ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q8KGE7 | MRKKAISRILALVVPVLLSLNSQAFATSVQDESPVTGSAVEAVHTVPSTVAAPVAGHAEAAAGQAAKAEEKPGDLIMHHILDNSTFSFEPFGEVHLPHLEVAGFDISITKHVVMIWLAAILLVVIASAAGASVKKMSANQAPKGVANVFESLVDFISNDVAKPNIGHGYEKFLPYLLTVFFFILVCNLLGLIPYGATATGNINVTLTLSVFTFVITQFSAFKAQGVKGYLQHLTAGTHWALWIIMVPIEILGQFTKPFALTIRLFANMTAGHIIILSLFFISFILKSYIVAVAVSIPFAIFIYLLELFVAFLQAYVFTML... | 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): 37818
Sequence Length: 352
Subcellular Location: Cell inner membrane
|
Q2S6N5 | MAGENPTASEYIQHHLQNLTFGNHPEHGWSFAHTAQEAKEMGFWAVHVDSLGWSIALGALFVWLFRKAAVKATSGVPSGLQNFVEIMVDFVDKSVKETFHGKNAVIAPLALTVFCWIFLMNLMDLVPVDFLPRLFQVITGDDHAYFKVVPTTDVNVTLGMSLSVFFLIIYYSIKVKGVGGFLGELTLQPFGKWMLPFNLLLEGVGLIAKPISLALRLFGNLYAGELLFILIALMPFWAQWALSVPWAIFHILVIVLQAFIFMMLTIVYLSMAHEDH | 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): 30919
Sequence Length: 276
Subcellular Location: Cell inner membrane
|
A9IQH9 | MTAHAPDPIHQFEVSRLIKISIGNMDLSFTNVSLFTVVTVVITAAFLFISSSSRGLVPTRMQSLSEMAYEFVASTLRESSGVQGMQFFPLVFSLFTFILVANFIGLFPYFYTVTSQIMITFSLAMVVILTVIGYGFYKHGISFLKLFVPSGVPVVVLPLVTMIEIISFLSRPISLSLRLFANMLAGHITLKVFAGFIVSMIGVGIVGVGGAVLPLIMTVAITALEFLVAFLQAYVFTVLTCMYLNDAIHPGH | 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): 27502
Sequence Length: 252
Subcellular Location: Cell inner membrane
|
Q6MRR3 | MSFNWTQLVPGVGHEYAHVATLGIATVAAVGIGAAARASLGKGEAAVLPASKFSLRGIFELLTEMTSGLADMVIGEHGKHYIPFFASVFFFILFNNLLGMIPGMTPATENMNTTFGFGVLMFLFYNFQGVKENGPVAYLKHFMGPVIFLAPLMFVIEIVSHIVRPFSLGLRLANVMMGDHTVLSVFLDLVPIGVPIPFYVMGLFVCFVQAFVFTLLSMVYVAFAIAHDH | 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): 24920
Sequence Length: 229
Subcellular Location: Cell inner membrane
|
Q2KU30 | MAAASGASPQSEYIQHHLVHLNNLGEKQSVIAQFNVINYDSLFWSGLMGLIVIFCLWLAARRATAGVPGRFQGFVEMIVDMVNDQAKGIVQNAKSREFVAPLALTVFLWIILMNALDLLPVDLFPTIWRVTGLGAEHGDPLYYHRILPTADLNVPMGMSLGVLLLMFYYGIKIKHPAGFVKELFTAPFHAHGLAALVLAPFNLLLNLIEYAAKSVSLGMRLFGNMFAGELIFMLIALLGGAWTGFNASSIGLGIGHVLAGSVWAIFHILIVLLQAFIFMMLTLVYIGQAHEGH | 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): 32076
Sequence Length: 293
Subcellular Location: Cell inner membrane
|
P00847 | MNENLFTSFITPVILGLPLVTLIVLFPSLLFPTSNRLVSNRFVTLQQWMLQLVSKQMMSIHNSKGQTWTLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLALMSISTTTALITFTILILLTILEFAVAMIQAYVFTLLVSLYLHDNT | 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... |
Q34946 | MMPDIFSSFDPYMFNTLFPLNSLFLVTNTAIILMIQSSFWVLNARTSAFKSPVNDTIFTQLSRTSTTHLKGLSTPLSTIFFMLVMINLMGLIPYMFSTSSHLVFTLSLGFPIWLSLMISTFAHSPKKSTAHFLPDGAPDWLNPFLVLIETTSVFVRPLTLSFRLAANMSAGHIVLSLMGIYCAAAWFSSVSSTALLILTAIGYILFEVAICLIQAYIFCLLLSLYSDDHAH | 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... |
A0LDW6 | MSAEAMHAAASAAPKMDPLHHFMVQKVVPIEIAGIDLSITNSTIWMWLAVAVAFLFMKWSFRGRAEDKLIPTKMQSLAEMTFTFVRQIVDQNIGGAEGRKYFPAIFTLFLLVLFCNLLGLIPGSFTPTSQLVVTATLALSVFFFATGLAIVKHGTGFIGFFVPSGVPPMLLILMVPIEIVSYLSRPVSLSVRLFANMTAGHTVLAIMFFFAATLPLGGLLMPAAFATVFTGFELFIGFIQAYIFTILTCVYINDALHLH | 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): 28338
Sequence Length: 259
Subcellular Location: Cell inner membrane
|
Q2W028 | MANPIEQFKIQPLVPLKVGSVDISFTNSSAMMVLSICLITLFLTLSVRSRALVPGRWQSMAEVFYEFIAGMLRDNVGQEGRKYFPFIFSLFMFVLFGNLLGMMPIPVIGFTYTSHVIVTFAMALVVFVGVTVIGFARHGTHYLRMFFPHGAPIATAVILIPIELISYFSRPFSLAVRLFANMTVGHIILKVMGGFVVSLGAFYLIPGAVPFAFLSAITVLEFGIALLQAYVFTILSCIYLHDAIHMH | 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): 27374
Sequence Length: 247
Subcellular Location: Cell inner membrane
|
