CAST1_RAT
ID CAST1_RAT Reviewed; 331 AA.
AC Q5BJZ0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Cytosolic arginine sensor for mTORC1 subunit 1 {ECO:0000312|RGD:1304774};
DE AltName: Full=GATS-like protein 3 {ECO:0000305};
GN Name=Castor1 {ECO:0000312|RGD:1304774};
GN Synonyms=Gatsl3 {ECO:0000312|RGD:1304774};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Functions as an intracellular arginine sensor within the
CC amino acid-sensing branch of the TORC1 signaling pathway. As a
CC homodimer or a heterodimer with CASTOR2, binds and inhibits the GATOR
CC subcomplex GATOR2 and thereby mTORC1. Binding of arginine to CASTOR1
CC allosterically disrupts the interaction of CASTOR1-containing dimers
CC with GATOR2 which can in turn activate mTORC1 and the TORC1 signaling
CC pathway. {ECO:0000250|UniProtKB:Q8WTX7}.
CC -!- SUBUNIT: Forms homodimers and heterodimers with CASTOR2 (By
CC similarity). Interacts with the GATOR2 complex which is composed of
CC MIOS, SEC13, SEH1L, WDR24 and WDR59; the interaction is negatively
CC regulated by arginine (By similarity). Interacts with TM4SF5; the
CC interaction is positively regulated by leucine and is negatively
CC regulated by arginine (By similarity). {ECO:0000250|UniProtKB:Q8WTX7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8WTX7}.
CC -!- DOMAIN: Based on x-ray crystallography data, the protein would be
CC constituted of 4 tandem ACT domains instead of the 2 predicted from the
CC sequence. {ECO:0000250|UniProtKB:Q8WTX7}.
CC -!- PTM: Phosphorylation at Ser-14 by AKT1, promoting the interaction
CC between CASTOR1 and RNF167. {ECO:0000250|UniProtKB:Q8WTX7}.
CC -!- PTM: Ubiquitinated by RNF167 via 'Lys-29'-polyubiquitination, leading
CC to its degradation, releasing the GATOR2 complex. Ubiquitination by
CC RNF167 is promoted by phosphorylation at Ser-14 by AKT1.
CC {ECO:0000250|UniProtKB:Q8WTX7}.
CC -!- SIMILARITY: Belongs to the GATS family. {ECO:0000305}.
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DR EMBL; BC091274; AAH91274.1; -; mRNA.
DR RefSeq; NP_001020299.1; NM_001025128.1.
DR RefSeq; XP_006251397.1; XM_006251335.3.
DR RefSeq; XP_006251398.1; XM_006251336.3.
DR AlphaFoldDB; Q5BJZ0; -.
DR SMR; Q5BJZ0; -.
DR STRING; 10116.ENSRNOP00000009150; -.
DR PaxDb; Q5BJZ0; -.
DR Ensembl; ENSRNOT00000009150; ENSRNOP00000009150; ENSRNOG00000006740.
DR GeneID; 360969; -.
DR KEGG; rno:360969; -.
DR UCSC; RGD:1304774; rat.
DR CTD; 652968; -.
DR RGD; 1304774; Castor1.
DR eggNOG; ENOG502QV83; Eukaryota.
DR GeneTree; ENSGT00390000006208; -.
DR HOGENOM; CLU_057799_0_0_1; -.
DR InParanoid; Q5BJZ0; -.
DR OMA; QGLWLYT; -.
DR OrthoDB; 1166424at2759; -.
DR PhylomeDB; Q5BJZ0; -.
DR TreeFam; TF331648; -.
DR Reactome; R-RNO-9639288; Amino acids regulate mTORC1.
DR PRO; PR:Q5BJZ0; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000006740; Expressed in adult mammalian kidney and 18 other tissues.
DR Genevisible; Q5BJZ0; RN.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0061700; C:GATOR2 complex; IEA:Ensembl.
DR GO; GO:0034618; F:arginine binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0140311; F:protein sequestering activity; ISS:UniProtKB.
DR GO; GO:1903577; P:cellular response to L-arginine; ISS:UniProtKB.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; ISS:UniProtKB.
DR GO; GO:1902531; P:regulation of intracellular signal transduction; IBA:GO_Central.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR030415; CASTOR1.
DR InterPro; IPR040778; CASTOR1_N.
DR InterPro; IPR027795; CASTOR_ACT_dom.
DR InterPro; IPR026249; CASTOR_fam.
DR PANTHER; PTHR31131:SF3; PTHR31131:SF3; 1.
DR Pfam; PF13840; ACT_7; 2.
DR Pfam; PF18700; Castor1_N; 1.
DR PRINTS; PR02078; GATSLIKEFMLY.
DR SUPFAM; SSF55021; SSF55021; 2.
PE 2: Evidence at transcript level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..331
FT /note="Cytosolic arginine sensor for mTORC1 subunit 1"
FT /id="PRO_0000348593"
FT DOMAIN 72..139
FT /note="ACT 1"
FT DOMAIN 262..322
FT /note="ACT 2"
FT REGION 155..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110..111
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:Q8WTX7"
FT BINDING 273
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:Q8WTX7"
FT BINDING 279..280
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:Q8WTX7"
FT BINDING 299..303
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:Q8WTX7"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WTX7"
SQ SEQUENCE 331 AA; 36476 MW; D03D352A77478953 CRC64;
MELHILEHRV RVLSLARPGL WLYTHPLIKL LFLPSRSRCK FFSLTETPED YTLMVDEEGF
KELPPSEFLQ VAEATWLVMN VSHSGSVVQA AGVTKIARSV IAPLAEHHVS VLMLSTYQTD
FILVREQDLS VVIHTLAREF QIYREVGGEP VPVTGDDSSN GFPQAQHGPS PTVHPIQSPQ
NRFCVLTLDP ETLPAVATTL IDVLFYSHSV PKEAASGGPE STSIPFFAFS LIEGYISIVM
DAETQKKFPS DLLLTSSSGE LWRMVRIGGQ PLGFDECGIV AQIAGPLAAV DVSAYYISTF
NFDHALVPED EISCVIDILQ RRQEGLASKD P
