ATP5F1C report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0015986Biological processproton motive force-driven ATP synthesis
GO_0006754Biological processATP biosynthetic process
GO_0006119Biological processoxidative phosphorylation
GO_0042776Biological processproton motive force-driven mitochondrial ATP synthesis
GO_1902600Biological processproton transmembrane transport
GO_0000275Cellular componentmitochondrial proton-transporting ATP synthase complex, catalytic sector F(1)
GO_0005753Cellular componentmitochondrial proton-transporting ATP synthase complex
GO_0005739Cellular componentmitochondrion
GO_0005759Cellular componentmitochondrial matrix
GO_0016020Cellular componentmembrane
GO_0005743Cellular componentmitochondrial inner membrane
GO_0046933Molecular functionproton-transporting ATP synthase activity, rotational mechanism
GO_0005515Molecular functionprotein binding
GO_0016887Molecular functionATP hydrolysis activity
GO_0003723Molecular functionRNA binding

IV. Literature review

[source]
Gene nameATP5F1C
Protein nameATP synthase subunit gamma, mitochondrial (ATP synthase F1 subunit gamma) (F-ATPase gamma subunit)
SynonymsATP5CL1
ATP5C1
ATP5C
DescriptionFUNCTION: 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. .

AccessionsENST00000335698.4 [P36542-2]
ENST00000356708.12 [P36542-1]
P36542