RRAGB_RAT
ID RRAGB_RAT Reviewed; 374 AA.
AC Q63487; Q6AZ37;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Ras-related GTP-binding protein B;
DE Short=Rag B {ECO:0000250|UniProtKB:Q5VZM2};
DE Short=RagB {ECO:0000303|PubMed:7499430};
DE EC=3.6.5.- {ECO:0000250|UniProtKB:Q5VZM2};
GN Name=RragB {ECO:0000312|RGD:619805};
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] {ECO:0000305, ECO:0000312|EMBL:CAA59467.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, AND GTP-BINDING.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:CAA59467.1};
RC TISSUE=Brain {ECO:0000312|EMBL:CAA59467.1};
RX PubMed=7499430; DOI=10.1074/jbc.270.48.28982;
RA Schuermann A., Brauers A., Massmann S., Becker W., Joost H.-G.;
RT "Cloning of a novel family of mammalian GTP-binding proteins (RagA, RagBs,
RT RagBl) with remote similarity to the Ras-related GTPases.";
RL J. Biol. Chem. 270:28982-28988(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Lung;
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: 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. In complex with RRAGC, but not with RRAGA, interacts
CC with RPTOR; this interaction is particularly efficient with GTP-loaded
CC RRAGB and GDP-loaded RRAGC (By similarity). Component of the lysosomal
CC folliculin complex (LFC), composed of FLCN, FNIP1 (or FNIP2),
CC RRAGA/RagA or RRAGB/RagB GDP-bound, RRAGC/RagC or RRAGD/RagD GTP-bound,
CC and Ragulator (By similarity). Interacts with SH3BP4; the interaction
CC with this negative regulator is most probably direct, preferentially
CC occurs with the inactive GDP-bound form of RRAGB, is negatively
CC regulated by amino acids and prevents interaction with RPTOR. Interacts
CC with the GATOR1 complex; inactivates RRAGB. The Rag heterodimer
CC interacts with SLC38A9; the probable amino acid sensor. Interacts with
CC SESN1, SESN2 and SESN3 (By similarity). {ECO:0000250|UniProtKB:Q5VZM2,
CC ECO:0000250|UniProtKB:Q7L523}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5VZM2}.
CC Lysosome {ECO:0000250|UniProtKB:Q5VZM2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000303|PubMed:7499430}; Synonyms=Long
CC {ECO:0000303|PubMed:7499430};
CC IsoId=Q63487-1; Sequence=Displayed;
CC Name=2 {ECO:0000303|PubMed:7499430}; Synonyms=Short
CC {ECO:0000303|PubMed:7499430};
CC IsoId=Q63487-2; Sequence=VSP_052074;
CC -!- TISSUE SPECIFICITY: 2 transcripts of 2.5 kb and 3.8 kb are expressed at
CC low levels in brain, testis, adrenal gland and thymus.
CC {ECO:0000269|PubMed:7499430}.
CC -!- SIMILARITY: Belongs to the GTR/RAG GTP-binding protein family.
CC {ECO:0000305}.
CC -!- CAUTION: According to a report, has no detectable intrinsic GTPase
CC activity. {ECO:0000269|PubMed:7499430}.
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DR EMBL; X85184; CAA59467.1; -; mRNA.
DR EMBL; BC078760; AAH78760.1; -; mRNA.
DR EMBL; BC087698; AAH87698.1; -; mRNA.
DR RefSeq; NP_446424.1; NM_053972.2. [Q63487-1]
DR RefSeq; XP_006256837.1; XM_006256775.3. [Q63487-2]
DR RefSeq; XP_006256841.1; XM_006256779.3. [Q63487-2]
DR RefSeq; XP_017457764.1; XM_017602275.1. [Q63487-1]
DR AlphaFoldDB; Q63487; -.
DR SMR; Q63487; -.
DR STRING; 10116.ENSRNOP00000004235; -.
DR PaxDb; Q63487; -.
DR Ensembl; ENSRNOT00000004235; ENSRNOP00000004235; ENSRNOG00000062421. [Q63487-1]
DR GeneID; 117043; -.
DR KEGG; rno:117043; -.
DR UCSC; RGD:619805; rat. [Q63487-1]
DR CTD; 10325; -.
DR RGD; 619805; RragB.
DR eggNOG; KOG3886; Eukaryota.
DR GeneTree; ENSGT00950000183031; -.
DR HOGENOM; CLU_044099_1_1_1; -.
DR InParanoid; Q63487; -.
DR OMA; LEIACHT; -.
DR OrthoDB; 951213at2759; -.
DR PhylomeDB; Q63487; -.
DR TreeFam; TF300616; -.
DR Reactome; R-RNO-1632852; Macroautophagy.
DR Reactome; R-RNO-165159; MTOR signalling.
DR Reactome; R-RNO-166208; mTORC1-mediated signalling.
DR Reactome; R-RNO-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-RNO-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-RNO-9639288; Amino acids regulate mTORC1.
DR PRO; PR:Q63487; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000003160; Expressed in cerebellum and 15 other tissues.
DR Genevisible; Q63487; RN.
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; IDA:RGD.
DR GO; GO:0003924; F:GTPase activity; ISO:RGD.
DR GO; GO:0051020; F:GTPase binding; ISO:RGD.
DR GO; GO:0032561; F:guanyl ribonucleotide binding; ISS:UniProtKB.
DR GO; GO:0034198; P:cellular response to amino acid starvation; ISO:RGD.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:1990253; P:cellular response to leucine starvation; ISO:RGD.
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:RGD.
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:RGD.
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; Alternative splicing; Cytoplasm; GTP-binding; Hydrolase;
KW Isopeptide bond; Lysosome; Nucleotide-binding; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..374
FT /note="Ras-related GTP-binding protein B"
FT /id="PRO_0000239950"
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"
FT VAR_SEQ 77..104
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7499430"
FT /id="VSP_052074"
FT CONFLICT 262
FT /note="D -> V (in Ref. 2; AAH78760)"
FT /evidence="ECO:0000305"
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
