CAST1_BOVIN
ID CAST1_BOVIN Reviewed; 329 AA.
AC Q0V8A3;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Cytosolic arginine sensor for mTORC1 subunit 1 {ECO:0000250|UniProtKB:Q8WTX7};
DE AltName: Full=GATS-like protein 3 {ECO:0000305};
GN Name=CASTOR1 {ECO:0000250|UniProtKB:Q8WTX7};
GN Synonyms=GATSL3 {ECO:0000250|UniProtKB:Q8WTX7};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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; BT026316; ABG81472.1; -; mRNA.
DR RefSeq; NP_001074983.1; NM_001081514.1.
DR AlphaFoldDB; Q0V8A3; -.
DR SMR; Q0V8A3; -.
DR STRING; 9913.ENSBTAP00000024074; -.
DR PaxDb; Q0V8A3; -.
DR PRIDE; Q0V8A3; -.
DR Ensembl; ENSBTAT00000024074; ENSBTAP00000024074; ENSBTAG00000018084.
DR GeneID; 506974; -.
DR KEGG; bta:506974; -.
DR CTD; 652968; -.
DR VEuPathDB; HostDB:ENSBTAG00000018084; -.
DR VGNC; VGNC:26791; CASTOR1.
DR eggNOG; ENOG502QV83; Eukaryota.
DR GeneTree; ENSGT00390000006208; -.
DR HOGENOM; CLU_057799_0_0_1; -.
DR InParanoid; Q0V8A3; -.
DR OMA; QGLWLYT; -.
DR OrthoDB; 1166424at2759; -.
DR TreeFam; TF331648; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000018084; Expressed in cortex of kidney and 105 other tissues.
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; IEA:Ensembl.
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..329
FT /note="Cytosolic arginine sensor for mTORC1 subunit 1"
FT /id="PRO_0000348589"
FT DOMAIN 72..138
FT /note="ACT 1"
FT DOMAIN 260..321
FT /note="ACT 2"
FT BINDING 111..112
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:Q8WTX7"
FT BINDING 274
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:Q8WTX7"
FT BINDING 280..281
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:Q8WTX7"
FT BINDING 300..304
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 329 AA; 36041 MW; FE070716F152E631 CRC64;
MELHILEHRV RVLSLARPGL WLYTHPLIKL LFLPRRSRCK FFSLTETPED YTLMVDEEGF
KELPPSEFLQ VAEATWLVLN VSSPSGAAVQ AAGVTKIARS VIAPLAEHHV SVLMLSTYQT
DFILVREQDL SVVIHTLARE FDIYREVGGE PVPVARDDSS NGFPRAQHGP SPTVHPIQSP
QNRFCVLTLD PETLPAIATT LIDVLFYSHS PPREAASGGP GSSSIAFFAF SLIEGYISIV
MDAETQKKFP SDLLLTSSSG ELWRMVRIGG QPLGFDECGI VAQIAGPLAA ADISAYYIST
FNFDHALVPE DGIGSVIEVL QRRQDGLGS
