ID ATPG_YEAST Reviewed; 311 AA. AC P38077; D6VQ39; Q54AF5; Q76MT6; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 27-MAR-2024, entry version 195. DE RecName: Full=ATP synthase subunit gamma, mitochondrial; DE AltName: Full=F-ATPase gamma subunit; DE Flags: Precursor; GN Name=ATP3; Synonyms=ATP3a, ATP3b; OrderedLocusNames=YBR039W; GN ORFNames=YBR0408; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 34-61; 77-86; RP 195-207; 220-240 AND 284-290, AND MUTAGENESIS OF ALA-273. RC STRAIN=ATCC 201238 / W303-1B, and D273-10B/A1; RX PubMed=7929329; DOI=10.1016/s0021-9258(18)47172-4; RA Paul M.-F., Ackermann S., Yue J., Arselin G., Velours J., Tzagoloff A.; RT "Cloning of the yeast ATP3 gene coding for the gamma-subunit of F1 and RT characterization of atp3 mutants."; RL J. Biol. Chem. 269:26158-26164(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF THR-297 AND ILE-303. RX PubMed=7498726; DOI=10.1093/genetics/140.2.435; RA Weber E.R., Rooks R.S., Shafer K.S., Chase J.W., Thorsness P.E.; RT "Mutations in the mitochondrial ATP synthase gamma subunit suppress a slow- RT growth phenotype of yme1 yeast lacking mitochondrial DNA."; RL Genetics 140:435-442(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES ATP3A AND ATP3B). RC STRAIN=ATCC 64665 / S288c / DC5; RX PubMed=12898710; DOI=10.1002/yea.1009; RA Ohnishi K., Ishibashi S., Kunihiro M., Satoh T., Matsubara K., Oku S., RA Ono B., Mabuchi T., Takeda M.; RT "Studies on the ATP3 gene of Saccharomyces cerevisiae: presence of two RT closely linked copies, ATP3a and ATP3b, on the right arm of chromosome RT II."; RL Yeast 20:943-954(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., RA Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). RN [5] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; 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 [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [7] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [8] 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). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 34-311. RX PubMed=17082766; DOI=10.1038/sj.emboj.7601410; RA Kabaleeswaran V., Puri N., Walker J.E., Leslie A.G.W., Mueller D.M.; RT "Novel features of the rotary catalytic mechanism revealed in the structure RT of yeast F1 ATPase."; RL EMBO J. 25:5433-5442(2006). RN [10] RP X-RAY CRYSTALLOGRAPHY (3.59 ANGSTROMS) OF 34-311. RX PubMed=19233840; DOI=10.1074/jbc.m900544200; RA Kabaleeswaran V., Shen H., Symersky J., Walker J.E., Leslie A.G.W., RA Mueller D.M.; RT "Asymmetric structure of the yeast F1 ATPase in the absence of bound RT nucleotides."; RL J. Biol. Chem. 284:10546-10551(2009). 