ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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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 reticul... |
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 ... |
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 reticul... |
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 reticul... |
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 al... |
Q757A7 | MSSSNQVKGFYFNAQRRLSRAQALCQNSQDTLHNMQLLLVRWQRTVSKLQFTIHCICNQTVFLAECILKKTVGQQLIETEWKRMLLDELQGEMQRSQEEITGKIDALRRTKNELDGSGATLADFISMENIFLLGDKLKDVPVVQEQVEHIKVQYESLVDKVVEQLQNNRVRKLEADFAAAFRSGKNDFNAFSMKYLQKIRQLETDLADILKSLTDHYDKCSLLKAGDLPAAEQAELFEVVKNDDQELDSIMGVLEVIVRDIKSLAKNVSIRLRQKERDKQQLKNAMGKAHSELLKYEEHLTVFQGIDDLIRNFKASCLHN... | 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 particula... |
Q6BYP8 | MSNRDSSEHGDSSNKIASNECNEATKLGFNFTQLWSQITTTYSLIDRNDSNMFNRDERVESEQEKKSVVILGKKYDDISVDDGVIEQDIYSKIWLTYRTGFEPIAKCLDGPQPLSFVQSMVFNRNPISSTFNNFHGLLDNDNFTTDVGWGCMIRTSQALLANTYQLLFLGRGFSYGRDRSPRHDEIIDMFMDEPRAPFSLHNFIKVASESPLKVKPGQWFGPNAASLSIKRLCDNVYESNGTGRVKVVISESSNLYDDIITQMFTTLNPVPDAILVLLPVRLGIDKVNPLYHASVLELLALRQSVGIAGGKPSSSFYFFG... | 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 quant... |
Q557H7 | MFTKYSHHNGYQDGSHLQPFQYQQQTYNQQSYLRQQQQAPQQISYGFNQPNSPTSSSSTPSSSTAMGNSFQNQRQINLQQQQQQEQFLQEQVFYQQQLLQQQSQIKEQQRQKEQKQKTNILNIYKEGKQKIMMSFYNLYRNYPTEPPHFSPSPIWLMGRCYTSKDNNSNNNSNNNQVPQTQPTQLQQSIGIFQNNNSNSNNNNNHNNNHNNNNNNLTTDLIYRPAIESGFLSDVASMIWFSYRKDFPPIENTNITTDIGWGCMLRTGQMILARALIKHLYKENDMVPEIERKKPHSNYSQVLAWFSDYPSKEHVYGIHQI... | 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 s... |
Q5B7L0 | MNATDIERCRKRIIQYIWDPEPKNDEEPGSPIWCLGTRYPPQCVEETADESRNPDHGQQQNTNTSAPGWPEAFLLDFESKIWMTYRSNFPPIPKDAGQEGSLSLTLGVRLRSQLIDAQGFTSDTGWGCMIRSGQSLLANSMAILLLGRDWRRGERLEEEGKLLSLFADSPHAPFSIHSFVKHGADFCGKHPGEWFGPTATARCIQGLAARYDQSNLQVYIADDNSDVHQDKFMSVSRDEKGTVRPTLILLGLRLGIDRITAVYWNGLKAVLQLPQSVGIAGGRPSASHYFVAVQGSHFFYLDPHNTRPALRYSESGTYTE... | 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 quant... |
W0TGM7 | MEFLTKITQQLGLVGEIDKVGSVFVLGEEYRPYIFKTQGKADDAETAFGSFLGNAQTNPQLLSDIETRIFFTYRTQFTPIPRDEEGPSPINLTLFFRDNPINTLENVLTDPDSFYSDIGWGCMIRTGQSLLANAIQRVKQTREFRVNLENIDIKEMSIIQWFQDDWKYPLSLHNFVKVEGKKSGMKPGQWFGPSSTARSIQSLINDFPDCGIDRCLISPQSADIYEDEMIRVFEENKRANVLLLFATRLGVNEINSIYWSDIFQILKSSYSVGIAGGKPSSSLYFFGYQNDYLFYLDPHQTQSSSLDMDDNSYYRSCHGH... | 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 quan... |