P26853 | MACSPLEQFAIIQLIPIHIGNLYFSFTNSSLFMLLTISLVLLLVHFVTLNGGNLVPNAWQSFVEMIYDFVLNLVNEQISGASSVKQRFFPLIYVTFTFLLFCNLIGMIPYSFTVTSHFIITLGLSFSLFIGITIVGFQTHGLHFFSILLPQGVPLPLAPFLVLLELISYCFRALSLGIRLFANMMAGHSLVKILSGFAWTMLSMGGILYLGQLAPFFIVFALTGLELGVAILQAYVFTILLCIYLNDAINLH | 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... |
O47494 | MGAAYFDQFKVVDLIAITNSSMMMMLAVAVALILLKGNRLIPNRWQAVMESIYDHFHGLVKDNSGPQYFPFVFTLFIFIVFLNILGLFPYVFTVTVHIVVTLGLSFSIVIGVTLGGLWKFKWNFLSILMPAGAPLALAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFGFNMLTTAGVFNIFPVLIMVFISLLEAAVAVIQAYVFSLLTTIYLADTIVLH | 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... |
Q2RFX3 | MTHVRPVEIFHLGPIPIYSTVVNTWIIMILLLAGIFLATRKLSFIPRGAQHVLEMFLEFFYGLLEEIIGKEGRRYLPLVATLFIFILSLNLSWFIPGMKPPTMDLSTTAAFAVTTIILVQIFGIRKLGLRGYIRHFFQPAPFLFPLNVIEELVKPVSLSLRLFGNLFGEEMVVTILFLMIPFLLPTPIMLLGVLMGTIQAFVFTLLTITYIANFVHGH | 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): 24723
Sequence Length: 218
Subcellular Location: Cell membrane
|
P00848 | MNENLFASFITPTMMGFPIVVAIIMFPSILFPSSKRLINNRLHSFQHWLVKLIIKQMMLIHTPKGRTWTLMIVSLIMFIGSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVITGFRHKLKSSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLMNISPPTATITFIILLLLTILEFAVALIQAYVFTLLVSLYLHDNT | 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... |
P80497 | MRQFDPWPVFFRREWSRNWPFLVGFAVTGAIITKMSLGFTEEERKNSRFAQRHKN | 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 (Probable). F-type ATPases consist of two structural domains, F(1) - containing th... |
Q02B01 | MFNDHLAGAGNALTGIVGMAPEARPWANFVTMQLLVVAIIVVLFAILRPRLSPDRPGKLQHTFELVYGFLHEQAEEQIGHEGHHYLAFFGTIFIFILFANLIGVVPGFEAPTMVPSVPAGCAIAAFFYYNIVGVQANGLGRYLAHFAGPMPLLAPLMIPIELVSHMARPLSLTIRLFANMYAGEQVTMVFLKLTFLFVPAVFMGLHVFVSFLQAYIFMLLTMMYVAGAVAHEH | 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): 25668
Sequence Length: 233
Subcellular Location: Cell inner membrane
|
A9FGS5 | MPEHTGFLTYLLAQLPGLRENARNIGKTFIGHHTVDYRGTEPIFMSLLIMVLFVLLASEVRGQYRRLNESVIPEDKLTLRTFFEAFFGYFYGMARDVMGPANAKRYFPLIGGSAAFIFFSNASALIPGVNPPTSNLNITIGCAVVVFVLFNYYGLKENGWSYVAHLAGPKWYLAPLIFPIEVISTCVRPVTLSIRLMLNIGVDHLVASIFLGLVALFVPVPLMFLAIIVIVVQTLVFCLLSCIYIGLATEKADHH | 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): 28338
Sequence Length: 255
Subcellular Location: Cell inner membrane
|
P80086 | SPLEQFSILMLIPM | 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... |
Q9TBI7 | MPQLNPNPWLFIMLMSWLTFSLIIQPKLLPFTPINPPSNKTPTTTKTSPWTWPWT | 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... |
A9RAH3 | MPQLVPFYFTNLLTFGMLAISMLLYLVSTIILPNILRLLVARTTMTKL | 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... |
Q36362 | MPQLLPTPWFTIFIYAWMVLLAVIPLKILSYVYPNHNYLRGLQKPSEHSWFWPWS | 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... |
P84345 | MPQMAPISWLLLFIIFSITFILFCSINYYSYMPNSPKSNELKNINLNSMNWKW | 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... |
Q7UH05 | MTTYSETLETAAQQFDQAVKSQPSQLTVTEIGTVEEVQRGIARVHGLPHVQVDEVLRFAGGHLGYAFNLDPDQVGCVLLDSSDQITAGSRVERMHSVLDTPVGDQLLGRVVDPVGRPLDGGRSLDDLPREPCERDAPPIMQRAPVTVPLQSGLKVVDAMIPIGRGQRQLLLGDRQTGKTAIAIDTIINQLGRDVICIYCSIGQRSTGVARVIENLRRHDALDHTIVVIGADDAPPGLQFLAPYAATTMGEHFMRQGRDVMIVYDDLTSHARAYRHLSLLLRRPPGREAFPGDIFYVHSRLLERSTHLIQSAGGGSLTALP... | 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): 54920
Sequence Length: 504
Subcellular Location... |
B8D8H1 | MRLNSTEISKLIKERIAQFEVFNQSYNEGSIISVSDGIIKINGLSNVMLGEMILLPNNEYAIALNIERDTVGAVVMGPYIHISEGAKVRCTGKILEVPVGDNFLGRVVNALGFPIDGKDSIQNDGFFPVEADAPGVIDRKSVNQPIQTGYKVIDSMIPIGRGQRELIIGDRQTGKTALAIDTIINQKQSGIKCIYVAIGQKLSTIINVVKKLEENNALFNTIIVVASASEAASLQYLAPYSGCAMAEFFRNKGEDSLIIYDDLSKHAVAYRQISLLLRRPPGREAFPGDIFYLHSRLLERASRVSMEYVQKITKNKITGK... | 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): 56636
