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MT-ATP6

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Petromyzon marinus
Length
237 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
26.158 kDa
Sequence
MTLDIFDQFTSPTMFGLPLAWLAMLAPSLMLVSQTPKFIKSRYHTLLTPILTSIAKQLFLPMNQQGHKWALICMASMMFILMINLLGLLPYTYTPTTQLSMNMGLAVPLWLATVLIGLQKKPTEALAHLLPEGTPAALIPMLIIIETISLFIRPIALGVRLTANLTAGHLLMQLVSMTTFVMIPVISISIITSLLLLLLTILELAVAVIQAYVFILLLTLYLQENVYVPPSSCMPHG

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Myxine glutinosa
Length
228 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane (By similarity).
Similarity
Belongs to the ATPase A chain family.
Mass
25.341 kDa
Sequence
MMMSLFNTFESPYFLGFPLMIFIAILISLTMFIPDNNLLIKNQSSMLASTFLKTMTKEIFSPIKKSGHSWALLLMTTLMFIFLNNITGLLPYTFTVTSQLSLNMAMAIPLWLGTIIMGATSQPSHSLAHLLPEGTPMTLAPFLIVIESISIIIRPLALGVRLTANITAGHLLIHLVSLALINLTKSLPLLFLTFSVFILLLILELAVSFIQAYVFVMLVSLYLEENLI

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Pelomedusa subrufa
Length
228 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
25.25 kDa
Sequence
MNLTLFDQFSSPNILAIPLMTISLLMLTIIFPMKHNRLLTNRLLSIQSKMIHIFTKQLMLPIPKSGHHWALILTSLMTLLLTSNLLGLLPYTFTPTTQLSMNLGFALPMWLATLLIGLRNQPTMSLAHLLPEGTPTPLIPTLILIESISLMIRPLALGVRISANLTAGHLLMQLTSSATLSLSSMPTLSFMTAILLFLLTILEMAVAMIQALVFVLLLSLYLQENTHN

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Anas platyrhynchos
Length
227 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.997 kDa
Sequence
MNLSFFDQFSSPHLLGHPLILLSLLLPALLFPSPGNRWINNRLSTIQLWLLHLITKQLMIPLNKNGHKWALMLTSLMTMLLTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNKPSASLAHLLPEGTPTPLIPALILIETTSLLIRPLALGVRLTANLTAGHLLIQLISTASIALKPILPTVSILTMAILLLLTILEVAVAMIQAYVFVLLLSLYLQENI

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Coturnix japonica
Length
227 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
25.026 kDa
Sequence
MNLSFFDQFSSPYLMGMPLILPSLLLPTLLFPTPGRRWISNRLSTLQLWVINLITKQLMTPLNKTGHKWALLLTSLILLLLSINLMGLLPYTFTPTTQLSMNMALAFPLWLATLLIGLRNQPSASLAHLLPEGTPTPLIPILIMIETTSLLIRPLALGVRLTANLTAGHLLIQLISTATIALLPTMPSISTLTALILLLLTILEVAVAMIQAYVFVLLLSLYLQENI

Gene
mt-atp6
Protein
ATP synthase subunit a
Organism
Cyprinus carpio
Length
227 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.988 kDa
Sequence
MMVSFFDQFASPSYLGIPNIAVAIALPWVLYPTPPARWINNRLITIQGWFINRFTNQLMLPLNVGGHKWALLLASLMIFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTIALGHLLPEGTPIPLIPVLIIIETISLLIRPLALGVRLTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV

Gene
mt-atp6
Protein
ATP synthase subunit a
Organism
Danio rerio
Length
227 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
25.093 kDa
Sequence
MMTSFFDQFASPYLLGIPLILVAMLLPWLLFPAPTSRWINNRLITVQTWLTGRFTNQLMTPLNFSGHKWALLFASLMVFLITINLLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMKNQPTIALGHLLPEGTPIPLIPALIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLPMMPAVAILTASVLFLLTLLEVAVAMIQAYVFILLLSLYLQENI

Gene
mt-atp6
Protein
ATP synthase subunit a
Organism
Salmo salar
Length
227 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane (By similarity).
Similarity
Belongs to the ATPase A chain family.
Mass
25.108 kDa
Sequence
MTLSFFDQFMSPTYLGIPLIAVALTLPWILFPTPSTRWLNNRLITLQGWFINRFTQQLLLPLNLGGHKWAVLLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTAALGHLLPEGTPVPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAAFVLMPIMPTVAILTSIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Scyliorhinus canicula
Length
227 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
25.382 kDa
Sequence
MIMSFFDQFLSPSFLGIPLIALAISIPWLMFPTPTNRWLNNRLLTLQAWFINRFIYQLMQPMNLGGHKWAILFTALMLFLITINLLGLLPYTFTPTTQLSLNMAFALPLWLTTVLIGMFNQPTIALGHLLPEGTPTPLVPVLIIIETISLFIRPLALGVRLTANLTAGHLLMQLIATAAFVLLTMMPTVALLTSLVLFLLTILEVAVAMIQAYVFVLLLSLYLQENV

Gene
mt-atp6
Protein
ATP synthase subunit a
Organism
Tetraodon nigroviridis
Length
227 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
25.077 kDa
Sequence
MTLSFFDQFLSPTLFGIPLIALALLLPWTLFPAPSSRWVNSRLLTLQSWFINRFTQQLLLPLNMGGHKWGPYILLVMVFLISINMLGLLPYTFTPTTQLSVNMALAVPVWLMTVIIGLRKNPTAALGHLLPEGTPVPLIPALILIETISLFIRPLALGVRLTANLTAGHLLIQLIATAAFVLLPLMPTVAILTTILLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV

Gene
mt-atp6
Protein
ATP synthase subunit a
Organism
Formosania lacustris
Length
227 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.931 kDa
Sequence
MAMSFFDQFASPSYLGIPLIAIAIALPWVLFPLPSLRWVNNRLITIQGWLINRFTNQLMLPLNTGGHKWALLLASLMVFLITINMLGLLPYTFTPTTQLSLNMGLAIPLWLATVIIGLRNQPTVALGDLLPEGTPLPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLPMMPTVAILTATVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV

Gene
mt-atp6
Protein
ATP synthase subunit a
Organism
Gadus morhua
Length
227 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
25.05 kDa
Sequence
MTLSLFDQFSSPSFLGIPMILMALALPWLLIPTPTSRWLSNRVVSLQGWFIARFTNQLFLPLNVGGHKWAPLLASLMMFLLTLNMLGLMPYIFTPTTQLSLNLGLAVPLWLATVLIGMRNQPTHALGHFLPEGTPTALIPILIIMQTISLFIRPLALGVRLTANLTAGHLLIHLISSAVFVLMPMMPVVAILTAVLLLLLTMLEVAVAMIQAYVFILLLSLYLQENV

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Squalus acanthias
Length
227 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane (By similarity).
Similarity
Belongs to the ATPase A chain family.
Mass
25.363 kDa
Sequence
MNLSFFDQFLSPSLLGIPLIAMAIMIPWLIFPTPTNRWLNNRLMTVQSWFINRFTYQLMQPMNFGGHKWATILTALMLFLITINLLGLLPYTFTPTTQLSLNMAFAIPLWLTTVLIGMLNQPTVALGHLLPEGTPTLLIPILIIIETISLFIRPLALGVRLTANLTAGHLLMQLIATAAFVLITIMPTVALLTSLILFLLTILEVAVAMIQAYVFVLLLSLYLQENV

