RRAGB_MOUSE
ID RRAGB_MOUSE Reviewed; 374 AA.
AC Q6NTA4; B1AVD6;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Ras-related GTP-binding protein B {ECO:0000305};
DE Short=Rag B {ECO:0000250|UniProtKB:Q5VZM2};
DE Short=RagB {ECO:0000250|UniProtKB:Q5VZM2};
DE EC=3.6.5.- {ECO:0000250|UniProtKB:Q5VZM2};
GN Name=Rragb {ECO:0000312|MGI:MGI:3038613};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000312|EMBL:AAH69180.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH69180.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH69180.1};
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).
RN [3]
RP INTERACTION WITH SESN1; SESN2 AND SESN3.
RX PubMed=25259925; DOI=10.1016/j.cell.2014.08.038;
RA Peng M., Yin N., Li M.O.;
RT "Sestrins function as guanine nucleotide dissociation inhibitors for Rag
RT GTPases to control mTORC1 signaling.";
RL Cell 159:122-133(2014).
CC -!- FUNCTION: Guanine nucleotide-binding protein that plays a crucial role
CC in the cellular response to amino acid availability through regulation
CC of the mTORC1 signaling cascade. Forms heterodimeric Rag complexes with
CC RRAGC or RRAGD and cycles between an inactive GDP-bound and an active
CC GTP-bound form. In its active form participates in the relocalization
CC of mTORC1 to the lysosomes and its subsequent activation by the GTPase
CC RHEB. Involved in the RCC1/Ran-GTPase pathway.
CC {ECO:0000250|UniProtKB:Q5VZM2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:Q5VZM2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:Q5VZM2};
CC -!- ACTIVITY REGULATION: The activation of GTP-binding proteins is
CC generally mediated by a guanine exchange factor (GEF), while
CC inactivation through hydrolysis of bound GTP is catalyzed by a GTPase
CC activating protein (GAP). The GATOR1 complex functions as a GAP and
CC stimulates RRAGB GTPase activity to turn it into its inactive GDP-bound
CC form. {ECO:0000250|UniProtKB:Q5VZM2}.
CC -!- SUBUNIT: Interacts with RRAGC and RRAGD; heterodimerization stabilizes
CC RRAG proteins (By similarity). In complex with RRAGC, but not with
CC RRAGA, interacts with RPTOR; this interaction is particularly efficient
CC with GTP-loaded RRAGB and GDP-loaded RRAGC (By similarity). Component
CC of the lysosomal folliculin complex (LFC), composed of FLCN, FNIP1 (or
CC FNIP2), RRAGA/RagA or RRAGB/RagB GDP-bound, RRAGC/RagC or RRAGD/RagD
CC GTP-bound, and Ragulator (By similarity). Interacts with SH3BP4; the
CC interaction with this negative regulator is most probably direct,
CC preferentially occurs with the inactive GDP-bound form of RRAGB, is
CC negatively regulated by amino acids and prevents interaction with RPTOR
CC (By similarity). Interacts with the GATOR1 complex; inactivates RRAGB
CC (By similarity). The Rag heterodimer interacts with SLC38A9; the
CC probable amino acid sensor. Interacts with SESN1, SESN2 and SESN3
CC (PubMed:25259925). {ECO:0000250|UniProtKB:Q5VZM2,
CC ECO:0000250|UniProtKB:Q7L523, ECO:0000269|PubMed:25259925}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5VZM2}.
CC Lysosome {ECO:0000250|UniProtKB:Q5VZM2}.
CC -!- SIMILARITY: Belongs to the GTR/RAG GTP-binding protein family.
CC {ECO:0000305}.
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DR EMBL; AL672293; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069180; AAH69180.1; -; mRNA.
DR EMBL; BC070407; AAH70407.1; -; mRNA.
DR CCDS; CCDS30480.1; -.
DR RefSeq; NP_001004154.1; NM_001004154.2.
DR AlphaFoldDB; Q6NTA4; -.
DR SMR; Q6NTA4; -.
DR BioGRID; 232822; 1.
DR STRING; 10090.ENSMUSP00000039013; -.
DR iPTMnet; Q6NTA4; -.
DR PhosphoSitePlus; Q6NTA4; -.
DR jPOST; Q6NTA4; -.
