Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P21306 (ATP5E_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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, mitochondrial

Short name=ATPase subunit epsilon
Gene names
Name:ATP15
Ordered Locus Names:YPL271W
ORF Names:P0345
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length62 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

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 has three main subunits: a, b and c.

Subcellular location

Mitochondrion. Mitochondrion inner membrane.

Miscellaneous

Present with 4280 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the eukaryotic ATPase epsilon family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 6261ATP synthase subunit epsilon, mitochondrial
PRO_0000071667

Amino acid modifications

Modified residue521Phosphothreonine Ref.7

Secondary structure

........... 62
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21306 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 0CD754A9DEFFD08C

FASTA626,743
        10         20         30         40         50         60 
MSAWRKAGIS YAAYLNVAAQ AIRSSLKTEL QTASVLNRSQ TDAFYTQYKN GTAASEPTPI 


TK 

« Hide

References

« Hide 'large scale' references
[1]"ATP synthase of yeast mitochondria. Isolation and disruption of the ATP epsilon gene."
Guelin E., Chevallier J., Rigoulet M., Guerin B., Velours J.
J. Biol. Chem. 268:161-167(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: D273-10B/A/H/U.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"Isolation and complete amino acid sequence of the mitochondrial ATP synthase epsilon-subunit of the yeast Saccharomyces cerevisiae."
Arselin G., Gandar J.-C., Guerin B., Velours J.
J. Biol. Chem. 266:723-727(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-62.
Strain: ATCC 60782 / S / NCYC 232 / American yeast foam.
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ATCC 76625 / YPH499.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X64767 Genomic DNA. Translation: CAA46014.1.
Z73627 Genomic DNA. Translation: CAA98007.1.
AY558140 Genomic DNA. Translation: AAS56466.1.
BK006949 Genomic DNA. Translation: DAA11165.1.
PIRA45315.
RefSeqNP_015052.1. NM_001184085.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HLDX-ray2.801/I/R2-61[»]
2WPDX-ray3.43I2-62[»]
3FKSX-ray3.591/I/R2-62[»]
3OE7X-ray3.191/I/R2-62[»]
3OEEX-ray2.741/I/R2-62[»]
3OEHX-ray3.001/I/R2-62[»]
3OFNX-ray3.20I/R2-62[»]
3ZIAX-ray2.50I/S2-62[»]
4B2Qelectron microscopy37.00I/i2-60[»]
ProteinModelPortalP21306.
SMRP21306. Positions 2-60.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35942. 58 interactions.
DIPDIP-3031N.
IntActP21306. 6 interactions.
MINTMINT-547186.
STRING4932.YPL271W.

Protein family/group databases

TCDB3.A.2.1.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Proteomic databases

PaxDbP21306.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL271W; YPL271W; YPL271W.
GeneID855857.
KEGGsce:YPL271W.

Organism-specific databases

SGDS000006192. ATP15.

Phylogenomic databases

eggNOGNOG294695.
HOGENOMHOG000214506.
KOK02135.
OMAMSAWRKA.
OrthoDBEOG7NSBG1.

Enzyme and pathway databases

BioCycYEAST:G3O-34153-MONOMER.

Gene expression databases

ArrayExpressP21306.
GenevestigatorP21306.

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

EvolutionaryTraceP21306.
NextBio980466.

Entry information

Entry nameATP5E_YEAST
AccessionPrimary (citable) accession number: P21306
Secondary accession number(s): D6W399
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references