Gene
mt-atp6
Protein
ATP synthase subunit a
Organism
Carassius auratus
Length
227 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane (By similarity).
Similarity
Belongs to the ATPase A chain family.
Mass
25.066 kDa
Sequence
MMVSFFDQFASPSYLGIPLIAIAIALPWVLYPTSSSRWINNRLITIQGWFINRFTNQLMLPLNVGGHKWALLLASLMIFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLMPMMPTVAILTATVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Gallus gallus
Length
227 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.797 kDa
Sequence
MNLSFFDQFSSPCLLGIPLILPSLLLPALLLPSPGNRWINNRLSTIQLWFTHLITKQLMTPLNKAGHKWALLLTSLILMLLSINLLGLLPYTFTPTTQLSMNMALALPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAGHLLIQLISTATIALLPMMPSISALTALILFLLTILEVAVAMIQAYVFVLLLSLYLQENI

Gene
mt-atp6
Protein
ATP synthase subunit a
Organism
Polypterus ornatipinnis
Length
227 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
25.25 kDa
Sequence
MTLSFLDQFASQSFLGIPLIAIAILIPWMLFPSPYKRWMSNRLITFQSWFIARTTNQLMLPLNTGAHKWAMILTALLLFLMTLNLLGLLPYTFTPTTQLSMNMALAVPLWLATVLIGMRNQPTHSLAHLLPEGTPTPLIPILIIIETISLFIRPLALGVRLTANLTAGHLLIQLISTATFVMLSIMPTIATLTFIVLALLTILEIAVAMIQAYVLVLLLSLYLQENV

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Struthio camelus
Length
227 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
25.048 kDa
Sequence
MNLSFFDQFASPQLLGIPLILLSLLFPTLLLPSPNNRWINNRLSTLQLWFLQLITKQLMMPLNKAGHKWALILTSLMTFLLLINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPSISLGHLLPEGTPTPLIPALILIETTSLLIRPLALGVRLTANLTAGHLLIQLISTATLALLPTMPTISVLTATVLLLLTILELAVAMIQAYVFVLLLSLYLQENI

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Rhinoceros unicornis
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.918 kDa
Sequence
MNENLFASFTTPTMMGLPIVILIIMSPSIMFPSPNRLINNRLISIQQWLLQLTSKQMMSTHNNKGQTWTLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVLTGFRHKTKASLAHFLPQGTPTFLIPMLVIIETISLFIQPVALAVRLTANITAGHLLMHLIGGATLALMNISPTTSFITFITLVLLTILEFAVALIQAYVFTLLVSLYLHDNT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Ornithorhynchus anatinus
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
25.18 kDa
Sequence
MNENLFAPFITPTVLGISVLPLIMIFPCLLFSTSNRWVPNRLIALQLWLVRLITKQMMMMHNKQGRMWTLMLITLIIFIASTNLLGLLPYTFTPTTQLSMNMGMAIPLWMGTVLMGFRNKPKASLAHFLPQGTPTPLIPMLIIIETISLFIQPLALAVRLTANITAGHLLIHLIGSATLALSSISLTVSTITFTILFLLTILEFAVALIQAYVFTLLVSLYLHDNT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Pan paniscus
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.758 kDa
Sequence
MNENLFASFAAPTILGLPAAVLIILFPPLLVPTSKHLINNRLITTQQWLIQLTSKQMMTMHNTKGRTWSLMLVSLIIFIATTNLLGLLPHSFTPTTQLSMNLAMAIPLWAGTVVMGFRFKTKNALAHFLPQGTPTPLIPMLIIIETISLFIQPMALAVRLTANITAGHLLMHLIGSATLALSTISLPSTLIIFTILILLTVLEIAVALIQAYVFTLLVSLYLHDNT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Pan troglodytes
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.77 kDa
Sequence
MNENLFASFAAPTILGLPAAVLIILFPPLLVPTSKHLINNRLITTQQWLIQLTSKQMMTMHSTKGRTWSLMLVSLIIFITTTNLLGLLPHSFTPTTQLSMNLAMAIPLWAGAVVMGFRFKTKNALAHFLPQGTPTPLIPMLVIIETISLLIQPMALAVRLTANITAGHLLMHLIGSATLALSTINLPYALIIFTILILLTILEIAVALIQAYVFTLLVSLYLHDNT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Papio hamadryas
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.865 kDa
Sequence
MNENLFTSFSAPTILGQPATIPIIMFPTLLIPTSKHLINNQLTTVQQNLIKLTLKQMMAPHNAKGQSWSLMLMSLITFITMTNLLGLLPHSFTPTTQLSMNLAMAIPLWAGTIITGLRFKTKNFLAHMLPQGTPTPLIPMLVMIETISLLIQPMALAVRLTANITAGHLLMHLIGNTMLTLSTINLSTTLLTSVLLMLLTILEIAVALIQAYVFTLLVNLYLHNNT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Didelphis virginiana
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
25.145 kDa
Sequence
MNENLFAPFITPTILGITTLPIIITFPCLILSSPKRWLPNRIQILQMWLIRLITKQMMTMHNKQGRTWTLMLMSLILFIASTNLLGLLPYSFTPTTQLSMNIGMAIPLWAGTVIMGFRNKPKMSLAHFLPQGTPTPLIPMLIIIETISLFIQPLALAVRLTANITAGHLLIHLIGSATLALSSISMTVSTITFSILFLLTLLEIAVAMIQAYVFTLLVSLYLHDNS