A5DSB4 | MSLMSDDSEVFVQAPTVANAELNIEAKPEANAQVNAEADSDANLGNNLGEQQTTDESAFGRNIGKFTAFVKEITGSGTEVEEQEKRNNHTISVDPSSNHENTSFEPTTYKILGRTYTSTTDASARVQELLWLSYRCGFEPIPKSDDGPQPITFFPSIVFNRLTLVNLSNLRSLLDKDHFTSDAGWGCMIRTSQNLLANALLRLFHTTGGQPQNFAVTKTEADVIELFQDTLSAPFSLHNFIKAANSLSLNIKPGQWFGPSAASLSIKKLVNDYNLIQQERRSERDSGRDSGHKVPTPNLKLHSKSADSDSDSDSDAISKR... | 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 quant... |
Q523C3 | MDSAVAGAADIGRYGRRIVRMIWDPEPTNDPIANRPAWCLGYEYTLETNITSKTKGEDSKLSTATSSDQQRPPAQANKVPQMPSAQLPTEAAATALSGNTTPPTPEAALEPTKITSQPAAIDTPPDSVDSSFDSSMAYDDVPDDGGWPPAFLNDFESRIWMTYRSGFEPIPRSTDPTASSRMSFAMRLKTMADQQAGFTTDSGWGCMIRTGQSLLANSLLTCRLGRSWRRGQAPDEERKLLSLFADDPRAPYSIHNFVAHGAAKCGKYPGEWFGPSATARCIHALANATENSFRVYSTGDLPDVYEDSFMEVAKPDGKTF... | 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 quan... |
A2Q1V6 | MVLKDLCDRIVAAKCSSKSSTEIVDNTQVPASSKAGSSDSKFPKASLWSTFFTSGFSVDETYSESSSSEKKTVHSRNSGWAAAVRKVVSGGSMRRFQERVLGSCRTDVSSSDGDIWLLGVCHKISQHESTGDVDIRNVFAAFEQDFFSRILITYRKGFDAIEDSKYTSDVNWGCMLRSSQMLVAQALLFHKLGRSWRKTVDKPVDKEYIDILQLFGDSEAAAFSIHNLLQAGKGYGLAVGSWVGPYAMCRTWEVLARNQREKNEQGEQLLPMAIYVVSGDEDGERGGAPVVCIEDACKRCLEFSRGLVPWTPLLLLVPLV... | 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 si... |
A7KAL5 | MTMDMEKCKRIVQYFWDPEPRNDVPAASIWCLGREYAPSQPPSDPASNNPRSPSRQPNASTLNDTTWPKAFLSDFGSRIWITYRSNFTPIPRTKTPEATSSMTLGVRLRSQLMDPQGFTSDTGWGCMIRSGQSLLANTFSVLLLGRDWRRGEKVEEESKLISMFADHPEAPFSIHRFVNRGAESCGKYPGEWFGPSATAKCIQLLSTQSEVPQLRVYLTNDTSDVYEDKFAHVAHDESGRIQPTLILIGTRLGIDNVTPAYWDGLRAALTYPQSVGIAGGRPSASHYFVGAQDCHLFFLDPHTTRPATLYRPDGLYTQEE... | 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 quan... |
Q0U199 | MNDFERFGRNVVRTFYDPPPCNESNEPIWLLGQRYDSRPPLPKPAPSDSSTTATATAQAERNEDESWIRTSIDDKERKEAPNGEDPTQYGNWPSAFLDDFESRVWMTYRSGFSPIQKSQDPKATSAMSFRVRMQNLASPGFTSDAGFGCMIRSGQCILANALQILRLGRDWRWQENHADKDHAEILSLFADDPQAPFSIHRFVEHGAAVCGKYPGEWFGPSAAARCIQDLANKHREAGLKVYVSGDGADVYEDKLKQVAVDEDGLWQPTLILVGTRLGIDKITPVYWEALKASLQIPQSIGIAGGRPSASHYFVGVQGNN... | 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 quant... |
A7KAI3 | MASHSLNTLHTVFEYIWDRELPNDDFTNTLTVLGRTYAPGPPPHQEKAPDLRTLFHKFKPDQAADTEASWPREFLRDVHSRIWLTYRSGFPLIKRAEDGPSPLSFGSLIRGTVDLATVTKGFTTDAGWGCMIRTSQSLLANSLLQLRLGRGWRYDQTRECAKHAEIVSWFVDIPTAPFSIHNFVEQGANCAGKKPGEWFGPSAAARSIQVLCEANYDKTGLKVYFTASGDIYEDELFELAQQGAELRPVLILAGIRLGVKNVNPLYWDFLKKTLGWPQSVGIAGGRPSSSHYFFGFQGDYLFYLDPHVPQKALLIASEAP... | 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 quan... |
A5DEF7 | MTWDTKNQFETTKTSQELPATSQDHISDNKMNSEPSHRLSQFWSSLTRSSSESITAEPVVILGHTYREGDRDREGDSEVQKQVKKRYWMSYRSGFEPIKKHEDGPSPLSFVQSMIFNKNVGNTFANIHSLVDNDNFTTDVGWGCMIRTSQSVLANAIDRAGYEVDVELFADTSSAAFSLHNFVKVASDSPLRVRPGQWFGPSAASLSIKRLCEARNSSTNVPLSVLVCESGDIYDDQIQTFPVLLLLPLRLGIDHVNNVYHSSLLQLLEVPQSAGIAGGKPSSSLYFFGYQGTSLLYLDPHYPQNVSAGVGSYHSSSYQK... | 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 quant... |
Q8NJJ3 | MYRFLGLGTHPNDDQNKIHVLGRQYDPIKTQETEGKDLDLNSRFQQVLDSIKDGNKKSTTYSQSFIDDVYSKIWLTYRAGFPPIARDKDSPTFTLGALLRGQFDFNEIGFTSDAGWGCMIRTSQSLLANALLFLHLGRDWVFKAKDPANVEHDRIISWFVDIPDEPFSIHNFVQQGIKCCDKKPGEWFGPSAASRAIKNLCKEYPPCGLRVYFSSDCGDVYDTEVRELAYGDSDTFTPILVLLGIRLGVEKVNLYIGDLLRECLSLKQSVGISGRKTSFLALLSIGFQGDYLFYLIPTFPKKALTFGKHGEPVHRLQTKK... | 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 quant... |
A3LQU0 | MAREDASVPRSHDSADASPNSTAKEIPVPQPPLLNLNLNLNMNSGFNLSNWWHQITSIEADSSDDRNNNNSNNGINAAESDSAQSQPIVVLGHSYQTTEEAHEDIIKKLCLTYRYGFERIPRAVNGPSPLSFMQSVIFSKSLLYNLQNFNNFIEKENFTTDVGWGCMIRTSQSLLANTFVRLLDKQSDIIALFNDTYLAPFSLHNFIRVASSSPLKVKPGEWFGPNAASLSIKRLCDGYYDNSTSETILPRINVLISESTDLYDSQIAQLLEPSTETKGLLVLLPVRLGIDSINSYYFSSLLHLLSLEQSVGIAGGKPSS... | 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 quant... |
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 quan... |
Q6TGJ4 | MRKLCGNGSTSMISTDSYKNTTFFVIAFSTFLISCIDYTKLFSSLSTPEAVGRLEDVLIGQCITKGSFAHTLFLIILSAFFIFQVANFAMSVPRLLDMYRFYTHLLGVPDADIQTLPWPEIVRLIGDIRKHNPVTSLSNGQATALADMVGNDAKAPVKKLDAHDIANRILRQENYLIALFNKDLLDLRVRIPVPHIFTAFIPSSMLILSADPPLPSLQSEPERKFLSFGANHLTKALEWNLRFCLLGYLFDRRGQVRKEFVREKRRKDLVQGLRRRFVFMGILNAIFAPFIILYLLIYSFFRYFEEYHKNPSSIGSRQYT... | 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 ro... |
P0CM41 | MGKGEGYLDPTILSVASGSRNSGKGKERTRRKGGHKYHSLHVQDEEEEEPPESDALRTRGKVGLNAYEKALWKWVNVDDLDGFLQEVYDYYKGKGIYCIVLARVLNLLTTFFVIAFSTFLISCIDYSKLFSSISTAEAVGRLEDVLVAQCITKFVHFKLYILNKTNSSAYDYRGSFAHTLFLIILSAFFIFQVASFAMSVPRLLDMYRFYTHLLGVPDADIQTLPWPEIVRLIGDIRKHNPVTSLSNGQATALADMVGNDAKAPAKKLDAHDIANRILRQENYLIALFNKDLLDLRVRIPVPHVLTAFIPSSILISSADA... | 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 ro... |
Q54NA3 | MSHEDRGGDYYPMMDDPEDRNFIQAKYPNSTGHMSSGGGSNHMSFDDNHGIEMLRDDEHSLLHESPVSIPAIHNLDSFLTDVYNYFRGKGFMCIFFNDLFELVSSLFVVLFFTFLVCFVDYSKLFSEQMPPPALRESVNFSAPIPIWLMVFLVIFSLYWLSKLFSFFSSIKTNWEISSFYKNTLKINEDDIQTIEWREVVSKIVLVPRLCIVKENMNALDIANRIMRKENYIIGLINQRILNLSIPFPFLRNLTFITKTLEWSLMYSLFNYIFDENGIIKSEFQDPTQRKRLSRGLSRRFMTIGILGLFTTPFIFFFLLI... | 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 preaut... |
Q5B6U6 | MMASNVLSRLLPQTGQSVYETIRQHDNDSDASDVEERAGLVYDDDVNLGNRFSDRELEEAMADATREGSSSPSDTFLTPQIAQRGERSASSGPRMRKPNNPRFMRSVTPRPEFVEDDLDDDHDDDVPASLLMEGQHDDEYLRTRLPPPPSHHFSDPQPSRSARSPRREHIRTFAFVVGFTTFLTNCIDYRLVRTSKSLDQILISKCTSRMSASSTFLLWLLCLFWIGKIFQLILDIRRLKNMHDFYHYLLGVSDAEIQTISWQEVVSRLMTLRDANPATAGAVSAFNRRLLGSQSKQRMDAHDIANRLMRKENYLIALIN... | 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 ro... |
