ID   A0A9J8BR96_CYPCA        Unreviewed;       335 AA.
AC   A0A9J8BR96;
DT   28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2023, sequence version 1.
DT   18-JUN-2025, entry version 12.
DE   RecName: Full=Cytosolic arginine sensor for mTORC1 subunit 1 {ECO:0000256|ARBA:ARBA00013329};
DE   AltName: Full=GATS-like protein 3 {ECO:0000256|ARBA:ARBA00031657};
OS   Cyprinus carpio carpio.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Cyprinus.
OX   NCBI_TaxID=630221 {ECO:0000313|Ensembl:ENSCCRP00000159847.1, ECO:0000313|Proteomes:UP001108240};
RN   [1] {ECO:0000313|Ensembl:ENSCCRP00000159847.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2025) to UniProtKB.
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:0000256|ARBA:ARBA00002751}.
CC   -!- SUBUNIT: Forms homodimers and heterodimers with CASTOR2. Interacts with
CC       the GATOR2 complex which is composed of MIOS, SEC13, SEH1L, WDR24 and
CC       WDR59; the interaction is negatively regulated by arginine. Interacts
CC       with TM4SF5; the interaction is positively regulated by leucine and is
CC       negatively regulated by arginine. {ECO:0000256|ARBA:ARBA00046845}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the GATS family.
CC       {ECO:0000256|ARBA:ARBA00006827}.
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DR   Ensembl; ENSCCRT00000124194.1; ENSCCRP00000159847.1; ENSCCRG00000026528.2.
DR   GeneTree; ENSGT00390000006208; -.
DR   Proteomes; UP001108240; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0034618; F:arginine binding; IEA:TreeGrafter.
DR   GO; GO:1904262; P:negative regulation of TORC1 signaling; IEA:TreeGrafter.
DR   FunFam; 3.30.2130.10:FF:000003; Cytosolic arginine sensor for mTORC1 subunit 1; 1.
DR   FunFam; 3.30.2130.10:FF:000004; Cytosolic arginine sensor for mTORC1 subunit 1; 1.
DR   Gene3D; 3.30.2130.10; VC0802-like; 2.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR049479; CASTOR1_ACT-like.
DR   InterPro; IPR040778; CASTOR1_N.
DR   InterPro; IPR027795; CASTOR_ACT_dom.
DR   InterPro; IPR026249; CASTOR_fam.
DR   InterPro; IPR051719; CASTOR_mTORC1.
DR   PANTHER; PTHR31131; CHROMOSOME 1, WHOLE GENOME SHOTGUN SEQUENCE; 1.
DR   PANTHER; PTHR31131:SF3; CYTOSOLIC ARGININE SENSOR FOR MTORC1 SUBUNIT 1; 1.
DR   Pfam; PF13840; ACT_7; 2.
DR   Pfam; PF21389; CASTOR1_ACT-like; 1.
DR   Pfam; PF18700; Castor1_N; 1.
DR   PRINTS; PR02078; GATSLIKEFMLY.
DR   SUPFAM; SSF55021; ACT-like; 2.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP001108240};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          9..69
FT                   /note="CASTOR1 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18700"
FT   DOMAIN          75..139
FT                   /note="CASTOR ACT"
FT                   /evidence="ECO:0000259|Pfam:PF13840"
FT   DOMAIN          178..260
FT                   /note="Cytosolic arginine sensor for mTORC1 subunit 1/2
FT                   ACT-like"
FT                   /evidence="ECO:0000259|Pfam:PF21389"
FT   DOMAIN          261..311
FT                   /note="CASTOR ACT"
FT                   /evidence="ECO:0000259|Pfam:PF13840"
SQ   SEQUENCE   335 AA;  37374 MW;  C5BEEDD811CF6C76 CRC64;
     MDLHILDHKL RVTSISKTGL QQYTHPLIKL IFLRNRTRCK FFSLTETPEN YTVVLDEEGF
     KELQPSEHLQ VEGSTWLPLN VVSNGNTSSS SQAVGVTKIA KSVIAPLAEQ HVSVFMLSTY
     QTDFILVREK DLSVVVETLV EEFNIFREEG GESVPVHSQD ACNGLQRNGR EVPHATVHPV
     LIPENQFCVM SLDPDTLPAI ATTLIDVLFY SNSPKEGASV DQDMKCIKFF SFSLIDGYVS
     LVMDTEAQRQ FPADLLFTSS SGELWRMARI GGQPLGFDEC GIVAQISQPL ADSDISAYYI
     STFSFDHALV SHFAHSFCFY THNILALRID GQMVT
//