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Protein

ATP synthase subunit 9, mitochondrial

Gene

OLI1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Sitei59Reversibly protonated during proton transportBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processHydrogen ion transport, Ion transport, Transport
LigandLipid-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-34383-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 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
Proteomesi
  • UP000002311 Componenti: Mitochondrion

Organism-specific databases

SGDiS000007274 OLI1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei14 – 34HelicalSequence analysisAdd BLAST21
Transmembranei52 – 72HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

CF(0), Membrane, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001122401 – 76ATP synthase subunit 9, mitochondrialAdd BLAST76

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-formylmethionine1 Publication1

Keywords - PTMi

Formylation

Proteomic databases

PaxDbiP61829
PRIDEiP61829

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.

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi34780, 11 interactors
DIPiDIP-3041N
IntActiP61829, 1 interactor
STRINGi4932.Q0130

Structurei

Secondary structure

176
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 14Combined sources13
Helixi15 – 18Combined sources4
Helixi19 – 39Combined sources21
Helixi41 – 43Combined sources3
Helixi44 – 73Combined sources30

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5BPSX-ray2.10A/B/C/D/E/K/L/M/N/O1-76[»]
5BQ6X-ray2.30A/B/C/D/E/K/L/M/N/O1-76[»]
5BQAX-ray2.10A/B/C/D/E/K/L/M/N/O1-76[»]
5BQJX-ray2.10A/B/C/D/E/K/L/M/N/O1-76[»]
6B2Zelectron microscopy3.600/1/2/3/4/5/6/7/8/9/B/C/D/E/F/G/H/I/J/K1-76[»]
6B8Helectron microscopy3.600/1/2/3/4/5/6/7/8/9/J/L/M/N/P/Q/R/S/T/U1-76[»]
ProteinModelPortaliP61829
SMRiP61829
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61829

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase C chain family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000006210
HOGENOMiHOG000235245
InParanoidiP61829
KOiK02128
OMAiASFAPMM
OrthoDBiEOG092C5ZJA

Family and domain databases

Gene3Di1.20.20.10, 1 hit
HAMAPiMF_01396 ATP_synth_c_bact, 1 hit
InterProiView protein in InterPro
IPR000454 ATP_synth_F0_csu
IPR020537 ATP_synth_F0_csu_DDCD_BS
IPR038662 ATP_synth_F0_csu_sf
IPR002379 ATPase_proteolipid_c-like_dom
IPR035921 F/V-ATP_Csub_sf
PANTHERiPTHR10031 PTHR10031, 1 hit
PfamiView protein in Pfam
PF00137 ATP-synt_C, 1 hit
PRINTSiPR00124 ATPASEC
SUPFAMiSSF81333 SSF81333, 1 hit
PROSITEiView protein in PROSITE
PS00605 ATPASE_C, 1 hit

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)DescriptionActionsGraphical viewLength
Natural varianti46T → L in strain: DS400/A3 and KL14-4A. 1
Natural varianti53L → F in strain: DS400/A3, DS401 and oligomycin-resistant mutant. 1
Natural varianti57L → V in oligomycin-resistant mutant and cross-resistance to venturicidin. 1
Natural varianti65C → S in oligomycin-resistant mutant. 1

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
KP263414 Genomic DNA Translation: AIZ98894.1
PIRiA23024 LWBYA
RefSeqiNP_009319.1, NC_001224.1
YP_009144710.1, NC_027264.1

Genome annotation databases

EnsemblFungiiQ0130; Q0130; Q0130
GeneIDi24573116
854584
KEGGisce:Q0130

Similar proteinsi

Entry informationi

Entry nameiATP9_YEAST
AccessioniPrimary (citable) accession number: P61829
Secondary accession number(s): A0A0A7P075, P00841, Q37750
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 25, 2018
This is version 128 of the entry and version 1 of the sequence. See 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
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Main funding by: National Institutes of Health