKNEFSELYKPRPQIFLEEILSILLTPLVLLVSLPNSTDQIVDFFREFTIHVDGLGYVCLFSVFNFQQGHANQKQAAAADAPDNREEYYSTKHGKMAASFYGFLDHYVINPKTGLPGNQLPGSRQQFQHPPSFPGLQSPTLAADMRHSRMMRERGRSSGVQIQGSQGRTPQFRTPMPQPSPMASILLDPHHQPAPGAFGSRSMHRSRQMAVPHRGGYMSDRDIIEEAVTEDGQDDARFGKLGDEDIDESGGALDESTWQTSPTKTLSRENSGANPQETEVGVLGLIHQFQQAHMHLRR | 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 (By similarity). Different machineries are required for anterograde trafficking to the PAS during either the Cvt pathway or bulk autophagy and for retrograde trafficking . Plays a role in appressorium formation and pathogenicity .
PTM: Acetylated by HAT1 at Lys-621, which increases the ability to bind vesicles during nutrient starvation induction.
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): 104559
Sequence Length: 917
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
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Q7S4D7 | MADGVIARLMSGGRGARSFYEELRGRDNVSDVDDRAGLLDEENLNQHFNDYDLENAEGLRLEDSRATVDGRIPRGRAQLSGRPPRPAATTHWGTSHDDDGDNDVPASLLVERYDRGAAPLGSPGKPRSQHAGSRAHPAPGLSKGRTHQQRPHIDQELQPPLHSDAAPSSLLAGAITGNAKKMAEWRWANITNLDSFMQDVYSYYRGSGMWCIVVERVLHLIKVAFVAFLLTFLSQCVDFKKIPSNQKLSQVLVPQCTRNMSGLWNIGLWLFAFYFMWKSIQYILDLRRLTHVRDFYIHLLNIPDEDMQTITWQEVVARIMVLRDQNVRTTRTITPQNQRWVLGSQSKERLDASDIANRLMRRENYMIAMINKDILDLTIPLPILRNRQLLSQTLEWTLMFSILDFVFDPKGQVHQEFLRSDRRGILSAKLRSRFIFAGVMILILSPFVAGYLIIVYFLEYYNEIQKNPSILSARSYTPLAEWKFREFNELPHLFKRRLDMSHPFASHYIDQFPKAKTSMVAKTVSFIAGSIATVLALISVFDPEMFLGFEITHDRTVLFYTAVFGAIWSVARGSVSEDNAVFDPEYALGNVVEYTHYQPEHWKDRWHSADVKAEFEELYKLKLVIFIEEILSILTTPFVLFFSLPKSADQIIDFFREFTIHVDGLGYVCYFAEFDFKKGSKSQAPAATAGEGDVRDDYYSTKHGKMEASMYGFINNYARNPKHLPPAMRQQFHLPPVFPGITSPTLAGDLAASRMGRSQRGRSKGPLPSRTPRPGAVMAEPSPMASILLDPRHQPIFPNNMSFVNTGHQFRGGNQGDGHMMGGGSMEEDVKGAARHGQQTHDDESEDSRAGLDESAWQVSPTKDLSRENSGRGLDSVVGEEAGNGAGVVHMLYQFNQAHLNRRLGGVR | 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 atg-2 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 apg-1. Apg-1 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): 102641
Sequence Length: 908
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 apg-7/atg9-containing vesicles, thereby enabling growth into autophagosomes.
Subcellular Location: Preautophagosomal structure membrane
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A7KAM0 | MMSSNILSRFLPPTGSPSVYETIRQHDAGSEYSDLEERAGLVIEDQQEQYSDRELEDALADAQDSEIVSPSTALLNQARSVKAPEERASPSGTRRRKSSRPRWMAQESPLGYELDDHDEDVPQSLLVEGHHEDLKPRLPPPPQSHNRSDRRRTPSPGPSSRPTEARWNERGVHQQPPPSESGHPIGRWFTGQHPGLANVDPKKKAMWRWANVEDLDNFLKDVYVYFLGNGIWSILLTRVLNLLTFAFVVGFSTFLTNCIDYPKVRRSKTLNDILVPQCTANMSGSSTFLLWLFSFFWIGKLFQYLLDIRRLKHLHDFYLYLLGVSDAEVQTISWQEVVSRLMALRDSNPSTAAAVSAKHRRFLGSQSKQRMDAHDIANRLMRKENYMIALVNKDILDLTLPIPFLKNRQLFSRTMEWNLNLCVMDYVFNEQGQLRTLFLKDTHRRALSDGLRRRFIFAGVMNIFVAPFIVVYFMMHYFFRYFNEFKKNPGQIGSRQYTPMAEWKFREFNELWHLFERRINMSYPFASRYIDQFPKDKTVQVARFVAFISGALASVLALASVIDPELFLGFEITHDRTVLFYLGIFGTVWAFARGLAPEETDVFDPEYALLELIDFTHYFPSGWKGRLHSDDVRKEFAILYQMKIVIFLEEILSMIFTPFVLWFSLPKCSDRLIDFFREFTVHVDGVGYLCSFAVFDFKKGTNVLSQAGPGRRDPGKQDLRTDYFSTKDGKMLASYYGFLDNYGTTHQATSRRPFHPPPTLPTLGSPTAGGFGALPDRPDHLQTRLGPTPGAPFGPQSMIGTSKPRQMGGFDHRSPAPSILLDPHHQPSTTGFRAAARIAPQQHQRSRLGRSHHPSTDPIDDEEEPLSQDGHDSTTRQSGARTGTSSAGAGTSDSNLGDSWRMNPLSNDEDEGDEGENIDAIAGGGGVLGLIQQFQKANTEGRRTNVGI | 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): 107622
Sequence Length: 948
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
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Q0UYL2 | MASNLLSRLLPSASDDLLEQEASNNQNRRTSSSTDERPDMDIDEENFGARFEAQDLNDLLAEASSSHMTTESRAASPEARRNAPPGINTAARAPAWRQPAPARAVPLDDDDDVPQSLLLEGGLDPPPNPHPRPDGLPPPVPGPSTRHTRAQWETTRQQQRLHGDDRGGAPVRDWGAIGRGGQFTADPKEKASWLWVNQTDLDTYMREVYEYYVGSGIYSMILRRTLSLLQSAFVVGFMTFLGWCIDYSKLSGSNKLSQVLVPKCTKEIHGFWIFALWVFTIYWLYSFYGLLTDIPRLRAMHDFYHYLLDVPDRDIQTIQWQQIVSRIMALRDLNLTTASNLSPETRKLLDSKSRQRLDAVDIASRLMRRDNYLIALFNKEILDVTVPIPFLGNRFIFSETTGWHVNLAVMEFVFSGPNGQFNQDFLKERNRRELVRRLRGRFFWTGIISIICAPFAVVFVLASYLFKYFTEYHKDPGQLSNRDFTTFAQWKFREFNELPHLFNRRRNMAYPYANLYLAQFPKDKTEQISSFVAFIAGAFASVLVAFTLLDSELFLTFEISPGKTAIFWIGVLTTIYRVARGSSPQEDQVTDPSYYLDHVIYHTRYKPDSWQDRLHTDEVRAEFAKLYQPKILIFAEEILSMVVTPFLLMFRLPQCSERIVDFFREFSIVVDGLGVTCSYSMFPFKKGTQNVNNAPANRSGAHKDDGDLREDYFMAKDNKMLASYYGFLDTYATTGKGNSARLPGRAGFHPPPQFPNAFGAMSQTAQPVDVGARGTSRGPAGRQPLQRRTPRSGPAGRDEPIASVLLDPHHQPSSASILRGSPRTGPSGRYRTPLQPVADTPGTRIEEESTIGDSWRTSRLAQDDDEEEEAPGANRGGVLQLLQQFSKAQAEGRGAGVGV | 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): 101537
Sequence Length: 899
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
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A7KAI7 | MGDLNKHTFLSRVFGSASNPLLNDDNNDIEFSINNLQDTFEEHQVESPPRAPHPINVNSEDESSSETESASNEDLLYDQKRELYQQVESELRQDDYDTVPESLMMERRRPHEGSTRTIGTKIPPSPAEPPIGPNITQWGEKARGIASRTLDNIPKTIAKGISFQLPANASSKLPPPPLSYRRETSVGGETEMAQNINEQRQLRGRLGLLSPMERALWLWSNVSNLDTFLEDVYGYYTGNGYRCIILSRVSDLLIIVFVVWLTSFMGNCVDYNQLMNGNATKYSDVVVDKCYSKISLSQKLFFLVLFAILVLRIKSFYSHFKDLKEIKNFYNLLLGVSDEELQTISWSTIVKKIKVLRDQNTNALISGNQNLRGDDLKSKKRLSAHDIANRLMRKENYMIAIFNKNVLAPALTIPFINHHFLTKTLEWNLKLCIFDFVFNTDGQLKQAVLSEHKRLALATEMRKRFRLAGILSIFLTPFLVIYFLLYFFLKFFYDIKTNPSLVGSREYSPYARWKLREFNELPHMFDKRLKMSRARATEYINQFPKEATNIILNFVAFVTGSLVTILVVLTVLGHENFLNFELTEGRTVLFYISTLGAVFTICKGSVSENDTVFDPEASLRYVAQFTHYLPNSWNGRFHTEEVKNEFCKLFNLRLILVLKEITSLIMLPYILYCRLPDVSEKVIDFFREFSVHVDGLGYVCTFAMFEFDSKDKPVRSQAANDDDDLKQEYYTADDDKMVKSYLYFLESYGNESVRKTGKEPAVDRISRRPGKKNLLRSAMMNNSMMDKSRGAQSTVRYPPQFRSPNLAESVYTKRQNIDLMEDTTAGLSTDTRNYLQTLNNSTLLGESFQHGFPVEDTTHHEEDADSEDDDEAGVLGLINQIYKHKEGVN | 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): 102069
Sequence Length: 889
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
