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PLP1_YEAST
ID   PLP1_YEAST              Reviewed;         230 AA.
AC   Q04004; D6VSG7;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=Phosducin-like protein 1;
GN   Name=PLP1; OrderedLocusNames=YDR183W; ORFNames=YD9395.17;
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 [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   [2]
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   [3]
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   [4]
RP   FUNCTION, AND INTERACTION WITH THE STE4-STE18 COMPLEX.
RX   PubMed=10749875; DOI=10.1074/jbc.m002163200;
RA   Flanary P.L., DiBello P.R., Estrada P., Dohlman H.G.;
RT   "Functional analysis of Plp1 and Plp2, two homologues of phosducin in
RT   yeast.";
RL   J. Biol. Chem. 275:18462-18469(2000).
RN   [5]
RP   FUNCTION.
RX   PubMed=14573467; DOI=10.1093/genetics/165.2.531;
RA   Lacefield S., Solomon F.;
RT   "A novel step in beta-tubulin folding is important for heterodimer
RT   formation in Saccharomyces cerevisiae.";
RL   Genetics 165:531-541(2003).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Not essential for growth. Inhibits early G-protein signaling
CC       events following pheromone stimulation. May help create
CC       heterodimerizable beta-tubulin by facilitating the efficient transfer
CC       of nascent beta-tubulin polypeptides to the folding apparatus.
CC       {ECO:0000269|PubMed:10749875, ECO:0000269|PubMed:14573467}.
CC   -!- SUBUNIT: Interacts with the G protein beta-gamma subunit complex (STE4-
CC       STE18 complex). {ECO:0000269|PubMed:10749875}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 2250 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the phosducin family. {ECO:0000305}.
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DR   EMBL; Z46727; CAA86690.1; -; Genomic_DNA.
DR   EMBL; AY558575; AAS56901.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12027.1; -; Genomic_DNA.
DR   PIR; S49780; S49780.
DR   RefSeq; NP_010469.3; NM_001180491.3.
DR   AlphaFoldDB; Q04004; -.
DR   SMR; Q04004; -.
DR   BioGRID; 32237; 110.
DR   DIP; DIP-1793N; -.
DR   IntAct; Q04004; 2.
DR   MINT; Q04004; -.
DR   STRING; 4932.YDR183W; -.
DR   iPTMnet; Q04004; -.
DR   MaxQB; Q04004; -.
DR   PaxDb; Q04004; -.
DR   PRIDE; Q04004; -.
DR   EnsemblFungi; YDR183W_mRNA; YDR183W; YDR183W.
DR   GeneID; 851764; -.
DR   KEGG; sce:YDR183W; -.
DR   SGD; S000002591; PLP1.
DR   VEuPathDB; FungiDB:YDR183W; -.
DR   eggNOG; KOG1672; Eukaryota.
DR   HOGENOM; CLU_072378_0_0_1; -.
DR   InParanoid; Q04004; -.
DR   OMA; QVLPCVI; -.
DR   BioCyc; YEAST:G3O-29772-MON; -.
DR   PRO; PR:Q04004; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q04004; protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IDA:SGD.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0006457; P:protein folding; IGI:SGD.
DR   GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR   InterPro; IPR024253; Phosducin_thioredoxin-like_dom.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF02114; Phosducin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chaperone; Coiled coil; Cytoplasm; Pheromone response;
KW   Reference proteome; Signal transduction inhibitor.
FT   CHAIN           1..230
FT                   /note="Phosducin-like protein 1"
FT                   /id="PRO_0000120172"
FT   REGION          81..230
FT                   /note="Thioredoxin fold"
FT                   /evidence="ECO:0000250"
FT   COILED          25..79
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
SQ   SEQUENCE   230 AA;  26623 MW;  7F2C1BF4F1A471CA CRC64;
     MEDKLDRYYT NVLSNAEKDK HTTVDSDDKS SGEENLDELL NELDRELDED HEFLSAYRSE
     RLQQISDHLK QVKKNVEDDG YGRLQCIDNE ADAIQICTKT TMVVIHFELE TFGKCQYMNE
     KLENLAKRYL TTRFIKVNVQ TCPFLVNKLN IKVLPFVVGY KNGLEKVRYV GFSKLGNDPN
     GFDIRRLEQS LAHSGVIEDT FEIRKHSSVN TERFASTNHD RSESDSDLDI
 
 
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