RHEB1_CAEEL
ID RHEB1_CAEEL Reviewed; 207 AA.
AC P34443;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=GTP-binding protein Rheb homolog 1;
DE Flags: Precursor;
GN Name=rheb-1; ORFNames=F54C8.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=17925224; DOI=10.1016/j.devcel.2007.07.016;
RA Haynes C.M., Petrova K., Benedetti C., Yang Y., Ron D.;
RT "ClpP mediates activation of a mitochondrial unfolded protein response in
RT C. elegans.";
RL Dev. Cell 13:467-480(2007).
CC -!- FUNCTION: Binds GTP and exhibits intrinsic GTPase activity.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Inactivation promotes nuclear redistribution of
CC dve-1, induction of ubl-5 and complex formation with dve-1.
CC {ECO:0000269|PubMed:17925224}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rheb family.
CC {ECO:0000305}.
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DR EMBL; Z22178; CAA80155.1; -; Genomic_DNA.
DR PIR; S40747; S40747.
DR RefSeq; NP_499079.1; NM_066678.3.
DR AlphaFoldDB; P34443; -.
DR SMR; P34443; -.
DR BioGRID; 41524; 1.
DR IntAct; P34443; 1.
DR STRING; 6239.F54C8.5; -.
DR iPTMnet; P34443; -.
DR EPD; P34443; -.
DR PaxDb; P34443; -.
DR PeptideAtlas; P34443; -.
DR PRIDE; P34443; -.
DR EnsemblMetazoa; F54C8.5.1; F54C8.5.1; WBGene00010038.
DR GeneID; 176327; -.
DR KEGG; cel:CELE_F54C8.5; -.
DR CTD; 176327; -.
DR WormBase; F54C8.5; CE00191; WBGene00010038; rheb-1.
DR eggNOG; KOG0395; Eukaryota.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; P34443; -.
DR OMA; SARHNEN; -.
DR OrthoDB; 1320427at2759; -.
DR PhylomeDB; P34443; -.
DR Reactome; R-CEL-1632852; Macroautophagy.
DR Reactome; R-CEL-165159; MTOR signalling.
DR Reactome; R-CEL-166208; mTORC1-mediated signalling.
DR Reactome; R-CEL-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-CEL-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-CEL-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-CEL-9639288; Amino acids regulate mTORC1.
DR SignaLink; P34443; -.
DR PRO; PR:P34443; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00010038; Expressed in germ line (C elegans) and 4 other tissues.
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:0032008; P:positive regulation of TOR signaling; ISS:WormBase.
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..204
FT /note="GTP-binding protein Rheb homolog 1"
FT /id="PRO_0000082714"
FT PROPEP 205..207
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281371"
FT REGION 180..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 42..50
FT /note="Effector region"
FT BINDING 20..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
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 204
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 204
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 207 AA; 23696 MW; 720031575DE8E15F CRC64;
MSSSLQSNRQ SLNRKVAVMG YPHVGKSALV LRFTQNIFPE RYESTIEDQH SKHIAAFHRD
YHLRVTDTAG QQEYTVFPRS CSLDINGFIL VYAIDDRKSF EMCSNIYEKI VRTYGDTSIP
IVIVGNKTDL STQRVVRAEE GEELARQWDA KFVEITARES NRVHEVFELL LREIEISRGN
LSPTERPNGN SPKRNPFKDD GKPCSIS
