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Q12165 (ATPD_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. 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 delta, mitochondrial
Alternative name(s):
F-ATPase delta subunit
Gene names
Name:ATP16
Ordered Locus Names:YDL004W
ORF Names:D2935, YD8119.03
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length160 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 turnover 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. HAMAP-Rule MF_00530

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 HAMAP-Rule MF_00530.

Sequence similarities

Belongs to the ATPase epsilon chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2222Mitochondrion Ref.1
Chain23 – 160138ATP synthase subunit delta, mitochondrial HAMAP-Rule MF_00530
PRO_0000002671

Secondary structure

............................. 160
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q12165 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: AE8D0BA364107977

FASTA16017,020
        10         20         30         40         50         60 
MLRSIIGKSA SRSLNFVAKR SYAEAAAASS GLKLQFALPH ETLYSGSEVT QVNLPAKSGR 

        70         80         90        100        110        120 
IGVLANHVPT VEQLLPGVVE VMEGSNSKKF FISGGFATVQ PDSQLCVTAI EAFPLESFSQ 

       130        140        150        160 
ENIKNLLAEA KKNVSSSDAR EAAEAAIQVE VLENLQSVLK 

« Hide

References

« Hide 'large scale' references
[1]"ATP synthase of yeast mitochondria. Isolation of the F1 delta subunit, sequence and disruption of the structural gene."
Giraud M.-F., Velours J.
Eur. J. Biochem. 222:851-859(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-72; 112-121 AND 141-160.
Strain: D273-10B/A.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(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]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ATCC 76625 / YPH499.
[6]"Molecular architecture of the rotary motor in ATP synthase."
Stock D., Leslie A.G., Walker J.E.
Science 286:1700-1705(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z21857 Genomic DNA. Translation: CAA79912.1.
Z48008 Genomic DNA. Translation: CAA88057.1.
Z48432 Genomic DNA. Translation: CAA88355.1.
Z74052 Genomic DNA. Translation: CAA98560.1.
AY558155 Genomic DNA. Translation: AAS56481.1.
BK006938 Genomic DNA. Translation: DAA11844.1.
PIRS45632.
RefSeqNP_010280.1. NM_001180063.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HLDX-ray2.80H/Q/Z23-160[»]
2WPDX-ray3.43H23-160[»]
2XOKX-ray3.01H1-160[»]
3FKSX-ray3.59H/Q/Z23-160[»]
3OE7X-ray3.19H/Q/Z24-160[»]
3OEEX-ray2.74H/Q/Z23-160[»]
3OEHX-ray3.00H/Q/Z23-160[»]
3OFNX-ray3.20H/Q23-160[»]
3ZIAX-ray2.50H/R23-160[»]
3ZRYX-ray6.50H23-160[»]
4B2Qelectron microscopy37.00H/h29-160[»]
ProteinModelPortalQ12165.
SMRQ12165. Positions 29-160.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32050. 10 interactions.
DIPDIP-3032N.
IntActQ12165. 3 interactions.
MINTMINT-2781010.

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

PaxDbQ12165.
PeptideAtlasQ12165.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL004W; YDL004W; YDL004W.
GeneID851560.
KEGGsce:YDL004W.

Organism-specific databases

CYGDYDL004w.
SGDS000002162. ATP16.

Phylogenomic databases

eggNOGCOG0355.
GeneTreeENSGT00390000017576.
HOGENOMHOG000216023.
KOK02134.
OMALPHQAIF.
OrthoDBEOG7S7SSS.

Enzyme and pathway databases

BioCycYEAST:G3O-29435-MONOMER.

Gene expression databases

GenevestigatorQ12165.

Family and domain databases

Gene3D2.60.15.10. 1 hit.
HAMAPMF_00530. ATP_synth_epsil_bac.
InterProIPR001469. ATPase_F1-cplx_dsu/esu.
IPR020546. ATPase_F1-cplx_dsu/esu_N.
[Graphical view]
PANTHERPTHR13822. PTHR13822. 1 hit.
PfamPF02823. ATP-synt_DE_N. 1 hit.
[Graphical view]
ProDomPD000944. ATPase_F1-cplx_dsu/esu. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF51344. SSF51344. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ12165.
NextBio968992.
PROQ12165.

Entry information

Entry nameATPD_YEAST
AccessionPrimary (citable) accession number: Q12165
Secondary accession number(s): D6VRY4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: 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