Q5VTU8 (AT5EL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:

ATP5EP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	51 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 PubMed:17924679 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
Technical term	Complete proteome Reference 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	proton-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
	Chain	1 – 51	51	ATP synthase subunit epsilon-like protein, mitochondrial		PRO_0000347182

Sequences

	Sequence		Length	Mass (Da)
	Q5VTU8 [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591024 Genomic DNA. Translation: CAH70632.1.
IPI	IPI00176527.
UniGene	Hs.574118.
3D structure databases
ProteinModelPortal	Q5VTU8.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000370414.
Polymorphism databases
DMDM	74746994.
Proteomic databases
PaxDb	Q5VTU8.
PRIDE	Q5VTU8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000381026; ENSP00000370414; ENSG00000180389.
Organism-specific databases
GeneCards	GC13P028519.
HGNC	HGNC:34026. ATP5EP2.
HPA	HPA042142.
neXtProt	NX_Q5VTU8.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG318665.
HOGENOM	HOG000214506.
HOVERGEN	HBG050611.
InParanoid	Q5VTU8.
OMA	QICAKVV.
OrthoDB	EOG43N7FH.
PhylomeDB	Q5VTU8.
Gene expression databases
Bgee	Q5VTU8.
Genevestigator	Q5VTU8.
Family and domain databases
Gene3D	1.10.1620.20. 1 hit.
InterPro	IPR006721. ATPase_F1-cplx_esu_mt. [Graphical view]
Pfam	PF04627. ATP-synt_Eps. 1 hit. [Graphical view]
SUPFAM	SSF48690. ATP_synth_E. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	ATP5EP2. human.

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:	May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.