RHEB1_CAEBR
ID RHEB1_CAEBR Reviewed; 206 AA.
AC A8XAD0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=GTP-binding protein Rheb homolog 1 {ECO:0000250|UniProtKB:P34443};
DE AltName: Full=Ras homolog enriched in brain protein 1 {ECO:0000250|UniProtKB:P34443};
DE Flags: Precursor;
GN Name=rheb-1 {ECO:0000312|EMBL:CAP29598.1}; ORFNames=CBG10088;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP29598.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP29598.1};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Binds GTP and exhibits intrinsic GTPase activity.
CC {ECO:0000250|UniProtKB:Q62639}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor
CC {ECO:0000255}; Cytoplasmic side {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rheb family.
CC {ECO:0000255}.
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DR EMBL; HE601459; CAP29598.1; -; Genomic_DNA.
DR RefSeq; XP_002641749.1; XM_002641703.1.
DR AlphaFoldDB; A8XAD0; -.
DR SMR; A8XAD0; -.
DR STRING; 6238.CBG10088; -.
DR EnsemblMetazoa; CBG10088.1; CBG10088.1; WBGene00031567.
DR GeneID; 8583743; -.
DR KEGG; cbr:CBG_10088; -.
DR CTD; 8583743; -.
DR WormBase; CBG10088; CBP08385; WBGene00031567; Cbr-rheb-1.
DR eggNOG; KOG0395; Eukaryota.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; A8XAD0; -.
DR OMA; SARHNEN; -.
DR OrthoDB; 1320427at2759; -.
DR Proteomes; UP000008549; Chromosome III.
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; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Cell membrane; GTP-binding; Lipoprotein; Magnesium; Membrane;
KW Metal-binding; Methylation; Nucleotide-binding; Prenylation;
KW Reference proteome.
FT CHAIN 1..203
FT /note="GTP-binding protein Rheb homolog 1"
FT /id="PRO_0000370746"
FT PROPEP 204..206
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q15382"
FT /id="PRO_0000370747"
FT REGION 180..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 42..50
FT /note="Effector region"
FT COMPBIAS 181..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 20..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q15382"
FT BINDING 23..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q15382"
FT BINDING 27
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q15382"
FT BINDING 39..45
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q15382"
FT BINDING 45
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q15382"
FT BINDING 70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8TAI7"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q15382"
FT BINDING 156..157
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q15382"
FT MOD_RES 203
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q15382"
FT LIPID 203
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q15382"
SQ SEQUENCE 206 AA; 23434 MW; 27219DDA4C7AB8BA CRC64;
MSSTATQPRY SLNRKVAVMG YPHVGKSSIV QRFTQNMFPD RYETTIEDQH TKHHTAFHRD
FNLRVTDTAG QQEYTVFPRS CSLDVAGFLL VYAIDDRKSF DICSSIYEKI ISVYGDPSIP
IIIVGNKCDL GTQRVVQQEE GKELAKQCEA KFVEITARET NRVNEVFELL LREIEISRGN
LRGPPQQQTK EQTSSDPNDP KNCVIS
