RHEB_BOVIN
ID RHEB_BOVIN Reviewed; 184 AA.
AC Q56JV3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=GTP-binding protein Rheb;
DE AltName: Full=Ras homolog enriched in brain;
DE Flags: Precursor;
GN Name=RHEB;
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 [LARGE SCALE MRNA].
RC TISSUE=Lymphoid epithelium;
RA Yu J., Meng Y., Wang Z., Hansen C., Li C., Moore S.S.;
RT "Analysis of sequences obtained from constructed full-length bovine cDNA
RT libraries.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Activates the protein kinase activity of mTORC1, and thereby
CC plays a role in the regulation of apoptosis. Stimulates the
CC phosphorylation of S6K1 and EIF4EBP1 through activation of mTORC1
CC signaling. Has low intrinsic GTPase activity (By similarity).
CC {ECO:0000250|UniProtKB:Q15382}.
CC -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP
CC and an active form bound to GTP. Inactivated by TSC1-TSC2 via the
CC GTPase activating protein (GAP) domain of TSC2 (By similarity).
CC {ECO:0000250|UniProtKB:Q15382}.
CC -!- SUBUNIT: Binds to mTORC1 in a guanyl nucleotide-independent manner.
CC Interacts directly with MTOR, MLST8 and RPTOR. Interacts with TSC2 (By
CC similarity). Interacts (when prenylated) with PDE6D; this promotes
CC release from membranes (By similarity). {ECO:0000250|UniProtKB:Q15382}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000250|UniProtKB:Q15382}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q15382}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q15382}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q15382}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q15382}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q15382}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q15382}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q15382}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q15382}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q15382}.
CC -!- PTM: Farnesylation is important for efficiently activating mTORC1-
CC mediated signaling. {ECO:0000250|UniProtKB:Q62639}.
CC -!- PTM: Phosphorylation by MAPKAPK5 impairs GTP-binding and inactivation.
CC {ECO:0000250|UniProtKB:Q921J2}.
CC -!- MISCELLANEOUS: The conserved catalytic Gln-64 found in other Ras-like
CC GTPases seems not to be involved in GTP hydrolysis in RHEB.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rheb family.
CC {ECO:0000305}.
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DR EMBL; AY911379; AAW82142.1; -; mRNA.
DR RefSeq; NP_001026934.1; NM_001031764.2.
DR AlphaFoldDB; Q56JV3; -.
DR BMRB; Q56JV3; -.
DR SMR; Q56JV3; -.
DR STRING; 9913.ENSBTAP00000050644; -.
DR PaxDb; Q56JV3; -.
DR PRIDE; Q56JV3; -.
DR GeneID; 528204; -.
DR KEGG; bta:528204; -.
DR CTD; 6009; -.
DR eggNOG; KOG0395; Eukaryota.
DR InParanoid; Q56JV3; -.
DR OrthoDB; 1320427at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032008; P:positive regulation of TOR signaling; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR037586; RHEB.
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 PANTHER; PTHR24070:SF264; PTHR24070:SF264; 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; Endoplasmic reticulum; Golgi apparatus; GTP-binding;
KW Lipoprotein; Magnesium; Membrane; Metal-binding; Methylation;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Reference proteome.
FT CHAIN 1..181
FT /note="GTP-binding protein Rheb"
FT /id="PRO_0000240343"
FT PROPEP 182..184
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281364"
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 20
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 130
FT /note="Phosphoserine; by MAPKAPK5"
FT /evidence="ECO:0000250|UniProtKB:Q921J2"
FT MOD_RES 181
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 181
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q15382"
SQ SEQUENCE 184 AA; 20479 MW; 65ACC4801DF927E9 CRC64;
MPQSKSRKIA ILGYRSVGKS SLTIQFVEGQ FVDSYDPTIK NTFTKLITVN GQEYHLQLVD
TAGQDEYSIF PQTYSIDING YILVYSVTSI KSFEVIKVIH GKLLDMVGKV QIPIMLVGNK
KDLHMERVIS YEEGKALAES WNAAFLESSA KENQTAVDVF RRIILEAEKI DGAASQGKSS
CSVM
