ATP9_YEAST
ID ATP9_YEAST Reviewed; 76 AA.
AC P61829; A0A0A7P075; P00841; Q37750;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=ATP synthase subunit 9, mitochondrial;
DE AltName: Full=Lipid-binding protein;
DE AltName: Full=Oligomycin resistance protein 1;
GN Name=OLI1; Synonyms=ATP9, OLI3, PHO2; OrderedLocusNames=Q0130;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP PROTEIN SEQUENCE.
RA Sebald W., Hoppe J., Wachter E.;
RT "Amino acid sequence of the ATPase proteolipid from mitochondria,
RT chloroplasts and bacteria (wild type and mutants).";
RL (In) Quagliariello E., Palmieri F., Papa S., Klingenberg M. (eds.);
RL Function and molecular aspects of biomembrane transport, pp.63-74,
RL Elsevier, Amsterdam (1979).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KL14-4A;
RX PubMed=156363; DOI=10.1073/pnas.76.4.1663;
RA Hensgens L.A.M., Grivell L.A., Borst P., Bos J.L.;
RT "Nucleotide sequence of the mitochondrial structural gene for subunit 9 of
RT yeast ATPase complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:1663-1667(1979).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DS401;
RA Tzagoloff A., Macino G., Nobrega M.P., Li M.;
RT "Organization of mitochondrial DNA in yeast.";
RL (In) Cummings D.J., Brost P., Dawid I.B., Weissman S.M., Fox C.F. (eds.);
RL Extrachromosomal DNA, pp.339-355, Academic Press, New York (1979).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DS400/A3;
RX PubMed=155696; DOI=10.1016/s0021-9258(17)30055-8;
RA Macino G., Tzagoloff A.;
RT "Assembly of the mitochondrial membrane system. The DNA sequence of a
RT mitochondrial ATPase gene in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 254:4617-4623(1979).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2860638; DOI=10.1093/nar/13.4.1327;
RA Ooi B.G., McMullen G.L., Linnane A.W., Nagley P., Novitski C.E.;
RT "Biogenesis of mitochondria: DNA sequence analysis of mit- mutations in the
RT mitochondrial oli1 gene coding for mitochondrial ATPase subunit 9 in
RT Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 13:1327-1339(1985).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9872396; DOI=10.1016/s0014-5793(98)01467-7;
RA Foury F., Roganti T., Lecrenier N., Purnelle B.;
RT "The complete sequence of the mitochondrial genome of Saccharomyces
RT cerevisiae.";
RL FEBS Lett. 440:325-331(1998).
RN [7]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [8]
RP PROTEIN SEQUENCE OF 1-8, AND FORMYLATION AT MET-1.
RX PubMed=2894987; DOI=10.1111/j.1432-1033.1988.tb13934.x;
RA Michon T., Galante M., Velours J.;
RT "NH2-terminal sequence of the isolated yeast ATP synthase subunit 6 reveals
RT post-translational cleavage.";
RL Eur. J. Biochem. 172:621-625(1988).
RN [9]
RP 3D-STRUCTURE MODELING.
RX PubMed=10576729; DOI=10.1126/science.286.5445.1700;
RA Stock D., Leslie A.G., Walker J.E.;
RT "Molecular architecture of the rotary motor in ATP synthase.";
RL Science 286:1700-1705(1999).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core and F(0)
CC - containing the membrane proton channel, linked together by a central
CC stalk and a peripheral stalk. During catalysis, ATP synthesis in the
CC catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation. Part of the complex
CC F(0) domain. A homomeric c-ring of probably 10 subunits is part of the
CC complex rotary element.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. In yeast, the dimeric form
CC of ATP synthase consists of 17 polypeptides: alpha, beta, gamma, delta,
CC epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d, E (Tim11), f, g, h, i/j
CC and k.
CC -!- INTERACTION:
CC P61829; P61829: OLI1; NbExp=2; IntAct=EBI-9016907, EBI-9016907;
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
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DR EMBL; L00007; AAA32146.1; -; Genomic_DNA.
DR EMBL; J01462; AAA32169.1; -; Genomic_DNA.
DR EMBL; V00707; CAA24079.1; -; Genomic_DNA.
DR EMBL; L36899; AAA67535.1; -; Genomic_DNA.
DR EMBL; X03968; CAA27605.1; -; Genomic_DNA.
DR EMBL; KP263414; AIZ98894.1; -; Genomic_DNA.
DR PIR; A23024; LWBYA.
DR RefSeq; NP_009319.1; NC_001224.1.
DR RefSeq; YP_009144710.1; NC_027264.1.
DR PDB; 2WPD; X-ray; 3.43 A; J/K/L/M/N/O/P/Q/R/S=1-76.
DR PDB; 2XOK; X-ray; 3.01 A; K/L/M/N/O/P/Q/R/S/T=1-76.
DR PDB; 3U2F; X-ray; 2.00 A; K/L/M/N/O=1-76.
DR PDB; 3U2Y; X-ray; 2.50 A; K/L/M/N/O=1-76.
DR PDB; 3U32; X-ray; 2.00 A; K/L/M/N/O=1-76.
DR PDB; 3UD0; X-ray; 2.00 A; K/L/M/N/O=1-76.
DR PDB; 3ZRY; X-ray; 6.50 A; J/K/L/M/N/O/P/Q/R/S=1-76.
DR PDB; 4B2Q; EM; 37.00 A; J/K/L/M/N/O/P/Q/R/S/j/k/l/m/n/o/p/q/r/s=1-76.
DR PDB; 4F4S; X-ray; 1.90 A; A/B/C/D/E/K/L/M/N/O=1-76.
