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ATP5PB

Gene
ATP5PB
Protein
ATP synthase F(0) complex subunit B1, mitochondrial
Organism
Bos taurus
Length
256 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. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Similarity
Belongs to the eukaryotic ATPase B chain family.
Mass
28.822 kDa
Sequence
MLSRVVLSAAAAAAPSLKNAALLGPGVLQATRIFHTGQPSLAPVPPLPEHGGKVRFGLIPEEFFQFLYPKTGVTGPYVLGTGLILYLLSKEIYVITPETFSAISTIGFLVYIVKKYGASVGEFADKLNEQKIAQLEEVKQASIKQIQDAIDMEKSQQALVQKRHYLFDVQRNNIAMALEVTYRERLHRVYREVKNRLDYHISVQNMMRQKEQEHMINWVEKRVVQSISAQQEKETIAKCIADLKLLSKKAQAQPVM

Gene
ATP5PB
Protein
ATP synthase F(0) complex subunit B1, mitochondrial
Organism
Homo sapiens
Length
256 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. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Similarity
Belongs to the eukaryotic ATPase B chain family.
Mass
28.909 kDa
Sequence
MLSRVVLSAAATAAPSLKNAAFLGPGVLQATRTFHTGQPHLVPVPPLPEYGGKVRYGLIPEEFFQFLYPKTGVTGPYVLGTGLILYALSKEIYVISAETFTALSVLGVMVYGIKKYGPFVADFADKLNEQKLAQLEEAKQASIQHIQNAIDTEKSQQALVQKRHYLFDVQRNNIAMALEVTYRERLYRVYKEVKNRLDYHISVQNMMRRKEQEHMINWVEKHVVQSISTQQEKETIAKCIADLKLLAKKAQAQPVM

Gene
Atp5pb
Protein
ATP synthase F(0) complex subunit B1, mitochondrial
Organism
Mus musculus
Length
256 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. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Similarity
Belongs to the eukaryotic ATPase B chain family.
Mass
28.949 kDa
Sequence
MLSRVVLSAAATAAPCLKNAAALGPGVLQATRAFHTGQPRLAPLPPLPEYGGKVRLGLIPEEFFQFLYPKTGVTGPYVLGTGLSLYFLSKEIYVITPETFSTISVVGLIVYVIKKYGASFGEFIDKLNEEKIAQLEEVKQSSMKQIQDAIDMEKAQQALVQKRHYLFDVQRNNIALALEVTYRERLHKAYKEVKNRLDYHISVQNMMRRKEEEHMIDWVEKHVVKSISVQQEKETIAKCIEDLKLLAKKAQAQPIM

Gene
ATP5PB
Protein
ATP synthase F(0) complex subunit B1, mitochondrial
Organism
Pongo abelii
Length
256 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. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Similarity
Belongs to the eukaryotic ATPase B chain family.
Mass
28.894 kDa
Sequence
MLSRVVLSAAATAASSLKNAAFLGPGVLQATRTFHTGQPHLAPVPPLPEYGGKVRYGLIPEEFFQFLYPKTGVTGPYVLGTGLILYALSKEIYVISAETFTALSLIGVMVYGIKKYGPAVADFADKLNEQKLAQLEEAKQTSIQQIQNAIDMEKSQQALVQKRHYLFDVQRNNIAMALEVTYRERLYRVYKEVKNRLDYHIYVQNMMRQKEQEHMVNWVEKHVVQSISTQQEKETIAKCIADLKLLAKKAQAQPVM

Gene
Atp5pb
Protein
ATP synthase F(0) complex subunit B1, mitochondrial
Organism
Rattus norvegicus
Length
256 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. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Similarity
Belongs to the eukaryotic ATPase B chain family.
Mass
28.869 kDa
Sequence
MLSRVVLSAAATAAPCLKNAAVLGPGVLQATRVFHTGQPRLAPLPPLPEYGGKVRLGLIPEEFFQFLYPKTGVTGPYVLGTGLSLYFLSKEIYVITPETFSTISVVGLIVYVIKKYGASIGEFIDKLNEEKIAQLEEIKQSSMKQIQDAINREKAQQALVQKRHYLFDVQRNNIALALEVTYRERLHKAYKEVKNRLDYHISVQDMMRRKEGEHMINWVEKHVIQSISAQQEKETIAKCIGDLKMLAKKAQAQPIM