ID A0A2U3XQM8_LEPWE Unreviewed; 396 AA.
AC A0A2U3XQM8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Ras-related GTP-binding protein {ECO:0000256|RuleBase:RU367014};
GN Name=RRAGD {ECO:0000313|RefSeq:XP_006733766.1};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006733766.1};
RN [1] {ECO:0000313|RefSeq:XP_006733766.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006733766.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_006733766.1; XM_006733703.2.
DR AlphaFoldDB; A0A2U3XQM8; -.
DR STRING; 9713.A0A2U3XQM8; -.
DR GeneID; 102731969; -.
DR KEGG; lww:102731969; -.
DR CTD; 58528; -.
DR OrthoDB; 166730at2759; -.
DR Proteomes; UP000245341; Unplaced.
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:SF5; RAS-RELATED GTP-BINDING PROTEIN D; 1.
DR Pfam; PF04670; Gtr1_RagA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000245341}.
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..25
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 396 AA; 44977 MW; 43AB2601972AA333 CRC64;
MSQVLGKPQP EDEDDDEEDE LVGLADYGDG PDSSDADPDS GAEEGVLDFS DPFSTEVKPR
ILLMGLRRSG KSSIQKVVFH KMSPNETLFL ESTNKICRED VSNSSFVNFQ IWDFPGQIDF
FDPTFDYEMI FRGTGALIFV IDSQDDYMEA LARLHLTVTR AYKVNTDINF EVFIHKVDGL
SDDHKIETQR DIHQRANDDL ADAGLEKIHL SFYLTSIYDH SIFEAFSKVV QKLIPQLPTL
ENLLNIFISN SGIEKAFLFD VVSKIYIATD STPVDMQTYE LCCDMIDVVI DISCIYGLKE
DGAGTPYDKE STAIIKLNNT TVLYLKEVTK FLALVCFVRE ESFERKGLID YNFHCFRKAI
HEVFEVRMKM VKSRKVQNRL QKKKGATPNG TPNVLL
//
