ATPG_YEAST
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 03-AUG-2022, entry version 188.
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}.
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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 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 AlphaFoldDB; P38077; -.
DR SMR; P38077; -.
DR BioGRID; 32740; 130.
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; P38077; -.
DR PRIDE; P38077; -.
DR EnsemblFungi; YBR039W_mRNA; YBR039W; YBR039W.
DR GeneID; 852327; -.
DR KEGG; sce:YBR039W; -.
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 BioCyc; YEAST:G3O-29013-MON; -.
DR Reactome; R-SCE-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-SCE-8949613; Cristae formation.
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; IC: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 InterPro; IPR035968; ATP_synth_F1_ATPase_gsu.
DR InterPro; IPR000131; ATP_synth_F1_gsu.
DR InterPro; IPR023632; ATP_synth_F1_gsu_CS.
DR PANTHER; PTHR11693; PTHR11693; 1.
DR Pfam; PF00231; ATP-synt; 1.
DR PRINTS; PR00126; ATPASEGAMMA.
DR SUPFAM; SSF52943; SSF52943; 1.
DR TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 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 slow-
FT 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 slow-
FT 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