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Q876N4 | MHKNNTTFLSRVFGINSRNIDVHNPLFADDSVIPLYDQNQSAYYDNAYSDYSSDEEDSKPRTSRQTDSNLHMTDHSGDGNDPFNQMDNSSRFSNSSSFHYNNTDQEDDNPELLLLQDEDSSLNRKNLDNSDFQSFAKKTFNQIPKIKFQLPKKEDYPTSHRQPPDIENQNGTLKSSVKKQIHFLDPMDKALWMWSNVSNLDTFLHQVYDYYTGNGFNCIMMNKFTELFTVVFIVWLFSFMGNCIDYDKLMNDRNVYQFSQVKIDKCYSKIGFFPQKLIYWLFFIGLCLKLYQIFLDYLVLKDMKLFFNLLLGLSDDELQTISWGLVVKRIMILRDKNINAIVSQNTDLTSRKRMNAHDIANRILRKENYMIAMYNKSILDLDIELPLIGKVQLLTNTLQWNLNIAILDYFFDSETGQINLPALKERNRHTISTELKKRLIFCGIINIVLAPILSIYFIMYYFLKFFYDFKTNPADISSREYSPYARWKLREFNELPHIFNRRLNISTESSNKYINQFPKETTTALLKFIMFISGSIVGVLVIVTILDPEFFLNFELTPGRTVLFYVSTLGAIFTICKNSIPDDTLVFDPEVSLRYLSQFTHYLPQEWEGKYHTEEVKNDFCKLYTLKLYLVGKEILSWLFLPYILCYKLPECADTISDFFREFSVHVDGLGYVCTFAMFQFNNQHNENGNANVHQNGNGNGGVPSAKSKSKKVPNPNRFTTKPSMRDMENDDKMIKSYMYFLESYGNDEIVQHQQALNRSLIYSTEISPTSGDDLNDSNILGLRQRNVATTGKRQNSIGNGLIYNGQNKRLSIGEAKTNVYSNPIASTVLDKDLQYKLANSYILNGMPGLNEANQPADRKNERKYSNDSPGVMKLVDKISQQHKA | 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). Essential for the formation of the sequestering membranes and assembly of the micropexophagy-specific membrane apparatus (MIPA) which mediates the fusion of the sequestering membranes and incorporation of the peroxisomes into the vacuole during micropexophagy .
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): 102597
Sequence Length: 885
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
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Q2HIE9 | MKEMSRYLWPKDSWGDKLRVLLAVGLLVGGKVLNVQVPFFFREIVDSLNVDIAATGGTVATVAGTMIFAYGASRIGAVVSQELRNAVFSSVAQKAIRRVATRTFGHLLNLDLNFHLSKQTGGLTRAIDRGTKGISFLLTSMVFHIVPTALEISMVCGILTYQFGWEFAAVTALTMSAYTAFTIWTTAWRTKFRRQANAADNKASTVAVDSLINYEAVKYFNNEKYEIGRYDKALHQYEKSSIKVATSLAFLNSGQNIIFSSALTIMMWLGAKGIVAGSLSVGDLVLINQLVFQLSVPLNFLGSVYRELRQSLLDMETLFNLQKVNLSIKEKPNAASLVLPKGGEIRFDNVSFGYYPDRPILNNLSVTIPAGKKVAVVGPSGCGKSTLLRLLFRSYDPQSGRIFIDDQDIRDVSLDSLRRSIGVVPQDTPLFNDTVELNIRYGNLDASREKVLEAARRAHIHDKIESWPHGYQTKVGERGLMISGGEKQRLAVSRLILKDPPLLFFDEATSALDTHTEQALMSNINEVLKEKRRTSVFVAHRLRTIYDADVIIVLKEGRVVEMGSHRELMEGNGLYTELWMAQEMSMHDQSLGRSEREAPVPVK | Function: Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export of Fe/S cluster precursors synthesized by NFS1 and other mitochondrial proteins (By similarity). Hydrolyzes ATP (By similarity). Binds glutathione and may function by transporting a glutathione-conjugated iron-sulfur compound (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67070
Sequence Length: 603
Subcellular Location: Mitochondrion inner membrane
EC: 7.-.-.-
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J9VWU3 | MGFGSCSRHALFTPAAFSGSFTTMTTSCFKRVYTAQIHGGDALGKRLPSVSSFSGQLPRHGLHRQSLAFFSTSHRRQTSPPPSPRTTSQSPTVPSKASTTPPTSLNTSKPIATESQDKTDWSIIVKLAGNIWPKNNPNVKFRVIGALTLLVAGKVLNVQVPFFFKTIVDSLNVPITESTTVWVLAGASIAGYGAARILTTLFGELRNAVFASVAQNAIRKVARETFEHLLNMDMKFHLERQTGGLTRAIDRGTKGISFILSSIVFHVIPTALEISMVCGILSWKFGWDFAAVTAITMLLYTWFTIKTTAWRTTFRKQANAADNKGATVAVDSLINYEAVKSFNNEKYEVAQYDTTLKAYEKASVKIATSLAALNSGQNFIFSSALTMMMLLGAQGIVKGTMTVGDLVLVNQLVFQLSLPLNFLGTVYRELRQSLIDMDVMFNLQSLNSAIKDTPTAKPLHLKGGEIEFRNVAFAYHPERPIFRDLSFKIPAGQKVAIVGPSGCGKSTVFRLLFRFYDSNSGQILIDGQDIKTVTLDSLRRSIGVVPQDTPLFHADILHNIRYGNLEATDEQVYEAARKAHVEGTIQRLPEKYATKVGERGLMISGGEKQRLAVARVLLKDPPVLFFDEATSALDVYTETELMRNINSILTGQGKTSVFIAHRLRTISDADLIIVLQDGYVAEQGTHEQLLAMPGGVYHRLWQAQLTESTQPTDEEIERQREELEVVDEKKKQ | Function: Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export of mitochondrial Fe/S cluster precursors synthesized by NFS1 and other mitochondrial proteins . Hydrolyzes ATP (By similarity). Binds glutathione and may function by transporting a glutathione-conjugated iron-sulfur compound (By similarity). Plays a role during copper stress, in a manner dependent on the copper metalloregulatory transcription factor CUF1 .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80771
Sequence Length: 732
Subcellular Location: Mitochondrion inner membrane
EC: 7.-.-.-
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Q5B1Q2 | MLRQAAQTRCWRTPARFVSHRPAFPRSNPVSAALGGTQFRKLSVKTQTDKNTLSDKKTAEADTSSSSSSAKSAAPSQQKTQNATTAQKNLLSESTVANKEQRKADWAIMREMAKYLWPKGDWGTKLRVGTALSLLVGAKVLNVEVPFYFKSIVDSMNVDFAAVGGTAYTVAGSMIIAYGATRIGATFFQELRNAVFASVAQKAIRKVARNVFEHLLRLDLNFHLSRQTGGLTRAIDRGTKGISFLLTSMVFHVVPTALEISLVCGILTHQYGIKFAAITATTMLAYSAFTIATTAWRTKFRKQANAADNRGATVAVDSLINYEAVKYFNNEKFEVARYDKALKAYEDASIKVTTSLAFLNSGQNMIFSSALAAMMYLAADGVATGSLTVGDLVMVNQLVFQLSVPLNFLGSVYRELRQSLLDMETLFNLQKVNVNIKEKPDAKPLELKQGGQIRFENVTFGYHPERPILKNASFTIPAGQKFAIVGPSGCGKSTILRLLFRYYDVQEGRILVDGQDIRHVTIESLRKAIGVVPQDTPLFNDTIEHNIRYGRLDASDEEVRKAARRAHIHELVERLPEGYRTAVGERGMMISGGEKQRLAISRLLLKDPQLLFFDEATSALDTYTEQALMQNINSILKEKGRTSVFVAHRLRTIYDCDQILVLKDGQVAELGSHRELLDLDGIYAELWSAQETSLAQDPEYERNAGLEGETAGEVEDKAPRQ | Function: Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export of Fe/S cluster precursors synthesized by nfs1 and other mitochondrial proteins (By similarity). Hydrolyzes ATP (By similarity). Binds glutathione and may function by transporting a glutathione-conjugated iron-sulfur compound (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 79800
Sequence Length: 721
Subcellular Location: Mitochondrion inner membrane
EC: 7.-.-.-
