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Protein

ATP synthase subunit delta, mitochondrial

Gene

ATP16

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

GO - Biological processi

  • ATP synthesis coupled proton transport Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29435-MONOMER.

Protein family/group databases

TCDBi3.A.2.1.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit delta, mitochondrial
Alternative name(s):
F-ATPase delta subunit
Gene namesi
Name:ATP16
Ordered Locus Names:YDL004W
ORF Names:D2935, YD8119.03
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome IV

Organism-specific databases

CYGDiYDL004w.
EuPathDBiFungiDB:YDL004W.
SGDiS000002162. ATP16.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial proton-transporting ATP synthase, central stalk Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2222Mitochondrion1 PublicationAdd
BLAST
Chaini23 – 160138ATP synthase subunit delta, mitochondrialPRO_0000002671Add
BLAST

Proteomic databases

MaxQBiQ12165.
PaxDbiQ12165.
PeptideAtlasiQ12165.

Expressioni

Gene expression databases

GenevestigatoriQ12165.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi32050. 11 interactions.
DIPiDIP-3032N.
IntActiQ12165. 4 interactions.
MINTiMINT-2781010.

Structurei

Secondary structure

1
160
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 374Combined sources
Beta strandi44 – 463Combined sources
Beta strandi51 – 544Combined sources
Beta strandi56 – 594Combined sources
Beta strandi61 – 633Combined sources
Beta strandi70 – 745Combined sources
Beta strandi78 – 836Combined sources
Beta strandi86 – 927Combined sources
Beta strandi95 – 1006Combined sources
Turni101 – 1033Combined sources
Beta strandi104 – 1107Combined sources
Beta strandi112 – 1143Combined sources
Helixi115 – 1173Combined sources
Helixi120 – 13314Combined sources
Beta strandi136 – 1394Combined sources
Helixi140 – 15617Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ12165.
SMRiQ12165. Positions 29-160.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12165.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase epsilon chain family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0355.
GeneTreeiENSGT00390000017576.
HOGENOMiHOG000216023.
InParanoidiQ12165.
KOiK02134.
OMAiLPHQAIF.
OrthoDBiEOG7S7SSS.

Family and domain databases

Gene3Di2.60.15.10. 1 hit.
HAMAPiMF_00530. ATP_synth_epsil_bac.
InterProiIPR001469. ATPase_F1-cplx_dsu/esu.
IPR020546. ATPase_F1-cplx_dsu/esu_N.
[Graphical view]
PANTHERiPTHR13822. PTHR13822. 1 hit.
PfamiPF02823. ATP-synt_DE_N. 1 hit.
[Graphical view]
ProDomiPD000944. ATPase_F1-cplx_dsu/esu. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF51344. SSF51344. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q12165-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRSIIGKSA SRSLNFVAKR SYAEAAAASS GLKLQFALPH ETLYSGSEVT
60 70 80 90 100
QVNLPAKSGR IGVLANHVPT VEQLLPGVVE VMEGSNSKKF FISGGFATVQ
110 120 130 140 150
PDSQLCVTAI EAFPLESFSQ ENIKNLLAEA KKNVSSSDAR EAAEAAIQVE
160
VLENLQSVLK
Length:160
Mass (Da):17,020
Last modified:November 1, 1996 - v1
Checksum:iAE8D0BA364107977
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS45632.
RefSeqiNP_010280.1. NM_001180063.1.

Genome annotation databases

EnsemblFungiiYDL004W; YDL004W; YDL004W.
GeneIDi851560.
KEGGisce:YDL004W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS45632.
RefSeqiNP_010280.1. NM_001180063.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ12165.
SMRiQ12165. Positions 29-160.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32050. 11 interactions.
DIPiDIP-3032N.
IntActiQ12165. 4 interactions.
MINTiMINT-2781010.

Protein family/group databases

TCDBi3.A.2.1.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Proteomic databases

MaxQBiQ12165.
PaxDbiQ12165.
PeptideAtlasiQ12165.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL004W; YDL004W; YDL004W.
GeneIDi851560.
KEGGisce:YDL004W.

Organism-specific databases

CYGDiYDL004w.
EuPathDBiFungiDB:YDL004W.
SGDiS000002162. ATP16.

Phylogenomic databases

eggNOGiCOG0355.
GeneTreeiENSGT00390000017576.
HOGENOMiHOG000216023.
InParanoidiQ12165.
KOiK02134.
OMAiLPHQAIF.
OrthoDBiEOG7S7SSS.

Enzyme and pathway databases

BioCyciYEAST:G3O-29435-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ12165.
NextBioi968992.
PROiQ12165.

Gene expression databases

GenevestigatoriQ12165.

Family and domain databases

Gene3Di2.60.15.10. 1 hit.
HAMAPiMF_00530. ATP_synth_epsil_bac.
InterProiIPR001469. ATPase_F1-cplx_dsu/esu.
IPR020546. ATPase_F1-cplx_dsu/esu_N.
[Graphical view]
PANTHERiPTHR13822. PTHR13822. 1 hit.
PfamiPF02823. ATP-synt_DE_N. 1 hit.
[Graphical view]
ProDomiPD000944. ATPase_F1-cplx_dsu/esu. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF51344. SSF51344. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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.

Entry informationi

Entry nameiATPD_YEAST
AccessioniPrimary (citable) accession number: Q12165
Secondary accession number(s): D6VRY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 27, 2015
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.