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Dugong dugon
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.78 kDa
Sequence
MNENLFTSFITPTMMGLPIVILVIVFPAMLYPSPNRLINNRLISIQQWLVQLILKQMLLIHNSKGRTWALMLISLILFIGSTNLLGLVPYTFTPTTQLSMNLGMAIPLWAGAVITGFRHKAKASLAHFLPQGTPITLIPMLVVIETISLFIQPMALAIRLTANITAGHLLMHLIGGAVLALTSISPAAATITFIILLLLTILEFAVALIQAYVFTLLVSLYLHDNT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Cricetulus griseus
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
25.04 kDa
Sequence
MNENLFSSFITPTLMGLPIIILIIMFPPVIMTSSKRLVNNRFHTFQQWLIKLITKQMMAIHSPKGRTWSLMLASLIIFIGSTNLLGLLPHTFTPTTQLSMNLGMAIPPWAGAVILGFRHKMKDSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISLPTAMITFIILIMLTILEFAVALIQAYVFTLLVSLYLHDNT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Dasypus novemcinctus
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.946 kDa
Sequence
MNENLFASFATPTMMGLPIIMLIIMFPSILFPTPKRMITNRVVSVQQWLINMIMKQMMNIHNNKGRTWTLMLISLITFIGTTNLLGLLPHTFTPTTQLSMNLGMAIPLWAGAVVTGFRHKTKASLAHFLPQGTPIPLIPMLIIIQTISLFIQPMALAVRLTANITAGHLLIHLIGGATLALMSISPTTASITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT

Gene
mt-atp6
Protein
ATP synthase subunit a
Organism
Xenopus laevis
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.943 kDa
Sequence
MNLSFFDQFMSPVILGIPLIAIAMLDPFTLISWPIQSNGFNNRLITLQSWFLHNFTTIFYQLTSPGHKWALLLTSLMLLLMSLNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIMASKPTNYALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAAFVLLSIMPTVAILTSIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Gorilla gorilla gorilla
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.776 kDa
Sequence
MNENLFASFIAPTILGLPAAVLIILLPPLLIPTSKYLINNRLIATQQWLIQLTSKQMMTMHNAKGRTWSLMLMWLIIFIATTNLLGLLPHSFTPTTQLSMNLAMAIPLWAGAVTTGFRSKTKNALAHLLPQGTPTPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGSATLAMSTTNLPSTLIIFTVLILLTMLEIAVALIQAYVFTLLVSLYLHENT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Halichoerus grypus
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.863 kDa
Sequence
MNENLFASFTTPTMMGLPIVILIVLFPSILFPSPDRLINNRLTSIQQWLIQLTSKQMLSIHNHKGQTWALMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRHKTKASLAHFLPQGTPLPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLALMDISTTTAFITFIVLILLTILEFAVALIQAYVFTLLVSLYLHDNT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Tachyglossus aculeatus aculeatus
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
25.11 kDa
Sequence
MNENLFASFITPTILGISILPLIMIFPCLLFSAPNRWMPNRLVALQLWLVRMVTKQMMSMHNKQGRMWTLMLITLIMFIASTNLLGLLPYTFTPTTQLSMNMGMAVPLWLGTVLMGFRNKPKSSLAHFLPQGTPTPLIPMLIIIETISLFIQPVALAVRLTANITAGHLLIHLIGSATLALSSISLTVSTITFTILFLLTILEIAVALIQAYVFTLLVSLYLHDNT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Lemur catta
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.842 kDa
Sequence
MNENLFASFITPTIVGIPIVILIIMTPYIIFPSPTRLINNRLTSLQQWLVQLILKQLMSIHNTKGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIKGFRHKTKASLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISPATASITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDNT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Lycodon semicarinatus
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
25.158 kDa
Sequence
MTMNMFEQFMSPELLMIPTALLSMLVPVLLIHHNPKLLGNRMTTAIAWLLMTIMSNMTNQLTPSGQKWCQVLTSLLLMILLSNLLGLLPYTFTSTSQLSMNMAMAIPLWMATIITGMTKKPSITLAHMLPEGSPTPLIPFMIIIETISLLMRPLALGVRLTANITAGHLLMTMVSTTTLNFITSHITLSIMTYLLLFLLCILELAVACIQAYVFVLLIILYLQENT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Oryctolagus cuniculus
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.746 kDa
Sequence
MNENLFSSFATPTLMGLPIVALIIMFPTLLFPSPSRLINNRLVSTQQWLAQLILKQMMLMHSPKGRTWSLMLISLIMFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRYKTKASLAHFLPQGTPIPLIPMLIVIETISLFIQPMALAVRLTANITAGHLLMHLIGGAALALVSISPTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT

Gene
Mt-atp6
Protein
ATP synthase subunit a
Organism
Rattus norvegicus
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
25.076 kDa
Sequence
MNENLFASFITPTMMGLPIVVTIIMFPSILFPSSERLISNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIGSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLMDISPPTATITFIILLLLTVLEFAVALIQAYVFTLLVSLYLHDNT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Equus asinus
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.987 kDa
Sequence
MNENLFASFATPTMMGLPIVILIIMFPSILFPSSNRLINNRLISIQQWLVQLTSKQMMTIHNNKGQTWTLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVFMGFRHKTKAALAHFLPQGTPIFLIPMLVIIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLALMDISPSTALITFIILILLTILEFAVAMIQAYVFTLLVSLYLHDNT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Felis catus
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.805 kDa
Sequence
MNENLFASFTTPTMMGLPIVILIIMFPSILFPSPNRLINNRLVSLQQWLVQLTSKQMLAIHNHKGQTWALMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRHKTKASLAHFLPQGTPVPLIPMLVVIETISLFIQPMALAVRLTANITAGHLLMHLIGGAALALMNISTSIALITFTILILLTILEFAVALIQAYVFTLLVSLYLHDNT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Balaenoptera musculus
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.967 kDa
Sequence
MNENLFAPFMIPVMLGIPITTLIIILPSILFPAPNRLINNRTISIQQWLTKLTSKQLMSVHSPKGQTWSLMLISLFLFIASTNLLGMLPHSFTPTTQLSMNVGMAIPLWAGTVATGFRNKTKMSLAHLLPQGTPTFLIPMLVIIETISLFIQPVALAVRLTANITAGHLLMHLIGETTLVLMSTSLFTAIITFTILALLTILEFRVALIQAYVFTLLVSLYLHDNT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Balaenoptera physalus
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
25.072 kDa
Sequence
MNENLFAPFMIPVMLGIPITTLIIILPSMLFPAPNRLINNRTIAIQQWLTKLTSKQLMNVHSPKGQTWSLMLISLFLFIASTNLLGMLPHSFTPTTQLSMNVGMAIPLWAGTVTTGFRNKTKMSLAHLLPQGTPTFLIPMLVIIETISLFIQPVAWAVRLTANITAGHLLMHLIGETTLALMNINLFSAFITFTILALLTILEFAVALIQAYVFTLLVSLYLHDNT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Macropus robustus
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
25.101 kDa
Sequence
MNENLFATFITPTILGITTLPIIMLFPCLLLTSPKRWLPNRIQILQVWLIRLITKQMLTIHNKQGRSWALMLMSLILFIASTNLLGLLPYSFTPTTQLSMNIGMAIPLWLATVLMGFRNKPKISLAHFLPQGTPTPLVPMLIIIETISLFIQPVALAVRLTANITAGHLLIHLIGSATLALCSISVTVSTITFIILFLLTILELAVAMIQAYVFTLLVSLYLHDNS