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Q7RX59 | MAPSIKLSTMATSLHRAHGTSALLRRPRLWAPRLSSIHATPTIANLRASFTTSSPRLFAPNGSAKDESKPAVSTVPKTTGRGPSDPLAAIDKTAQEQRKADWAIMKEMSKYLWPKGSWGDKARVLLAIGLLVGGKVLNVQVPFYFREIVDSLNIDFSTTGGSVTAVAGAMILGYGAARVGAVVSQELRNAVFASVAQKAIRKVARNTFEHLLNLDLSFHLSKQTGGLTRAIDRGTKGISFLLTSMVFHIVPTALEISMVCGILTYNFGWQYAALTALTMVSYTAFTILTTAWRTKFRRQANAADNKASTIAVDSLINYEAVKYFNNEAYEVGRYDKALAQYEKNSIKVATSLAFLNSGQNIIFSSALTVMMYMGAHGVATGQLTVGDLVLINQLVFQLSVPLNFLGSVYRELRQSLLDMETLFNLQKVNVTIKEQPNAKPLTLTRGGEIEFKDVTFGYHPESPILRDLSLTIPAGKKVAIVGPSGCGKSTLLRLLFRFYDPQKGAIYIDGQDIRSVTLESLRRAIGVVPQDTPLFNDTVEHNIRYGNLSATPEQVIEAAKAAHIHEKIISWRDGYNTKVGERGLMISGGEKQRLAVSRLILKDPPLLFFDEATSALDTHTEQALMENINAILKGLGQKGEKKTSLFVAHRLRTIYDSDLIIVLKEGRVAEQGTHRELMERNGVYAQLWRAQEMLMTEEGEVSKKGEKEEVGEKKEA | Function: Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export of Fe/S cluster precursors synthesized by egt-3 and other mitochondrial proteins (By similarity). Hydrolyzes ATP (By similarity). Binds glutathione and may function by transporting a glutathione-conjugated iron-sulfur compound (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 78758
Sequence Length: 716
Subcellular Location: Mitochondrion inner membrane
EC: 7.-.-.-
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Q2G506 | MPPETATNPKDARHDGWQTLKRFLPYLWPADNAVLRRRVVGAILMVLLGKATTLALPFAYKKAVDAMTLGGGAQPALTVALAFVLAYALGRFSGVLFDNLRNIVFERVGQDATRHLAENVFARLHKLSLRFHLARRTGEVTKVIERGTKSIDTMLYFLLFNIAPTVIELTAVIVIFWLNFGLGLVTATILAVIAYVWTTRTITEWRTHLREKMNRLDGQALARAVDSLLNYETVKYFGAESREEARYASAARAYADAAVKSENSLGLLNIAQALIVNLLMAGAMAWTVYGWSQGKLTVGDLVFVNTYLTQLFRPLDMLGMVYRTIRQGLIDMAEMFRLIDTHIEVADVPNAPALVVNRPSVTFDNVVFGYDRDREILHGLSFEVAAGSRVAIVGPSGAGKSTIARLLFRFYDPWEGRILIDGQDIAHVTQTSLRAALGIVPQDSVLFNDTIGYNIAYGRDGASRAEVDAAAKGAAIADFIARLPQGYDTEVGERGLKLSGGEKQRVAIARTLVKNPPILLFDEATSALDTRTEQDILSTMRAVASHRTTISIAHRLSTIADSDTILVLDQGRLAEQGSHLDLLRRDGLYAEMWARQAAESAEVSEAAE | Function: Mediates the ATP-dependent export of glutathione-conjugated substrates, such as heavy metal-glutathione conjugates. ATP hydrolysis is stimulated by glutathione binding. Protects cells against toxic heavy metal ions, such as silver and mercury ions. May also mediate the transport of glutathione-conjugated aromatic hydrocarbons, such as dinitrobenzene.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66867
Sequence Length: 608
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
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O14286 | MLERCPWKLISSPRNIPARSFLNSRGTYLVLRKSNILPLQHILRFSNFASKQCFPLRNGNNSASKALWNNKSKEKEPLNTSVKLASDVPDDKNVTGQMIVKDMLQYIWPKGKTNLKVRVVSALALLVAAKILNVQVPFYFKSIIDTMNTTLVQEVGALWSTVGAVVLGYGFARIFSTVFQELRNSVFAIVSQSAIRSVSSNVYQHLLNLDMNFHLSKQTGSITRAMDRGTKGISFILSSMVLHIIPITLEIAMVSGILTYKYGPSFSAIAATTVALYALFTVRTTSWRTVFRRQANAADSKASAAAIESLINYEAVKTFNNESYEMSRYEKHLSAYEKANVKVASSLAFLNSGQAIIFSTALTLMMYMGCRGIVTSNLTVGDLVMINQLVFQLSIPLNFLGSVYREMRQAFTDMEQLFSLKRINIQVKEAPDARDLVLKGGSIQFDNVHFSYNPNRPILNGCSFNIPAGAKVAFVGASGCGKSTILRLLFRFYDTDSGKILIDNQRLDQITLNSLRKAIGVVPQDTPLFNDTILYNIGYGNPKASNDEIVEAAKKAKIHDIIESFPEGYQTKVGERGLMISGGEKQRLAVSRLLLKNPEILFFDEATSALDTNTERALLRNINDLIKGSHKTSVFIAHRLRTIKDCDIIFVLEKGRVVEQGSHEQLMAKNSVYTSMWHSQESPFGESNKSGDA | Function: Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export of Fe/S cluster precursors synthesized by nfs1 and other mitochondrial proteins . Hydrolyzes ATP (By similarity). Binds glutathione and may function by transporting a glutathione-conjugated iron-sulfur compound (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 77056
Sequence Length: 693
Subcellular Location: Mitochondrion inner membrane
EC: 7.-.-.-
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A6ZYV0 | MLKCICRVYSQPLAQMVTSPLFKHMGSAGTYTILPITNLRHLSTKNCPLKIKSNRSEPLQFGDFERQVPCSRKSGSSKNVQKRLYELRQLKTVLSETFGVTEYASFFESLRNALHINNCSENEKKKLLYDIILHQHELYPEVARKIGFYLPGEVHRWFWYHIPKSESFNHYLFLLKSDVLLFTSNYCTRFTNRLIKGTEMERQLATFQIFLHDETNIKFIMEKVLKLHTFDSLIALVNGLVKAKNFRFIKVFIQALLQKLEQHCYSGKDGAKQKNLRYVKFNNTLLYYLLKSGNVELFIKTFQEELKFIVSSGLLNHIDGNEHILNFPIHHYLNLLRISNRQEELFNVISCLQSSPLMKYKLFKEFLMGELIASFQAFRDPKLVCKYLLSSYSSKASANILNALGIWGWLYHSKSTTLTAPTLARELKNKNNILPNTMRIGSPVTVPILTELYRSLLSSSSVSLESGQFKNCLLDLYYKYKSFLSEEAHKYRYWRNDTGILNVFLNYIRFQAREPRLAYNVLLDFYSQPFAKKVVLTTTLCPFSIVAYKNHTLTQAELSELLQVMHKNGVPLTFKFCSAMVMHYVKMRDEKGARSWYNKILFGGFEIRHMALIQIIKDQGWPFPKNFDETLLTELVENNNIKEPTDSTLFTDEDMFEEDGKPRFNDDDVNKCTNIIRETLKSLN | Function: Translation factor specific for subunit 6 of the mitochondrial ATPase. Required for assembly of the CF(0) component of the ATPase (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 79756
Sequence Length: 684
Subcellular Location: Mitochondrion inner membrane
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Q9SRP6 | MEDAAAPNSGSEFNPGARRGKSIDECQDMIRRSFRNPIVKFLMEQMEKSGCRVGDNFVKAVVCTGPVAGGYTKGRGITVCSNYLTIQDEVNQVVIHELIHAYDECRAKNLDWTNCAHHACSEIRAGHLSGDCHFKRELLRGFIKLRGHEQECIKRRVLKSLRGNPYCSEVAAKDAMEAVWDTCYNDTKPFDRAP | Function: Has a dual role in the assembly of mitochondrial ATPase (By similarity). Acts as a protease that removes the N-terminal 10 residues of mitochondrial ATPase CF(0) subunit 6 (ATP6) at the intermembrane space side (By similarity). Also involved in the correct assembly of the membrane-embedded ATPase CF(0) particle, probably mediating association of ATP6 with the subunit 9 ring (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21798
Sequence Length: 194
Subcellular Location: Mitochondrion inner membrane
EC: 3.4.24.-
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A6SSS5 | MSSSEGNKPPLVPDSTKESEPQFDPTARTRNWFSILLGTMPPSHQILYREDQYARHEKRDCDRCEEWRDYNLKYSPIVIFMQKNIRDLNGKLDADNIRCRRCPTRITEDGKTVRQGGGFSPEHGIQLCANEMRDSKHVEDTLAHEMVHAWDHLRWKVDWGDLRHAACSEIRAASLSGECRWAREFWTRNNYRVTQQHQDCVRRRAVKSVLARPWCKDDVQAVRVVNEVWDSCYSDTRPFDEIYK | Function: Has a dual role in the assembly of mitochondrial ATPase. Acts as a protease that removes N-terminal residues of mitochondrial ATPase CF(0) subunit 6 at the intermembrane space side. Also involved in the correct assembly of the membrane-embedded ATPase CF(0) particle, probably mediating association of subunit 6 with the subunit 9 ring (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28756
Sequence Length: 244
Subcellular Location: Mitochondrion inner membrane
