ATP5F1D report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0033615Biological processmitochondrial proton-transporting ATP synthase complex assembly
GO_0015986Biological processproton motive force-driven ATP synthesis
GO_0046688Biological processresponse to copper ion
GO_0009060Biological processaerobic respiration
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_0005759Cellular componentmitochondrial matrix
GO_0005743Cellular componentmitochondrial inner membrane
GO_0005739Cellular componentmitochondrion
GO_0043531Molecular functionADP binding
GO_0046933Molecular functionproton-transporting ATP synthase activity, rotational mechanism
GO_0005515Molecular functionprotein binding
GO_0005524Molecular functionATP binding

IV. Literature review

[source]
Gene nameATP5F1D
Protein nameATP synthase subunit delta, mitochondrial (ATP synthase F1 subunit delta) (F-ATPase delta subunit)
ATP synthase F1 subunit delta
SynonymsATP5D
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 turnover 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 of the central stalk which is part of the complex rotary element. 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 . .

AccessionsENST00000591660.5
P30049
ENST00000395633.5
A0A087WTL3
ENST00000215375.7
ENST00000591249.5