Sequence Length: 512
Subcellular Location... |
Q89B41 | MQISSSEICELISKKIAKFDIISSMHNEGRVISVSDGIIQIYGLSDVMQGEMLSLPGDKYAIALNLEKNVVGAIVMGEYTHITEGTKIISTGRIFEIPVGSKFLGRVINALGVPIDGKGRIQEEKFLPVEINAPGVIDRQKISEPLQTGYKSIDAMVPIGKGQRELIIGDRQTGKTSLAIDTIINQRNTKIKCIYVAIGQKFSTIVNLVRQLEDNQALNHTIVIVASASESAALQYLVPYSGCSLGEFFRDQGKDALIVYDDLSKHAIAYRQISLLLRRPPGREAFPGDIFYLHARLLERACRVNSNYLKNILGTVNKFS... | 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): 56888
Sequence Length: 514
Subcellular Location... |
Q9XXK1 | MLSKRIVTALNTAVKVQNAGIATTARGMAGASGSEVSKILEERILGTETGINLEETGKVLSIGDGIARVYGLKNIQAEEMVEFDSGIKGMAMNLDVDNVGVVVFGNDKVIREGDIVKRTGAIVDVPVGDGLLGRVVDALGNPIDGKGPIANARRSRVEVKAPGIIPRLSVREPMVTGVKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTIINQKRFNDAGDDKKKLFCIYVAVGQKRSTVAQIVKRLTDAGAMDYTIVVSATASDAAPLQFLAPYSGCAMGEHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGRE... | 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... |
Q4FP36 | MDINPSEVTKILKEQIKKFGDKAEVTEVGQVLSVGDGIARVYGLDNVQAGEMVEFSDGSKGMALNLESENVGVVIFGDDRKIKEGDVVKRTGSIVDTPVGKELLGRVVDGLGNPIDGKGALDKATKRSRVEVKAPGIIPRQSVSEPMQTGLKSIDSLVPVGRGQRELIIGDRQTGKTAVAIDAIINQKKINESGDEKQKLYCIYVAIGQKRSTVRQIQKTLEEAGAMEYTTIVAATASDAAPLQFLAPYTGCTMGEYYRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDEHGGG... | 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): 55569
Sequence Length: 511
Subcellular Location... |
P06541 | MSDSIETKNMGRIVQIIGPVLDIVFAKGQVPNIYNALTIRAKNSAGTEMAVTCEVQQLLGDNCVRAVSMNPTEGLMRGMEVVDTGKPLSVPVGKVTLGRIFNVLGEPVDNMGNVKVEETLPIHRTAPAFVDLDTRLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFAGVGERTREGNDLYTEMKESGVIVEKNLSDSKVALVYGQMNEPPGARMRVALTALTMAEYFRDVNKQDVLFFIDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQERITSTKDGSITSIQAVYVP... | 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... |
Q09MH1 | MRINPTTSGPGVSAFANKNLGHIAQIIGPVLDVAFPPGKMPNIYNALVVKGRDTVDQPINVTCEVQQLLGNNRVRAVAMSATDGLTRGMEVIDTGAPLSVPVGGVTLGRIFNVLGEPVDNLGPVDTRTTSPIHKSAPAFIQLDTRLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINDQNLSESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGS... | 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): 53636
Sequence Length: 49... |
Q0C100 | MSTPANGKGRISQVIGAVVDVEFDGELPSILNALETFNNGSRLVLEVAQHLGENTVRTIAMDSTEGLVRGQPVSDIGTPITVPVGPATLGRIMNVIGEPIDERGPVNADTYMPIHAQAPAFVDQATESEVLVTGIKVIDLLCPYAKGGKIGLFGGAGVGKTVLIMELVNNIAKLFGGYSVFAGVGERTREGNDLYHEMIESNVINLEGESRMSLVYGQMNEPPGARARVALTGLTQAEYFRDVEGKDVLFFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGALQERITSTNKGSITSVQAVYVPADDLTDPAPA... | 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): 50900
Sequence Length: 47... |
A8Z6C7 | MINKVKGKIIQIIGPVIDVLFENVSSLPMIYDSLEVFNPKGNQIILEVQQHIGECTVRCISMDITDGLKRGQDVFSLGTTISMPIGEEINGRVFNVVGNTIDGLGDLNNSKRISIHRNPPKFEYLSTNIDILYTGIKVIDLVEPYIKGGKIGLFGGAGVGKTVLIQELINNIAKGYGGLSVFAGVGERTREGNDLLREMISSGIIKYGDSFLEDMKNGKWDISKVDKNELKNSKATFVFGQMNEPPGARARVVLSGLTLAEYYRDSFRKGRDVLFFIDNIFRFTQAGSELSALLGRMPSAVGYQPTLASEMGTMQERITS... | 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): 54690
Sequence Length: 49... |
Q07233 | VLIMELINNVAKAHGGYTVFAGVGERTREGNDLYHEMIESGVISLKDKTSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTSKGSITSVQAIYVPADDLTDPA | 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... |