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Ovis aries
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.798 kDa
Sequence
MNENLFASFITPMMFGLPLVTLIVLFPSLLFPTSNRLVNNRLISLQQWMLQLVSKQMMSIHNTKGQTWALMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWGGAVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPVALAVRLTANITAGHLLIHLIGGATLALMSINTTTALITFIILILLTVLEFAVAMIQAYVFTLLVSLYLHDNT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Canis lupus familiaris
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.789 kDa
Sequence
MNENLFASFAAPSMMGLPIVVLIVMFPSILFPTPSRLINNRLISIQQWLIQLTSKQMLAIHNQKGRTWALMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRYKTKASLAHFLPQGTPLPLIPMLVVIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLALINISATTAFITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Canis lupus
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.789 kDa
Sequence
MNENLFASFAAPSMMGLPIVVLIVMFPSILFPTPSRLINNRLISIQQWLIQLTSKQMLAIHNQKGRTWALMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRYKTKASLAHFLPQGTPLPLIPMLVVIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLALINISATTAFITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Capra hircus
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.917 kDa
Sequence
MNENLFTSFITPMMLGLPLVTLIILFPSLLFPSSNRLINNRLVSLQQWALQLMSKQMMSIHNTKGQTWTLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRNKTKASLAHFYPQGTPTPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLALTSISPTTALITFIILILLTILEFELGTREAYVFTLLVSLYLHDNT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Ceratotherium simum
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.918 kDa
Sequence
MNENLFTSFATPTIMGLPIVILIIMFPSIMFPSPNRLINNRLVSTQQWLLQLTSKQMLSIHNNKGQTWALMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVFLGFRHKTKASLAHFLPQGTPVFLIPMLVIIETISLFIQPVALAVRLTANITAGHLLMHLIGGATLALMNISPTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Phoca vitulina
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.794 kDa
Sequence
MNENLFASFATPTMMGLPIVILIVLFPSILFPSPDRLINNRLASIQQWLIQLTSKQMLSIHNRKGQTWALMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRHKTKASLAHFLPQGTPLPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLALMDISTATAFITFTILILLTILEFAVALIQAYVFTLLVSLYLHDNT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Sus scrofa
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
25.039 kDa
Sequence
MNENLFASFIAPTMMGLPIVTLIIMFPSLLFPTPKRLINNRTISIQQWLIQLTSKQMMAIHNQKGQTWSLMLMSLIMFIGSTNILGLLPHSFTPTTQLSMNLGMAIPLWSATVFTGFRYKTKTSLAHFLPQGTPALLIPMLVIIETISLFIQPVALAVRLTANITAGHLLIHLIGGATLALLNINTMTAFITFTILILLTILEFAVALIQAYVFTLLVSLYLHDNT