I1S9X9 | MASNIFSRIKSPSGGSQSFYQQLRSGEDPEYDPGLDEENLGHRFDDFQAEGMDIGDSSMTVESVAPGSKGKGKATFRPTAHARSSGITSPRWQQDDDGDNEVPASLLMEPKDLDPPASPPNKRATNPGSSRTPASVGPSSARTRAQWEAATAQQQLHQDHPYTTPMGPQPIPVARGTMSNNPREKALWRWVNTSNLDSFMRDVYDYFEGGGLWCILCANALWLFQCIDYSRVPDSRSLHEVIVPQCTRKMSGLWNFAIWLYTFFFIWKCVQYFVEIRRLTYIRDFYIYLLDIPEQDMQTISWQDVVARIMALREENPKTA... | 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 ro... |
Q51WZ9 | MASNIFSRLVPQDRGRSFYEDLRQTDPDADLESRAGIDIDEENLNRSYHDYDLDEAERLAGDESHISHSRGDVAGANTVHRRGQKANTARWLGAGVEDDVDNDVPESLLVETPRAPQHLLLSPSRAGPSHPRPTAVPGPSTRQNQAQWEATRHQQRLHNDDTMPHGPFSGRAGQGRPEPPPVGLMAGDPYEQAMWRWVNVSNLDNFIKDVYAYYRAAGFWCIIVQRILELVNAAFVAVFLTFLSQCVDYHKLPHSKKMEDIIIPKCTQNMSLVWNVGLWLFAIYFICRCFGLIIQLRQLKHLRDFYTHLLKIPEADMQSV... | 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 ro... |
Q7S4D7 | MADGVIARLMSGGRGARSFYEELRGRDNVSDVDDRAGLLDEENLNQHFNDYDLENAEGLRLEDSRATVDGRIPRGRAQLSGRPPRPAATTHWGTSHDDDGDNDVPASLLVERYDRGAAPLGSPGKPRSQHAGSRAHPAPGLSKGRTHQQRPHIDQELQPPLHSDAAPSSLLAGAITGNAKKMAEWRWANITNLDSFMQDVYSYYRGSGMWCIVVERVLHLIKVAFVAFLLTFLSQCVDFKKIPSNQKLSQVLVPQCTRNMSGLWNIGLWLFAFYFMWKSIQYILDLRRLTHVRDFYIHLLNIPDEDMQTITWQEVVARIM... | 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 ro... |
A7KAM0 | MMSSNILSRFLPPTGSPSVYETIRQHDAGSEYSDLEERAGLVIEDQQEQYSDRELEDALADAQDSEIVSPSTALLNQARSVKAPEERASPSGTRRRKSSRPRWMAQESPLGYELDDHDEDVPQSLLVEGHHEDLKPRLPPPPQSHNRSDRRRTPSPGPSSRPTEARWNERGVHQQPPPSESGHPIGRWFTGQHPGLANVDPKKKAMWRWANVEDLDNFLKDVYVYFLGNGIWSILLTRVLNLLTFAFVVGFSTFLTNCIDYPKVRRSKTLNDILVPQCTANMSGSSTFLLWLFSFFWIGKLFQYLLDIRRLKHLHDFYLY... | 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 r... |
Q0UYL2 | MASNLLSRLLPSASDDLLEQEASNNQNRRTSSSTDERPDMDIDEENFGARFEAQDLNDLLAEASSSHMTTESRAASPEARRNAPPGINTAARAPAWRQPAPARAVPLDDDDDVPQSLLLEGGLDPPPNPHPRPDGLPPPVPGPSTRHTRAQWETTRQQQRLHGDDRGGAPVRDWGAIGRGGQFTADPKEKASWLWVNQTDLDTYMREVYEYYVGSGIYSMILRRTLSLLQSAFVVGFMTFLGWCIDYSKLSGSNKLSQVLVPKCTKEIHGFWIFALWVFTIYWLYSFYGLLTDIPRLRAMHDFYHYLLDVPDRDIQTIQW... | 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 ro... |
A7KAI7 | MGDLNKHTFLSRVFGSASNPLLNDDNNDIEFSINNLQDTFEEHQVESPPRAPHPINVNSEDESSSETESASNEDLLYDQKRELYQQVESELRQDDYDTVPESLMMERRRPHEGSTRTIGTKIPPSPAEPPIGPNITQWGEKARGIASRTLDNIPKTIAKGISFQLPANASSKLPPPPLSYRRETSVGGETEMAQNINEQRQLRGRLGLLSPMERALWLWSNVSNLDTFLEDVYGYYTGNGYRCIILSRVSDLLIIVFVVWLTSFMGNCVDYNQLMNGNATKYSDVVVDKCYSKISLSQKLFFLVLFAILVLRIKSFYSHF... | 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 r... |
