ATPF_YEAST
ID ATPF_YEAST Reviewed; 244 AA.
AC P05626; D6W3T8; E9P905; Q02830;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=ATP synthase subunit 4, mitochondrial;
DE Flags: Precursor;
GN Name=ATP4; OrderedLocusNames=YPL078C; ORFNames=LPF7C;
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].
RX PubMed=2892678; DOI=10.1111/j.1432-1033.1988.tb13745.x;
RA Velours J., Durrens P., Aigle M., Guerin B.;
RT "ATP4, the structural gene for yeast F0F1 ATPase subunit 4.";
RL Eur. J. Biochem. 170:637-642(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2553130; DOI=10.1016/0300-9084(89)90073-4;
RA Velours J., Arselin G., Paul M.-F., Galante M., Durrens P., Aigle M.,
RA Guerin B.;
RT "The yeast ATP synthase subunit 4: structure and function.";
RL Biochimie 71:903-915(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [4]
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 [5]
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 [6]
RP PROTEIN SEQUENCE OF 36-45.
RX PubMed=2883007; DOI=10.1111/j.1432-1033.1987.tb11166.x;
RA Velours J., Arselin de Chateaubodeau G., Galante M., Guerin B.;
RT "Subunit 4 of ATP synthase (F0F1) from yeast mitochondria. Purification,
RT amino-acid composition and partial N-terminal sequence.";
RL Eur. J. Biochem. 164:579-584(1987).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT phosphorylation in assembly of the ATP synthase.";
RL Mol. Cell. Proteomics 6:1896-1906(2007).
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(0) domain and the peripheric stalk, which acts as a stator to hold
CC the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC relative to the rotary elements.
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 -!- MISCELLANEOUS: Present with 12900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic ATPase B chain family.
CC {ECO:0000305}.
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DR EMBL; X06732; CAA29909.1; -; Genomic_DNA.
DR EMBL; X16721; CAA34703.1; -; Genomic_DNA.
DR EMBL; U41849; AAB68260.1; -; Genomic_DNA.
DR EMBL; AY692976; AAT92995.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11354.1; -; Genomic_DNA.
DR PIR; S61109; PWBYBC.
DR RefSeq; NP_015247.1; NM_001183892.1.
DR PDB; 6B2Z; EM; 3.60 A; N/b=36-244.
DR PDB; 6B8H; EM; 3.60 A; b/q=36-244.
DR PDB; 6CP3; EM; 3.80 A; Z=36-244.
DR PDB; 6CP5; EM; 4.20 A; Z=36-244.
DR PDB; 6CP6; EM; 3.60 A; Z=36-244.
DR PDB; 6CP7; EM; 4.10 A; Z=36-244.
DR PDB; 6WTD; EM; 4.20 A; Z=36-244.
DR PDBsum; 6B2Z; -.
DR PDBsum; 6B8H; -.
DR PDBsum; 6CP3; -.
DR PDBsum; 6CP5; -.
DR PDBsum; 6CP6; -.
DR PDBsum; 6CP7; -.
DR PDBsum; 6WTD; -.
DR AlphaFoldDB; P05626; -.
DR SMR; P05626; -.
DR BioGRID; 36102; 129.
DR ComplexPortal; CPX-3281; Mitochondrial proton-transporting ATP synthase complex.
DR DIP; DIP-3036N; -.
DR IntAct; P05626; 10.
DR MINT; P05626; -.
DR STRING; 4932.YPL078C; -.
DR TCDB; 3.A.2.1.3; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR iPTMnet; P05626; -.
DR MaxQB; P05626; -.
DR PaxDb; P05626; -.
DR PRIDE; P05626; -.
DR EnsemblFungi; YPL078C_mRNA; YPL078C; YPL078C.
DR GeneID; 856027; -.
DR KEGG; sce:YPL078C; -.
DR SGD; S000005999; ATP4.
DR VEuPathDB; FungiDB:YPL078C; -.
DR eggNOG; KOG3976; Eukaryota.
DR GeneTree; ENSGT00390000001958; -.
DR HOGENOM; CLU_077208_0_0_1; -.
DR InParanoid; P05626; -.
DR OMA; IYAISNE; -.
DR BioCyc; YEAST:G3O-33985-MON; -.
DR Reactome; R-SCE-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-SCE-8949613; Cristae formation.
DR PRO; PR:P05626; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P05626; 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); IBA:GO_Central.
DR GO; GO:0000274; C:mitochondrial proton-transporting ATP synthase, stator stalk; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:SGD.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IDA:SGD.
DR InterPro; IPR008688; ATP_synth_Bsub_B/MI25.
DR InterPro; IPR013837; ATP_synth_F0_suB.
DR PANTHER; PTHR12733; PTHR12733; 1.
DR Pfam; PF05405; Mt_ATP-synt_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; CF(0); Direct protein sequencing; Hydrogen ion transport;
KW Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Phosphoprotein; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2883007"
FT CHAIN 36..244
FT /note="ATP synthase subunit 4, mitochondrial"
FT /id="PRO_0000002524"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17761666"
FT CONFLICT 11
FT /note="A -> L (in Ref. 5; AAT92995)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="A -> R (in Ref. 1; CAA29909 and 2; CAA34703)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 244 AA; 26925 MW; BDBE0F6AD6E5392C CRC64;
MSMSMGVRGL ALRSVSKTLF SQGVRCPSMV IGARYMSSTP EKQTDPKAKA NSIINAIPGN
NILTKTGVLG TSAAAVIYAI SNELYVINDE SILLLTFLGF TGLVAKYLAP AYKDFADARM
KKVSDVLNAS RNKHVEAVKD RIDSVSQLQN VAETTKVLFD VSKETVELES EAFELKQKVE
LAHEAKAVLD SWVRYEASLR QLEQRQLAKS VISRVQSELG NPKFQEKVLQ QSISEIEQLL
SKLK
