ID   REBL1_RAT               Reviewed;         183 AA.
AC   Q7TNZ5;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=GTPase RhebL1;
DE   AltName: Full=Ras homolog enriched in brain-like protein 1;
DE            Short=Rheb-like protein 1;
DE   Flags: Precursor;
GN   Name=Rhebl1;
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].
RC   STRAIN=Sprague-Dawley; TISSUE=Ovary;
RX   PubMed=16328882; DOI=10.1007/s11033-005-0984-x;
RA   Yuan J., Shan Y., Chen X., Tang W., Luo K., Ni J., Wan B., Yu L.;
RT   "Identification and characterization of RHEBL1, a novel member of Ras
RT   family, which activates transcriptional activities of NF-kappa B.";
RL   Mol. Biol. Rep. 32:205-214(2005).
CC   -!- FUNCTION: Binds GTP and exhibits intrinsic GTPase activity. May
CC       activate NF-kappa-B-mediated gene transcription. Promotes signal
CC       transduction through MTOR, activates RPS6KB1, and is a downstream
CC       target of the small GTPase-activating proteins TSC1 and TSC2 (By
CC       similarity). {ECO:0000250|UniProtKB:Q8TAI7}.
CC   -!- SUBUNIT: Interacts with MTOR. {ECO:0000250|UniProtKB:Q8TAI7}.
CC   -!- SUBCELLULAR LOCATION: Endomembrane system
CC       {ECO:0000250|UniProtKB:Q8TAI7}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:Q8TAI7}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q8TAI7}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q8TAI7}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rheb family.
CC       {ECO:0000305}.
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DR   EMBL; AY327411; AAP92803.1; -; mRNA.
DR   RefSeq; NP_877977.1; NM_182825.1.
DR   AlphaFoldDB; Q7TNZ5; -.
DR   SMR; Q7TNZ5; -.
DR   STRING; 10116.ENSRNOP00000036452; -.
DR   PhosphoSitePlus; Q7TNZ5; -.
DR   PaxDb; Q7TNZ5; -.
DR   PRIDE; Q7TNZ5; -.
DR   Ensembl; ENSRNOT00000089523; ENSRNOP00000074953; ENSRNOG00000054385.
DR   GeneID; 359959; -.
DR   KEGG; rno:359959; -.
DR   UCSC; RGD:727778; rat.
DR   CTD; 121268; -.
DR   RGD; 727778; Rhebl1.
DR   eggNOG; KOG0395; Eukaryota.
DR   GeneTree; ENSGT00940000161665; -.
DR   HOGENOM; CLU_041217_9_8_1; -.
DR   InParanoid; Q7TNZ5; -.
DR   OMA; HQGHGKT; -.
DR   OrthoDB; 1320427at2759; -.
DR   PhylomeDB; Q7TNZ5; -.
DR   TreeFam; TF314986; -.
DR   PRO; PR:Q7TNZ5; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000054385; Expressed in thymus and 18 other tissues.
DR   Genevisible; Q7TNZ5; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
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; ISO:RGD.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IBA:GO_Central.
DR   GO; GO:0031929; P:TOR signaling; 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   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   2: Evidence at transcript level;
KW   Cytoplasm; GTP-binding; Lipoprotein; Magnesium; Membrane; Metal-binding;
KW   Methylation; Nucleotide-binding; Prenylation; Reference proteome.
FT   CHAIN           1..180
FT                   /note="GTPase RhebL1"
FT                   /id="PRO_0000324296"
FT   PROPEP          181..183
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000324297"
FT   MOTIF           35..43
FT                   /note="Effector region"
FT   BINDING         16..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q15382"
FT   BINDING         32..38
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q15382"
FT   BINDING         38
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q15382"
FT   BINDING         63
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TAI7"
FT   BINDING         119..122
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q15382"
FT   BINDING         149..150
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q15382"
FT   MOD_RES         180
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           180
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   183 AA;  20749 MW;  9C051CABDBA8A6D3 CRC64;
     MPLVRYRKVA ILGYRSVGKT SLAHQFVEGE FLKGYDPTVE NTYSKTVTLG KDEFHLHLVD
     TAGQDKYSIL PYSFIIGVHG YVLVYNVTSL RSFQIVKNLY QKLQEGHGKT RLPVLLVGNK
     ADLSADREVQ AVEGKKLAES WGATFMESSA RDNQLIQDIF IRVIQEIARV ENSYGQDRRC
     CLM