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Q5VTU8 (AT5EL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase subunit epsilon-like protein, mitochondrial
Gene names
Name:ATP5EP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length51 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5151ATP synthase subunit epsilon-like protein, mitochondrial
PRO_0000347182

Sequences

Sequence LengthMass (Da)Tools
Q5VTU8 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: 3352CE8EC90F6DCE

FASTA515,807
        10         20         30         40         50 
MVAYWRQAGL SYIRYSQICA KVVRDALKTE FKANAKKTSG NSVKIVKVKK E 

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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. expand/collapse author list , 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.
UniGeneHs.574118.

3D structure databases

ProteinModelPortalQ5VTU8.
SMRQ5VTU8. Positions 2-48.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000370414.

Polymorphism databases

DMDM74746994.

Proteomic databases

PaxDbQ5VTU8.
PRIDEQ5VTU8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000381026; ENSP00000370414; ENSG00000180389.

Organism-specific databases

GeneCardsGC13P028519.
HGNCHGNC:34026. ATP5EP2.
HPAHPA042142.
neXtProtNX_Q5VTU8.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG318665.
HOGENOMHOG000214506.
HOVERGENHBG050611.
InParanoidQ5VTU8.
OrthoDBEOG7GQXZP.
PhylomeDBQ5VTU8.
TreeFamTF300278.

Gene expression databases

BgeeQ5VTU8.
GenevestigatorQ5VTU8.

Family and domain databases

Gene3D1.10.1620.20. 1 hit.
InterProIPR006721. ATPase_F1-cplx_esu_mt.
[Graphical view]
PfamPF04627. ATP-synt_Eps. 1 hit.
[Graphical view]
SUPFAMSSF48690. SSF48690. 1 hit.
ProtoNetSearch...

Other

ChiTaRSATP5EP2. human.
PROQ5VTU8.

Entry information

Entry nameAT5EL_HUMAN
AccessionPrimary (citable) accession number: Q5VTU8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: December 7, 2004
Last modified: May 14, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM