ID G9KLX1_MUSPF Unreviewed; 315 AA.
AC G9KLX1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Ras-related GTP-binding protein {ECO:0000256|RuleBase:RU367014};
DE Flags: Fragment;
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|EMBL:AES05900.1};
RN [1] {ECO:0000313|EMBL:AES05900.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Lungs {ECO:0000313|EMBL:AES05900.1};
RX PubMed=23236062; DOI=10.1128/JVI.02476-12;
RA Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F.,
RA Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., Ross T.M.,
RA Farooqui A., Kelvin D.J.;
RT "Sequencing, annotation, and characterization of the influenza ferret
RT infectome.";
RL J. Virol. 87:1957-1966(2013).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JP017302; AES05900.1; -; mRNA.
DR AlphaFoldDB; G9KLX1; -.
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 NON_TER 1
FT /evidence="ECO:0000313|EMBL:AES05900.1"
FT NON_TER 315
FT /evidence="ECO:0000313|EMBL:AES05900.1"
SQ SEQUENCE 315 AA; 36263 MW; 9697A09754FB23D8 CRC64;
KPRILLMGLR RSGKSSIQKV VFHKMSPNET LFLESTNKIY KDDISNSSFV NFQIWDFPGQ
MDFFDPTFDY EMIFRGTGAL IYVIDAQDDY MEALTRLHIT VSKAYKVNPD MNFEVFIHKV
DGLSDDHKIE TQRDIHQRAN DDLADAGLEK LHLSFYLTSI YDHSIFEAFS KVVQKLIPQL
PTLENLLNIF ISNSGIEKAF LFDVVSKIYI ATDSSPVDMQ SYELCCDMID VVIDVSCIYG
LKEDGSGSAY DKESMAIIKL NNTTVLYLKE VTKFLALVCF VREESFERKG LIDYNFHCFR
KATHEVFKPS MRSSR
//