DR PDB; 5BPS; X-ray; 2.10 A; A/B/C/D/E/K/L/M/N/O=1-76.
DR PDB; 5BQ6; X-ray; 2.30 A; A/B/C/D/E/K/L/M/N/O=1-76.
DR PDB; 5BQA; X-ray; 2.10 A; A/B/C/D/E/K/L/M/N/O=1-76.
DR PDB; 5BQJ; X-ray; 2.10 A; A/B/C/D/E/K/L/M/N/O=1-76.
DR PDB; 6B2Z; EM; 3.60 A; 0/1/2/3/4/5/6/7/8/9/B/C/D/E/F/G/H/I/J/K=1-76.
DR PDB; 6B8H; EM; 3.60 A; 0/1/2/3/4/5/6/7/8/9/J/L/M/N/P/Q/R/S/T/U=1-76.
DR PDB; 6CP3; EM; 3.80 A; K/L/M/N/O/P/Q/R/S/T=1-76.
DR PDB; 6CP5; EM; 4.20 A; K/L/M/N/O/P/Q/R/S/T=1-76.
DR PDB; 6CP6; EM; 3.60 A; K/L/M/N/O/P/Q/R/S/T=1-76.
DR PDB; 6CP7; EM; 4.10 A; K/L/M/N/O/P/Q/R/S/T=1-76.
DR PDB; 6WTD; EM; 4.20 A; K/L/M/N/O/P/Q/R/S/T=1-76.
DR PDBsum; 2WPD; -.
DR PDBsum; 2XOK; -.
DR PDBsum; 3U2F; -.
DR PDBsum; 3U2Y; -.
DR PDBsum; 3U32; -.
DR PDBsum; 3UD0; -.
DR PDBsum; 3ZRY; -.
DR PDBsum; 4B2Q; -.
DR PDBsum; 4F4S; -.
DR PDBsum; 5BPS; -.
DR PDBsum; 5BQ6; -.
DR PDBsum; 5BQA; -.
DR PDBsum; 5BQJ; -.
DR PDBsum; 6B2Z; -.
DR PDBsum; 6B8H; -.
DR PDBsum; 6CP3; -.
DR PDBsum; 6CP5; -.
DR PDBsum; 6CP6; -.
DR PDBsum; 6CP7; -.
DR PDBsum; 6WTD; -.
DR AlphaFoldDB; P61829; -.
DR SMR; P61829; -.
DR BioGRID; 34780; 13.
DR ComplexPortal; CPX-3281; Mitochondrial proton-transporting ATP synthase complex.
DR DIP; DIP-3041N; -.
DR IntAct; P61829; 2.
DR STRING; 4932.Q0130; -.
DR TCDB; 3.A.2.1.3; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PaxDb; P61829; -.
DR PRIDE; P61829; -.
DR EnsemblFungi; Q0130_mRNA; Q0130; Q0130.
DR GeneID; 24573116; -.
DR GeneID; 854584; -.
DR KEGG; sce:Q0130; -.
DR SGD; S000007274; OLI1.
DR VEuPathDB; FungiDB:Q0130; -.
DR eggNOG; KOG3025; Eukaryota.
DR GeneTree; ENSGT00940000176138; -.
DR HOGENOM; CLU_148047_4_1_1; -.
DR InParanoid; P61829; -.
DR OMA; CMGFCIL; -.
DR BioCyc; YEAST:G3O-34383-MON; -.
DR Reactome; R-SCE-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-SCE-8949613; Cristae formation.
DR EvolutionaryTrace; P61829; -.
DR PRO; PR:P61829; -.
DR Proteomes; UP000002311; Mitochondrion.
DR RNAct; P61829; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IC:ComplexPortal.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IPI:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IDA:SGD.
DR Gene3D; 1.20.20.10; -; 1.
DR HAMAP; MF_01396; ATP_synth_c_bact; 1.
DR InterPro; IPR000454; ATP_synth_F0_csu.
DR InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
DR InterPro; IPR038662; ATP_synth_F0_csu_sf.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR PANTHER; PTHR10031; PTHR10031; 1.
DR Pfam; PF00137; ATP-synt_C; 1.
DR PRINTS; PR00124; ATPASEC.
DR SUPFAM; SSF81333; SSF81333; 1.
DR PROSITE; PS00605; ATPASE_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; CF(0); Direct protein sequencing; Formylation;
KW Hydrogen ion transport; Ion transport; Lipid-binding; Membrane;
KW Mitochondrion; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..76
FT /note="ATP synthase subunit 9, mitochondrial"
FT /id="PRO_0000112240"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 59
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:2894987"
FT VARIANT 46
FT /note="T -> L (in strain: DS400/A3 and KL14-4A)"
FT VARIANT 53
FT /note="L -> F (in strain: DS400/A3, DS401 and oligomycin-
FT resistant mutant)"
FT VARIANT 57
FT /note="L -> V (in oligomycin-resistant mutant and cross-
FT resistance to venturicidin)"
FT VARIANT 65
FT /note="C -> S (in oligomycin-resistant mutant)"
FT HELIX 2..14
FT /evidence="ECO:0007829|PDB:4F4S"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:4F4S"
FT HELIX 19..39
FT /evidence="ECO:0007829|PDB:4F4S"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:4F4S"
FT HELIX 44..73
FT /evidence="ECO:0007829|PDB:4F4S"
SQ SEQUENCE 76 AA; 7759 MW; 82B4477D6F75D758 CRC64;
MQLVLAAKYI GAGISTIGLL GAGIGIAIVF AALINGVSRN PSIKDTVFPM AILGFALSEA
TGLFCLMVSF LLLFGV
