ATP7_YEAST
ID ATP7_YEAST Reviewed; 174 AA.
AC P30902; D6VXS0;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=ATP synthase subunit d, mitochondrial;
GN Name=ATP7; OrderedLocusNames=YKL016C;
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], CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT SER-2, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1832157; DOI=10.1016/s0021-9258(18)55335-7;
RA Norais N., Prome D., Velours J.;
RT "ATP synthase of yeast mitochondria. Characterization of subunit d and
RT sequence analysis of the structural gene ATP7.";
RL J. Biol. Chem. 266:16541-16549(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8154185; DOI=10.1002/yea.320091208;
RA Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J.,
RA Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.;
RT "Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI
RT from Saccharomyces cerevisiae reveals 23 open reading frames including the
RT FAS1 gene.";
RL Yeast 9:1343-1348(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 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
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 6820 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ATPase d subunit 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; M74048; AAA34445.1; -; Genomic_DNA.
DR EMBL; X74152; CAA52265.1; -; Genomic_DNA.
DR EMBL; Z28016; CAA81851.1; -; Genomic_DNA.
DR EMBL; AY558349; AAS56675.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09140.1; -; Genomic_DNA.
DR PIR; A41168; A41168.
DR RefSeq; NP_012909.3; NM_001179582.3.
DR PDB; 6B2Z; EM; 3.60 A; O/d=2-174.
DR PDB; 6B8H; EM; 3.60 A; d/r=2-174.
DR PDB; 6CP3; EM; 3.80 A; 7=2-174.
DR PDB; 6CP5; EM; 4.20 A; 7=2-174.
DR PDB; 6CP6; EM; 3.60 A; 7=2-174.
DR PDB; 6CP7; EM; 4.10 A; 7=2-174.
DR PDB; 6WTD; EM; 4.20 A; 7=2-174.
DR PDBsum; 6B2Z; -.
DR PDBsum; 6B8H; -.
DR PDBsum; 6CP3; -.
DR PDBsum; 6CP5; -.
DR PDBsum; 6CP6; -.
DR PDBsum; 6CP7; -.
DR PDBsum; 6WTD; -.
DR AlphaFoldDB; P30902; -.
DR SMR; P30902; -.
DR BioGRID; 34116; 262.
DR ComplexPortal; CPX-3281; Mitochondrial proton-transporting ATP synthase complex.
DR DIP; DIP-3039N; -.
DR IntAct; P30902; 12.
DR MINT; P30902; -.
DR STRING; 4932.YKL016C; -.
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; P30902; -.
DR MaxQB; P30902; -.
DR PaxDb; P30902; -.
DR PRIDE; P30902; -.
DR EnsemblFungi; YKL016C_mRNA; YKL016C; YKL016C.
DR GeneID; 853853; -.
DR KEGG; sce:YKL016C; -.
DR SGD; S000001499; ATP7.
DR VEuPathDB; FungiDB:YKL016C; -.
DR eggNOG; KOG3366; Eukaryota.
DR GeneTree; ENSGT00390000003582; -.
DR HOGENOM; CLU_080463_0_0_1; -.
DR InParanoid; P30902; -.
DR OMA; VSKGRWA; -.
DR BioCyc; YEAST:G3O-31825-MON; -.
DR Reactome; R-SCE-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-SCE-8949613; Cristae formation.
DR PRO; PR:P30902; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P30902; 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: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:0015986; P:proton motive force-driven ATP synthesis; IDA:SGD.
DR Gene3D; 6.10.280.70; -; 1.
DR InterPro; IPR008689; ATP_synth_F0_dsu_mt.
DR InterPro; IPR036228; ATP_synth_F0_dsu_sf_mt.
DR PANTHER; PTHR12700; PTHR12700; 1.
DR Pfam; PF05873; Mt_ATP-synt_D; 1.
DR PIRSF; PIRSF005514; ATPase_F0_D_mt; 1.
DR SUPFAM; SSF161065; SSF161065; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP synthesis; CF(0); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1832157"
FT CHAIN 2..174
FT /note="ATP synthase subunit d, mitochondrial"
FT /id="PRO_0000071681"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:1832157"
SQ SEQUENCE 174 AA; 19810 MW; C6420CBEDF1BB45E CRC64;
MSLAKSAANK LDWAKVISSL RITGSTATQL SSFKKRNDEA RRQLLELQSQ PTEVDFSHYR
SVLKNTSVID KIESYVKQYK PVKIDASKQL QVIESFEKHA MTNAKETESL VSKELKDLQS
TLDNIQSARP FDELTVDDLT KIKPEIDAKV EEMVKKGKWD VPGYKDRFGN LNVM
