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RHEB_YEAST
ID   RHEB_YEAST              Reviewed;         209 AA.
AC   P25378; D6VR37; Q8NKJ6;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2003, sequence version 2.
DT   03-AUG-2022, entry version 189.
DE   RecName: Full=Rheb-like protein RHB1;
DE   AltName: Full=GTP-binding protein RSG1;
DE   Flags: Precursor;
GN   Name=RHB1; Synonyms=RSG1; OrderedLocusNames=YCR027C; ORFNames=YCR27C;
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=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
RN   [2]
RP   SEQUENCE REVISION TO 92.
RA   Valles G., Volckaerts G.;
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
RX   PubMed=2989539; DOI=10.1016/0022-2836(85)90278-5;
RA   Pure G.A., Robinson G.W., Naumovski L., Friedberg E.C.;
RT   "Partial suppression of an ochre mutation in Saccharomyces cerevisiae by
RT   multicopy plasmids containing a normal yeast tRNAGln gene.";
RL   J. Mol. Biol. 183:31-42(1985).
RN   [6]
RP   CHARACTERIZATION, ISOPRENYLATION AT CYS-206, AND MUTAGENESIS.
RX   PubMed=10753927; DOI=10.1074/jbc.275.15.11198;
RA   Urano J., Tabancay A.P., Yang W., Tamanoi F.;
RT   "The Saccharomyces cerevisiae Rheb G-protein is involved in regulating
RT   canavanine resistance and arginine uptake.";
RL   J. Biol. Chem. 275:11198-11206(2000).
RN   [7]
RP   INTERACTION WITH BTN2, AND SUBCELLULAR LOCATION.
RX   PubMed=12456008; DOI=10.1128/ec.1.4.606-612.2002;
RA   Chattopadhyay S., Pearce D.A.;
RT   "Interaction with Btn2p is required for localization of Rsglp: Btn2p-
RT   mediated changes in arginine uptake in Saccharomyces cerevisiae.";
RL   Eukaryot. Cell 1:606-612(2002).
RN   [8]
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   [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: Involved in the regulation of arginine and lysine uptake.
CC       Acts through the CAN1 permease.
CC   -!- SUBUNIT: Interacts with BTN2. {ECO:0000269|PubMed:12456008}.
CC   -!- INTERACTION:
CC       P25378; P53286: BTN2; NbExp=2; IntAct=EBI-15113, EBI-3796;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12456008};
CC       Peripheral membrane protein {ECO:0000269|PubMed:12456008}. Note=Cell
CC       periphery, adjacent to the plasma membrane.
CC   -!- MISCELLANEOUS: Present with 1600 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rheb family.
CC       {ECO:0000305}.
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DR   EMBL; X59720; CAC42979.1; -; Genomic_DNA.
DR   EMBL; AY693092; AAT93111.1; -; Genomic_DNA.
DR   EMBL; X02445; CAA26291.1; -; Genomic_DNA.
DR   EMBL; BK006937; DAA07506.1; -; Genomic_DNA.
DR   PIR; S19438; S19438.
DR   RefSeq; NP_009956.2; NM_001178742.1.
DR   AlphaFoldDB; P25378; -.
DR   SMR; P25378; -.
DR   BioGRID; 31009; 68.
DR   DIP; DIP-1597N; -.
DR   IntAct; P25378; 4.
DR   MINT; P25378; -.
DR   STRING; 4932.YCR027C; -.
DR   iPTMnet; P25378; -.
DR   MaxQB; P25378; -.
DR   PaxDb; P25378; -.
DR   PRIDE; P25378; -.
DR   EnsemblFungi; YCR027C_mRNA; YCR027C; YCR027C.
DR   GeneID; 850392; -.
DR   KEGG; sce:YCR027C; -.
DR   SGD; S000000622; RHB1.
DR   VEuPathDB; FungiDB:YCR027C; -.
DR   eggNOG; KOG0395; Eukaryota.
DR   GeneTree; ENSGT00940000165909; -.
DR   HOGENOM; CLU_041217_9_8_1; -.
DR   InParanoid; P25378; -.
DR   OMA; SARHNEN; -.
DR   BioCyc; YEAST:G3O-29342-MON; -.
DR   Reactome; R-SCE-165159; MTOR signalling.
DR   Reactome; R-SCE-9639288; Amino acids regulate mTORC1.
DR   PRO; PR:P25378; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P25378; protein.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; ISS:SGD.
DR   GO; GO:1903826; P:L-arginine transmembrane transport; IMP:SGD.
DR   GO; GO:0015819; P:lysine transport; IMP:SGD.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:SGD.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR020849; Small_GTPase_Ras-type.
DR   PANTHER; PTHR24070; PTHR24070; 1.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; GTP-binding; Lipoprotein; Membrane;
KW   Methylation; Nucleotide-binding; Prenylation; Reference proteome.
FT   CHAIN           1..206
FT                   /note="Rheb-like protein RHB1"
FT                   /id="PRO_0000082713"
FT   PROPEP          207..209
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000281370"
FT   MOTIF           45..53
FT                   /note="Effector region"
FT   BINDING         23..30
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         70..74
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         129..132
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         206
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000305"
FT   LIPID           206
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:10753927"
SQ   SEQUENCE   209 AA;  23338 MW;  39F40E70342D7AD5 CRC64;
     MEYATMSSSN STHNFQRKIA LIGARNVGKT TLTVRFVESR FVESYYPTIE NEFTRIIPYK
     SHDCTLEILD TAGQDEVSLL NIKSLTGVRG IILCYSIINR ASFDLIPILW DKLVDQLGKD
     NLPVILVGTK ADLGRSTKGV KRCVTKAEGE KLASTIGSQD KRNQAAFIEC SAELDYNVEE
     TFMLLLKQME RVEGTLGLDA ENNNKCSIM
 
 
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