Reviewed, UniProtKB/Swiss-Prot Q5VTU8 (AT5EL_HUMAN)

Names and origin

Protein names

Recommended name:
    ATP synthase subunit epsilon-like protein, mitochondrial

Gene names

Name:

ATP5EP2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	51 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Mitochondrial membrane ATP synthase (F1F0 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, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F1 domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits By similarity.
Subunit structure	F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L) By similarity.
Subcellular location	Mitochondrion. Mitochondrion inner membrane By similarity.
Sequence similarities	Belongs to the eukaryotic ATPase epsilon family.
Caution	Defined as a pseudogene by HGNC. However, proteomic data on a specific peptide from Ref.2 suggest the existence of this protein.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Membrane Mitochondrion Mitochondrion inner membrane
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) Inferred from electronic annotation. Source: InterPro
Molecular function	hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 51	50	ATP synthase subunit epsilon-like protein, mitochondrial		PRO_0000347182
Amino acid modifications
	Modified residue	39	1	Phosphoserine Ref.2
	Modified residue	42	1	Phosphoserine Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q5VTU8-1 [UniParc]. Last modified December 7, 2004. Version 1. Checksum: 3352CE8EC90F6DCE	FASTA	51	5,807
	10 20 30 40 50 MVAYWRQAGL SYIRYSQICA KVVRDALKTE FKANAKKTSG NSVKIVKVKK E

References

[1]

"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed: 15057823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

[2]

"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39 AND SER-42, MASS SPECTROMETRY. Tissue: Epithelium.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL591024 Genomic DNA. Translation: CAH70632.1.
IPI	IPI00176527.
3D structure databases
SMR	Q5VTU8. Positions 2-48.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5VTU8.
Genome annotation databases
Ensembl	ENST00000381026; ENSP00000370414; ENSG00000180389; Homo sapiens. [Genome view]
NMPDR	fig|9606.3.peg.8672.
Organism-specific databases
GeneCards	GC13P027420.
HGNC	HGNC:34026. ATP5EP2.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q5VTU8.
HOVERGEN	Q5VTU8.
OMA	QICAKVV
OrthoDB	EOG9BCH66
Gene expression databases
Genevestigator	Q5VTU8.
Family and domain databases
InterPro	IPR006721. ATPase_F1-cplx_esu_mt. [Graphical view]
Gene3D	G3DSA:1.10.1620.20. ATPase_F1_e_mt. 1 hit.
Pfam	PF04627. ATP-synt_Eps. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AT5EL_HUMAN

Accession

Primary (citable) accession number: Q5VTU8

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	December 7, 2004
Last modified:	November 24, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.