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Ras-related GTP-binding protein B (Rag B) (RagB)

 RRAGB_RAT               Reviewed;         374 AA.
Q63487; Q6AZ37;
13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 112.
RecName: Full=Ras-related GTP-binding protein B;
Short=Rag B {ECO:0000250|UniProtKB:Q5VZM2};
Short=RagB {ECO:0000303|PubMed:7499430};
Name=RragB {ECO:0000312|RGD:619805};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1] {ECO:0000305, ECO:0000312|EMBL:CAA59467.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING,
TISSUE SPECIFICITY, AND GTP-BINDING.
STRAIN=Sprague-Dawley {ECO:0000312|EMBL:CAA59467.1};
TISSUE=Brain {ECO:0000312|EMBL:CAA59467.1};
PubMed=7499430; DOI=10.1074/jbc.270.48.28982;
Schuermann A., Brauers A., Massmann S., Becker W., Joost H.-G.;
"Cloning of a novel family of mammalian GTP-binding proteins (RagA,
RagBs, RagBl) with remote similarity to the Ras-related GTPases.";
J. Biol. Chem. 270:28982-28988(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Guanine nucleotide-binding protein that plays a crucial
role in the cellular response to amino acid availability through
regulation of the mTORC1 signaling cascade. Forms heterodimeric
Rag complexes with RRAGC or RRAGD and cycle between an inactive
GDP-bound and an active GTP-bound form. In its active form
participates in the relocalization of mTORC1 to the lysosomes and
its subsequent activation by the GTPase RHEB. Involved in the
RCC1/Ran-GTPase pathway. {ECO:0000250|UniProtKB:Q5VZM2,
ECO:0000269|PubMed:7499430}.
-!- ENZYME REGULATION: The activation of GTP-binding proteins is
generally mediated by a guanine exchange factor (GEF), while
inactivation through hydrolysis of bound GTP is catalyzed by a
GTPase activating protein (GAP). The GATOR1 complex functions as a
GAP and stimulates RRAGB GTPase activity to turn it into its
inactive GDP-bound form. {ECO:0000250|UniProtKB:Q5VZM2}.
-!- SUBUNIT: Interacts with RRAGC and RRAGD; heterodimerization
stabilizes RRAG proteins. In complex with RRAGC, but not with
RRAGA, interacts with RPTOR; this interaction is particularly
efficient with GTP-loaded RRAGB and GDP-loaded RRAGC. Interacts
with SH3BP4; the interaction with this negative regulator is most
probably direct, preferentially occurs with the inactive GDP-bound
form of RRAGB, is negatively regulated by amino acids and prevents
interaction with RPTOR. Interacts with the GATOR1 complex;
inactivates RRAGB. The Rag heterodimer interacts with SLC38A9; the
probable amino acid sensor. Interacts with SESN1, SESN2 AND SESN3.
{ECO:0000250|UniProtKB:Q5VZM2}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5VZM2}.
Lysosome {ECO:0000250|UniProtKB:Q5VZM2}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000269|PubMed:7499430}; Synonyms=Long
{ECO:0000269|PubMed:7499430};
IsoId=Q63487-1; Sequence=Displayed;
Note=According to PubMed:7499430 may not bind GTP.;
Name=2 {ECO:0000269|PubMed:7499430}; Synonyms=Short
{ECO:0000269|PubMed:7499430};
IsoId=Q63487-2; Sequence=VSP_052074;
-!- TISSUE SPECIFICITY: 2 transcripts of 2.5 kb and 3.8 kb are
expressed at low levels in brain, testis, adrenal gland and
thymus. {ECO:0000269|PubMed:7499430}.
-!- SIMILARITY: Belongs to the GTR/RAG GTP-binding protein family.
{ECO:0000305}.
-!- CAUTION: Has no detectable intrinsic GTPase activity according to
PubMed:7499430. {ECO:0000305}.
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EMBL; X85184; CAA59467.1; -; mRNA.
