ID B4DQG4_HUMAN Unreviewed; 365 AA.
AC B4DQG4;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Ras-related GTP-binding protein {ECO:0000256|RuleBase:RU367014};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG60926.1};
RN [1] {ECO:0000313|EMBL:BAG60926.1}
RP NUCLEOTIDE SEQUENCE.
RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA Sugano S., Nomura N., Isogai T.;
RT "NEDO human cDNA sequencing project focused on splicing variants.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|RuleBase:RU367014}.
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:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367014}.
CC Lysosome {ECO:0000256|RuleBase:RU367014}.
CC -!- SIMILARITY: Belongs to the GTR/RAG GTP-binding protein family.
CC {ECO:0000256|ARBA:ARBA00007756, ECO:0000256|RuleBase:RU367014}.
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DR EMBL; AK298788; BAG60926.1; -; mRNA.
DR RefSeq; NP_001258780.1; NM_001271851.1.
DR AlphaFoldDB; B4DQG4; -.
DR MaxQB; B4DQG4; -.
DR PeptideAtlas; B4DQG4; -.
DR DNASU; 64121; -.
DR GeneID; 64121; -.
DR CTD; 64121; -.
DR OrthoDB; 166730at2759; -.
DR BioGRID-ORCS; 64121; 177 hits in 1169 CRISPR screens.
DR GenomeRNAi; 64121; -.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:UniProtKB-UniRule.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IEA:UniProtKB-UniRule.
DR CDD; cd11385; RagC_like; 1.
DR Gene3D; 3.30.450.190; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR006762; Gtr1_RagA.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039400; RagC/D.
DR PANTHER; PTHR11259; RAS-RELATED GTP BINDING RAG/GTR YEAST; 1.
DR PANTHER; PTHR11259:SF6; RAS-RELATED GTP-BINDING PROTEIN C; 1.
DR Pfam; PF04670; Gtr1_RagA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|RuleBase:RU367014};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU367014};
KW Lysosome {ECO:0000256|RuleBase:RU367014};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU367014}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 365 AA; 40230 MW; 95347C6682134322 CRC64;
MSLQYGAEET PLAGSYGAAD SFPKDFGCGV EEEEEEAAAA GGGVGAGAGG GCGPGGADSS
KPRILLMGLR RSGKSSIQKI WDFPGQMDFF DPTFDYEMIF RGTGALIYVI DAQDDYMEAL
TRLHITVSRA YKVNPDMNFE VFIHKVDGLS DDHKIETQRD IHQRANDDLA DAGLEKLHLS
FYLTSIYDHS IFEAFSKVVQ KLIPQLPTLE NLLNIFISNS GIEKAFLFDV VSKIYIATDS
SPVDMQSYEL CCDMIDVVID VSCIYGLKED GSGSAYDKES MAIIKLNNTT VLYLKEVTKF
LALVCILREE SFERKGLIDY NFHCFRKAIH EVFEVGVTSH RSCGHQTSAS SLKALTHNGT
PRNAI
//