Q6CFT7 | MVLPRLIPRLSRSAFKVAQANNRVFNAPFRGMASSAGVGSGKIRTVIGAVVDVQFEQDNLPAILNALTIDRGEGNKLVLEVAQHLGENTVRTIAMDGTEGLVRGTSVADTGAPITIPVGRGTLGRIINVCGEPIDERGPIEATKFLPIHADPPTFAEQSTTAEVLETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFCGVGERTREGNDLYREMKETGVINLEGESKVTLVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDM... | 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... |
P00830 | MVLPRLYTATSRAAFKAAKQSAPLLSTSWKRCMASAAQSTPITGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLAT... | 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... |
Q6A8C4 | MTTAVGASQQLDEVGDRRGTGTEFANEIFAVVDVLNRESGLRRAVSDTGSETKARQGLIDAVFTSKVSPDCKELLDATTTCKWRSPAALTRALERQGVRAVLRGARQADRFEAVADELFHVSRLVRGQAALQVALGDPNRSVADRQELLMKLVGGQVSEETLVLARRAVVASDSTFEQVIDGYLHVAAEMADRRRAIVTTAKALTDAQRAEMVKQLERITGSPIELSEVVDPTVLGGALINLGDEVIDSTVAHRLDQARRELG | 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... |
Q9TM27 | MILLLTNSKIIYPYSEALFSIAKDQEKFEVIKNDMELFVTFTKNLNGFKKFLETPLINKNKKIKVVKDVFSKILNSTTLNFISILINKNRIMFVSNISEKYNQLVLKDKSVKLVKIACARQLSEKQAQALSEVLKHKFKCLSVKLIFNIEPELIAGFKIFIESQVIDVSLQGELKEFEWYLTK | 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... |
Q85FQ9 | MKQKIVEPYAQALFRLKDDIDLTPLWEMARDSKFMQLLMNPSIPKEKKWQLFQPFDKLVQSWLEVIWKKKRMNLLAEICASYLELRKKKEGIVTVFVTSATPLTDTQTQQLEVQLTRMCQAKHLQCEYQVDAQLLAGLKIQMNGQLIDTSWQTQLKQLMKSLW | 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... |
Q11YP2 | MKETRVAYRYAKSLIDLAAENGVLDRVNADMAGIESVFKQNHQLVAVMKNPIVQGDKKHAILEALFGGKVDNFTMSLLSLLTKKHREAVVFEISSEFQRQYREKMGIKIVEVTTTQPITEDQRANFKAIMASKASKVELIEKIDEKILGGFVLKMDDQQIDESVIAKLNKIKNKFTEQVINY | 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... |
Q477Z4 | MAESVTIARPYAEALFRTAKESGNLAKWSEQVSLLGQVAANPDVSSAIGDPNVAAPQLVDLFRSACGTAVDAELSNFIQLLSNNDRLGLLPEIAGLYETYKRAEEGTKQADIVSAFPIDDNQVKALIPQLEAVFKTKLEAAVSVDPTLIGGIKVIVGDQMLDASVRGKLDAMATALNN | 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... |
Q3Z8Z5 | MAKRVYAIAMRYAQALYELAKEQKSLDKWQEDLQDLSSLTEDASVAEFLSNPKIASARKHKVLAKLSNIDPLMLNLVDMLVATRRLGIMRAVSGEYNRLLNEARGVEDAIVTTAKPSSEADIEIIRQQLSKITGKKINVVTATDPGLIAGLKARIGDKLIDGSVSRRLVLLQNEISQGRI | 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... |
B1I6L7 | MIKGAVAARYAQALFDVARDNNRIAETENELRGFMRLLDESRDLQQVLYNPQVPVELKKEIVREAFGKELSGTTLNFLCLVLDRRREVYLKGIADHFIALANETRNIIEAEVTSALELSVVHKVNLMQVLSRMTGKELRIRYQVDPDIIGGLVVRLGDRIIDGSIKRQLERLKDSIRETKVG | 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... |
Q2RFX6 | MSEQNVARRYARALFNIAREQGTAGEFANGLEEVSRTLAENSDFRRVLYHQLIPVREKQKLIDTIFPDINPLLKNFLHLVLAKGRERALPEMAAQFRRLVDQAENILPVEVTSAITLREDILAGLKERLAGITRRNIRLSSRVNPELIGGVVIRLGDRVLDASVKKKLELLGEHLKRA | 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... |
A5IYE2 | MFIKANADGYALALYDLHKEEKHVSSTYENILSFYELLSNDKEVFSFFNSSKIGLEEKHKIADELVQENKNLKTFANFLKLLISKNNSPLLLQALSIYIRLVESELNILRAKLISAFEIDNQTKIKIIEKLENKYNKKIKLTTFIDKSLIFGFKIVIGNDIIEQNAKADLEKISSLINNKNGDLNG | 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... |
P33254 | MDTNIMGFARALVDLAHEEDKVHLFYDNLKVVFDLVKENQDLMSLMNSQVLSKNQKHEIIDVVFKDHLTQTIVDFLKVVIDNREFFHIKSIIKKFFRMIEEEEHTIFINVVSAHELNDDQKAQLVEKLHKKFASQVKILYQTDPSLIAGIRIQSNDLLIDNSIDGKLKLLKHQLRTFSKEN | 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... |
P47642 | MINAQAFGTALFQLSEEQKQVKKIYEECHFFLKLMRNFKDGSLSFLLNSYTLTKPDKIRLVDKLFKNHFCQVFVDFLKVIILKGYFTLVEQAIKYFFDNVESQKHIQFIKIITAFELSSKQLNKIIAIMEKRFKTKVVYKTEIDRSLISGIRIESSSHLFEKNVRDELKRIMAHFI | 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... |
Q6MS91 | MILKETTINNYATALFNIAVKEKLVDDYIIQVDALIKSLADKDEFNKLVTYSNKEQKKQAILIIENTFSSFGFDIYLINALKILVENQLFINTRMILKVLYKKLLAYKNIVLGEVYSTEKLTKTQLNAIKKKISNKVNKKVELVNKIDPTLIGGIKVSVEDKVFDGSIKAKLEALKKQMNT | 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... |
