Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

ATP synthase subunit 9, mitochondrial

Gene

OLI1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 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 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 F0 domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei59 – 591Reversibly protonated during proton transportBy similarity

GO - Molecular functioni

  1. hydrogen ion transmembrane transporter activity Source: InterPro
  2. lipid binding Source: UniProtKB-KW

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
  2. ATP synthesis coupled proton transport Source: SGD
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-34383-MONOMER.
ReactomeiREACT_334110. Mitochondrial protein import.

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 9, mitochondrial
Alternative name(s):
Lipid-binding protein
Oligomycin resistance protein 1
Gene namesi
Name:OLI1
Synonyms:ATP9, OLI3, PHO2
Ordered Locus Names:Q0130
Encoded oniMitochondrion
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Mitochondrion

Organism-specific databases

CYGDiQ0130.
EuPathDBiFungiDB:Q0130.
SGDiS000007274. OLI1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei14 – 3421HelicalSequence AnalysisAdd
BLAST
Transmembranei52 – 7221HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrial inner membrane Source: Reactome
  4. mitochondrial intermembrane space Source: Reactome
  5. mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

CF(0), Membrane, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7676ATP synthase subunit 9, mitochondrialPRO_0000112240Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-formylmethionine1 Publication

Keywords - PTMi

Formylation

Expressioni

Gene expression databases

ExpressionAtlasiP61829. differential.
GenevestigatoriP61829.

Interactioni

Subunit structurei

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. In yeast, the dimeric form of ATP synthase consists of 17 polypeptides: alpha, beta, gamma, delta, epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d, E (Tim11), f, g, h, i/j and k.

Protein-protein interaction databases

BioGridi34780. 11 interactions.
DIPiDIP-3041N.
MINTiMINT-4981559.

Structurei

Secondary structure

1
76
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1413Combined sources
Helixi15 – 184Combined sources
Helixi19 – 3921Combined sources
Helixi41 – 433Combined sources
Helixi44 – 7330Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WPDX-ray3.43J/K/L/M/N/O/P/Q/R/S1-76[»]
2XOKX-ray3.01K/L/M/N/O/P/Q/R/S/T1-76[»]
3U2FX-ray2.00K/L/M/N/O1-76[»]
3U2YX-ray2.50K/L/M/N/O1-76[»]
3U32X-ray2.00K/L/M/N/O1-76[»]
3UD0X-ray2.00K/L/M/N/O1-76[»]
3ZRYX-ray6.50J/K/L/M/N/O/P/Q/R/S1-76[»]
4B2Qelectron microscopy37.00J/K/L/M/N/O/P/Q/R/S/j/k/l/m/n/o/p/q/r/s1-76[»]
4F4SX-ray1.90A/B/C/D/E/K/L/M/N/O1-76[»]
ProteinModelPortaliP61829.
SMRiP61829. Positions 2-75.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61829.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase C chain family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0636.
GeneTreeiENSGT00390000006210.
HOGENOMiHOG000235245.
InParanoidiP61829.
KOiK02128.
OMAiIGMAFAE.
OrthoDBiEOG72NS3W.

Family and domain databases

Gene3Di1.20.20.10. 1 hit.
HAMAPiMF_01396. ATP_synth_c_bact.
InterProiIPR000454. ATPase_F0-cplx_csu.
IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
IPR002379. ATPase_proteolipid_c_like_dom.
[Graphical view]
PfamiPF00137. ATP-synt_C. 1 hit.
[Graphical view]
PRINTSiPR00124. ATPASEC.
SUPFAMiSSF81333. SSF81333. 1 hit.
PROSITEiPS00605. ATPASE_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P61829-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLVLAAKYI GAGISTIGLL GAGIGIAIVF AALINGVSRN PSIKDTVFPM
60 70
AILGFALSEA TGLFCLMVSF LLLFGV
Length:76
Mass (Da):7,759
Last modified:July 21, 1986 - v1
Checksum:i82B4477D6F75D758
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti46 – 461T → L in strain: DS400/A3 and KL14-4A.
Natural varianti53 – 531L → F in strain: DS400/A3, DS401 and oligomycin-resistant mutant.
Natural varianti57 – 571L → V in oligomycin-resistant mutant and cross-resistance to venturicidin.
Natural varianti65 – 651C → S in oligomycin-resistant mutant.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L00007 Genomic DNA. Translation: AAA32146.1.
J01462 Genomic DNA. Translation: AAA32169.1.
V00707 Genomic DNA. Translation: CAA24079.1.
L36899 Genomic DNA. Translation: AAA67535.1.
X03968 Genomic DNA. Translation: CAA27605.1.
AJ011856 Genomic DNA. Translation: CAA09838.1.
PIRiA23024. LWBYA.
RefSeqiNP_009319.1. NC_001224.1.

