ID   REBL1_BOVIN             Reviewed;         181 AA.
AC   Q7YS69;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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; AY293823; AAP47271.1; -; mRNA.
DR   RefSeq; NP_858054.1; NM_181668.1.
DR   AlphaFoldDB; Q7YS69; -.
DR   SMR; Q7YS69; -.
DR   STRING; 9913.ENSBTAP00000008614; -.
DR   PaxDb; Q7YS69; -.
DR   PRIDE; Q7YS69; -.
DR   GeneID; 353300; -.
DR   KEGG; bta:353300; -.
DR   CTD; 121268; -.
DR   eggNOG; KOG0395; Eukaryota.
DR   InParanoid; Q7YS69; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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   2: Evidence at transcript level;
KW   Cytoplasm; GTP-binding; Lipoprotein; Magnesium; Membrane; Metal-binding;
KW   Methylation; Nucleotide-binding; Prenylation; Reference proteome.
FT   CHAIN           1..178
FT                   /note="GTPase RhebL1"
FT                   /id="PRO_0000324290"
FT   PROPEP          179..181
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000324291"
FT   MOTIF           33..41
FT                   /note="Effector region"
FT   BINDING         30..36
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q15382"
FT   BINDING         36
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q15382"
FT   BINDING         61
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TAI7"
FT   BINDING         117..120
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q15382"
FT   BINDING         147..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q15382"
FT   MOD_RES         178
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           178
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   181 AA;  20333 MW;  0A418DAF8CAFC5C8 CRC64;
     MPLVRLSQLV PLLLKGKTSL AHQFVEGEFL EDYDPTVENT YSKIVTVGKD EFHLHLVDTA
     GQDEYSILPY SFIIGVHGYV LVYSVTSLHS FQVIESLYQK LHEGHGKTRL PVVLVGNKAD
     LSPDREVQAV EGKKLAASWG ATFMESSARN NQLTQGIFTK VIQEIARVEN SYGQERRCHL
     M