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ATP19_YEAST
ID   ATP19_YEAST             Reviewed;          68 AA.
AC   P81451; D6W1Z0;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=ATP synthase subunit K, mitochondrial;
GN   Name=ATP19; OrderedLocusNames=YOL077W-A; ORFNames=YOL078BW;
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=9178509;
RX   DOI=10.1002/(sici)1097-0061(199705)13:6<583::aid-yea111>3.0.co;2-y;
RA   Tzermia M., Katsoulou C., Alexandraki D.;
RT   "Sequence analysis of a 33.2 kb segment from the left arm of yeast
RT   chromosome XV reveals eight known genes and ten new open reading frames
RT   including homologues of ABC transporters, inositol phosphatases and human
RT   expressed sequence tags.";
RL   Yeast 13:583-589(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(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   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   [5]
RP   IDENTIFICATION, AND PROTEIN SEQUENCE OF 1-14.
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=9857174; DOI=10.1093/emboj/17.24.7170;
RA   Arnold I., Pfeiffer K., Neupert W., Stuart R.A., Schaegger H.;
RT   "Yeast mitochondrial F1F0-ATPase exists as a dimer: identification of three
RT   dimer-specific subunits.";
RL   EMBO J. 17:7170-7178(1998).
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 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. The
CC       K chain binds the dimeric form by interacting with the G and E chains.
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 inner membrane; Single-pass
CC       membrane protein.
CC   -!- MISCELLANEOUS: Present with 1320 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ATP19 family. {ECO:0000305}.
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DR   EMBL; Z74820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY692842; AAT92861.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10706.1; -; Genomic_DNA.
DR   PIR; S78739; S78739.
DR   RefSeq; NP_014564.1; NM_001184377.1.
DR   PDB; 6B2Z; EM; 3.60 A; T/k=1-68.
DR   PDB; 6B8H; EM; 3.60 A; k/x=1-68.
DR   PDBsum; 6B2Z; -.
DR   PDBsum; 6B8H; -.
DR   AlphaFoldDB; P81451; -.
DR   SMR; P81451; -.
DR   BioGRID; 34324; 18.
DR   ComplexPortal; CPX-3281; Mitochondrial proton-transporting ATP synthase complex.
DR   DIP; DIP-7393N; -.
DR   STRING; 4932.YOL077W-A; -.
DR   MaxQB; P81451; -.
DR   PaxDb; P81451; -.
DR   PRIDE; P81451; -.
DR   TopDownProteomics; P81451; -.
DR   EnsemblFungi; YOL077W-A_mRNA; YOL077W-A; YOL077W-A.
DR   GeneID; 854077; -.
DR   KEGG; sce:YOL077W-A; -.
DR   SGD; S000007339; ATP19.
DR   VEuPathDB; FungiDB:YOL077W-A; -.
DR   eggNOG; ENOG502S99W; Eukaryota.
DR   HOGENOM; CLU_172736_1_2_1; -.
DR   InParanoid; P81451; -.
DR   OMA; FQPHQLA; -.
DR   BioCyc; YEAST:G3O-33886-MON; -.
DR   PRO; PR:P81451; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P81451; protein.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0065003; P:protein-containing complex assembly; IMP:SGD.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IDA:ComplexPortal.
DR   InterPro; IPR021278; ATP19.
DR   PANTHER; PTHR28074; PTHR28074; 1.
DR   Pfam; PF11022; ATP19; 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; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..68
FT                   /note="ATP synthase subunit K, mitochondrial"
FT                   /id="PRO_0000071699"
FT   TRANSMEM        15..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   68 AA;  7534 MW;  4FE05C1D93501283 CRC64;
     MGAAYHFMGK AIPPHQLAIG TLGLLGLLVV PNPFKSAKPK TVDIKTDNKD EEKFIENYLK
     KHSEKQDA
 
 
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