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Pongo abelii
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.801 kDa
Sequence
MNESLFTPFITPTVLGLPAAVLVILFPPLLIPTSKHLINNRLIIIQQWLIRLILKQMMTTHNAKGRTWSLMLTSLIIFIASTNLLGLLPYSFTPTTQLSMNLAMAIPLWASTVAMGLRFKAKITLTHLLPQGTPTPLIPMLIIIETVSLFIQPLALAVRLTANITAGHLLMHLIGSSALAMLAINLPLTLITLTILTLLTILETAIALIQAYVFTLLVSLYLHDNS

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Pongo pygmaeus
Length
226 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.933 kDa
Sequence
MNEDLFTPFTTPTVLGLPAAILVILFPPLLVPTSKHFINNRLITTQQWLIRLTLKQMMITHNTKGRTWSLMLTSLIIFIASTNLLGLFPYSFTPTTQLSMNLAMAIPLWASTVAMGLRFKAKISLAHLLPQGTPTPLIPMLIIIETISLFIQPLALAVRLTANITAGHLLMHLIGSATLTMLTINLPLTLITLTILTLLTILEIAVALIQAYVFTLLVSLYLHDNS

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Alligator mississippiensis
Length
225 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.883 kDa
Sequence
MNLFDQFLTPSLLGISLLMPALLMTTILLLNPKNQWLSHPTTTIKSWFINQAAKQIMTPINPTGHKHSLILISLLILLSLTNLLGLLPYTFTPTTQLSMNMAIALPLWLVTVLIGLRTQPTTSLAHLLPEGTPMLLIPILILIETISLLIRPIALGVRLTANLTAGHLLIQLISIATLNLWFMMPPLSLLTSTVLILLLLLEFAVAMIQAYVFVLLLSLYLQENS

Gene
mt-atp6
Protein
ATP synthase subunit a
Organism
Oncorhynchus mykiss
Length
223 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.597 kDa
Sequence
MTLSFFDQFMSPTYLGIPLIAVALTLPWILFPTPSARWLNNRLITLQGWFINRFTQQLLLPLNLGGHKWAALLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTAALGHLLPEGTPVPLIPVLIIIETISLFIRPALGVRLTANLTAGHQLIATAAFVLLPMMPTVAILTSIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Loxodonta africana
Length
222 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.576 kDa
Sequence
MNEELSTFFYVPVGTMMLAIAFPAILLPTPNRLITNRWITIQQWLIQLIMKQLLSIHNTKGLSWSLMLITLTLFIGLTNLLGLLPYSFAPTTQLTVNLSMAIPLWTGTVVPGFRYKTKISLAHLLPQGTPMFLIPMIIIIETISLLIRPVTLAVRLTANITAGHSLIHLTGTATLTLSSIHSMTITVTFVTVILLTILELAVALIQAYVFALLISLYLHENA

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Elephas maximus
Length
222 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.539 kDa
Sequence
MNEELSAFFDVPVGTMMLAIAFPAILLPTPNRLITNRWITIQQWLIQLIMKQLLSIHNMKGLSWSLMLITLTLFIGLTNLLGLLPYSFAPTTQLTVNLSMAIPLWTGTVVLGFRYKTKISLAHLLPQGTPTFLIPMIIIIETISLLIRPITLAVRLTANITAGHLLIHLTGSAALTLLSVHLMTITVTFITVVMLTILELAVALIQAYVFALLISLYLHESA

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Mammuthus primigenius
Length
222 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.435 kDa
Sequence
MNEELSAFFDVPVGTMMLAIAFPAILLPTPNRLITNRWITIQQWLVKLIMKQLLSIHNTKGLSWSLMLITLTLFIGLTNLLGLLPYSFAPTAQLTVNLSMAIPLWTGTVILGFRYKTKISLAHLLPQGTPTFLIPMIIIIETISLLIRPVTLAVRLTANITAGHLLIHLTGTAALTLLSIHSMTITVTFITVVVLTILELAVALIQAYVFALLISLYLHESA