Genome annotation databases

EnsemblFungiiQ0130; Q0130; Q0130.
GeneIDi854584.
KEGGisce:Q0130.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L00007 Genomic DNA. Translation: AAA32146.1.
J01462 Genomic DNA. Translation: AAA32169.1.
V00707 Genomic DNA. Translation: CAA24079.1.
L36899 Genomic DNA. Translation: AAA67535.1.
X03968 Genomic DNA. Translation: CAA27605.1.
AJ011856 Genomic DNA. Translation: CAA09838.1.
PIRiA23024. LWBYA.
RefSeqiNP_009319.1. NC_001224.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WPDX-ray3.43J/K/L/M/N/O/P/Q/R/S1-76[»]
2XOKX-ray3.01K/L/M/N/O/P/Q/R/S/T1-76[»]
3U2FX-ray2.00K/L/M/N/O1-76[»]
3U2YX-ray2.50K/L/M/N/O1-76[»]
3U32X-ray2.00K/L/M/N/O1-76[»]
3UD0X-ray2.00K/L/M/N/O1-76[»]
3ZRYX-ray6.50J/K/L/M/N/O/P/Q/R/S1-76[»]
4B2Qelectron microscopy37.00J/K/L/M/N/O/P/Q/R/S/j/k/l/m/n/o/p/q/r/s1-76[»]
4F4SX-ray1.90A/B/C/D/E/K/L/M/N/O1-76[»]
ProteinModelPortaliP61829.
SMRiP61829. Positions 2-75.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34780. 11 interactions.
DIPiDIP-3041N.
MINTiMINT-4981559.

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.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiQ0130; Q0130; Q0130.
GeneIDi854584.
KEGGisce:Q0130.

Organism-specific databases

CYGDiQ0130.
EuPathDBiFungiDB:Q0130.
SGDiS000007274. OLI1.

Phylogenomic databases

eggNOGiCOG0636.
GeneTreeiENSGT00390000006210.
HOGENOMiHOG000235245.
InParanoidiP61829.
KOiK02128.
OMAiIGMAFAE.
OrthoDBiEOG72NS3W.

Enzyme and pathway databases

BioCyciYEAST:G3O-34383-MONOMER.
ReactomeiREACT_334110. Mitochondrial protein import.

Miscellaneous databases

EvolutionaryTraceiP61829.
NextBioi977052.
PROiP61829.

Gene expression databases

ExpressionAtlasiP61829. differential.
GenevestigatoriP61829.

Family and domain databases

Gene3Di1.20.20.10. 1 hit.
HAMAPiMF_01396. ATP_synth_c_bact.
InterProiIPR000454. ATPase_F0-cplx_csu.
IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
IPR002379. ATPase_proteolipid_c_like_dom.
[Graphical view]
PfamiPF00137. ATP-synt_C. 1 hit.
[Graphical view]
PRINTSiPR00124. ATPASEC.
SUPFAMiSSF81333. SSF81333. 1 hit.
PROSITEiPS00605. ATPASE_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Amino acid sequence of the ATPase proteolipid from mitochondria, chloroplasts and bacteria (wild type and mutants)."
    Sebald W., Hoppe J., Wachter E.
    (In) Quagliariello E., Palmieri F., Papa S., Klingenberg M. (eds.); Function and molecular aspects of biomembrane transport, pp.63-74, Elsevier, Amsterdam (1979)
    Cited for: PROTEIN SEQUENCE.
  2. "Nucleotide sequence of the mitochondrial structural gene for subunit 9 of yeast ATPase complex."
    Hensgens L.A.M., Grivell L.A., Borst P., Bos J.L.
    Proc. Natl. Acad. Sci. U.S.A. 76:1663-1667(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: KL14-4A.
  3. "Organization of mitochondrial DNA in yeast."
    Tzagoloff A., Macino G., Nobrega M.P., Li M.
    (In) Cummings D.J., Brost P., Dawid I.B., Weissman S.M., Fox C.F. (eds.); Extrachromosomal DNA, pp.339-355, Academic Press, New York (1979)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: DS401.
  4. "Assembly of the mitochondrial membrane system. The DNA sequence of a mitochondrial ATPase gene in Saccharomyces cerevisiae."
    Macino G., Tzagoloff A.
    J. Biol. Chem. 254:4617-4623(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: DS400/A3.
  5. "Biogenesis of mitochondria: DNA sequence analysis of mit- mutations in the mitochondrial oli1 gene coding for mitochondrial ATPase subunit 9 in Saccharomyces cerevisiae."
    Ooi B.G., McMullen G.L., Linnane A.W., Nagley P., Novitski C.E.
    Nucleic Acids Res. 13:1327-1339(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "The complete sequence of the mitochondrial genome of Saccharomyces cerevisiae."
    Foury F., Roganti T., Lecrenier N., Purnelle B.
    FEBS Lett. 440:325-331(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  7. "NH2-terminal sequence of the isolated yeast ATP synthase subunit 6 reveals post-translational cleavage."
    Michon T., Galante M., Velours J.
    Eur. J. Biochem. 172:621-625(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-8, FORMYLATION AT MET-1.
  8. "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 nameiATP9_YEAST
AccessioniPrimary (citable) accession number: P61829
Secondary accession number(s): P00841, Q37750
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 29, 2015
This is version 102 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

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.