ATPK_YEAST
ID ATPK_YEAST Reviewed; 101 AA.
AC Q06405; D6VT09;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=ATP synthase subunit f, mitochondrial;
DE Flags: Precursor;
GN Name=ATP17; OrderedLocusNames=YDR377W; ORFNames=D9481.21;
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], PARTIAL PROTEIN SEQUENCE,
RP CHARACTERIZATION, AND MASS SPECTROMETRY.
RC STRAIN=D273-10B/A/H/U;
RX PubMed=9288937; DOI=10.1111/j.1432-1033.1997.01111.x;
RA Spannagel C., Vaillier J., Arselin G., Graves P.-V., Velours J.;
RT "The subunit f of mitochondrial yeast ATP synthase -- characterization of
RT the protein and disruption of the structural gene ATP17.";
RL Eur. J. Biochem. 247:1111-1117(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
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 [4]
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).
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. Minor subunit located with subunit a in the membrane.
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 -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- MASS SPECTROMETRY: Mass=10565; Mass_error=2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9288937};
CC -!- MISCELLANEOUS: Present with 14600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ATPase F chain family. {ECO:0000305}.
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DR EMBL; U72652; AAB70108.1; -; Genomic_DNA.
DR EMBL; U28373; AAB64813.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12219.1; -; Genomic_DNA.
DR PIR; S61172; S61172.
DR RefSeq; NP_010665.3; NM_001180685.3.
DR PDB; 6B2Z; EM; 3.60 A; Q/f=7-101.
DR PDB; 6B8H; EM; 3.60 A; f/t=7-101.
DR PDB; 6CP3; EM; 3.80 A; U=7-101.
DR PDB; 6CP5; EM; 4.20 A; U=7-101.
DR PDB; 6CP6; EM; 3.60 A; U=7-101.
DR PDB; 6CP7; EM; 4.10 A; U=7-101.
DR PDB; 6WTD; EM; 4.20 A; U=7-101.
DR PDBsum; 6B2Z; -.
DR PDBsum; 6B8H; -.
DR PDBsum; 6CP3; -.
DR PDBsum; 6CP5; -.
DR PDBsum; 6CP6; -.
DR PDBsum; 6CP7; -.
DR PDBsum; 6WTD; -.
DR AlphaFoldDB; Q06405; -.
DR SMR; Q06405; -.
DR BioGRID; 32436; 59.
DR ComplexPortal; CPX-3281; Mitochondrial proton-transporting ATP synthase complex.
DR DIP; DIP-3033N; -.
DR IntAct; Q06405; 4.
DR STRING; 4932.YDR377W; -.
DR MaxQB; Q06405; -.
DR PaxDb; Q06405; -.
DR PRIDE; Q06405; -.
DR EnsemblFungi; YDR377W_mRNA; YDR377W; YDR377W.
DR GeneID; 851983; -.
DR KEGG; sce:YDR377W; -.
DR SGD; S000002785; ATP17.
DR VEuPathDB; FungiDB:YDR377W; -.
DR eggNOG; ENOG502S739; Eukaryota.
DR HOGENOM; CLU_152700_1_0_1; -.
DR InParanoid; Q06405; -.
DR OMA; TIDYQMH; -.
DR BioCyc; YEAST:G3O-29926-MON; -.
DR PRO; PR:Q06405; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06405; 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:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IMP:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IDA:SGD.
DR InterPro; IPR019727; ATP_synth_F0_fsu_mt_fun.
DR PANTHER; PTHR28161; PTHR28161; 1.
DR Pfam; PF10791; F1F0-ATPsyn_F; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; CF(0); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transport.
FT TRANSIT 1..6
FT /note="Mitochondrion"
FT CHAIN 7..101
FT /note="ATP synthase subunit f, mitochondrial"
FT /id="PRO_0000002637"
SQ SEQUENCE 101 AA; 11312 MW; 3DEF593AE4435551 CRC64;
MIFKRAVSTL IPPKVVSSKN IGSAPNAKRI ANVVHFYKSL PQGPAPAIKA NTRLARYKAK
YFDGDNASGK PLWHFALGII AFGYSMEYYF HLRHHKGAEE H
