位置:首页 > 蛋白库 > ROY1_YEAST
ROY1_YEAST
ID   ROY1_YEAST              Reviewed;         553 AA.
AC   Q04847; D6W084;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Non-SCF-type F-box protein ROY1;
DE   AltName: Full=Repressor of YPT52;
GN   Name=ROY1; OrderedLocusNames=YMR258C; ORFNames=YM9920.12C;
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=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(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   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   [5]
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   [6]
RP   FUNCTION, DOMAIN, AND INTERACTION WITH SKP1.
RX   PubMed=19652464; DOI=10.2131/jts.34.413;
RA   Hwang G.W., Wada N., Kuge S., Naganuma A.;
RT   "Overexpression of the novel F-box protein Ymr258c confers resistance to
RT   methylmercury in Saccharomyces cerevisiae.";
RL   J. Toxicol. Sci. 34:413-416(2009).
RN   [7]
RP   INDUCTION.
RX   PubMed=19235764; DOI=10.1002/yea.1655;
RA   Roberts G.G. III, Hudson A.P.;
RT   "Rsf1p is required for an efficient metabolic shift from fermentative to
RT   glycerol-based respiratory growth in S. cerevisiae.";
RL   Yeast 26:95-110(2009).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH SKP1.
RX   PubMed=19882662; DOI=10.1002/pmic.200900497;
RA   Kato M., Kito K., Ota K., Ito T.;
RT   "Remodeling of the SCF complex-mediated ubiquitination system by
RT   compositional alteration of incorporated F-box proteins.";
RL   Proteomics 10:115-123(2010).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SKP1 AND YPT52.
RX   PubMed=21389113; DOI=10.1091/mbc.e10-08-0716;
RA   Liu Y., Nakatsukasa K., Kotera M., Kanada A., Nishimura T., Kishi T.,
RA   Mimura S., Kamura T.;
RT   "Non-SCF-type F-box protein Roy1/Ymr258c interacts with a Rab5-like GTPase
RT   Ypt52 and inhibits Ypt52 function.";
RL   Mol. Biol. Cell 22:1575-1584(2011).
CC   -!- FUNCTION: Non-SCF-type F-box protein involved in the endocytic with the
CC       vacuolar sorting pathway. Acts as a repressor of YPT52 by inhibiting
CC       the formation of active, GTP-bound, YPT52. Involved in the defense
CC       mechanism against methylmercury toxicity. {ECO:0000269|PubMed:19652464,
CC       ECO:0000269|PubMed:21389113}.
CC   -!- SUBUNIT: Interacts with SKP1 and YPT32; SKP1 is required for the
CC       interaction with YPT32. {ECO:0000269|PubMed:19652464,
CC       ECO:0000269|PubMed:19882662, ECO:0000269|PubMed:21389113}.
CC   -!- INTERACTION:
CC       Q04847; P52286: SKP1; NbExp=4; IntAct=EBI-27556, EBI-4090;
CC       Q04847; P36018: YPT52; NbExp=3; IntAct=EBI-27556, EBI-29407;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasmic vesicle membrane;
CC       Peripheral membrane protein.
CC   -!- INDUCTION: Expression is RSF1 and RSF2 dependent.
CC       {ECO:0000269|PubMed:19235764}.
CC   -!- DOMAIN: The F-box domain is required for interaction with SKP1 and
CC       defense against methylmercury toxicity. {ECO:0000269|PubMed:19652464}.
CC   -!- MISCELLANEOUS: Present with 3080 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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; Z48639; CAA88585.1; -; Genomic_DNA.
DR   EMBL; AY692563; AAT92582.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10158.1; -; Genomic_DNA.
DR   PIR; S53080; S53080.
DR   RefSeq; NP_013985.1; NM_001182765.1.
DR   AlphaFoldDB; Q04847; -.
DR   BioGRID; 35436; 57.
DR   DIP; DIP-4403N; -.
DR   IntAct; Q04847; 4.
DR   MINT; Q04847; -.
DR   STRING; 4932.YMR258C; -.
DR   MaxQB; Q04847; -.
DR   PaxDb; Q04847; -.
DR   PRIDE; Q04847; -.
DR   EnsemblFungi; YMR258C_mRNA; YMR258C; YMR258C.
DR   GeneID; 855300; -.
DR   KEGG; sce:YMR258C; -.
DR   SGD; S000004871; ROY1.
DR   VEuPathDB; FungiDB:YMR258C; -.
DR   eggNOG; ENOG502R4NW; Eukaryota.
DR   HOGENOM; CLU_446963_0_0_1; -.
DR   InParanoid; Q04847; -.
DR   OMA; LWNGCEC; -.
DR   BioCyc; YEAST:G3O-32933-MON; -.
DR   PRO; PR:Q04847; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q04847; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0005095; F:GTPase inhibitor activity; IDA:SGD.
DR   GO; GO:0006897; P:endocytosis; IGI:SGD.
DR   GO; GO:0034260; P:negative regulation of GTPase activity; IDA:SGD.
DR   GO; GO:0006623; P:protein targeting to vacuole; IGI:SGD.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoplasmic vesicle; Membrane; Nucleus; Reference proteome.
FT   CHAIN           1..553
FT                   /note="Non-SCF-type F-box protein ROY1"
FT                   /id="PRO_0000203342"
FT   DOMAIN          3..49
FT                   /note="F-box"
SQ   SEQUENCE   553 AA;  64405 MW;  2F764964A6C23EC2 CRC64;
     MAFQDQDIFI VFSHASLFLN QNDLLSLSLT SKKMHDMIAI PRLYSNIHIT KNPVLRTNKW
     FLDGGKTYVS GYRSVLKTGD KNDIFLYDRI ERLLETSHLK CIKQLTIDED LFHNREEGLQ
     LLQRLVNEIT DLDVIESLDI KDPTLFELCS AKYYRLSSLK KRVVYGETGF DGIKLWQNFK
     SLKWQLPESL DLQNVIIPEV GVMLMKQLNG GELEIKDEAY SSLRVFEYFD SLNLRFKNLR
     RLKLNHVHKQ GDGSATSMRL SSRAFKDVVN LSNLKALELE FSCEVDDCEC DDDFLQDITG
     NLVSLTSLGF IEKTFTKKGY HYMDEKWDLV VNKFILNLPN VSKDLRLLSI RHDPPLNGKG
     IDTVDGNLLR RKKLYEKVLP KLTSLETIIA PTVLQSITSY EMYACDLLWN GCKCAFCSKY
     LPLFDKYIMN HQYFSTPDAR YLDIIPIVFA AYTGKSLAKR FDPQKNWDLD LLQYAPEDTT
     WNFHGFERIH HFASYECYFD ESSFEPLATI ISHFFYPYMN YLIKILPNLR QTMLSGIYFS
     VSPELHTYET IYD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025