REBL1_MOUSE
ID REBL1_MOUSE Reviewed; 184 AA.
AC Q9D8T3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 161.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; AY327413; AAP92805.1; -; mRNA.
DR EMBL; AK007708; BAB25203.1; -; mRNA.
DR EMBL; AK135858; BAE22699.1; -; mRNA.
DR EMBL; BC016521; AAH16521.1; -; mRNA.
DR CCDS; CCDS27809.1; -.
DR RefSeq; NP_081243.1; NM_026967.4.
DR AlphaFoldDB; Q9D8T3; -.
DR SMR; Q9D8T3; -.
DR BioGRID; 213261; 5.
DR MINT; Q9D8T3; -.
DR STRING; 10090.ENSMUSP00000024518; -.
DR iPTMnet; Q9D8T3; -.
DR PhosphoSitePlus; Q9D8T3; -.
DR jPOST; Q9D8T3; -.
DR MaxQB; Q9D8T3; -.
DR PaxDb; Q9D8T3; -.
DR PRIDE; Q9D8T3; -.
DR ProteomicsDB; 254909; -.
DR Antibodypedia; 25823; 142 antibodies from 23 providers.
DR DNASU; 69159; -.
DR Ensembl; ENSMUST00000024518; ENSMUSP00000024518; ENSMUSG00000023755.
DR GeneID; 69159; -.
DR KEGG; mmu:69159; -.
DR UCSC; uc011zzb.1; mouse.
DR CTD; 121268; -.
DR MGI; MGI:1916409; Rhebl1.
DR VEuPathDB; HostDB:ENSMUSG00000023755; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000161665; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; Q9D8T3; -.
DR OMA; HQGHGKT; -.
DR OrthoDB; 1320427at2759; -.
DR PhylomeDB; Q9D8T3; -.
DR TreeFam; TF314986; -.
DR BioGRID-ORCS; 69159; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Rhebl1; mouse.
DR PRO; PR:Q9D8T3; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9D8T3; protein.
DR Bgee; ENSMUSG00000023755; Expressed in cleaving embryo and 220 other tissues.
DR ExpressionAtlas; Q9D8T3; baseline and differential.
DR Genevisible; Q9D8T3; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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:MGI.
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:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IBA:GO_Central.
DR GO; GO:0031929; P:TOR signaling; ISO:MGI.
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..181
FT /note="GTPase RhebL1"
FT /id="PRO_0000324294"
FT PROPEP 182..184
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000324295"
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 181
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 181
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 184 AA; 20934 MW; 8F6A6849A533A0DE CRC64;
MPLVRYRKVA ILGYRSVGKT SLAHQFVEGE FLEGYDPTVE NTYSKTVTLG KDEFHLHLVD
TAGQDEYSIL PYSLIIGVHG YVLVYSVNSL RSFQIVKNLY QKLHEGHGKT RLSVLLVGNK
ADLSPEREVQ AVEGKKLAES WGAMFMESSA RDNQLTQDVF IKVIQEIARV ENSYGRQDRR
CYLM