EC: 3.4.24.-
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Q2H8S7 | MATPPPPQLSSTSTQPPSPSSASSNPQQPSPPKTQPPLPRFLDNDPARTGYDPTVKWWLNYFRIMTGQVTREGVEHYREDRYKANEARDCARCEADRAYLFAYSPTIRFLRDKVAALNGTLDETNVVCRRCPARVAEDGRVVRQGGGFSPEHGILICANEMRDRSHLEDTLAHEMVHAWDHLRWKVDWSGGGNLRHAACTEIRASMLSGECRWTRETMTRGNWTLTQQFQNCVRMRAIQSVMARPTCRDDVHATKVVNEVWDSCFSDKRPFEEVYR | Function: Has a dual role in the assembly of mitochondrial ATPase. Acts as a protease that removes N-terminal residues of mitochondrial ATPase CF(0) subunit 6 at the intermembrane space side. Also involved in the correct assembly of the membrane-embedded ATPase CF(0) particle, probably mediating association of subunit 6 with the subunit 9 ring (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31556
Sequence Length: 276
Subcellular Location: Mitochondrion inner membrane
EC: 3.4.24.-
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Q1E910 | MAEAASSGSNSTSPPKDNGYIPGDDAWTICRNLWRGLTGKMTQEGMEQFRVARDVRNEKEDCKRCEDQRDYLLQYSPLIRFLQDNIQQLGGNISKHNIFCRRCKNRQAGGFDPDYGIQICANEMRNQGHLEDTLAHEMIHAYDHMRFKVDWDDNLRHAACAEIRASNLSGECRWMREFFSRGQWKFAQHHQECVRRRAILSVQARPACKDEQHATQVVNEVWDSCFRDTRPFDEIYR | Function: Has a dual role in the assembly of mitochondrial ATPase. Acts as a protease that removes N-terminal residues of mitochondrial ATPase CF(0) subunit 6 at the intermembrane space side. Also involved in the correct assembly of the membrane-embedded ATPase CF(0) particle, probably mediating association of subunit 6 with the subunit 9 ring (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27737
Sequence Length: 237
Subcellular Location: Mitochondrion inner membrane
EC: 3.4.24.-
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P0CQ26 | MPENPSSSPTEPPEQSAAFEKWRSGLAQFTGLGLSESEKAERERLKAQGKLAKDWDKCEGWKRDLMNYSPMITFLLNHLKLAGCPFPSSAMQCHPCPENRAGGFSPDHGILLCQDRFFNKKHMEDTLAHELVHAFDHCRFKVDWGNLRHHACSEIRAANLSGDCRFTREVKRGFYAFNKQHQACVKRRAILSVLANPACTSPEMAEKAVNEVWESCFTDTRPFDEIY | Function: Has a dual role in the assembly of mitochondrial ATPase. Acts as a protease that removes N-terminal residues of mitochondrial ATPase CF(0) subunit 6 at the intermembrane space side. Also involved in the correct assembly of the membrane-embedded ATPase CF(0) particle, probably mediating association of subunit 6 with the subunit 9 ring (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25850
Sequence Length: 227
Subcellular Location: Mitochondrion inner membrane
EC: 3.4.24.-
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P93298 | MRRIFLFDENSLNSSSTIDTSSASTIDTSFASQCTNFSSGQASGTQDTHAGIFEDCPGLNPNDERVVELQCEIREKCEALTQDPEMGLILGEALHAESDNVPFLQSIADDLTQNGVSGEAFQEALNIVGQAAASPLDQFEIVPLIPMHIGNFYFSFTNSSLFMLLTLSFFLLLIHFVTKKGGGNLVPNAWQSLVELLYDFVLNLVKEQIGGLSGNVKQMFFPCILVTFLFLLFCNLQGMIPYSFTVTSHFLITLALSFSIFIGITIVGFQRHGLHFFSFLLPAGVPLPLAPFLVLLELISYCFRALSLGIRLFANMMAGHSLVKILSGFAWTMLCMNDIFYFIGALGPLFIVLALTGLELGVAILQAYVFTILICIYLNDAINLH | 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): 42342
Sequence Length: 385
Subcellular Location: Mitochondrion inner membrane
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B2KEW6 | MIEEILTHHIIDHKLTYKLFGVIPLSSNLITLFCITIGVFILFTLIAKFRRPVLLMTAIEGLVVFIRDEIVVANFGEHGKKLTPYFCTLFIFLLFSNSLGMIPQMRTITGSISVTIGMALTSLSLIIFLGVKQNGLLGYLKHFVPEGTPWFLAPLLFFLEILGLFTKTAALALRLFANMIAGHMVIICFICLIFIMTAINKYAGIFTAIPSTGLSLFVNLLEVLVILIQTYVFTLLTAIFAGEAYAHH | 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): 27595
Sequence Length: 248
Subcellular Location: Cell membrane
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Q830Z9 | MEEKKLLFNIGPIWFDGTIVLMVLLTCIIVFAFVYACTRNMKLRPKGKQTVIEWLVDFIRGIITDNLPRKEVSNFHLMAFTLFMFVLVSNILGLVTKIVVGDDLSVWKSPTADPIVTLTLAMMMIVLTHFFGMKRFGFKGYLVNSYLRPVGFLLPVKLMEEFTNLLTLGLRLYGNIFAGEVLLGLIAGTVASVGLWVIPLAIPLEMIWVAFSIFIGCIQAFIFVTLSMVYMSHKIETEE | 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): 27002
Sequence Length: 239
Subcellular Location: Cell membrane
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Q0RDA8 | MEVFVVPVLADEGFEGPTKEVFQTPHWFDVGIGSVNLYLNKATALTIFAALFVGVIFWLGFRRAKIIPRGIQNLCESAYDFVDLQIARGVIGEKGARYTPYLLVLFSFVLVSNVLAIIPAAQFPATSRIAVPMVLAVVTWVMFIYAGIKSNGAGAYFKEMIDPAPTAPLAIRLLLGPIEILSTLIVRPFTLAIRLFANMFAGHLLLLVFSLGADYLLPKPPFVFGVASLLVAIVLTAFELVIDALQAYIITILTAAYIGGAMAHGEHEVAPSEELAEHAPVGVPAAAHA | 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): 31110
Sequence Length: 289
Subcellular Location: Cell membrane
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P21535 | MFITSPLEQFELNNYFGFYLFNYHFDFSNFGFYLGLSALIAISLAIINLTPYGSGAKIVPQKFGIAMEAIYFTMLNLVENQIHSSKTVSGQSYFPFIWSLFVLILFSNLLRLIPYGYATTAQLIFTLGLSISILIGATILGLQQHKAKVFGLFLPSGTPTPLIPLLVLIEFVSYIARGLSLGIRLGANIIAGHLTMSILGGLIFTFMGLNLITFIIGFLPITVLVAISLLEFGIAFIQAYVFAILTCGFINDSLNLH | 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.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28294
Sequence Length: 257
Subcellular Location: Mitochondrion inner membrane
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O79406 | MIMSFFDQFLSPSFLGIPLIALAISIPWLMFPTPTNRWLNNRLLTLQAWFINRFIYQLMQPMNLGGHKWAILFTALMLFLITINLLGLLPYTFTPTTQLSLNMAFALPLWLTTVLIGMFNQPTIALGHLLPEGTPTPLVPVLIIIETISLFIRPLALGVRLTANLTAGHLLMQLIATAAFVLLTMMPTVALLTSLVLFLLTILEVAVAMIQAYVFVLLLSLYLQENV | 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.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25382
Sequence Length: 227
Subcellular Location: Mitochondrion inner membrane
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Q7SI16 | MAARNAALKVDWAKITTSLGLRGQTAASLQAFKKRNDDARRKLQQLSELPTTVDFAAYRSTLKNQAIVNEIEKRFTSFKPATYDVNRQLKAIEAFEVEAIKNAEATKTKVDLELKDLEKTLTNIETARPFDELTVDEVAAAEPSIDEKTSKLVSKGRWSVPGYKERFGDLSVL | 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. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/atp6 static relative to the rotary elements (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19365
