SAMTR_MOUSE
ID SAMTR_MOUSE Reviewed; 403 AA.
AC Q8BXK4; A6H608;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 111.
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, ECO:0000312|MGI:MGI:2141466};
GN Synonyms=Samtor {ECO:0000255|HAMAP-Rule:MF_03044};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC32852.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK046745; BAC32852.1; ALT_FRAME; mRNA.
DR EMBL; BC145708; AAI45709.1; -; mRNA.
DR EMBL; BC145710; AAI45711.1; -; mRNA.
DR CCDS; CCDS51723.1; -.
DR RefSeq; NP_780521.2; NM_175312.4.
DR AlphaFoldDB; Q8BXK4; -.
DR STRING; 10090.ENSMUSP00000040578; -.
DR iPTMnet; Q8BXK4; -.
DR PhosphoSitePlus; Q8BXK4; -.
DR SwissPalm; Q8BXK4; -.
DR MaxQB; Q8BXK4; -.
DR PaxDb; Q8BXK4; -.
DR PeptideAtlas; Q8BXK4; -.
DR PRIDE; Q8BXK4; -.
DR ProteomicsDB; 260823; -.
DR Antibodypedia; 50763; 11 antibodies from 7 providers.
DR DNASU; 101148; -.
DR Ensembl; ENSMUST00000045235; ENSMUSP00000040578; ENSMUSG00000042742.
DR GeneID; 101148; -.
DR KEGG; mmu:101148; -.
DR UCSC; uc012eic.1; mouse.
DR CTD; 154743; -.
DR MGI; MGI:2141466; Bmt2.
DR VEuPathDB; HostDB:ENSMUSG00000042742; -.
DR eggNOG; ENOG502QRK4; Eukaryota.
DR GeneTree; ENSGT00390000010382; -.
DR HOGENOM; CLU_036404_1_1_1; -.
DR InParanoid; Q8BXK4; -.
DR OMA; DNHWTKK; -.
DR OrthoDB; 836637at2759; -.
DR PhylomeDB; Q8BXK4; -.
DR TreeFam; TF324724; -.
DR Reactome; R-MMU-9639288; Amino acids regulate mTORC1.
DR BioGRID-ORCS; 101148; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Bmt2; mouse.
DR PRO; PR:Q8BXK4; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8BXK4; protein.
DR Bgee; ENSMUSG00000042742; Expressed in manus and 223 other tissues.
DR ExpressionAtlas; Q8BXK4; baseline and differential.
DR Genevisible; Q8BXK4; MM.
DR GO; GO:1990130; C:GATOR1 complex; ISO:MGI.
DR GO; GO:0140007; C:KICSTOR complex; ISO:MGI.
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..403
FT /note="S-adenosylmethionine sensor upstream of mTORC1"
FT /id="PRO_0000321540"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 170
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03044"
FT BINDING 188
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03044"
SQ SEQUENCE 403 AA; 45952 MW; 2ECD73F0623FB4CF CRC64;
MEPGPGGRGA ARGQRPPNAA QPREQERKLE QEKLSGVVKS VHRRLRKKYR EVGDFDKIWR
EHCEDAETLC EYAVAMKNLA DNHWAKTCEG EGRIEWCCSV CREYFQNGGK RKALEKDEKR
AVLATKTTPA LNVHESSKLE GPLTNLSFTS PDFITELLQA SGKIRLLDVG SCFNPFLKFE
EFLTVGIDIV PAVESVYKCD FLNLQLQQPL QLAQDAIDAF LKQLRNPIDA LPGELFHVVV
FSLLLSYFPS PYQRWICCKK AHELLVLNGL LLIITPDSSH QNRHAMMMKS WKIAIESLGF
KRFKYSKFSH MHLMAFRKTS LKTTSDLVSR NYPGMLYIPQ DFNSVEEEEY SNTSCYVRSD
LEDEQLAYGF TELPEAPYDS DSGESQASSI PFYELEDPIL LLS
