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 02-SEP-2026, entry version 171. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AH001281; 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 PDB; 7TJZ; EM; 4.40 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TK1; EM; 7.10 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TK2; EM; 6.50 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TK3; EM; 6.30 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TK4; EM; 7.00 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TK5; EM; 7.80 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TK6; EM; 6.50 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TK7; EM; 6.70 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TK8; EM; 4.70 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TK9; EM; 6.00 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TKA; EM; 7.10 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TKB; EM; 6.30 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TKC; EM; 5.80 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TKD; EM; 7.70 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TKE; EM; 7.10 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TKF; EM; 7.10 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TKG; EM; 4.50 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TKH; EM; 4.40 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TKI; EM; 7.10 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TKJ; EM; 7.50 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TKK; EM; 7.30 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TKL; EM; 6.40 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TKM; EM; 4.50 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TKN; EM; 7.10 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TKO; EM; 4.80 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TKP; EM; 4.60 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TKQ; EM; 4.50 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TKR; EM; 6.50 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 7TKS; EM; 7.50 A; 0/1/2/3/4/5/6/7/8/9=1-76. DR PDB; 8F29; EM; 4.00 A; K/L/M/N/O/P/Q/R/S/T=1-75. DR PDB; 8F39; EM; 3.50 A; K/L/M/N/O/P/Q/R/S/T=1-75. DR PDB; 8FKJ; EM; 4.20 A; K/L/M/N/O/P/Q/R/S/T=2-75. DR PDB; 8FL8; EM; 4.20 A; K/L/M/N/O/P/Q/R/S/T=1-75. DR AlphaFoldDB; P61829; -. DR EMDB; EMD-21894; -. DR EMDB; EMD-25954; -. DR EMDB; EMD-25955; -. DR EMDB; EMD-25956; -. DR EMDB; EMD-25957; -. DR EMDB; EMD-25958; -. DR EMDB; EMD-25959; -. DR EMDB; EMD-25960; -. DR EMDB; EMD-25961; -. DR EMDB; EMD-25962; -. DR EMDB; EMD-25963; -. DR EMDB; EMD-25964; -. DR EMDB; EMD-25965; -. DR EMDB; EMD-25966; -. DR EMDB; EMD-25967; -. DR EMDB; EMD-25968; -. DR EMDB; EMD-25969; -. DR EMDB; EMD-25970; -. DR EMDB; EMD-25971; -. DR EMDB; EMD-25972; -. DR EMDB; EMD-25973; -. DR EMDB; EMD-25974; -. DR EMDB; EMD-25975; -. DR EMDB; EMD-25976; -. DR EMDB; EMD-25977; -. DR EMDB; EMD-25978; -. DR EMDB; EMD-25979; -. DR EMDB; EMD-25980; -. DR EMDB; EMD-28809; -. DR EMDB; EMD-28835; -. DR EMDB; EMD-7036; -. DR EMDB; EMD-7546; -. DR EMDB; EMD-7547; -. DR EMDB; EMD-7548; -. DR EMDB; EMD-7549; -. DR SMR; P61829; -. DR BioGRID; 34780; 14. DR ComplexPortal; CPX-3281; Mitochondrial proton-transporting ATP synthase complex. DR DIP; DIP-3041N; -. DR FunCoup; P61829; 1218. 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; 4932-Q0130; -. DR PeptideAtlas; P61829; -. DR EnsemblFungi; Q0130_mRNA; Q0130; Q0130. DR GeneID; 24573116; -. DR GeneID; 854584; -. DR KEGG; sce:Q0130; -. DR AGR; SGD:S000007274; -. DR SGD; S000007274; OLI1. DR VEuPathDB; FungiDB:Q0130; -. DR eggNOG; KOG3025; Eukaryota. DR HOGENOM; CLU_148047_4_1_1; -. DR InParanoid; P61829; -. DR OMA; YIFGKMI; -. DR OrthoDB; 438052at2759; -. DR BioCyc; YEAST:G3O-34383-MONOMER; -. DR BioGRID-ORCS; 854584; 0 hits in 10 CRISPR screens. 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:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal. DR GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0045259; C:proton-transporting ATP synthase complex; IPI:SGD. DR GO; GO:0033177; C:proton-transporting two-sector ATPase complex, proton-transporting domain; IEA:InterPro. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro. DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IDA:ComplexPortal. DR CDD; cd18182; ATP-synt_Fo_c_ATP5G3; 1. DR FunFam; 1.20.20.10:FF:000014; ATP synthase subunit 9, mitochondrial; 1. DR Gene3D; 1.20.20.10; F1F0 ATP synthase subunit C; 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; ATP SYNTHASE LIPID-BINDING PROTEIN, MITOCHONDRIAL; 1. DR PANTHER; PTHR10031:SF0; ATPASE PROTEIN 9; 1. DR Pfam; PF00137; ATP-synt_C; 1. DR PRINTS; PR00124; ATPASEC. DR SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 1. DR PROSITE; PS00605; ATPASE_C; 1. 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 PDBsum; 7TJZ; -. DR PDBsum; 7TK1; -. DR PDBsum; 7TK2; -. DR PDBsum; 7TK3; -. DR PDBsum; 7TK4; -. DR PDBsum; 7TK5; -. DR PDBsum; 7TK6; -. DR PDBsum; 7TK7; -. DR PDBsum; 7TK8; -. DR PDBsum; 7TK9; -. DR PDBsum; 7TKA; -. DR PDBsum; 7TKB; -. DR PDBsum; 7TKC; -. DR PDBsum; 7TKD; -. DR PDBsum; 7TKE; -. DR PDBsum; 7TKF; -. DR PDBsum; 7TKG; -. DR PDBsum; 7TKH; -. DR PDBsum; 7TKI; -. DR PDBsum; 7TKJ; -. DR PDBsum; 7TKK; -. DR PDBsum; 7TKL; -. DR PDBsum; 7TKM; -. DR PDBsum; 7TKN; -. DR PDBsum; 7TKO; -. DR PDBsum; 7TKP; -. DR PDBsum; 7TKQ; -. DR PDBsum; 7TKR; -. DR PDBsum; 7TKS; -. DR PDBsum; 8F29; -. DR PDBsum; 8F39; -. DR PDBsum; 8FKJ; -. DR PDBsum; 8FL8; -. 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 FT oligomycin-resistant mutant)" FT VARIANT 57 FT /note="L -> V (in oligomycin-resistant mutant and FT cross-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 TURN 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 //