ATP synthase subunit gamma, mitochondrial
Name | ATP synthase subunit gamma, mitochondrial |
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Synonyms | ATP5C ATP5CL1 F-ATPase gamma subunit |
Gene Name | ATP5C1 |
Organism | Human |
Amino acid sequence | >lcl|BSEQ0007365|ATP synthase subunit gamma, mitochondrial MFSRAGVAGLSAWTLQPQWIQVRNMATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAE RELKPARIYGLGSLALYEKADIKGPEDKKKHLLIGVSSDRGLCGAIHSSIAKQMKSEVAT LTAAGKEVMLVGIGDKIRGILYRTHSDQFLVAFKEVGRKPPTFGDASVIALELLNSGYEF DEGSIIFNKFRSVISYKTEEKPIFSLNTVASADSMSIYDDIDADVLQNYQEYNLANIIYY SLKESTTSEQSARMTAMDNASKNASEMIDKLTLTFNRTRQAVITKELIEIISGAAALD |
Number of residues | 298 |
Molecular Weight | 32995.665 |
Theoretical pI | 9.71 |
GO Classification |
Functions
poly(A) RNA binding proton-transporting ATPase activity, rotational mechanism transmembrane transporter activity proton-transporting ATP synthase activity, rotational mechanism Processes
respiratory electron transport chain ATP biosynthetic process oxidative phosphorylation small molecule metabolic process mitochondrial ATP synthesis coupled proton transport cellular metabolic process Components
mitochondrion membrane mitochondrial inner membrane mitochondrial matrix mitochondrial proton-transporting ATP synthase complex extracellular exosome myelin sheath mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) |
General Function | Transmembrane transporter activity |
Specific 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(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. |
Transmembrane Regions | |
GenBank Protein ID | 665586 |
UniProtKB ID | P36542 |
UniProtKB Entry Name | ATPG_HUMAN |
Cellular Location | Mitochondrion |
Gene sequence | >lcl|BSEQ0012682|ATP synthase subunit gamma, mitochondrial (ATP5C1) ATGTTCTCTCGCGCGGGTGTCGCTGGGCTGTCGGCCTGGACCTTGCAGCCGCAATGGATT CAAGTTCGAAATATGGCAACTTTGAAAGATATCACCAGGAGACTAAAGTCCATCAAAAAC ATCCAGAAAATTACCAAGTCTATGAAAATGGTAGCGGCAGCAAAATATGCCCGAGCTGAG AGAGAGCTGAAACCAGCTCGAATATATGGATTGGGATCTTTAGCTCTGTATGAAAAAGCT GATATCAAGGGGCCTGAAGACAAGAAGAAACACCTCCTTATTGGTGTGTCCTCAGATCGA GGACTGTGTGGTGCTATTCATTCCTCCATTGCTAAACAGATGAAAAGCGAGGTTGCTACA CTAACAGCAGCTGGGAAAGAAGTTATGCTTGTTGGAATTGGTGACAAAATCAGAGGCATA CTTTATAGGACTCATTCTGACCAGTTTCTGGTGGCATTCAAAGAAGTGGGAAGAAAGCCC CCCACTTTTGGAGATGCGTCAGTCATTGCCCTTGAATTACTAAATTCTGGATATGAATTT GATGAAGGCTCCATCATCTTTAATAAATTCAGGTCTGTCATCTCCTATAAGACAGAAGAA AAGCCCATCTTTTCCCTTAATACCGTTGCAAGTGCTGACAGCATGAGTATCTATGACGAT ATTGATGCTGACGTGCTGCAAAATTACCAAGAATACAATCTGGCCAACATCATCTACTAC TCTCTGAAGGAGTCCACCACTAGTGAGCAGAGTGCCAGGATGACAGCCATGGACAATGCC AGCAAGAATGCTTCTGAGATGATTGACAAATTGACATTGACATTCAACCGTACCCGCCAA GCTGTCATCACAAAAGAGTTGATTGAAATTATCTCTGGTGCTGCAGCTCTGGATTAA |
GenBank Gene ID | D16562 |
GeneCard ID | None |
GenAtlas ID | |
HGNC ID | HGNC:833 |
Chromosome Location | 10 |
Locus | 10p15.1 |
References |
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Related FRC
FRCD ID | Name | Exact Mass | Structure |
---|---|---|---|
Aurovertin B |
460.523 |
||
Quercetin |
302.238 |