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P61829 (ATP9_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 9, mitochondrial
Alternative name(s):
Lipid-binding protein
Oligomycin resistance protein 1
Gene names
Name:OLI1
Synonyms:ATP9, OLI3, PHO2
Ordered Locus Names:Q0130
Encoded onMitochondrion
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length76 AA.
Sequence statusComplete.
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 F0 domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element. HAMAP-Rule MF_01396

Subunit structure

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.

Subcellular location

Mitochondrion membrane; Multi-pass membrane protein Potential HAMAP-Rule MF_01396.

Sequence similarities

Belongs to the ATPase C chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7676ATP synthase subunit 9, mitochondrial HAMAP-Rule MF_01396
PRO_0000112240

Regions

Transmembrane14 – 3421Helical; Potential
Transmembrane52 – 7221Helical; Potential

Sites

Site591Reversibly protonated during proton transport By similarity

Amino acid modifications

Modified residue11N-formylmethionine HAMAP-Rule MF_01396

Natural variations

Natural variant461T → L in strain: DS400/A3 and KL14-4A.
Natural variant531L → F in strain: DS400/A3, DS401 and oligomycin-resistant mutant.
Natural variant571L → V in oligomycin-resistant mutant and cross-resistance to venturicidin.
Natural variant651C → S in oligomycin-resistant mutant.

Secondary structure

........ 76
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P61829 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 82B4477D6F75D758

FASTA767,759
        10         20         30         40         50         60 
MQLVLAAKYI GAGISTIGLL GAGIGIAIVF AALINGVSRN PSIKDTVFPM AILGFALSEA 

        70 
TGLFCLMVSF LLLFGV 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRLWBYA. A23024.
RefSeqNP_009319.1. NM_001184366.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP61829.
SMRP61829. Positions 2-75.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34780. 10 interactions.
DIPDIP-3041N.
MINTMINT-4981559.

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.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiQ0130; Q0130; Q0130.
GeneID854584.
KEGGsce:Q0130.

Organism-specific databases

CYGDQ0130.
SGDS000007274. OLI1.

Phylogenomic databases

eggNOGCOG0636.
GeneTreeENSGT00390000006210.
HOGENOMHOG000235245.
KOK02128.
OMANPETEEK.
OrthoDBEOG72NS3W.

Enzyme and pathway databases

BioCycYEAST:G3O-34383-MONOMER.
ReactomeREACT_118590. Mitochondrial Protein Import (yeast).

Gene expression databases

GenevestigatorP61829.

Family and domain databases

Gene3D1.20.20.10. 1 hit.
HAMAPMF_01396. ATP_synth_c_bact.
InterProIPR000454. ATPase_F0-cplx_csu.
IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
IPR002379. ATPase_proteolipid_c_like_dom.
[Graphical view]
PfamPF00137. ATP-synt_C. 1 hit.
[Graphical view]
PRINTSPR00124. ATPASEC.
SUPFAMSSF81333. SSF81333. 1 hit.
PROSITEPS00605. ATPASE_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP61829.
NextBio977052.

Entry information

Entry nameATP9_YEAST
AccessionPrimary (citable) accession number: P61829
Secondary accession number(s): P00841, Q37750
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

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