ID   CAST1_PONAB             Reviewed;         329 AA.
AC   Q5R9D1;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 52.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR859458; CAH91629.1; -; mRNA.
DR   RefSeq; NP_001125958.1; NM_001132486.1.
DR   AlphaFoldDB; Q5R9D1; -.
DR   SMR; Q5R9D1; -.
DR   STRING; 9601.ENSPPYP00000013058; -.
DR   GeneID; 100172893; -.
DR   KEGG; pon:100172893; -.
DR   CTD; 652968; -.
DR   eggNOG; ENOG502QV83; Eukaryota.
DR   InParanoid; Q5R9D1; -.
DR   OrthoDB; 1166424at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0034618; F:arginine binding; ISS:UniProtKB.
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   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_0000348592"
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;  36405 MW;  6C1F644CA286ED2B CRC64;
     MELHILEHRV RVLSVARPGL WLYTHPLIKL LFLPRRSRCK FFSLTETPED YTLMVDEEGF
     KELPPSEFLQ VAEATWLVLN VSSHSGAAVQ AAGVTKIARS VIAPLAEHHV SVLMLSTYQT
     DFILVREQDL SVVIHTLAQE FDIYREVGGE PVPVTRDDFS NGFPRTQHGP SPTVHPIQSP
     QNRFCVLTLD PETLPAIATT LIDVLFYSHR TPKEAASSSP EPSSITFFAF SLIEGYISIV
     MDAETQKKFP SDLLLTSSSG ELWRMVRIGG QPLGFDECGI VAQIAGPLAA ADISAYYIST
     FNFDHALVPE DGIGSVIEVL QRRQEGLAS