Sequence length	69 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

Function	Mitochondrial membrane ATP synthase (F(1)F(O) 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. Minor subunit located with subunit a in the membrane.
Subunit structure	F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(0) seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L).
Subcellular location	Mitochondrion. Mitochondrion inner membrane.
Sequence similarities	Belongs to the ATPase e subunit family.

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Membrane Mitochondrion Mitochondrion inner membrane
PTM	Phosphoprotein
Gene Ontology (GO)
Cellular component	mitochondrial proton-transporting ATP synthase complex Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a human homolog of rat ATP synthase subunit e from human fetal brain." Fujiwara T., Kawai A., Shimizu F., Shinomiya K., Hirano H., Okuno S., Ozaki K., Katagiri T., Takeda S., Kuga Y., Shimada Y., Nagata M., Takaichi A., Watanabe T., Horie M., Nakamura Y., Takahashi E., Hirai Y. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal brain.
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
+	Additional computationally mapped references.

Sequence databases
	D50371 mRNA. Translation: BAA23322.1. BT006922 mRNA. Translation: AAP35568.1. BC003679 mRNA. Translation: AAH03679.1. BC105610 mRNA. Translation: AAI05611.1.
RefSeq	NP_009031.1.
UniGene	Hs.85539
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	P56385.
Genome annotation databases
Ensembl	ENSG00000169020. Homo sapiens. [Contig view]
GeneID	521.
KEGG	hsa:521.
Organism-specific databases
HGNC	HGNC:846. ATP5I.
MIM	601519. gene.
PharmGKB	PA25136.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	P56385.
HOVERGEN	P56385.
Enzyme and pathway databases
Reactome	REACT_1698. Nucleotide metabolism.
Gene expression databases
ArrayExpress	P56385.
CleanEx	HS_ATP5I.
GermOnline	ENSG00000169020. Homo sapiens.
Family and domain databases
InterPro	IPR008386. ATPase_F0_E_mt. [Graphical view]
Pfam	PF05680. ATP-synt_E. 1 hit. [Graphical view]
ProDom	P56385. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
SOURCE	Search...
ProtoNet	Search...

Names and origin

Protein attributes