Q98QU2 | MIDNHYVQSSAKALSQIAFEEKKEKLFLNQLFIIKNIFSYNPEVVEYLASGSIKLENKKKFIEEIFDLIEPLILNFLLMAVEDNKIKYLDNIFLKAILTINKKLNIENGIIYTTLKLSDKKLLEIEKKLSVFLKKEVKLLNLIDKELISGYEIQVGDFKQRNNVASWIDQMALSIKKGD | 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... |
Q4A601 | MYVKVNPSSYSVAIYEIAKESNKIKTFHEQFSFVKKVIEKNPQLITFLKNDEIALEKRFELIDEIFGSLEVDVKNSIKVALVRNMIFVLRKIIVDFLKITNYELGIKFAKVITAYPLSDSELEKIQKKLNEKTKKIVEISTEVDEKLLSGYKIIFSNQLYERNYNNDLQKIKKTIIKGKEDEK | 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... |
Q1CWT4 | MVNVSIARRYARALLDVASEAGRTDAVAEQLTAFADVIAKNAELTDVLVNPAYTREQRLRVVESVMQAIPGGVEATLANTLRLLVDRNRLGYLADIARLFRDMADARAGRVRGHVTSAAPLPADALAQLQQTLQQLTQRNVLLETRVDPSLLGGVSAQVGSILYDGSIRTQLEEMRRELKQR | 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... |
B2A3G5 | MIIPKRYAEALFQLAKEREKINEITQSFNQLIERLRSNEEVFKLLSYPVVDIAEKKQVADELTADLEQEIRDYLKVLIDNKRTDELAEIHDTFLDLVRTEENRTLCEVKTPIPLDEDELKKIQDLLAQMSEGEVEIETTTDESIIGGIVVRIGDRVFDYSLKGQLNSLREQLKKTTITS | 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... |
B4RJF7 | MAEFATIARPYAKALFGLAQEKNQIESWLGGLEKLAAVVQEGKVALLIDRPETNASEKADILIDLVGLKDKELKNFVIVLAGQKRLSILPEVYAQYQDLTLSFNHIKSAVIYSAYPLTDKQVGELAQMLNKRFDSELKISVEIEPELIGGIKVEVGDQVLDLSVQGKLSALYTTMTN | 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... |
Q2GER4 | MQQYIAGRYAQSLYAVCGPRLESDANKFLGLLSENNFLSFAKVKTSTKLHVLDRLHLPCELKNLCKLLLANHRGFLCTTVLLGYIEIVKKNRKEADARVESYSRLSATAKKEVADALLIKFPYLKKINIAQKVNRSILGGLTIKINSIMIDLSIAGRLAKCKSIGQSTILEIFQ | 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... |
Q4L7Y7 | MANVANKYAKALFDVAIDKDRLDLMYDELSEVSEATKNYGEDLRAIDSNPNQPASERRKFVGIVFGDANYYLKNMLMILANNRHLVLINSIFKEFKSLYNEYHNEDSAIVESVYQLSDEELDRIKDLILKQTNLSQVHITTKINPELIGGFRVKVGTTVLDGSVKKDLEQIERKFRRVN | 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... |
Q49Z53 | MANIAKKYAKALFDTAKDADILDDMYDEFSTINEAVQSENKKLQALDADPQKDVEQRRRFVSIVFGQTNQYLQNMLTILASNRHLGHIHEIYIAFETLYNEEHNQDYAVIESVYQLSEEELSSIEEIIKARTKLSKIMITNKINPELIGGIRVKVGTKVMDASIKNDLAQLERQFIRVK | 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... |
Q8E5V1 | MNKKTQALIEQYSKSLVEVAIEHKIVEKIQQEVAALIDIFETSELEGVLSSLAVSHDEKQHFVKTLQTSCSTYLVNFLEVIVQNEREALLYPILKSVDQELIKVNGQYPIQITTAVALSPEQKERLFDIAKTKLALPNGQLVEHIDPSIVGGFVVNANNKVIDASVRNQLHQFKMKLK | 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... |
P07678 | MKTIHVSVVTPDGPVYEDDVEMVSVKAKSGELGILPGHIPLVAPLEISAARLKKGGKTQYIAVSGGFLEVRPDNVTILAQAAERAEDIDVLRAKARKSGRTPLQSQQDDIDFKRAELALKRAMNRLSVAEMK | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14334
Sequence Length: 132
Subcellular Location: Cell membrane
|
P37812 | MKTVKVNIVTPDGPVYDADIEMVSVRAESGDLGILPGHIPTVAPLKIGAVRLKKDGQTEMVAVSGGFVEVRPDHVTILAQAAETAEGIDKERAEAARQRAQERLNSQSDDTDIRRAELALQRALNRLDVAGK | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14209
Sequence Length: 132
Subcellular Location: Cell membrane
|
Q6G1X0 | MENNRVNHFLFELVSPEKPVFSEQVVSVVLPSASGALTVMANHAPLVASIVLGSMYVLTSSGEKLFAVCGGVANITSSGCSVLVERVVVVQHLSFHDLEQRILRVRATLEGDSNDGISHKIEDFFHQLKVGDAGLTEA | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14818
Sequence Length: 138
Subcellular Location: Cell inner membrane
|
Q6MGM8 | MNMKLTIVTPEKRILVGQEVDEVTVPAFKGELNILPGHAPLITTLETGVMKWKLKGKEKQDLAVISWGYCQVSPEGVNILANIADLPEEIDLQATKEFLALSEKKIMNELITDEDWAEFQRDWAHARAKIEAAEQQPAKK | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15737
Sequence Length: 140
Subcellular Location: Cell inner membrane
|
Q06J28 | MKLKVKIAIPGKVVWENEVDEVNIQTTTGKIGILPNHAPIIATVETSVLRMKSDESQNPILMVISDGYLSLEKNSIFIATDRCILEDNINASKLEEDYKTALERYNNAEKPGKKYIANKALKRINACYEILSYRNND | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15472