DR MaxQB; Q6NTA4; -.
DR PaxDb; Q6NTA4; -.
DR PeptideAtlas; Q6NTA4; -.
DR PRIDE; Q6NTA4; -.
DR ProteomicsDB; 299814; -.
DR Antibodypedia; 447; 150 antibodies from 26 providers.
DR DNASU; 245670; -.
DR Ensembl; ENSMUST00000039720; ENSMUSP00000039013; ENSMUSG00000041658.
DR GeneID; 245670; -.
DR KEGG; mmu:245670; -.
DR UCSC; uc012hqx.1; mouse.
DR CTD; 10325; -.
DR MGI; MGI:3038613; Rragb.
DR VEuPathDB; HostDB:ENSMUSG00000041658; -.
DR eggNOG; KOG3886; Eukaryota.
DR GeneTree; ENSGT00950000183031; -.
DR HOGENOM; CLU_044099_1_1_1; -.
DR InParanoid; Q6NTA4; -.
DR OMA; LEIACHT; -.
DR OrthoDB; 951213at2759; -.
DR PhylomeDB; Q6NTA4; -.
DR TreeFam; TF300616; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR Reactome; R-MMU-165159; MTOR signalling.
DR Reactome; R-MMU-166208; mTORC1-mediated signalling.
DR Reactome; R-MMU-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-MMU-9639288; Amino acids regulate mTORC1.
DR BioGRID-ORCS; 245670; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Rragb; mouse.
DR PRO; PR:Q6NTA4; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q6NTA4; protein.
DR Bgee; ENSMUSG00000041658; Expressed in hypothalamus and 59 other tissues.
DR ExpressionAtlas; Q6NTA4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:1990131; C:Gtr1-Gtr2 GTPase complex; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0051020; F:GTPase binding; ISO:MGI.
DR GO; GO:0032561; F:guanyl ribonucleotide binding; ISS:UniProtKB.
DR GO; GO:0034198; P:cellular response to amino acid starvation; ISO:MGI.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:1990253; P:cellular response to leucine starvation; ISO:MGI.
DR GO; GO:0009267; P:cellular response to starvation; IBA:GO_Central.
DR GO; GO:0032008; P:positive regulation of TOR signaling; ISS:UniProtKB.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; ISO:MGI.
DR GO; GO:0008104; P:protein localization; ISS:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; IBA:GO_Central.
DR GO; GO:0032006; P:regulation of TOR signaling; ISO:MGI.
DR CDD; cd11384; RagA_like; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006762; Gtr1_RagA.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039397; RagA/B.
DR PANTHER; PTHR11259; PTHR11259; 1.
DR Pfam; PF04670; Gtr1_RagA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; GTP-binding; Hydrolase; Isopeptide bond; Lysosome;
KW Nucleotide-binding; Reference proteome; Ubl conjugation.
FT CHAIN 1..374
FT /note="Ras-related GTP-binding protein B"
FT /id="PRO_0000239949"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 47..54
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q00582"
FT BINDING 123..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q00582"
FT BINDING 188..191
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q00582"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZM2"
FT CROSSLNK 203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q7L523"
FT CROSSLNK 281
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q7L523"
FT CROSSLNK 291
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q7L523"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q7L523"
SQ SEQUENCE 374 AA; 43191 MW; 4F1F13AF06DDA16B CRC64;
MEESDSEKKT EKENVGPKVE PPLGEPEGSL GWAMPNAAMK KKVLLMGKSG SGKTSMRSII
FANYIARDTR RLGATILDRI HSLQINSSLS TYSLVDSVGN TKTFDVEHSH VRFLGNLVLN
LWDCGGQDTF MENYFTSQRD NIFRNVEVLI YVFDVESREL EKDMHYYQSC LEAILQNSPE
AKIFCLVHKM DLVQEDQRDL IFKEREEDLR RLSRPLECSC FRTSIWDETL YKAWSSIVYQ
LIPNVQQLEM NLRNFAEIIE ADEVLLFERA TFLVISHYQC KEQRDAHRFE KISNIIKQFK
LSCSKLAASF QSMEVRNSNF AAFIDIFTSN TYVMVVMSDP SIPSAATLIN IRNARKHFEK
LERVDGPKQC LLMR