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 CC F(0) - containing the membrane proton channel, linked together by a CC central stalk and a peripheral stalk. During catalysis, ATP synthesis CC in the catalytic domain of F(1) is coupled via a rotary mechanism of CC the central stalk subunits to proton translocation. Part of the complex CC F(1) domain and the central stalk which is part of the complex rotary CC element. The gamma subunit protrudes into the catalytic domain formed CC of alpha(3)beta(3). Rotation of the central stalk against the CC surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in CC three separate catalytic sites on the beta subunits. CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core CC - and CF(0) - the membrane proton channel. CF(1) has five subunits: CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main CC subunits: a, b and c. CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane; CC Peripheral membrane protein. CC -!- MISCELLANEOUS: Present with 28100 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- MISCELLANEOUS: PubMed:12898710 reports two tandemly repeated copies of CC ATP3 (ATP3a and ATP3b) on the right arm of chromosome II in several CC laboratory strains, including S288c. This has not been confirmed by the CC yeast genome sequencing project. CC -!- SIMILARITY: Belongs to the ATPase gamma 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; U09305; AAA62605.1; -; Genomic_DNA. DR EMBL; U08318; AAA88816.1; -; Unassigned_DNA. DR EMBL; AB036928; BAC97839.1; -; Genomic_DNA. DR EMBL; AB036929; BAC97840.1; -; Genomic_DNA. DR EMBL; Z35908; CAA84981.1; -; Genomic_DNA. DR EMBL; AY557865; AAS56191.1; -; Genomic_DNA. DR EMBL; BK006936; DAA07159.1; -; Genomic_DNA. DR PIR; S55891; S55891. DR RefSeq; NP_009595.1; NM_001178387.1. DR PDB; 2HLD; X-ray; 2.80 A; G/P/Y=34-311. DR PDB; 2WPD; X-ray; 3.43 A; G=34-311. DR PDB; 2XOK; X-ray; 3.01 A; G=1-311. DR PDB; 3FKS; X-ray; 3.59 A; G/P/Y=34-311. DR PDB; 3OE7; X-ray; 3.19 A; G/P/Y=34-311. DR PDB; 3OEE; X-ray; 2.74 A; G/P/Y=34-311. DR PDB; 3OEH; X-ray; 3.00 A; G/P/Y=34-311. DR PDB; 3OFN; X-ray; 3.20 A; G/P/Y=34-311. DR PDB; 3ZIA; X-ray; 2.50 A; G/Q=34-311. DR PDB; 3ZRY; X-ray; 6.50 A; G=34-311. DR PDB; 4B2Q; EM; 37.00 A; G/g=34-311. DR PDB; 6B8H; EM; 3.60 A; G/j=34-311. DR PDB; 6CP3; EM; 3.80 A; G=34-311. DR PDB; 6CP6; EM; 3.60 A; G=34-311. DR PDB; 7TJT; EM; 3.20 A; G=34-311. DR PDB; 7TJU; EM; 3.30 A; G=34-311. DR PDB; 7TJV; EM; 3.60 A; G=34-311. DR PDB; 7TJW; EM; 4.00 A; G=34-311. DR PDB; 7TJX; EM; 4.00 A; G=34-311. DR PDB; 7TJY; EM; 3.80 A; G=34-311. DR PDB; 7TJZ; EM; 4.40 A; G=34-311. DR PDB; 7TK0; EM; 4.40 A; G=34-311. DR PDB; 7TK1; EM; 7.10 A; G=34-311. DR PDB; 7TK2; EM; 6.50 A; G=34-311. DR PDB; 7TK3; EM; 6.30 A; G=34-311. DR PDB; 7TK4; EM; 7.00 A; G=34-311. DR PDB; 7TK5; EM; 7.80 A; G=34-311. DR PDB; 7TK6; EM; 6.50 A; G=34-311. DR PDB; 7TK7; EM; 6.70 A; G=34-311. DR PDB; 7TK8; EM; 4.70 A; G=34-311. DR PDB; 7TK9; EM; 6.00 A; G=34-311. DR PDB; 7TKA; EM; 7.10 A; G=34-311. DR PDB; 7TKB; EM; 6.30 A; G=34-311. DR PDB; 7TKC; EM; 