Sequence Length: 137
Subcellular Location: Plastid
|
Q74GX9 | MAEKLKVDLVTPYKKILSEEVDEITATGALGEFSVLPGHAPFLTSLKIGELTYKKSGQIVHLALNWGYFEVEDDKVTVLVETAERADEIDLERAKAALGRAEAALKKLSPEDKDYRVMEAALERALIRMQVAGKAARK | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15243
Sequence Length: 138
Subcellular Location: Cell inner membrane
|
Q7NHG9 | MALQIKIVAPNKVVFDDQVDEVVLPSVSGQLGILTNHAPLITGLSNGVMRVRKQGTFIPIAVLTGVAEVDNNEVSVVAMAAELGSGIDVDRARAALARAEQTLATSQNKTELLQAQTALERANARLRAAGAL | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13825
Sequence Length: 132
Subcellular Location: Cell inner membrane
|
A9H9B1 | MMPIKVEIVSPEKVLFSRAVDMALIPGLEGDIAAMPDHAPMMLLLRGGVVELHQDGAVTDRFFVAGGFADMTETSCTILADQATALSDLSVEAAQARLAELEASYDKADKMNVPVLDLLMAKMQSARAEIEAAGGPAVQGA | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14830
Sequence Length: 141
Subcellular Location: Cell inner membrane
|
Q0BQE9 | MAQTSLEIVSPEKRLLSRSVDMVVIPAAEGELGVLPGHAPMIVLLQGGTIRLYQNGQVTDRLYVAGGFAEITPERCTVLADQARPVAEISATEAEKRLADAEAAYATVDKLDITALDAAMESIQAARAMVEAARH | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14358
Sequence Length: 135
Subcellular Location: Cell inner membrane
|
O78492 | MSIHISIIAPDRTVWDANAEEVILPSSTGQLGILKGHAPLLTALDIGVMRVRVDRDWTPIVLLGGFAEIENDELTILVNGAEEASQIDRDQAQRDLEEMTVKFNEATTNKERIEATQNLRKARARLQAVSA | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14473
Sequence Length: 131
Subcellular Location: Plastid
|
P84559 | QIIEANLALRR | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 1297
Sequence Length: 11
Subcellular Location: Plastid
|
Q7VA75 | MSLTLRVLAPDKSVFDDTVEEVILPSTTGLLGILPGHISMVTAIDIGVLKLRSSNGNWDSIALMGGFAEVESDDVTVLVNAAELGKSIDKATAEKEFEQAKAALNKLEDQAGNSADKLKAKESLNKARARSQAVGE | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14367
Sequence Length: 136
Subcellular Location: Cellular thylakoid membrane
|
Q82J85 | MAAELHVELVAADRQVWSGEATLVVARTTSGDIGVMPGHQPLLGVLESGPVTIRTSDGETVVAAVHGGFISFADNKLSLLAEIAELADEIDAQRAERELERAKAEGDATAERRADVRLRAVSAR | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13129
Sequence Length: 124
Subcellular Location: Cell membrane
|
P0A2Z6 | MAAELHVALVAADREVWSGEATLVVARTTSGDIGVMPGHQPLLGVLESGPVTIRTSDGGTVVAAVHGGFISFADNKLSLLAEVAELSDEIDVHRAERKLEQAKTEGDAHAERRADVRLRAAAGR | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13018
Sequence Length: 124
Subcellular Location: Cell membrane
|
Q04N64 | MAQLTVQIVTPDGLVYDHHASYVSVRTLDGEMGILPRHENMIAVLAVDEVKVKRIDDKDHVNWIAVNGGVIEIANDMITIVADSAERARDIDISRAERAKLRAERAIEEAQDKHLIDQERRAKIALQRAINRINVGNRL | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15638
Sequence Length: 139
Subcellular Location: Cell membrane
|
Q9TM29 | MQDILNIYLSSEESGGLFDFDATLPLMASQFLLIMLILDITFYKPINKVLKDRENYILKTLESATQISEKTKETLARYEEVILKSKKESQQLIDSIKTKTEHDIVNELIQTQNSTREFISKSIKELYRKKEQTLKVLEEDTENLSDKIYLKLINPKQ | 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... |
Q85FR1 | MSTGLFDFNGTLPVMGLQVVLLSWLLEQILYSPIQGVIQKRQNKIQQELQLAADQLQKAQQLTQEYQTQLQKAREKARERIRQVQQEAQTMMEDQLKQAQQQMTQLFNEAMQQLEQQKQQALMNLSNQVDEVAKFILSKLMKQ | 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... |
P48085 | MTQWIIWLAIETEAAKPEGGLFDFDATLPVMMVQLLVLMLILNAVFYKPLIKILDERKEYIQSNFNEAEKCLAQAAELTTQYETKITDARQNASKLTNTTRSEIQRFVSEKLEEAQKKADSELASATNKLELQKDEALKSLESEVQTLSTKILEKLLGIQIANT | 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... |
A8ZVQ5 | MRKNNGIKWWGWVTLSVLVMVAGDGTLAFAQETGGSAGWRPVYDNVMLVINFLILVFLLAKLLKNPLKNFLKTRHDEVAKELERLETERERAANDVADTKKQVAAEGTHILEIRERIIAEGERTKLAIIENAKKESEFLIEAARRRIQGRFQEARQAFRSELIESAMSIVSRRLPQEIGPQDQARQVDLFFTSLDQAQSKFSSARSASR | 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... |