Q876N4 | MHKNNTTFLSRVFGINSRNIDVHNPLFADDSVIPLYDQNQSAYYDNAYSDYSSDEEDSKPRTSRQTDSNLHMTDHSGDGNDPFNQMDNSSRFSNSSSFHYNNTDQEDDNPELLLLQDEDSSLNRKNLDNSDFQSFAKKTFNQIPKIKFQLPKKEDYPTSHRQPPDIENQNGTLKSSVKKQIHFLDPMDKALWMWSNVSNLDTFLHQVYDYYTGNGFNCIMMNKFTELFTVVFIVWLFSFMGNCIDYDKLMNDRNVYQFSQVKIDKCYSKIGFFPQKLIYWLFFIGLCLKLYQIFLDYLVLKDMKLFFNLLLGLSDDELQT... | 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 ro... |
Q2HIE9 | MKEMSRYLWPKDSWGDKLRVLLAVGLLVGGKVLNVQVPFFFREIVDSLNVDIAATGGTVATVAGTMIFAYGASRIGAVVSQELRNAVFSSVAQKAIRRVATRTFGHLLNLDLNFHLSKQTGGLTRAIDRGTKGISFLLTSMVFHIVPTALEISMVCGILTYQFGWEFAAVTALTMSAYTAFTIWTTAWRTKFRRQANAADNKASTVAVDSLINYEAVKYFNNEKYEIGRYDKALHQYEKSSIKVATSLAFLNSGQNIIFSSALTIMMWLGAKGIVAGSLSVGDLVLINQLVFQLSVPLNFLGSVYRELRQSLLDMETLFN... | 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 gluta... |
J9VWU3 | MGFGSCSRHALFTPAAFSGSFTTMTTSCFKRVYTAQIHGGDALGKRLPSVSSFSGQLPRHGLHRQSLAFFSTSHRRQTSPPPSPRTTSQSPTVPSKASTTPPTSLNTSKPIATESQDKTDWSIIVKLAGNIWPKNNPNVKFRVIGALTLLVAGKVLNVQVPFFFKTIVDSLNVPITESTTVWVLAGASIAGYGAARILTTLFGELRNAVFASVAQNAIRKVARETFEHLLNMDMKFHLERQTGGLTRAIDRGTKGISFILSSIVFHVIPTALEISMVCGILSWKFGWDFAAVTAITMLLYTWFTIKTTAWRTTFRKQANA... | 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 glutat... |
Q5B1Q2 | MLRQAAQTRCWRTPARFVSHRPAFPRSNPVSAALGGTQFRKLSVKTQTDKNTLSDKKTAEADTSSSSSSAKSAAPSQQKTQNATTAQKNLLSESTVANKEQRKADWAIMREMAKYLWPKGDWGTKLRVGTALSLLVGAKVLNVEVPFYFKSIVDSMNVDFAAVGGTAYTVAGSMIIAYGATRIGATFFQELRNAVFASVAQKAIRKVARNVFEHLLRLDLNFHLSRQTGGLTRAIDRGTKGISFLLTSMVFHVVPTALEISLVCGILTHQYGIKFAAITATTMLAYSAFTIATTAWRTKFRKQANAADNRGATVAVDSLI... | 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 gluta... |
Q7RX59 | MAPSIKLSTMATSLHRAHGTSALLRRPRLWAPRLSSIHATPTIANLRASFTTSSPRLFAPNGSAKDESKPAVSTVPKTTGRGPSDPLAAIDKTAQEQRKADWAIMKEMSKYLWPKGSWGDKARVLLAIGLLVGGKVLNVQVPFYFREIVDSLNIDFSTTGGSVTAVAGAMILGYGAARVGAVVSQELRNAVFASVAQKAIRKVARNTFEHLLNLDLSFHLSKQTGGLTRAIDRGTKGISFLLTSMVFHIVPTALEISMVCGILTYNFGWQYAALTALTMVSYTAFTILTTAWRTKFRRQANAADNKASTIAVDSLINYEA... | 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 glut... |
Q2G506 | MPPETATNPKDARHDGWQTLKRFLPYLWPADNAVLRRRVVGAILMVLLGKATTLALPFAYKKAVDAMTLGGGAQPALTVALAFVLAYALGRFSGVLFDNLRNIVFERVGQDATRHLAENVFARLHKLSLRFHLARRTGEVTKVIERGTKSIDTMLYFLLFNIAPTVIELTAVIVIFWLNFGLGLVTATILAVIAYVWTTRTITEWRTHLREKMNRLDGQALARAVDSLLNYETVKYFGAESREEARYASAARAYADAAVKSENSLGLLNIAQALIVNLLMAGAMAWTVYGWSQGKLTVGDLVFVNTYLTQLFRPLDMLGM... | 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 arom... |
