BHMT2_MOUSE
ID BHMT2_MOUSE Reviewed; 363 AA.
AC Q91WS4; B1B1C9; Q8C1U2; Q9EQE8;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=S-methylmethionine--homocysteine S-methyltransferase BHMT2;
DE Short=SMM-hcy methyltransferase;
DE EC=2.1.1.10;
DE AltName: Full=Betaine--homocysteine S-methyltransferase 2;
GN Name=Bhmt2;
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 [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11087663; DOI=10.1006/geno.2000.6319;
RA Chadwick L.H., McCandless S.E., Silverman G.L., Schwartz S., Westaway D.,
RA Nadeau J.H.;
RT "Betaine-homocysteine methyltransferase-2: cDNA cloning, gene sequence,
RT physical mapping, and expression of the human and mouse genes.";
RL Genomics 70:66-73(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Gall bladder, and Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18230605; DOI=10.1074/jbc.m710449200;
RA Szegedi S.S., Castro C.C., Koutmos M., Garrow T.A.;
RT "Betaine-homocysteine S-methyltransferase-2 is an S-methylmethionine-
RT homocysteine methyltransferase.";
RL J. Biol. Chem. 283:8939-8945(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism.
CC Converts homocysteine to methionine using S-methylmethionine (SMM) as a
CC methyl donor. {ECO:0000269|PubMed:18230605}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homocysteine + S-methyl-L-methionine = H(+) + 2 L-
CC methionine; Xref=Rhea:RHEA:26337, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:58199, ChEBI:CHEBI:58252; EC=2.1.1.10;
CC Evidence={ECO:0000269|PubMed:18230605};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-methionine from L-homocysteine (BhmT route): step 1/1.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in fetal heart, lung, liver, kidney and
CC eye. {ECO:0000269|PubMed:11087663}.
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DR EMBL; AF257474; AAG41357.1; -; mRNA.
DR EMBL; AK090308; BAC41163.1; -; mRNA.
DR EMBL; AK145901; BAE26737.1; -; mRNA.
DR EMBL; AC158524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT030023; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013515; AAH13515.1; -; mRNA.
DR CCDS; CCDS26689.1; -.
DR RefSeq; NP_075022.2; NM_022884.2.
DR AlphaFoldDB; Q91WS4; -.
DR SMR; Q91WS4; -.
DR STRING; 10090.ENSMUSP00000015941; -.
DR iPTMnet; Q91WS4; -.
DR PhosphoSitePlus; Q91WS4; -.
DR SwissPalm; Q91WS4; -.
DR jPOST; Q91WS4; -.
DR MaxQB; Q91WS4; -.
DR PaxDb; Q91WS4; -.
DR PeptideAtlas; Q91WS4; -.
DR PRIDE; Q91WS4; -.
DR ProteomicsDB; 273683; -.
DR Antibodypedia; 24546; 120 antibodies from 21 providers.
DR DNASU; 64918; -.
DR Ensembl; ENSMUST00000015941; ENSMUSP00000015941; ENSMUSG00000042118.
DR GeneID; 64918; -.
DR KEGG; mmu:64918; -.
DR UCSC; uc007rlk.1; mouse.
DR CTD; 23743; -.
DR MGI; MGI:1891379; Bhmt2.
DR VEuPathDB; HostDB:ENSMUSG00000042118; -.
DR eggNOG; KOG1579; Eukaryota.
DR GeneTree; ENSGT00390000003122; -.
DR HOGENOM; CLU_047457_0_0_1; -.
DR InParanoid; Q91WS4; -.
DR OMA; CRFGPRT; -.
DR OrthoDB; 731388at2759; -.
DR PhylomeDB; Q91WS4; -.
DR TreeFam; TF329202; -.
DR Reactome; R-MMU-1614635; Sulfur amino acid metabolism.
DR UniPathway; UPA00051; UER00083.
DR BioGRID-ORCS; 64918; 5 hits in 75 CRISPR screens.
DR PRO; PR:Q91WS4; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q91WS4; protein.
DR Bgee; ENSMUSG00000042118; Expressed in left lobe of liver and 134 other tissues.
DR Genevisible; Q91WS4; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro.
DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; ISO:MGI.
DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0071267; P:L-methionine salvage; ISO:MGI.
DR GO; GO:0009086; P:methionine biosynthetic process; ISO:MGI.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; ISO:MGI.
DR GO; GO:0033477; P:S-methylmethionine metabolic process; ISO:MGI.
DR Gene3D; 3.20.20.330; -; 1.
DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT.
DR InterPro; IPR003726; HCY_dom.
DR InterPro; IPR036589; HCY_dom_sf.
DR Pfam; PF02574; S-methyl_trans; 1.
DR PIRSF; PIRSF037505; Betaine_HMT; 1.
DR SUPFAM; SSF82282; SSF82282; 1.
DR PROSITE; PS50970; HCY; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Methyltransferase; Phosphoprotein; Reference proteome;
KW Transferase; Zinc.
FT CHAIN 1..363
FT /note="S-methylmethionine--homocysteine S-methyltransferase
FT BHMT2"
FT /id="PRO_0000273225"
FT DOMAIN 11..305
FT /note="Hcy-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT CONFLICT 13
FT /note="I -> V (in Ref. 1; AAG41357)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="S -> G (in Ref. 4; AAH13515)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="R -> G (in Ref. 1; AAG41357)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="N -> S (in Ref. 1; AAG41357)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 39872 MW; C7367F1B10B07EEF CRC64;
MAPAGSTRAK KGILERLDSG EVVVGDSGFL FTLEKRGFVK AGLWTPEAVV EHPSAVRQLH
TEFLRAGADV LQTFTFSATE DNMASKWEAV NAAACDLAQE VAGGGGALVA GGICQTSLYK
YHKDETRIKN IFRLQLEVFA RKNVDFLIAE YFEHVEEAVW AVEVLREVGA PVAVTMCIGP
EGDMHDVTPG ECAVKLARAG ADIIGVNCRF GPWTSLQTMK LMKEGLRDAS LQAHLMVQCL
GFHTPDCGKG GFVDLPEYPF GLEPRVATRW DIQKYAREAY NLGIRYIGGC CGFEPYHIRA
IAEELAPERG FLPPASEKHG SWGSGLNMHT KPWIRARARR EYWENLLPAS GRPFCPSLSK
PDA
