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RHES_RAT
ID   RHES_RAT                Reviewed;         266 AA.
AC   P63033; Q9WVD3;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=GTP-binding protein Rhes;
DE   AltName: Full=Ras homolog enriched in striatum;
DE   AltName: Full=SE6C;
DE   Flags: Precursor;
GN   Name=Rasd2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND GTP-BINDING.
RC   STRAIN=Sprague-Dawley; TISSUE=Corpus striatum;
RX   PubMed=10467249;
RX   DOI=10.1002/(sici)1097-4547(19990915)57:6<782::aid-jnr3>3.0.co;2-9;
RA   Falk J.D., Vargiu P., Foye P.E., Usui H., Perez J., Danielson P.E.,
RA   Lerner D.L., Bernal J., Sutcliffe J.G.;
RT   "Rhes: a striatal-specific Ras homolog related to Dexras1.";
RL   J. Neurosci. Res. 57:782-788(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=11976265; DOI=10.1038/sj.bjp.0704680;
RA   Chan S.L.F., Monks L.K., Gao H., Deaville P., Morgan N.G.;
RT   "Identification of the monomeric G-protein, Rhes, as an efaroxan-regulated
RT   protein in the pancreatic beta-cell.";
RL   Br. J. Pharmacol. 136:31-36(2002).
RN   [3]
RP   TISSUE SPECIFICITY, AND INDUCTION BY THYROID HORMONE.
RX   PubMed=11597759; DOI=10.1016/s0169-328x(01)00140-1;
RA   Vargiu P., Morte B., Manzano J., Perez J., de Abajo R., Sutcliffe J.G.,
RA   Bernal J.;
RT   "Thyroid hormone regulation of rhes, a novel Ras homolog gene expressed in
RT   the striatum.";
RL   Brain Res. Mol. Brain Res. 94:1-8(2001).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=15199135; DOI=10.1128/mcb.24.13.5788-5796.2004;
RA   Spano D., Branchi I., Rosica A., Pirro M.T., Riccio A., Mithbaokar P.,
RA   Affuso A., Arra C., Campolongo P., Terracciano D., Macchia V., Bernal J.,
RA   Alleva E., Di Lauro R.;
RT   "Rhes is involved in striatal function.";
RL   Mol. Cell. Biol. 24:5788-5796(2004).
RN   [5]
RP   FUNCTION, GTP-BINDING, SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-263,
RP   MUTAGENESIS OF CYS-263, AND INTERACTION WITH PIK3CA.
RX   PubMed=14724584; DOI=10.1038/sj.onc.1207161;
RA   Vargiu P., De Abajo R., Garcia-Ranea J.A., Valencia A., Santisteban P.,
RA   Crespo P., Bernal J.;
RT   "The small GTP-binding protein, Rhes, regulates signal transduction from G
RT   protein-coupled receptors.";
RL   Oncogene 23:559-568(2004).
RN   [6]
RP   TISSUE SPECIFICITY, AND INDUCTION BY EFAROXAN AND GLIBENCLAMIDE.
RX   PubMed=16945334; DOI=10.1016/j.bbrc.2006.08.102;
RA   Taylor J.P., Jackson D.A., Morgan N.G., Chan S.L.;
RT   "Rhes expression in pancreatic beta-cells is regulated by efaroxan in a
RT   calcium-dependent process.";
RL   Biochem. Biophys. Res. Commun. 349:809-815(2006).
RN   [7]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=18929545; DOI=10.1016/j.brainres.2008.09.066;
RA   Harrison L.M., Lahoste G.J., Ruskin D.N.;
RT   "Ontogeny and dopaminergic regulation in brain of Ras homolog enriched in
RT   striatum (Rhes).";
RL   Brain Res. 1245:16-25(2008).
RN   [8]
RP   FUNCTION, INTERACTION WITH UBE2I, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   CYS-263.
RX   PubMed=19498170; DOI=10.1126/science.1172871;
RA   Subramaniam S., Sixt K.M., Barrow R., Snyder S.H.;
RT   "Rhes, a striatal specific protein, mediates mutant-huntingtin
RT   cytotoxicity.";
RL   Science 324:1327-1330(2009).
CC   -!- FUNCTION: GTPase signaling protein that binds to and hydrolyzes GTP.
CC       Regulates signaling pathways involving G-proteins-coupled receptor and
CC       heterotrimeric proteins such as GNB1, GNB2 and GNB3. May be involved in
CC       selected striatal competencies, mainly locomotor activity and motor
CC       coordination. {ECO:0000269|PubMed:10467249,
CC       ECO:0000269|PubMed:11976265, ECO:0000269|PubMed:14724584,
CC       ECO:0000269|PubMed:18929545, ECO:0000269|PubMed:19498170}.
CC   -!- SUBUNIT: Monomer (Potential). Interacts with GNB1, GNB2 and GNB3 (By
CC       similarity). Interacts with PIK3CA and UBE2I. {ECO:0000250,
CC       ECO:0000269|PubMed:14724584, ECO:0000269|PubMed:19498170, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14724584,
CC       ECO:0000269|PubMed:19498170}; Lipid-anchor
CC       {ECO:0000269|PubMed:14724584, ECO:0000269|PubMed:19498170}. Note=Found
CC       in granular structures throughout the cytosol.