O14286 | MLERCPWKLISSPRNIPARSFLNSRGTYLVLRKSNILPLQHILRFSNFASKQCFPLRNGNNSASKALWNNKSKEKEPLNTSVKLASDVPDDKNVTGQMIVKDMLQYIWPKGKTNLKVRVVSALALLVAAKILNVQVPFYFKSIIDTMNTTLVQEVGALWSTVGAVVLGYGFARIFSTVFQELRNSVFAIVSQSAIRSVSSNVYQHLLNLDMNFHLSKQTGSITRAMDRGTKGISFILSSMVLHIIPITLEIAMVSGILTYKYGPSFSAIAATTVALYALFTVRTTSWRTVFRRQANAADSKASAAAIESLINYEAVKTFN... | 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-conjugat... |
A6ZYV0 | MLKCICRVYSQPLAQMVTSPLFKHMGSAGTYTILPITNLRHLSTKNCPLKIKSNRSEPLQFGDFERQVPCSRKSGSSKNVQKRLYELRQLKTVLSETFGVTEYASFFESLRNALHINNCSENEKKKLLYDIILHQHELYPEVARKIGFYLPGEVHRWFWYHIPKSESFNHYLFLLKSDVLLFTSNYCTRFTNRLIKGTEMERQLATFQIFLHDETNIKFIMEKVLKLHTFDSLIALVNGLVKAKNFRFIKVFIQALLQKLEQHCYSGKDGAKQKNLRYVKFNNTLLYYLLKSGNVELFIKTFQEELKFIVSSGLLNHIDG... | 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) partic... |
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 ... |
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 ... |
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 ... |
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 ... |
P93298 | MRRIFLFDENSLNSSSTIDTSSASTIDTSFASQCTNFSSGQASGTQDTHAGIFEDCPGLNPNDERVVELQCEIREKCEALTQDPEMGLILGEALHAESDNVPFLQSIADDLTQNGVSGEAFQEALNIVGQAAASPLDQFEIVPLIPMHIGNFYFSFTNSSLFMLLTLSFFLLLIHFVTKKGGGNLVPNAWQSLVELLYDFVLNLVKEQIGGLSGNVKQMFFPCILVTFLFLLFCNLQGMIPYSFTVTSHFLITLALSFSIFIGITIVGFQRHGLHFFSFLLPAGVPLPLAPFLVLLELISYCFRALSLGIRLFANMMAGH... | 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 extramemb... |
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 extramemb... |
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 extramemb... |
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 extramemb... |
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 extramemb... |
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 ex... |
Q0C0Z8 | MDISPAEISGILKSQIENFGVEAEVSDVGQVLSVGDGIARVYGLDSVQAGELVEFNGGIKGMALNLEKDNVGVVIFGEDRSIKEGDTVKRTSEIVAAPVGKALLGRVVNALGEPIDGKGPLKDVAARSQVDVKAPGIIPRKSVHEPMMTGIKAIDGMIPVGRGQRELIIGDRQTGKTAICIDTILNQKPTNDAAKSDKDKLFCVYVAIGQKRSTVAQVVKVLEERGALDYTIVVSATASESAPLQYLAPFTGCTMGEWFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNDDNGN... | 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... |
Q5FKY2 | MSIKAEEISSLIKQQLEHYDDKLDINEVGVVTYVGDGIARAHGLDDVLSGELLKFDNGSFGIAQNLESNDVGIIILGQFDNIREGDRVQRTGRIMEVPVGDALIGRVVNPLGQPVDGLGEIKSDKTRPIEAKAPGVMDRQSVNQPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSLAIDTILNQKGQDVICIYVAIGQKESTVRTQVETLKRFGAMDYTIVVEAGPSEPAPMLYIAPYAGTAMGEEFMYNGKDVLIVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKLSDKLGGGSLTALPIIQ... | 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... |