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Latimeria chalumnae
Length
220 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.403 kDa
Sequence
MSLNFFDQFMSPTLLGVPLIAVAMMFPWTLLPTPTNRWLNNRTLTLQNWFIGRFTNQLLQPLNTGGHKWAMILMSLNLLGLLPYTFTPTTQLSLNMGLAIPFWLATVLLGLRNQPTAALGHLLPEGTPTLLIPILIIIETISLLIRPFALGVRLTANLTAGHLLMQLIATAAFVLLPMMPTVALLTTLVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV

Gene
mt-atp6
Protein
ATP synthase subunit a
Organism
Oncorhynchus masou
Length
219 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
24.061 kDa
Fragment
single
Sequence
FMSPTYLGIPLIAVALTLPWILFPTPSARWLNNRLITLQGWFINRFTQQLLLPLNLGGHKWAALLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTAALGHLLPEGTPVPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAAFVLLPLMPTVAILTSIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Rhopalosiphum padi
Length
217 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane (By similarity).
Similarity
Belongs to the ATPase A chain family.
Mass
25.442 kDa
Sequence
MTTNLFNIFDPSTTIFNLEMNWISTLLIILFMPNFLWILPNRMNWLLFKMFNMLNNEMLMLYKMKKTKSPAFLFISLFMFILLNNFFSLFPYIFSSSSHMVFSVTLAIPFWMFFIILSTCKNTKNMIAHLIPLNTPIYLAPLMTIIETMSIIIRPMSLSIRLTANLIAGHLLMTLLNFNSLMIIIIFIQMFMMIFELCVALIQSYVFSILSSLYSSE

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Tropidurus hispidus
Length
212 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane (By similarity).
Similarity
Belongs to the ATPase A chain family.
Mass
23.225 kDa
Fragment
single
Sequence
PQMMGIPLILIAIFLPTLLIYTSPTRLSTNRMTTLQLWLTNTITKQLFLPVNTPGHKWAAMLMTLMIXLLSMNLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTASLGHLLPEGTPTPLIPLLIIIETVSLFIRPLALGVRLTANLTAGHLLIQLISTAAFVLLPMMTLTALSTFIVLVLLTGLEIAVAMIQAYVFTLLLTLYL

Gene
MT-ATP6
Protein
ATP synthase subunit a
Organism
Tropidurus montanus
Length
212 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
23.227 kDa
Fragment
single
Sequence
PQMMGIPLILIAIILPMLLMFTSSTRLSSNRMTTMQLWVMNTITKQLFLPVNMPGHKWAAMLITLMIFLLSMNMLGLLPYTFTPTTQLSMNMALAAPLWLATVLTGLRNQPTASLGHLLPEGTPTPLIPLLIIIETVSLFIRPLALGVRLTANLTAGHLLIQLISTAAFVLMPTMPMAALSTLIVLMLLTGLEIAVAMIQAYVFTLLLTLYL

Gene
mt-atp6
Protein
ATP synthase subunit a
Organism
Thunnus obesus
Length
133 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
14.982 kDa
Fragment
single
Sequence
LALTLPWVLFPTPTSRWLNNRLLTLQNWFIGRFGHELFTPVNLPGHKWAVLLTSLMLFLISLNMLGLLPYTFTPTTQLSLNMGLAFPLWLATVIIGMRNQPTEALGHLLPEGTPTLLIPVLIVIETISLFIRP

Gene
mt-atp6
Protein
ATP synthase subunit a
Organism
Salmo trutta
Length
105 amino acids
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Similarity
Belongs to the ATPase A chain family.
Mass
11.291 kDa
Fragment
single
Sequence
RNQPTAALGHLLPEGTPVPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAAFVLLPMMPTVAILTSIVLFLLTLLEIAVAMIQAYVFVLLLSLYL