5.80 A; G=34-311. DR PDB; 7TKD; EM; 7.70 A; G=34-311. DR PDB; 7TKE; EM; 7.10 A; G=34-311. DR PDB; 7TKF; EM; 7.10 A; G=34-311. DR PDB; 7TKG; EM; 4.50 A; G=34-311. DR PDB; 7TKH; EM; 4.40 A; G=34-311. DR PDB; 7TKI; EM; 7.10 A; G=34-311. DR PDB; 7TKJ; EM; 7.50 A; G=34-311. DR PDB; 7TKK; EM; 7.30 A; G=34-311. DR PDB; 7TKL; EM; 6.40 A; G=34-311. DR PDB; 7TKM; EM; 4.50 A; G=34-311. DR PDB; 7TKN; EM; 7.10 A; G=34-311. DR PDB; 7TKO; EM; 4.80 A; G=34-311. DR PDB; 7TKP; EM; 4.60 A; G=34-311. DR PDB; 7TKQ; EM; 4.50 A; G=34-311. DR PDB; 7TKR; EM; 6.50 A; G=34-311. DR PDB; 7TKS; EM; 7.50 A; G=34-311. DR PDB; 8F2K; EM; 2.90 A; G=34-308. DR PDBsum; 2HLD; -. DR PDBsum; 2WPD; -. DR PDBsum; 2XOK; -. DR PDBsum; 3FKS; -. DR PDBsum; 3OE7; -. DR PDBsum; 3OEE; -. DR PDBsum; 3OEH; -. DR PDBsum; 3OFN; -. DR PDBsum; 3ZIA; -. DR PDBsum; 3ZRY; -. DR PDBsum; 4B2Q; -. DR PDBsum; 6B8H; -. DR PDBsum; 6CP3; -. DR PDBsum; 6CP6; -. DR PDBsum; 7TJT; -. DR PDBsum; 7TJU; -. DR PDBsum; 7TJV; -. DR PDBsum; 7TJW; -. DR PDBsum; 7TJX; -. DR PDBsum; 7TJY; -. DR PDBsum; 7TJZ; -. DR PDBsum; 7TK0; -. 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; 8F2K; -. DR AlphaFoldDB; P38077; -. DR EMDB; EMD-25931; -. DR EMDB; EMD-25932; -. DR EMDB; EMD-25933; -. DR EMDB; EMD-25934; -. DR EMDB; EMD-25939; -. DR EMDB; EMD-25946; -. DR EMDB; EMD-25947; -. DR EMDB; EMD-25948; -. DR EMDB; EMD-25949; -. 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-7546; -. DR EMDB; EMD-7548; -. DR SMR; P38077; -. DR BioGRID; 32740; 161. DR ComplexPortal; CPX-3281; Mitochondrial proton-transporting ATP synthase complex. DR DIP; DIP-3035N; -. DR IntAct; P38077; 42. DR MINT; P38077; -. DR STRING; 4932.YBR039W; -. DR TCDB; 3.A.2.1.3; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily. DR MaxQB; P38077; -. DR PaxDb; 4932-YBR039W; -. DR PeptideAtlas; P38077; -. DR EnsemblFungi; YBR039W_mRNA; YBR039W; YBR039W. DR GeneID; 852327; -. DR KEGG; sce:YBR039W; -. DR AGR; SGD:S000000243; -. DR SGD; S000000243; ATP3. DR VEuPathDB; FungiDB:YBR039W; -. DR eggNOG; KOG1531; Eukaryota. DR GeneTree; ENSGT00390000006837; -. DR HOGENOM; CLU_050669_4_1_1; -. DR InParanoid; P38077; -. DR OMA; MQITSAM; -. DR OrthoDB; 393at2759; -. DR BioCyc; YEAST:G3O-29013-MONOMER; -. DR BioGRID-ORCS; 852327; 5 hits in 10 CRISPR screens. DR EvolutionaryTrace; P38077; -. DR PRO; PR:P38077; -. DR Proteomes; UP000002311; Chromosome II. DR RNAct; P38077; Protein. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal. DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; NAS:ComplexPortal. DR GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IBA:GO_Central. DR GO; GO:0005756; C:mitochondrial proton-transporting ATP synthase, central stalk; IDA:SGD. