ID   SAMTR_XENTR             Reviewed;         400 AA.
AC   A4IIA7; Q5M798;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2004) 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; BC088770; AAH88770.1; -; mRNA.
DR   EMBL; BC135938; AAI35939.1; -; mRNA.
DR   RefSeq; NP_001076819.1; NM_001083350.2.
DR   AlphaFoldDB; A4IIA7; -.
DR   STRING; 8364.ENSXETP00000058945; -.
DR   DNASU; 496879; -.
DR   Ensembl; ENSXETT00000100843; ENSXETP00000092818; ENSXETG00000037231.
DR   GeneID; 496879; -.
DR   KEGG; xtr:496879; -.
DR   CTD; 154743; -.
DR   Xenbase; XB-GENE-999766; bmt2.
DR   eggNOG; ENOG502QRK4; Eukaryota.
DR   HOGENOM; CLU_036404_1_1_1; -.
DR   InParanoid; A4IIA7; -.
DR   OrthoDB; 836637at2759; -.
DR   Reactome; R-XTR-9639288; Amino acids regulate mTORC1.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000037231; Expressed in egg cell and 13 other tissues.
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   Pfam; PF11968; Bmt2; 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..400
FT                   /note="S-adenosylmethionine sensor upstream of mTORC1"
FT                   /id="PRO_0000321544"
FT   BINDING         168
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03044"
FT   BINDING         186
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03044"
SQ   SEQUENCE   400 AA;  45958 MW;  09E01A8116E3FD19 CRC64;
     MEPVLQARGK RENVLGNARE ERCVPGFPSA CEQKLEQEKL SGVVKRVHRD LRKKYREAGD
     FEKIWLEHCK DKGRLCEYAV AMKALADNHW AKKCEGEGRI EWCLGVCQEY FFNGGKKKAI
     EKDARRATLN KLQSPNHAED GVSDFSVPNI KPLNDEYMTG KIRLLDVGSC YNPFLKYEDF
     LAVGIDIVPA VETVCKCDFL NLQIQRPLQF APDAIDAFLK QLESPIDYLP AELFHVVVFS
     LLLSYFPSPY QRWICCKKAH ELLTLNGLLL IITPDSSHQN RHAVMMKSWK IAIESLGFRR
     MTYSKFSHMH LMAFRKTSLK TTSDLITMNY PDMLYIPQDF NYDGEEDYFS PCCARSELED
     EQLACGFTEL PDTPYDSDSG ESQNSTMPFY EFEDPILLLT