Sequence Length: 173
Subcellular Location: Mitochondrion inner membrane
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O94390 | MSKVASAAGKAIDWASVASKLKLDAATASAIANFRSRHAQAVAKLGTLREQATTVDFATYRSVLANKEIVNRIESSMKSFKPVKIDLNSQLKAINAFEAKASEGAKKNVELVKAELQNLSATLKNIEQARPTEEITIEDMKQAVPEIEKIVETMVTKGKWVIPGYREKFGDLSIM | 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. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19138
Sequence Length: 175
Subcellular Location: Mitochondrion inner membrane
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Q6CFH9 | MSVAAARSSAVKVDWGKIVSSLGLTGATVSSLQAFRKRHEEAKKNAYELQNQPTTVDFAHYRKVLKNQKVVDEIEQHFKSFKPVTYDVSKQLKTIDAFEAKAIEDAKATEGKVNQEIGDLQKTLENIESARPFDQLSVDDVFKARPDLEKKIEEMVKKGRWSVPGYNEKFGSVVLM | 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 ATP synthases 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 . Part of the complex F(0) domain and the peripheral stalk, which acts as a stator to hold the catalytic alpha/ATP1(3)beta/ATP2(3) subcomplex and subunit a/ATP6 static relative to the rotary elements .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19821
Sequence Length: 176
Subcellular Location: Mitochondrion inner membrane
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Q0C0Z8 | MDISPAEISGILKSQIENFGVEAEVSDVGQVLSVGDGIARVYGLDSVQAGELVEFNGGIKGMALNLEKDNVGVVIFGEDRSIKEGDTVKRTSEIVAAPVGKALLGRVVNALGEPIDGKGPLKDVAARSQVDVKAPGIIPRKSVHEPMMTGIKAIDGMIPVGRGQRELIIGDRQTGKTAICIDTILNQKPTNDAAKSDKDKLFCVYVAIGQKRSTVAQVVKVLEERGALDYTIVVSATASESAPLQYLAPFTGCTMGEWFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNDDNGNGSLTALPVIETQANDVSAYIPTNVISITDGQIFLETDLFNSGIRPAVNVGLSVSRVGSAAQTKAMKKVAGSMKGELAQYREMAAFAKFGSDLDAATQRLLNRGARLTELLKQPQYSPLLMEEQVVIIYAGTRGYLDKVALKDVTRYEKELLVHMRGAKKELLAKLREKKELTSEIEDEIKKALDDFTSKFA | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55417
Sequence Length: 511
Subcellular Location: Cell inner membrane
EC: 7.1.2.2
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Q5FKY2 | MSIKAEEISSLIKQQLEHYDDKLDINEVGVVTYVGDGIARAHGLDDVLSGELLKFDNGSFGIAQNLESNDVGIIILGQFDNIREGDRVQRTGRIMEVPVGDALIGRVVNPLGQPVDGLGEIKSDKTRPIEAKAPGVMDRQSVNQPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSLAIDTILNQKGQDVICIYVAIGQKESTVRTQVETLKRFGAMDYTIVVEAGPSEPAPMLYIAPYAGTAMGEEFMYNGKDVLIVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKLSDKLGGGSLTALPIIQTEAGDISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVSRVGGNAQIKAMKKVAGTLRTDLTAYRELESFAQFGSDLDQATQAKLNRGQRTVEVLKQPLHDPIPVEKQVLILYALTHGYLDAIPVEDISRFQNELFDNFDSSHADLLKTIRETGKLPDDKELSAAIEEFSESFTPSEK | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54932
Sequence Length: 503
Subcellular Location: Cell membrane
EC: 7.1.2.2
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Q6YXK3 | MVKIRPDEISSIIRKQIEDYSQEIKVVNVGTVLQVGDGIARIYGLDKVMAGELVEFEDNSIGIALNLESDNVGVVLMGDGLTIQEGSSVKATGKIAQIPVSDGYLGRVVNALAQPIDGKGQIPASEFRLIESSAPGIISRRSVYEPMQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQKGQNVICVYVAIGQKASSVAQVVNTFEERGALEYTIVVAEAANSPATLQYLAPYTGAALAEYFMYRKQHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQSQSSPLAVEEQVATIYTGVNGYLDVLEVDQVKKFLVQLREYLTTNKPQFAEIIRSTKVFTEQAEGILKEAIKEHTELFLLQEDK | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55273
Sequence Length: 507
Subcellular Location: Plastid
EC: 7.1.2.2
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C0HK51 | ATAKAAPTEVSSILESKIRGVSDEANLDETGRVLSVGDGIARVFGLNNCQAEELVEFASGVKGMALNLEPGQVGIVLFGSDREVKEGEIVKRTGKIVDVPIGPGMLGRVVDALGNPIDGKGPIEATGYAIAQLKAPGILPRRSVFEPMQTGLKAVDALVPIGRGQRELIIGDRQTGKTAVALDTILNQKRWNDGNDESKKLYCVYVAVGQKRSTVAQLVQTLEQNDAMKYSIVVAATASEAAPLQYLAPFTACAIAEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSDANGGGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLSRGERLTQLLKQKQYSPQASEEQVPVIYAGVNGFLDNIPIERIPEFEEQFIAYLKANEGDILEAIRTKGELSSELLDKLKSATETFVATF | 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 ATP synthases 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 (By similarity). Subunits alpha/ATP1 and beta/ATP2 form the catalytic core in F(1) (By similarity). Rotation of the central stalk against the surrounding alpha/ATP1(3)beta/ATP2(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta/ATP2 subunits (By similarity). Subunit alpha/ATP1 does not bear the catalytic high-affinity ATP-binding sites (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54950
Sequence Length: 510
Subcellular Location: Mitochondrion inner membrane
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P84582 | IVNTGTVLQVGDGIARIAQIPVSEAYLGRVINALAKPIDGRLIESPAPGIISRASSVAQVVNALQERKFLVELRTQFQEIISSTKLRNQADQTITLIR | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 10621
Sequence Length: 98
Subcellular Location: Plastid
EC: 7.1.2.2
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P17674 | MSIKAEEISALIKQQIENYQSEIKVSDVGTVIQVGDGIARAHGLDNVMAGELVEFSNGVMGMAQNLEENNVGIIILGPYTEIREGDEVRRTGRIMEVPVGEQLIGRVVNSLGQPVDGLGPVETTKTRPIEGAAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTSVAIDTILNQKDQDMVCIYVAIGQKESTVRNVVETLRKHGALDYTIVVTASASQPAPLLFLAPYAGVTMGEEFMYNGKHVLVIYDDLTKQASAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDAKGGGSLTALPFIETQAGDVSAYIPTNVISITDGQIFLQSDLFFSGVRPAINAGLSVSRVGGSAQIKAMKKVAGTLRLDLASYRELESFAQFGSDLDQATQAKLNRGARTVEILKQGLHKPLRVEKQVAVLYALTKGFLDDVPVSDITRFEDEYLTWLESNRKEVLESIRTTGGLPEAGLFESALEEFKKTFIASE | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54603
Sequence Length: 502
Subcellular Location: Cell membrane
EC: 7.1.2.2
