ID A0A3B3T9E4_9TELE Unreviewed; 480 AA.
AC A0A3B3T9E4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Ras-related GTP-binding protein {ECO:0000256|RuleBase:RU367014};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000039063.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000039063.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3B3T9E4; -.
DR STRING; 1676925.ENSPKIP00000039063; -.
DR Ensembl; ENSPKIT00000020062.1; ENSPKIP00000039063.1; ENSPKIG00000016566.1.
DR GeneTree; ENSGT00950000183031; -.
DR Proteomes; UP000261540; 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}.
FT REGION 18..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 480 AA; 54638 MW; 7998C3AD05F82066 CRC64;
MCLRIKFCML RNALKGSRLP PSPSREGGTA HGRIQKRRRR RREVKVHNGM DVSSDKVEKL
LCLCSLISGN LGMTSEAHST YSEEEDGDEE AMAYYDDDDL DAFADEDLDC SCEEGVLGLS
DPFGGEVKPR ILLMGLRRSG KSSIQKVVFH KMSPNETLFL ESTNKICRED VSNSSFVSFQ
IWDFPGQIDF FDPTFDYEMI FRGTGALIFV IDSQDDYVEA LSRLHLTVTR AYKVNPNINF
EVFIHKVDGL SDDHKIEKQR DIHKRANDDL ADAALERIHL RFLSFYSVKT FYVNFYVTSF
YLYLETNMMS ISHPSAPSFY LTSIYDHSIF EAFSKVVQKL IPQLPTLENL LNIFISNSGI
EKAFLFDVVS KIYIATDSSP VDMQTYELCC DMIDVVIDIS CIYGLTGEEA GIPYDKESMA
IIRLNNTTVM YLKEVTKFLA LVCFLREESF ERKGQRVFVC QGHKFSQLPG HGSDPVACIF
//