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro. DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IDA:SGD. DR CDD; cd12151; F1-ATPase_gamma; 1. DR Gene3D; 3.40.1380.10; -; 1. DR InterPro; IPR035968; ATP_synth_F1_ATPase_gsu. DR InterPro; IPR000131; ATP_synth_F1_gsu. DR InterPro; IPR023632; ATP_synth_F1_gsu_CS. DR NCBIfam; TIGR01146; ATPsyn_F1gamma; 1. DR PANTHER; PTHR11693; ATP SYNTHASE GAMMA CHAIN; 1. DR PANTHER; PTHR11693:SF22; ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL; 1. DR Pfam; PF00231; ATP-synt; 1. DR PIRSF; PIRSF039089; ATP_synthase_gamma; 1. DR PRINTS; PR00126; ATPASEGAMMA. DR SUPFAM; SSF52943; ATP synthase (F1-ATPase), gamma subunit; 1. DR PROSITE; PS00153; ATPASE_GAMMA; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP synthesis; CF(1); Direct protein sequencing; KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Reference proteome; Transit peptide; KW Transport. FT TRANSIT 1..33 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:7929329" FT CHAIN 34..311 FT /note="ATP synthase subunit gamma, mitochondrial" FT /id="PRO_0000002691" FT VARIANT 207 FT /note="S -> I (in strain: D273-10B/A1)" FT VARIANT 308 FT /note="S -> F (in allele ATP3a)" FT MUTAGEN 273 FT /note="A->V: Lower activity." FT /evidence="ECO:0000269|PubMed:7929329" FT MUTAGEN 297 FT /note="T->A: In ATP3-5; dominant suppressor of the FT slow-growth phenotype of yme1 strains lacking mitochondrial FT DNA." FT /evidence="ECO:0000269|PubMed:7498726" FT MUTAGEN 303 FT /note="I->T: In ATP3-1; dominant suppressor of the FT slow-growth phenotype of yme1 strains lacking mitochondrial FT DNA." FT /evidence="ECO:0000269|PubMed:7498726" FT HELIX 36..79 FT /evidence="ECO:0007829|PDB:3ZIA" FT HELIX 83..87 FT /evidence="ECO:0007829|PDB:3ZIA" FT STRAND 105..110 FT /evidence="ECO:0007829|PDB:3ZIA" FT HELIX 120..134 FT /evidence="ECO:0007829|PDB:3ZIA" FT STRAND 139..144 FT /evidence="ECO:0007829|PDB:3ZIA" FT HELIX 145..154 FT /evidence="ECO:0007829|PDB:3ZIA" FT HELIX 156..158 FT /evidence="ECO:0007829|PDB:3ZIA" FT STRAND 159..165 FT /evidence="ECO:0007829|PDB:3ZIA" FT STRAND 167..169 FT /evidence="ECO:0007829|PDB:3ZIA" FT HELIX 173..186 FT /evidence="ECO:0007829|PDB:3ZIA" FT HELIX 189..191 FT /evidence="ECO:0007829|PDB:3ZIA" FT STRAND 193..201 FT /evidence="ECO:0007829|PDB:3ZIA" FT STRAND 203..206 FT /evidence="ECO:0007829|PDB:3ZIA" FT STRAND 209..215 FT /evidence="ECO:0007829|PDB:3ZIA" FT HELIX 218..222 FT /evidence="ECO:0007829|PDB:3ZIA" FT HELIX 227..229 FT /evidence="ECO:0007829|PDB:3ZIA" FT STRAND 234..236 FT /evidence="ECO:0007829|PDB:3ZIA" FT HELIX 239..308 FT /evidence="ECO:0007829|PDB:3ZIA" SQ SEQUENCE 311 AA; 34351 MW; ADC71F3C1E0CDF91 CRC64; MLSRIVSNNA TRSVMCHQAQ VGILYKTNPV RTYATLKEVE MRLKSIKNIE KITKTMKIVA STRLSKAEKA KISAKKMDEA EQLFYKNAET KNLDVEATET GAPKELIVAI TSDKGLCGSI HSQLAKAVRR HLNDQPNADI VTIGDKIKMQ LLRTHPNNIK LSINGIGKDA PTFQESALIA DKLLSVMKAG TYPKISIFYN DPVSSLSFEP SEKPIFNAKT IEQSPSFGKF EIDTDANVPR DLFEYTLANQ MLTAMAQGYA AEISARRNAM DNASKNAGDM INRYSILYNR TRQAVITNEL VDIITGASSL G //