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A3DIM9 | MATENVGTVVQIIGPVIDIRFERGKLPSIYNAIKINSEGIDIVAEVMQYTGNDTVRCVSMNSTDGLKRGMKAVDTGEPIKVPVGKEVLGRVFNVLGEPIDGKGDVKATTYLPIHREAPGLDEQKPVTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIRNIATEHGGYSVFTGVGERSREGNDLWNEMNESGVIEKTALVFGQMNEPPGSRMRVGLTGLTMAEYFRDELGQDVLLFIDNIFRFIQAGSEVSALLGRIPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFTHLDATTVLSRHIVEQGIYPAVDPLDSTSRVLDRRIVGDEHYTVARKVQEILQRYKELQDIIAILGLDELSEEDKLIVFRARKIQRFLSQPFFVAEAYTGYKGKFVRIKDTIRGFKEIIEGKMDDIPEAAFYMAGTIDEVYERAKKM | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 51013
Sequence Length: 464
Subcellular Location: Cell membrane
EC: 7.1.2.2
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P50002 | MAQNIGKVVQVIGPVVDVKFQKDKLPKLNNAVNIELNGHTLVIEVAQQLGDDIVRCIAMDSTDGLMRNQEAVDTGSAIQVPVGKATLGRMFNVLGEPIDGKPFDTKDVVMHPIHRHPPSFEEQQTQPEMFETGIKVVDLICPYVRGGKIGLFGGAGVGKTVLIQELINNIATQHGGLSVFAGVGERTREGNDLYYEMMESGVINKTALCFGQMNEPPGARMRIALAGLTMAEYFRDDEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTSKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRAITEKGIYPAVDPLDSTSRILDPKIVGQEHYETAREVQEILQRYKELQDIIAILGMDELSDADKITVSRARKVERFLSQPFNVAEQFTGTAGVYVTIGDTIKGFKEILEGQHDDLPESAFLLVGTIEDAVVKAKKIKG | Function: Produces ATP from ADP in the presence of a sodium ion gradient across the membrane. The beta chain is the catalytic subunit.
Catalytic Activity: ATP + H2O + 4 Na(+)(in) = ADP + H(+) + 4 Na(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 50663
Sequence Length: 466
Subcellular Location: Cell membrane
EC: 7.2.2.1
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Q4FQ37 | MSSGRIVQIIGAVLDVEFNRNEVPRIYDALQVDGTETTLEVQQQLGDGIVRTIAMGSTEGLKRNLSVTNTGGPISVPVGVGTLGRIMDVLGRPIDEEGPVEADERWSIHREAPSYAEQSNSTELLETGIKVIDLLCPFAKGGKVGLFGGAGVGKTVNMMELINNIALKHEGLSVFAGVGERTREGNDFYHEMQEAGVVNTEDFSKSKVAMVYGQMNEPPGNRLRVALSGLTMAEYFRDTKDPATGKGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGMLQERITSTQSGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRDIASQGIYPAVDPLDSTSRQLDPLVIGEEHYNVARGVQEVLQRYKELKDIIAILGMDELSEEDKLVVYRARKIQRFLSQPFHVAEVFTGAPGKYVPLRDTIASFKAIIAGEYDSLPEQAFYMAGGIDEVVAKAEKMKSSAA | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 51731
Sequence Length: 477
Subcellular Location: Cell inner membrane
EC: 7.1.2.2
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A0T0R6 | MVETTNKGYVCQIIGPVLDIEFPGGKLPPIYSAIKIETADGIGNIVEVQQLLGDNKVRAVSMRSTDGLKRGVEAVDLGAPITVPVGVPTLGRIFNVIGEPVDEQGDVVVDQTLPIHRDAPAFTELETKPSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYEEMKESGVINSSNFAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTTQGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLDSTSTMLQPGIVSEVHYETAETVKETLQRYKELQDIIAILGIDELSEEDRLVVARARKVERFLSQPFFVAEIFTGSPGKYVSLEETIKGFTMILNGELDDLPEQSFYLVGNIDEAIAKAETLK | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 51142
Sequence Length: 474
Subcellular Location: Plastid
EC: 7.1.2.2
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Q89B42 | MSSTKDELQLYAKAIYNCAISNHQSLDHWKTMLQLMANILNNEIIKNLISKAYFSQHVISLFIDLCCNKVNQYGINLIKILAENKRLMLLEKLYKEFINLCELYQGVVNITVISAHKLNEEYISKINIMLKKRFFKKINVTYVIDESIIGGLIIKFCDTVINASIHSRLEKLLNILQY | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20691
Sequence Length: 178
Subcellular Location: Cell membrane
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Q6B8Q9 | MSSQGFMSKIALPYAEALVESASSASALDQINQDLSLISEILNQSQELKTFFYNPLITTEIKKNVVSSLFTNQVHSLVIRFLLVLIDRRRIALLDVIISKYLELVYQLQSTVIAEVLTPVLLTDVQQSALINKIKDMTNSKTVKLVITIKPMLIAGFIIKIGSKTIDTSLYGRLKHISAYLNAVS | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20573
Sequence Length: 185
Subcellular Location: Plastid
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O78476 | MIAMNNKLAQPYAMAFLEFSLDAKQTLDTTIADLTQIKTILHDSVDLSKTLSNPLLSIKAKKEVIKAIFEPNISKNTLKFLLVLCDRGRSANLSSIIDNTIELAYKKASIEIAYVTTATAFSSNQQEALVEKLKSMTSTEQIKLNITVDKTLIGGFKVQIGSKVIDTSIQGQLRQLASHLGSSAI | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20219
Sequence Length: 185
Subcellular Location: Plastid
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Q9K6H2 | MSNHAVANRYAVALFELAQEKGLHESFVSELELIKAVFQDTPELMQFLTHPKTELTQKRELLEKTFKGKVNDTIFNTLVVLVERKRIDLIIPVVQKFKSLSYDAQKIAEAFVYSAKPLSEAEKDQLSVLFAKKVGKAKLLIENIVDPSIIGGLKIRIGDRIYDGSIKGQLDVLHRELVSGPRS | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20605
Sequence Length: 183
Subcellular Location: Cell membrane
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B8CZ13 | MINNEVSRKYSSALLEVALESDNLSRFKEELEGISKALKQYDDLKKILYHPRVLPDDKKEVIHQVFSDKVSEPVFNFLNLIVDKRREVYLDFIIRDFIKQANRKEGLVKIEVVSAIELSEKQREQLKNKLKKALNKKIELKTKIDPGIIGGIIIKIGDRLIDGSIKHQLDSIKESIEKIPVTELGVIQNES | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21978
Sequence Length: 191
Subcellular Location: Cell inner membrane
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Q7VJ24 | MFNIISKKYTQALVDSGSNLDETLSILKGLSLALKDKRNADIIASPFLSKTQKEQFLLESVGKVDMKLQNFFRLLAQSDRILLIPYISDELERRLLARKKEYAATLTAKESLDTKTLEKIQDSLAKKLGVKLSIKQRLSEVDGIKLSVEDLGIEVSFSKERFSNDLKHHILKAL | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19695
Sequence Length: 174
Subcellular Location: Cell inner membrane
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B0TI53 | MLTGAVARRYAQALLEIGIQTKTLDALEGELGRFVEMIGHPELQRFLFHPSIVVAEKKDLVGRLLATGAFSETARAFILLVIDRRRESYFADIFREFVRLANKVRNIEEARVTSAVELAPEQVERLRSQLAAATGKAIVLRMAVDPDLIGGLVVAFGDRIIDGSVAGKIRDLRESLLRSPLPSLS | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20424
Sequence Length: 185
Subcellular Location: Cell membrane
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B2XT89 | MSTNSRAGDAYAYALLKVLFNETKDFDSFSDLVGDVLDFVTIFNTCPSIEEFFANPTYSPIQKKQFLYDFFGRSLNPILMSFLYLLCDTKRIIYISSIISIFLETLLKNTNSHIVEVQTPTGKDYKLDISKLETTLSGWFNKIQKNNDEAVNFLNFDESLVIFTVKEVPGLLGGFRLNFVTDSKVIDFSIAGKIKRLAAVLNY | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 23059