CC   -!- TISSUE SPECIFICITY: Prominently expressed in the striatum, weakly in
CC       the cerebral cortex and the CA fields of the hippocampus. Highly
CC       expressed in the hippocampus and cerebellum, only during the postnatal
CC       period. Also expressed in pancreatic endocrine cells (islets of
CC       Langerhans), adrenal gland and stomach and in a thyroid cell line.
CC       {ECO:0000269|PubMed:10467249, ECO:0000269|PubMed:11597759,
CC       ECO:0000269|PubMed:15199135, ECO:0000269|PubMed:16945334,
CC       ECO:0000269|PubMed:18929545}.
CC   -!- DEVELOPMENTAL STAGE: Low levels detected at E16 through P10, and
CC       increased between P10 and P15 during the development of brain; the
CC       amount did decrease in the adult brain.
CC   -!- INDUCTION: By thyroid hormone, efaroxan and glibenclamide.
CC       {ECO:0000269|PubMed:11597759, ECO:0000269|PubMed:16945334}.
CC   -!- PTM: Farnesylated. Farnesylation is required for membrane targeting.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. RasD family.
CC       {ECO:0000305}.
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DR   EMBL; AF134409; AAD38928.1; -; mRNA.
DR   RefSeq; NP_598252.1; NM_133568.1.
DR   AlphaFoldDB; P63033; -.
DR   SMR; P63033; -.
DR   STRING; 10116.ENSRNOP00000020017; -.
DR   PaxDb; P63033; -.
DR   Ensembl; ENSRNOT00000020017; ENSRNOP00000020017; ENSRNOG00000014761.
DR   GeneID; 171099; -.
DR   KEGG; rno:171099; -.
DR   UCSC; RGD:628594; rat.
DR   CTD; 23551; -.
DR   RGD; 628594; Rasd2.
DR   eggNOG; KOG0395; Eukaryota.
DR   GeneTree; ENSGT00940000161129; -.
DR   HOGENOM; CLU_041217_9_3_1; -.
DR   InParanoid; P63033; -.
DR   OMA; EREKCTI; -.
DR   OrthoDB; 1398885at2759; -.
DR   PhylomeDB; P63033; -.
DR   TreeFam; TF316238; -.
DR   PRO; PR:P63033; -.
DR   Proteomes; UP000002494; Chromosome 19.
DR   Bgee; ENSRNOG00000014761; Expressed in frontal cortex and 17 other tissues.
DR   Genevisible; P63033; RN.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0031681; F:G-protein beta-subunit binding; ISO:RGD.
DR   GO; GO:0005525; F:GTP binding; IDA:MGI.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IPI:UniProtKB.
DR   GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI:UniProtKB.
DR   GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:UniProtKB.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
DR   GO; GO:0033235; P:positive regulation of protein sumoylation; IDA:UniProtKB.
DR   GO; GO:0043949; P:regulation of cAMP-mediated signaling; IDA:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0001963; P:synaptic transmission, dopaminergic; ISO:RGD.
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   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   Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation; Reference proteome.
FT   CHAIN           1..263
FT                   /note="GTP-binding protein Rhes"
FT                   /id="PRO_0000082722"
FT   PROPEP          264..266
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000281377"
FT   REGION          189..235
FT                   /note="Interaction with GNB1, GNB2 and GNB3"
FT                   /evidence="ECO:0000250"
FT   MOTIF           48..56
FT                   /note="Effector region"
FT   BINDING         26..33
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         73..77
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         140..143
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         263
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           263
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:14724584"
FT   MUTAGEN         263
FT                   /note="C->A: Loss of plasma membrane localization."
FT                   /evidence="ECO:0000269|PubMed:14724584,
FT                   ECO:0000269|PubMed:19498170"
FT   MUTAGEN         263
FT                   /note="C->S: Rather found in granular structures
FT                   translocated to the nucleus."
FT                   /evidence="ECO:0000269|PubMed:14724584,
FT                   ECO:0000269|PubMed:19498170"
SQ   SEQUENCE   266 AA;  30197 MW;  21B00C11CADD40B0 CRC64;
     MMKTLSSGNC TLNVPAKNSY RMVVLGASRV GKSSIVSRFL NGRFEDQYTP TIEDFHRKVY
     NIHGDMYQLD ILDTSGNHPF PAMRRLSILT GDVFILVFSL DSRESFDEVK RLQKQILEVK
     SCLKNKTKEA AELPMVICGN KNDHSELCRQ VPAMEAELLV SGDENCAYFE VSAKKNTNVN
     EMFYVLFSMA KLPHEMSPAL HHKISVQYGD AFHPRPFCMR RTKVAGAYGM VSPFARRPSV
     NSDLKYIKAK VLREGQARER DKCSIQ
 
 
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