Q6YXK3 | MVKIRPDEISSIIRKQIEDYSQEIKVVNVGTVLQVGDGIARIYGLDKVMAGELVEFEDNSIGIALNLESDNVGVVLMGDGLTIQEGSSVKATGKIAQIPVSDGYLGRVVNALAQPIDGKGQIPASEFRLIESSAPGIISRRSVYEPMQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQKGQNVICVYVAIGQKASSVAQVVNTFEERGALEYTIVVAEAANSPATLQYLAPYTGAALAEYFMYRKQHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIV... | 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... |
C0HK51 | ATAKAAPTEVSSILESKIRGVSDEANLDETGRVLSVGDGIARVFGLNNCQAEELVEFASGVKGMALNLEPGQVGIVLFGSDREVKEGEIVKRTGKIVDVPIGPGMLGRVVDALGNPIDGKGPIEATGYAIAQLKAPGILPRRSVFEPMQTGLKAVDALVPIGRGQRELIIGDRQTGKTAVALDTILNQKRWNDGNDESKKLYCVYVAVGQKRSTVAQLVQTLEQNDAMKYSIVVAATASEAAPLQYLAPFTACAIAEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSDANGG... | 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 ex... |
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:... |
P17674 | MSIKAEEISALIKQQIENYQSEIKVSDVGTVIQVGDGIARAHGLDNVMAGELVEFSNGVMGMAQNLEENNVGIIILGPYTEIREGDEVRRTGRIMEVPVGEQLIGRVVNSLGQPVDGLGPVETTKTRPIEGAAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTSVAIDTILNQKDQDMVCIYVAIGQKESTVRNVVETLRKHGALDYTIVVTASASQPAPLLFLAPYAGVTMGEEFMYNGKHVLVIYDDLTKQASAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDAKGGGSLTALPFIE... | 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... |
A3DIM9 | MATENVGTVVQIIGPVIDIRFERGKLPSIYNAIKINSEGIDIVAEVMQYTGNDTVRCVSMNSTDGLKRGMKAVDTGEPIKVPVGKEVLGRVFNVLGEPIDGKGDVKATTYLPIHREAPGLDEQKPVTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIRNIATEHGGYSVFTGVGERSREGNDLWNEMNESGVIEKTALVFGQMNEPPGSRMRVGLTGLTMAEYFRDELGQDVLLFIDNIFRFIQAGSEVSALLGRIPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFTHL... | 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: 46... |
P50002 | MAQNIGKVVQVIGPVVDVKFQKDKLPKLNNAVNIELNGHTLVIEVAQQLGDDIVRCIAMDSTDGLMRNQEAVDTGSAIQVPVGKATLGRMFNVLGEPIDGKPFDTKDVVMHPIHRHPPSFEEQQTQPEMFETGIKVVDLICPYVRGGKIGLFGGAGVGKTVLIQELINNIATQHGGLSVFAGVGERTREGNDLYYEMMESGVINKTALCFGQMNEPPGARMRIALAGLTMAEYFRDDEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTSKGSITSVQAVYVPADDLTDPAPATTFAHL... | 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
Subcell... |
Q4FQ37 | MSSGRIVQIIGAVLDVEFNRNEVPRIYDALQVDGTETTLEVQQQLGDGIVRTIAMGSTEGLKRNLSVTNTGGPISVPVGVGTLGRIMDVLGRPIDEEGPVEADERWSIHREAPSYAEQSNSTELLETGIKVIDLLCPFAKGGKVGLFGGAGVGKTVNMMELINNIALKHEGLSVFAGVGERTREGNDFYHEMQEAGVVNTEDFSKSKVAMVYGQMNEPPGNRLRVALSGLTMAEYFRDTKDPATGKGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGMLQERITSTQSGSITSVQAVYVPADDLTDPS... | 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: 47... |
A0T0R6 | MVETTNKGYVCQIIGPVLDIEFPGGKLPPIYSAIKIETADGIGNIVEVQQLLGDNKVRAVSMRSTDGLKRGVEAVDLGAPITVPVGVPTLGRIFNVIGEPVDEQGDVVVDQTLPIHRDAPAFTELETKPSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYEEMKESGVINSSNFAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTTQGSITSIQAVYVPADDLTDP... | 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: 47... |
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 c... |
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 c... |
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 c... |
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 c... |
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 c... |
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 c... |
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 c... |
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 c... |
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 c... |
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 c... |
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 c... |
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 c... |
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 c... |
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 c... |
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 ex... |
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
|
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
|
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
|
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
|
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
|
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
|
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
|
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
|
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
|
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
|
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 c... |
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 c... |
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 c... |
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 c... |
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 c... |
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 c... |
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 c... |
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 c... |
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 c... |
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 c... |
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 c... |
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 c... |
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 c... |
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