A8LKH8 | MATEATGAVEAAPGMPQLDFSTFPNQIFWLIITLVAIYLILTKVALPRIGSVLAERSGTITNDLAAAEELKLAAVEAEKAYNQALADARAEAQKIVAEARAEIQADLDVATAKADAEIAAKSAEAEKAIAEIREGAMASVTEVATDTAQALVAALLPSAKDADVSAAVAERVKG | 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... |
P35012 | MQYQYINSYSLLAAGGLFDFDATLSFIALEFLLLTSVLNLIYYQPISKVIDSREDYIRENLNKASLYLDQANELTKKYELELITARKEAIKMVTTSQTEAQEFVNAQISQAQKEAQQLIQSSMMQFEKEKNKAIYSLEKQVEQLSEQIKNKLISIYI | 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... |
Q7NCS0 | MDMLFDPGWAAHLLLLAAEEAAAAEAESGGLFDFGGTLVLQIVNFLLLMTILSAVFYGPISRVIEERSEYIRSNAGSAQRRFDEAKALADQYEQELRTTRLEAQQVIAAAEAEAQKIRAQQLAEAQREAQERIAQAQADLDKQKQAALASLSGEVEAISRTLSEKLLSDSARRF | 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... |
Q5FNY7 | MTVDWWTIGLQVINVSVLIWLLSRFFWRPICAVISRRQQEIAAQLAQVTDGQKQLEADRAAVKEARSSFEQERARIVQQAQQEAQSERQAILAKAQQDAAALEAGAKQSIAQEEAENQARWRSDAAALSCDIAGQLLAQTGCCRPARETLFDRLLKAIATLPDRERLSLRDGFTFATATAPSPDERQAYESALMTAVGEHPVITWAVDPALVEGFAVKTPYLTVASNWQADLVRIREGLSHAGH | 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... |
Q0BQY4 | MQAHELSGAPWHHPVFWVAVAFVLFFVLFGRKIWGALTSKLDSYADEVRQNLDEARKLRREAEAMLEDARRRKEQALAEAKRLLESAHAEAARAAQALSDDAEASIRRREKMANDRIAAAEKAAVDEVRFAAADIASRAAKDILAREFGPYADAALIDSAISKLPQALRAA | 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... |
O78478 | MTNYLYILALQIAEAESEGGLFDFNATLPLMAVQILLFMVILNAVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLIISVAQKEAQDIVALEIKQAQKDTELLVNEATSQLNSQKQKALSALEDQVNTLTEQIKSKLLSNQLIS | 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... |
Q0AK30 | MMIRAEDAGHGEEQTLLEWLAAQPGDPSFYAFLALLIFFGLLLHMGVHRTIAKTLDDRAEGISNELDEAKRLREDAAEMLASYQRKQREAEAEAEAIIAQAKTEAKSLKAEARKEMTERLERRTAMAEQRIAQAEAQAAADVKAAAAELAAQAAEEILKTQLKKSDLNKLVDADIKTVGQRLN | 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... |
Q603U6 | MDLNPSTFVLEIVNFLVLVWLLKRFLYQPVSAAIEERRRQIARTVAEARDTQTAAETLRMQYESRLADWESEKRQAREAFKQEIEAERQRALDELEKALDAEREKARVLIERQRRDMESDLERQALRLSRQFASRFLERLAGPEMEAALLRMFGEDLAAMSPEQWQALTRALEEQEHPEAEIASAFPLKPESCAELTEMIEARTGRAVAWRFREDPALICGIRLRAGHRVLAANVGEELKFFADGAENSLGGG | 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... |
B1ZJN3 | MAEQNILTTPSPNADTTIVPPGSPHTHTEQPSGGHGGAFPPFESHTFLAQLIWLALAFGLLYYLMSKVALPRIEAILGDRAGRLSSDLNEAQRMKAEADAAGAAYETSLREAQAKAQAIAQETRNSLSAEADAKRKTLEAELNQRLAASEATIRARTSEAMGNVRTIAGETASAIVERLTGQAPDQASLNRALDATPAVH | 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... |
Q8RC19 | MKEGKALELFNLSTFVFTIINLLVLYYILKRLLFKPVTKFLEDRENKIKSALEDADKQREEAYSLKAQYEEKLQNAENEGRAIIEKAQKEAEERASEIIKSANKEAESIIEKAKEEAVLEKIKAMHELRAEMSHLIIEAASKVLEKKLPVEDEDLIKEVIEEAGSWNK | 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... |
A4XKX4 | MFDLAIFENMFFWAIINFLILYLIYRKFFFKKVTAFMEKRSKMIQEQLDFAAKSKEEAIKLKEEYENILSQAHAKANEIVQNAMIEAQKQADKIIEDAKLEANKIIENALKQLDIEKKKQINELKNQFVSIALLAASKVIEKNLNTEENRKIVENIFDEAGVA | 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... |
A7ZC33 | MKIKILFFLALPFLAYASEHGGTNYDIVERTLNFLLFFAILVYFAAKPLKALYQSRIDRIANKLESIQEKLRESKAKKDDVLKRVEEAKQNANALIETAKKEAVNLAAKVKKEAQNDIANIEKGYKEQKEFEERKMTKGVVNEILSDIFSSDSLKVDQKELVNIILKKVS | 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... |
A7I173 | MNKFLFFIFVFVGISFAGDDTATKDYDIVWRTINFAIFFGILFYLIKGPIKNAYNARINRISSRLEAIQTKLKESKEKKEASKKNLEDVKQKCVELIETAKKEAIQLDEKIQQSAQIDIAQMQKSFAEQKEFEIRRLKKSVTAEILDELFNEKSVNLSQNELINLVQKKVV | 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... |
Q3A942 | MHFDWSDFIWTLINFFVLLFILKILLYKPVLKTIEDRKKSIEESLEKAAKAQEEAERIKAEYDGMIAKAREEAREIIAKAQKTAQAEKEEIIATAQREAQSLLADAKATIAQEKEKALRELRQEIGNLAVLAAGKILNRAVTLEDHQKLVDEFLNEVKM | 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... |