Sequence Length: 203
Subcellular Location: Plastid
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Q0I5X0 | MSELTTIARPYAKAVFDFAVEQSEKDKSTVEKWANMLEFLSELIRHDKVQTYLTSTSSTFKLADTVISICSEQLDQYGQNLVRLMAENKRLSVLPAVFNEFKSYVEEYKSLSQVEVISAQQLNDVQQQKIITAMEKRLARKVILNCRIDSSLIAGAIIRTNDFVIDGSCRGQINRLANELRL | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20717
Sequence Length: 182
Subcellular Location: Cell inner membrane
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A5V3X2 | MENSGGIQASLSGRYATALFGLARDEKAIDAVSASLQSLKAALTESDDFRRLTTSPLVSRDEAMKAVAATAASLGIDPLTTKFLGVLAQNRRLGQLGAVIRSFGTLSARHRGETTAEVTSAHPLTATQVKALKAKLKTQLDRDVAVDLTVDPSILGGLIVKIGSRQIDGSIRSKLNSLAIAMKG | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19272
Sequence Length: 184
Subcellular Location: Cell inner membrane
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Q7UFB8 | MVKLPSLKFLRRSTDETPNVSETASHSTVLDVGAEKLGKTYARALLAATQADGSTDAVVSDLNAICDEALLHNPKLQLAFQSPQIDADEKCRVVDRLFGGNSHPTLIKLMKVMAKRGRLGYLVAVRDAAVDLFDEAAGRVVAEVRTAVPMTEQLRGEVTQQLSSRFGKTVRLRESVDTELIGGMVIRVGDTVFDSSVASRLDKLGKSAAAGFARQLIEQSDRFSSSS | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24508
Sequence Length: 227
Subcellular Location: Cell inner membrane
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P72244 | MSEPASISAAIAGRYATAIFDLAQEAKGIDALSADVDALTAALAGSAELRDLISSPVYTREEQGDAIAAVAAKMGLSAPLANGLKLMATKRRLFALPQLLKGLAAAIAEAKGEMTADVTSATALSAAQAEKLAATLAKQTGKTVKLNVAVDESLIGGMIVKLGSRMIDTTVKAKLASLQNAMKEVG | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18913
Sequence Length: 186
Subcellular Location: Cellular chromatophore membrane
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Q2RV21 | MSSHKAGVTGVAERYATALYELAEDRGALDQVSADLRSLKAMLDESGDLRRVIASPVIGRDDQRKALTALAEKAGFHEIVRNFLGVVAAKHRSFAVPGMIGAFLERLAARRGEVTARIVSATALTSAQKSALTTALNKATGNTVTIDASVDPALLGGMVVRVGSRMVDSSLSTKLKRLQLAMKGVG | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19576
Sequence Length: 186
Subcellular Location: Cell inner membrane
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A7IH28 | MAAQGARHGLQVRERCGVADTIVSGMAGRYATALFELATEAGAVDSVKADLDRLSALIAESADLARLVKSPVFSAEEQLKAISAVLDQAGISGLAGNFVRRVAQNRRLFALPRMVADYASLVAAMRGETTAQVTVPAPLSDAHFFALKDALAQQTGKDVILDVTVDPSILGGLIVKLGSRMVDASLKTKLNSIRHAMKEVR | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21243
Sequence Length: 201
Subcellular Location: Cell inner membrane
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Q6C877 | MFSVARTAIRGAARPAVRIARRGYAETASVDKLRLTLALPHQSIYNQKEVTQVNIPSTAGELGILANHVPTIQQLKPGVVEVIETNGETKSYFISGGFATVQPDSELSVNSIEAFQAEDFSPEAIKSLTAEAQKNAQSADEAVAAEAEIELEVLEALAHFAK | 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 ATP synthases 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 . Part of the complex F(1) domain and the central stalk which is part of the complex rotary element . Rotation of the central stalk against the surrounding alpha/ATP1(3)beta/ATP2(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta/ATP2 subunits .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17349
Sequence Length: 162
Subcellular Location: Mitochondrion inner membrane
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B2KEX4 | MKKLTFSFISPERPIVQNQEADFVALPAFEGEMGVLPGHVNSVVILMPGFVRFKNNGEEKEFAIIDGFAEVFKDHIDVFASEASLSEEKQSEEQKQRLERAKKALSSQDADIDIELAEIQLKTQILKMKMKKRKM | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15359
Sequence Length: 135
Subcellular Location: Cell membrane
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B1H0B4 | MNKFEVEILSPEGIVFKGATPSVSFPTTRGIITVLSGHINLITKLNSGEIIIEATDGTKKIIVSGGFIEIVNNNVNVVAEFAAHSDEISRQKIKQAIDHAKDMKNKRKEFVNMYAIESQLKKSAVDLKSGLEIKRKKI | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15223
Sequence Length: 138
Subcellular Location: Cell inner membrane
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P29709 | MATFKLEVVTPLKKVLDRDAEMVIMRTIEGDMGVMADHAPFVAELAVGEMKIKSANGEEAYFVSGGFLEISKEKTMILADEAIDVKEIDVERAKREAEIAKETLVKLKEDKDIAVTQKSLQEALTKVRIAEQYMHHL | Function: Produces ATP from ADP in the presence of a sodium gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15351
Sequence Length: 137
Subcellular Location: Cell inner membrane
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Q88BX5 | MAMTVHCDIVSAEGEIFSGLVEMVVAHGNLGDLGIAPGHAPLITNLKPGPITLTKQGGAHEVFYISGGFLEVQPNMVKVLADTVQRAADLDEAQAQEALKAAENALNLKGADFDYGAAAARLAEAAAQLRTVQQMRKGK | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14538
Sequence Length: 139
Subcellular Location: Cell inner membrane
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Q0AUD4 | MAESTFMLEVVTPERILYRDEIQFMVAPGIEGELGIMKNHAPLVAALNIGVLRYQTSTGVDKRMAISGGFMEVIDNGTRVLAETAEHGSEIDVLRAKAAKERAEKRLEVRSEEINHARAKMALQRAIARIRASEKPL | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15202
Sequence Length: 137
Subcellular Location: Cell membrane
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A0T0R7 | MVMDIRVLTPDRVICSTTADEVILPGLTGQVGVLDGHATLITALDTGLLRIKLADKWTPIILCGGLAEIDRNRVTVLVNDVEELVAVELSEATKELEKATSAIENAETSKARLDASVELKKATARLEGINYLS | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14284
Sequence Length: 133
Subcellular Location: Plastid
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Q47M83 | MAVSKKLFVELVTPERELWAGEGDMVIAKTVEGEIGIQPGHVPVLALLAPGSVVRVLGARESGEVRAAVHGGFMSVTLSDRVSILAEIAELAEEIDVERARAALKSAEREALGDAEMRARVARARGRLRAAKAEEAA | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14537
Sequence Length: 137
Subcellular Location: Cell membrane
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Q9X1U5 | MKVKIVTPYGIVYDRESDFISFRTVEGSMGILPRRAPIVTQLSVCDVKIKSGDDEYHLKVAGGFLLCDGKDVIIITEEAGREEDISPDRFMEARERVERVRRFFQSSL | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12329
