ID   SAMTR_CHICK             Reviewed;         408 AA.
AC   Q5ZJ87;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, 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}; ORFNames=RCJMB04_20b4;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720547; CAG32206.1; -; mRNA.
DR   RefSeq; NP_001025905.1; NM_001030734.1.
DR   AlphaFoldDB; Q5ZJ87; -.
DR   STRING; 9031.ENSGALP00000038109; -.
DR   PaxDb; Q5ZJ87; -.
DR   Ensembl; ENSGALT00000038899; ENSGALP00000038109; ENSGALG00000009440.
DR   GeneID; 417776; -.
DR   KEGG; gga:417776; -.
DR   CTD; 154743; -.
DR   VEuPathDB; HostDB:geneid_417776; -.
DR   eggNOG; ENOG502QRK4; Eukaryota.
DR   GeneTree; ENSGT00390000010382; -.
DR   InParanoid; Q5ZJ87; -.
DR   OMA; DNHWTKK; -.
DR   OrthoDB; 836637at2759; -.
DR   PhylomeDB; Q5ZJ87; -.
DR   PRO; PR:Q5ZJ87; -.
DR   Proteomes; UP000000539; Chromosome 1.
DR   Bgee; ENSGALG00000009440; Expressed in spermatid and 12 other tissues.
DR   ExpressionAtlas; Q5ZJ87; baseline and differential.
DR   GO; GO:1990130; C:GATOR1 complex; IEA:Ensembl.
DR   GO; GO:0140007; C:KICSTOR complex; IEA:Ensembl.
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..408
FT                   /note="S-adenosylmethionine sensor upstream of mTORC1"
FT                   /id="PRO_0000321541"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..28
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         175
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03044"
FT   BINDING         193
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03044"
SQ   SEQUENCE   408 AA;  46514 MW;  9B6ECD448833F2AC CRC64;
     MEAAPRSRPR PGGAAASPPP PPPPPPPEQE RKLEQEKLSG VVKSVHRRLR KKYREVGDFD
     KIWREHCEDE ETLCEYAVAM KNLADNHWAK TCEGEGRIEW CCSVCREYFQ NGGKRKALEK
     DEKRALLASK STPALNASQP PKIEDPLPNF GLTNHEAITE ELLHSLGKIR LLDVGSCFNP
     FLKFEEFLTV GIDIVPAVES VYKCDFLNLQ IQQPLQLAQD AIDAFLKQLK NPIDSLPGEL
     FHVVVFSLLL SYFPSPYQRW ICCKKAHELL VLNGLLLVIT PDSSHQNRRA MMMKSWKIAI
     ESLGFKRFKY SKFSHMHLMA FRKTSLQTTS DLVSRNYPGM LYIPQDFNSI EDEEYSNTSC
     YIRSDMEDEQ LAYGFMELPD APYDSDSGES QSSSIPFYEL EDPVLLLS