P56086 | MFVVKMVLGFLILLSPLCATGLDISQTDIIERSLNFLLFVGILWYFSAKKLRSFLRSKSLEISKRLEEIQAQLKVSKENKKKLLKELEQAKEKAELIVSDANKEAYMITQKYELQTKMDVENLIKNSKALMDLEVKKIKRELVESVFKDLRESKKVSFNAQDCVNILKQRL | 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... |
A9AVV0 | MDKLGVDLPLLISQIVNFCLLAFLLNTFLYKPVLNALQARSERIRESLDNAEKVKQQLARVDADYEAKLQEARREGQTIISQAQERARAQEAELLVVARNNAAKIEEEARGKVEQERQQVLRGLQGQLASLVTETASNVLGRELQTKGHDELINKSIDQLGRLN | 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... |
B2XT88 | MENLTNIFLFLSNENEGIQLNTDIFEANIINLALLIVLVINVAKDVLGSILSARKASILDKIEEADKKLNEADKRFTEARLQWSQANIFGEDLEKKTYQRINAFHESQNLKNKDALLREYFSTLVVLDLKNEQVQKQVRNYVMELALIEVYGVFTKLVANKKFQENYSNYSVLLLEKLIGEK | 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... |
Q0C0X0 | MKKTTSLLIAALAVAPLAHAAEGGFVGGLMYAATDPVTFVAFLCMVTFLLIAARMGAFKTILGGLDTRASNIRKELEEAASLREQAAEALALAERRAQDADKEAEAIIDQAKRDAKAMLEEARRDLAEKISRREAQAAARITRAETEATSEVRRAAADAATAAARRILSEQTSVDQFEAAARDIERALS | 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... |
A8Z5R3 | MTPSLGLIFWQSVIFLISFIILSKFAWNPINKLLEKREKYIIDSINNAEKAKEYLKNIKLKKKNILKNTEKMKYFIINEAFKKKEQIEKEAKKKAKLESYLIINKTQLLIENKKKIAIEKIKNEILNMSIIISEKILNKELEINEKNNNYFFNKKLLIIMKFSYKIFIKRYAKGFFFLVFNSKKEIFIKNEIEKFFSYKKELYKKNYFKFKYTFFKKKRKDNFF | 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... |
B2A3G6 | MVDPNLVTFVLTIVNILVLFYLLKRFLFKPIGEFMENRKNEIKQNLEDAEKERQEAEKLKEQYYEKLRGAKSEAQEIIQQARQREEEIIKEAKQEAKQEADDMIARAREEINQEQKKAIESLRSEVSDLTIQITERVLNDTIDKDQQKKLVQKYLKEVGRVS | 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... |
Q9TL15 | MFHFLALTPLAHSEGFGLNTNILETNILNLAAVFALLAYVGTDFVSSLLKTRKESILKSLRDADERYQDAVNQLKQALQELETARTNAAEIRRQSEINAEAIRQRLELLTQEEMARLEEAKETIIKLEEEKAVAEVCTKVISMALVRAEKKIISSMDEAMHRRVMDMYLNLLREVY | 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... |
Q3J6M7 | MNVTVTLIGQMVAFGILVWFVNRFLWGPLTNLMEERKKRVADGLAAAERGKHERELAEKRAKETLHEAKEKAAEIITQAQKRAGEIIEEAKEAAQAEGERLKVSANAEIQQEMNRAREDLRGQVVSIAVAGASKILKRELDEKANEALVKELVAQI | 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... |
A6Q4C4 | MKQKLLMLLLLGSVSLFANEAAASGGTDIIPRTVNFLIFAAILYYLAAEPIKRFFQERKEGIAKRLEEVEAKLKEAKEEKAQAEAELKKAKELAQEIVETAKQEIEILTKEIKEQAKQEIEMLEKSFEESMELEKRKRVRAITKEVLEELFEEKALELEKEKFVNLIVKKVA | 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... |
Q5Z0Y5 | MYEYSVLAAESGEDVNPLIPATYDIVWSVVCVAIIAVVFYKYVIPRLTKVLNERADKIEGGIAKAEAAQAEAQQTLEQYQQQLADARLEAARIREDARTQGQQILAQMRAEAQAESDRIVAAGHAQLEAQRQQILTELRSEVGRTAVDLAEKIIGQSVSDEAKQAASIERFLSELDSSDAGIGVGR | 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... |
P12407 | MGTFLLLMAEASAVGGELAEGGAEGGFGLNTNILDTNLINLAIIITVLFVFGRKVLGNTLKTRRENIETAIKNAEQRAADAAKQLKEAQQKLEQAQAEAERIKKSAQDNAQTAGQAIIAQAAVDIERLQEAGAADLNAELDRAIAQLRQRVVALALQKVESELQGGISEDAQKTLIDRSIAQLGGGV | 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... |
P95785 | MSTLINGTSLGNLLIVTGSFILLLLLVKKFAWSQLAAIFKAREEKIAKDIDDAENSRQNAQVLENKRQVELNQAKDEAAQIIDNAKETGKAQESKIITEAHEEAGRLKDKANQDIATSKAEALSSVKADVADLSVLLAEKIMAKNLDKTAQGDLIDSYLDKLGDA | 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... |
A9WGS5 | MPSSREIKRRIRSVKNVAQITRAMEMVSASKMRRAQRNVLATRPYADRMREVMANLTARVVGAARRGTLLEKRETVKSVALLVVTPDRGLCGSLVANVLRRAGRFITEQRAMGRTVDVYTFGRKGRDFFLRTGFAPAGEATRLGDAPKLEAILGVAISAINGFQSGKYDELYIIYSEFINTLVQRPAIKQLLPVESPDISTTTNVDYTYEPGEEEVLNSILPRYVETQIYQAVLESIASEHSARMVAMRNATNNAKDLVRDLTLSFNKARQAAITKEVSEIASGAAALTS | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32075
Sequence Length: 290
Subcellular... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.