ATP synthase subunit 9, mitochondrial - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P61829 (ATP9_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 74. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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 on

Mitochondrion

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	76 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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.
Sequence similarities	Belongs to the ATPase C chain family.

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Membrane Mitochondrion
Domain	Transmembrane Transmembrane helix
Ligand	Lipid-binding
PTM	Formylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	ATP catabolic process Inferred from direct assay. Source: GOC ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro ATP synthesis coupled proton transport Inferred from direct assay. Source: SGD
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Inferred from physical interaction Ref.7. Source: SGD
Molecular function	hydrogen ion transmembrane transporter activity Inferred from electronic annotation. Source: InterPro lipid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 76

ATP synthase subunit 9, mitochondrial

PRO_0000112240

Regions

Transmembrane

14 – 34

Helical; Potential

Transmembrane

52 – 72

Helical; Potential

Sites

Site

Reversibly protonated during proton transport By similarity

Amino acid modifications

Modified residue

N-formylmethionine

Natural variations

Natural variant

T → L in strain: DS400/A3 and KL14-4A.

Natural variant

L → F in strain: DS400/A3, DS401 and oligomycin-resistant mutant.

Natural variant

L → V in oligomycin-resistant mutant and cross-resistance to venturicidin.

Natural variant

C → S in oligomycin-resistant mutant.

Secondary structure

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P61829 [UniParc].

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

7,759

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

        70 
TGLFCLMVSF LLLFGV

« Hide

References

	« Hide 'large scale' referencesShow '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: 156363] [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: 155696] [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: 2860638] [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: 9872396] [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: 2894987] [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: 10576729] [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.

PIR

LWBYA. A23024.

RefSeq

NP_009319.1. NM_001184366.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2WPD	X-ray	3.43	J/K/L/M/N/O/P/Q/R/S	1-76	[»]
2XOK	X-ray	3.01	K/L/M/N/O/P/Q/R/S/T	1-76	[»]

ProteinModelPortal

P61829.

SMR

P61829. Positions 1-76.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-3041N.

STRING

P61829.

Protein family/group databases

TCDB

3.A.2.1.3. H+- or Na+-translocating F-type, V-type and A-type ATPase (F-ATPase) superfamily.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

Q0130; Q0130; Q0130.

GeneID

854584.

KEGG

sce:Q0130.

NMPDR

fig|4932.3.peg.1871.

Organism-specific databases

CYGD

Q0130.

SGD

S000007274. OLI1.

Phylogenomic databases

eggNOG

fuNOG12572.

HOGENOM

HBG753983.

OrthoDB

EOG4J9R8T.

Gene expression databases

ArrayExpress

P61829.

Genevestigator

P61829.

GermOnline

Q0130. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000454. ATPase_F0-cplx_csu.
IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
IPR002379. ATPase_F0/V0-cplx_csu.
[Graphical view]

Gene3D

G3DSA:1.20.20.10. ATPase_F0/V0_c. 1 hit.

K02128.

Pfam

PF00137. ATP-synt_C. 1 hit.
[Graphical view]

PRINTS

PR00124. ATPASEC.

SUPFAM

SSF81333. ATPase_F0/V0_c. 1 hit.

PROSITE

PS00605. ATPASE_C. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

977052.

Entry information

Entry name

ATP9_YEAST

Accession

Primary (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:	December 14, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents