ID   SAMTR_DANRE             Reviewed;         393 AA.
AC   Q0P410;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=S-adenosylmethionine sensor upstream of mTORC1 {ECO:0000255|HAMAP-Rule:MF_03044};
DE   AltName: Full=Probable methyltransferase BMT2 homolog {ECO:0000255|HAMAP-Rule:MF_03044};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03044};
GN   Name=bmt2 {ECO:0000255|HAMAP-Rule:MF_03044};
GN   Synonyms=samtor {ECO:0000255|HAMAP-Rule:MF_03044};
GN   ORFNames=zgc:153606 {ECO:0000303|Ref.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: S-adenosyl-L-methionine-binding protein that acts as an
CC       inhibitor of mTORC1 signaling via interaction with the GATOR1 and
CC       KICSTOR complexes. Acts as a sensor of S-adenosyl-L-methionine to
CC       signal methionine sufficiency to mTORC1: in presence of methionine,
CC       binds S-adenosyl-L-methionine, leading to disrupt interaction with the
CC       GATOR1 and KICSTOR complexes and promote mTORC1 signaling. Upon
CC       methionine starvation, S-adenosyl-L-methionine levels are reduced,
CC       thereby promoting the association with GATOR1 and KICSTOR, leading to
CC       inhibit mTORC1 signaling. Probably also acts as a S-adenosyl-L-
CC       methionine-dependent methyltransferase. {ECO:0000255|HAMAP-
CC       Rule:MF_03044}.
CC   -!- SUBUNIT: Interacts with the GATOR1 complex; interaction is disrupted
CC       when bmt2/samtor binds S-adenosyl-L-methionine. Interacts with the
CC       KICSTOR complex; interaction is disrupted when bmt2/samtor binds S-
CC       adenosyl-L-methionine. {ECO:0000255|HAMAP-Rule:MF_03044}.
CC   -!- SIMILARITY: Belongs to the BMT2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03044}.
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DR   EMBL; BC122347; AAI22348.1; -; mRNA.
DR   RefSeq; NP_001070615.1; NM_001077147.1.
DR   AlphaFoldDB; Q0P410; -.
DR   STRING; 7955.ENSDARP00000084049; -.
DR   PaxDb; Q0P410; -.
DR   GeneID; 558558; -.
DR   KEGG; dre:558558; -.
DR   CTD; 154743; -.
DR   ZFIN; ZDB-GENE-060825-17; bmt2.
DR   eggNOG; ENOG502QRK4; Eukaryota.
DR   InParanoid; Q0P410; -.
DR   OrthoDB; 836637at2759; -.
DR   PhylomeDB; Q0P410; -.
DR   Reactome; R-DRE-9639288; Amino acids regulate mTORC1.
DR   PRO; PR:Q0P410; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:1904047; F:S-adenosyl-L-methionine binding; ISS:UniProtKB.
DR   GO; GO:0034198; P:cellular response to amino acid starvation; ISS:UniProtKB.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:1904262; P:negative regulation of TORC1 signaling; ISS:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_03044; BMT2; 1.
DR   InterPro; IPR021867; Bmt2/SAMTOR.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR21008; PTHR21008; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..393
FT                   /note="S-adenosylmethionine sensor upstream of mTORC1"
FT                   /id="PRO_0000321542"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         160
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03044"
FT   BINDING         178
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03044"
SQ   SEQUENCE   393 AA;  44782 MW;  83D3DDDD2DF53813 CRC64;
     MDLRSSAETD PDLSENHPGS VPAELQSRKQ EQEKLSGVVK SVHRKLRRKY IEVGDFDKIW
     REHCEDEQTL SEYAMAMKNL ADNHWANKCE GEGRIEWCRS VCQEYFQDGG MRRVLEKDEK
     SARHATAGNA NTDTNAPPQL SSISTSSTFQ LGKIRLLDVG SCFNPFLKFD EFLTVGIDIV
     PAVESVYKCD FLNLQLQQPL QLASDALDAF LRQLRGPIDA LPAELFHVVV FSLLLSYFPS
     PYQRWLCCKK AHELLTLNGL LLIITPDSSH QGRHALMMRS WRVAVESLGF KRYKYVKFSH
     MHLIAFRKVS PTTSSDLVSR NYPEMLYIPQ DFNTFDEDGF ADCYEPPRSD FEDDQMACSF
     AELPETPYDS DSGESQSSSA PFYELEDPIL LQS