EMBL; BC078760; AAH78760.1; -; mRNA.
EMBL; BC087698; AAH87698.1; -; mRNA.
RefSeq; NP_446424.1; NM_053972.2. [Q63487-1]
RefSeq; XP_006256837.1; XM_006256775.3. [Q63487-2]
RefSeq; XP_006256841.1; XM_006256779.3. [Q63487-2]
RefSeq; XP_017457764.1; XM_017602275.1. [Q63487-1]
UniGene; Rn.203382; -.
UniGene; Rn.209947; -.
ProteinModelPortal; Q63487; -.
SMR; Q63487; -.
STRING; 10116.ENSRNOP00000066990; -.
PaxDb; Q63487; -.
PRIDE; Q63487; -.
Ensembl; ENSRNOT00000004235; ENSRNOP00000004235; ENSRNOG00000003160. [Q63487-1]
Ensembl; ENSRNOT00000075249; ENSRNOP00000066990; ENSRNOG00000050535. [Q63487-1]
GeneID; 108348096; -.
GeneID; 117043; -.
KEGG; rno:108348096; -.
KEGG; rno:117043; -.
UCSC; RGD:619805; rat. [Q63487-1]
CTD; 10325; -.
RGD; 619805; RragB.
eggNOG; KOG3886; Eukaryota.
eggNOG; ENOG410XQ0R; LUCA.
GeneTree; ENSGT00550000074769; -.
HOGENOM; HOG000173258; -.
HOVERGEN; HBG052715; -.
InParanoid; Q63487; -.
KO; K16185; -.
OMA; SNYIARD; -.
OrthoDB; EOG091G050Q; -.
PhylomeDB; Q63487; -.
TreeFam; TF300616; -.
Reactome; R-RNO-1632852; Macroautophagy.
Reactome; R-RNO-165159; mTOR signalling.
Reactome; R-RNO-166208; mTORC1-mediated signalling.
Reactome; R-RNO-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-RNO-8943724; Regulation of PTEN gene transcription.
PRO; PR:Q63487; -.
Proteomes; UP000002494; Chromosome X.
Bgee; ENSRNOG00000003160; -.
Genevisible; Q63487; RN.
GO; GO:0005737; C:cytoplasm; ISS:HGNC.
GO; GO:0034448; C:EGO complex; IBA:GO_Central.
GO; GO:1990131; C:Gtr1-Gtr2 GTPase complex; IBA:GO_Central.
GO; GO:0005764; C:lysosome; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005525; F:GTP binding; IDA:RGD.
GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
GO; GO:0032561; F:guanyl ribonucleotide binding; ISS:UniProtKB.
GO; GO:0034613; P:cellular protein localization; ISS:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
GO; GO:0009267; P:cellular response to starvation; IBA:GO_Central.
GO; GO:0032008; P:positive regulation of TOR signaling; ISS:UniProtKB.
GO; GO:0010506; P:regulation of autophagy; IBA:GO_Central.
InterPro; IPR006762; Gtr1_RagA.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11259; PTHR11259; 1.
Pfam; PF04670; Gtr1_RagA; 1.
SUPFAM; SSF52540; SSF52540; 2.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
GTP-binding; Lysosome; Nucleotide-binding; Reference proteome.
CHAIN 1 374 Ras-related GTP-binding protein B.
/FTId=PRO_0000239950.
NP_BIND 47 54 GTP. {ECO:0000250|UniProtKB:Q00582}.
NP_BIND 123 127 GTP. {ECO:0000250|UniProtKB:Q00582}.
NP_BIND 188 191 GTP. {ECO:0000250|UniProtKB:Q00582}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q5VZM2}.
VAR_SEQ 77 104 Missing (in isoform 2).
{ECO:0000303|PubMed:7499430}.
/FTId=VSP_052074.
CONFLICT 262 262 D -> V (in Ref. 2; AAH78760).
{ECO:0000305}.
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


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