Sequence Length: 108
Subcellular Location: Cell inner membrane
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Q8DLG7 | MVMTVRVIAPDKTVWDAPAEEVILPSTTGQLGILSNHAPLLTALETGVMRVRQDREWVAIALMGGFAEVENNEVTILVNGAERGDTIDLEKAKAEFAAAQAALAQAEQGESKQAKIQATQAFRRARARLQAAGGVVEI | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14750
Sequence Length: 138
Subcellular Location: Cellular thylakoid membrane
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B5YI25 | MENKLKLEVITPYGEVINEEVDEVYTTGAEGDFGVFPGHCAFMTAIRIGSLSYKKDGQMHYLFVNRGYCEVLNDRVLVLVGSAERVEEIDVERAKAALARAEERLRKAQAGETDIDLARAQAALERATIRIQLATKLIPR | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15627
Sequence Length: 140
Subcellular Location: Cell inner membrane
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Q7UFB9 | MKRLLAISSLTLLASLVLLVVSPARSLAAQDEVTVVDALADAADSEDGDHDHDHEGDDHGHDEAAGDEHGHGDGDHAATPLLSFDGGSAIWNLIIFLCVLAILSKFVWPAVLGGLQAREEKIREDLESAEKASAEAKQMLSDYQLKLDEAASQVQTMLADARRDAEANGQKIVDAAKVEAAAQRERALSDIENAKKVAMAEMAGQTSKLAMQVARSVVGRELSADDHADLIRQSMERLPSQN | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 25894
Sequence Length: 242
Subcellular Location: Cell inner membrane
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O05332 | MANETNAVEAAAAVAGHAAEAAEKGGMPQLDFSTFPNQIFWLLLALGAIYWLLKNIAIPRIAAILADRAGTISGDLAAAEQYKLKAKDAEAAYAKALADARAQAQKIIAETRAVIQKDLDAATAKADADIAARVAQSEVKIAEIRAGALEAVQIVATDTATAIVTALGGKADMGALNAAVGQRVKG | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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 (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19065
Sequence Length: 186
Subcellular Location: Cellular chromatophore membrane
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B6IX46 | MTQEVAPPAAAQDDAHGTAEHIAEGVAAETAEHAKGGLPQLNPDTYPTQIFWLAVTFGLLLFLMSKVALPRVAEVLEARQEKIADDLDRAGALKAEADAVIENYERELAEARAKAQKVLSDATLAAESETTQRLGELAADLAERARAAEARIEQARRAALGNIRGVAAETAVAAAAKLAGLDLDPATAEAAVEEALNRVRQEVV | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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 (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21509
Sequence Length: 204
Subcellular Location: Cell inner membrane
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A5CQ56 | MLTPHNVMAAGEEAPSILLPAVYDIVWSAVVFVVLLVVIWKYALPRVYAMLDGRTEAIAGGIEKAERAQAEADAAKAELTAQLAEARAEAGRIREQARVDATAIAAEIKEQATADAARITASAQQQIEAERQQAVVSLRSEVGSLAIDLASGVIGQSLTDDQRSTALVDRFLADLEASETAGRTGSAS | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19801
Sequence Length: 188
Subcellular Location: Cell membrane
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O05098 | MEFNLVTIGFTIVNFIILMLILKHFFFDKVNKVIDDRNNEVALTIKKADAQNEEARLLKVESEKNLEDSKLQGKTIVENYKVKAEKVSEEITAEAKTEAQNILERAKRETQREKEKAEDEIKNQVVELAVLISSKALENSINEAEHRKLIEDFVSKVGI | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18245
Sequence Length: 159
Subcellular Location: Cell membrane
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B1KSS4 | MNISIPQIIAAILNFIILLLIVKHFWFDKITAVVDSRQSEIINKIEDTDKNQKLALELKEKNELELGNAKKQGKTIVEEYKSKAENVYEDIVKEAHEEADRIIKKSRLEAERQKKNAEEEIRAEAVELAVLVSSKTLEKTIDDLEHRRLIKDFISKVGI | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18336
Sequence Length: 159
Subcellular Location: Cell membrane
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Q180X1 | MEKALVGITWEFVFQIVNTFIIFLLLRKLLFKPVLNIIESRENDIKSDLAEGEKAKNEGLALKKEYESKINFAKDEGQEIIKQATIRAEQKSDDIVNTAKKDALDIKEKANKDIEQERQKVINEIKNDISNIALLAASKVIEKDLDKSKHEELIENFIKEVGEAK | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18884
Sequence Length: 165
Subcellular Location: Cell membrane
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A0Q2Z8 | MNFSIPTFVWTIINFLLLLVVLSYFLFKPVNEIIDKRSKDIEGDIEQARIDKDKAEELRIANEEEYKAAKKEGKIIVENYKAKAENVSEEIISDAHKEAEIIIERAKKEIQREREKAEYEIKNKTIELSLELSKKALERSIDEKMHRELIEEFISKVGN | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18654
Sequence Length: 159
Subcellular Location: Cell membrane
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Q0ZS23 | MQFASFISLDWGVVFQIVNTIVMYLILKKLLFKPVTKFMNDRQESIANSIKEAEETKKEAYALKAEYEAKINASKEEGQEIIKEASRKAEMRADEIIKNAQNEANRLMEKAHIEIEREKQKVVNELKDEISNIAILAASKVIEADIDKNKHEKLISDFIKEVGEATWQN | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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 (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19444
Sequence Length: 169
Subcellular Location: Cell membrane
|
Q6KI77 | MLELGIFSSNTQNIGQSISERFAGIFPSWPIMLATLVSFTILLVVLTKLIYKPVKKMMKNRRDFIQNNIDESTKQVEKSNELLEKSNIEILDAKIKANTIIKDAQILAEEIKNNSIKDAKDKSKQLLEETKIYIRQQKVLFAKESKKEIVEIAGEMTKKILSESDVKLEDSKFLENLLKNDITK | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21091
Sequence Length: 184
Subcellular Location: Cell membrane
|
Q9MUT1 | MTDILTNIFTILSRMSLAEGFGFNTDIFETNILNLAVVLGILLTSGREFFVSLLQNRQQNILQSINDADERYKEAAEKLQQAQNEFEQAKLEADQILAQSKKTASEIEVGLMNLIKEDTKKLLDMKQATISFEEEKAISEIRRQVIRLALQRALEQSKSRLNRRLQKRVTRLNIGLLGRLVTPNDV | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21235
Sequence Length: 186
Subcellular Location: Plastid
|
B3PLV4 | MNFNINQSSISDAITKTFGNLTINWPFFVFSFLTLILVVTIVTLLVYKPLKKMLKNRQNFIQNNIDESIKAKEAALKVQEEIDEKIIESSKHANQIIEQAKLERERIINNGIEVSNKKAEIIIEQANILVTKSQAEFENKQRKIIVENAVEIAKKIIGREIRDKDNLKMIEEMLES | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20315
Sequence Length: 176
Subcellular Location: Cell membrane
|
Q1GXM6 | MNINLTLIAQAISFAILIWFTTKFVWPYLLNAIETRQKTIADGLAAAERGKQELDMATQRSAEVVNDAKQKATSIIAQAEKRASEIVEEAKANAKAEGDRIIAGAKAEIDQEVNRAKEGLRQQVSALAVAGAEKILRKEIDAKAHADLLNAIANEL | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16951
Sequence Length: 156
Subcellular Location: Cell inner membrane
|
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