MAT2B_MOUSE
ID MAT2B_MOUSE Reviewed; 334 AA.
AC Q99LB6; Q5NC89; Q76LX2; Q8BVX6; Q8BYT9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Methionine adenosyltransferase 2 subunit beta;
DE AltName: Full=Methionine adenosyltransferase II beta;
DE Short=MAT II beta;
GN Name=Mat2b;
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] (ISOFORM 1).
RC STRAIN=ddY; TISSUE=Kidney;
RX PubMed=16022199; DOI=10.3177/jnsv.51.118;
RA Sakata S.F., Okumura S., Matsuda K., Horikawa Y., Maeda M., Kawasaki K.,
RA Chou J.Y., Tamaki N.;
RT "Effect of fasting on methionine adenosyltransferase expression and the
RT methionine cycle in the mouse liver.";
RL J. Nutr. Sci. Vitaminol. 51:118-123(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-86 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Egg;
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] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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: Regulatory subunit of S-adenosylmethionine synthetase 2, an
CC enzyme that catalyzes the formation of S-adenosylmethionine from
CC methionine and ATP. Regulates MAT2A catalytic activity by changing its
CC kinetic properties, increasing its affinity for L-methionine. Can bind
CC NADP (in vitro). {ECO:0000250|UniProtKB:Q9NZL9}.
CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC S-adenosyl-L-methionine from L-methionine: step 1/1.
CC {ECO:0000250|UniProtKB:Q9NZL9}.
CC -!- SUBUNIT: Heterotrimer; composed of a catalytic MAT2A homodimer that
CC binds one regulatory MAT2B chain. Heterohexamer; composed of a central,
CC catalytic MAT2A homotetramer flanked on either side by a regulatory
CC MAT2B chain. NADP binding increases the affinity for MAT2A.
CC {ECO:0000250|UniProtKB:Q9NZL9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99LB6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99LB6-2; Sequence=VSP_025541;
CC -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family.
CC MAT2B subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC29963.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=CAI25424.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB070267; BAD06938.1; -; mRNA.
DR EMBL; AK038303; BAC29963.1; ALT_SEQ; mRNA.
DR EMBL; AK075947; BAC36076.1; -; mRNA.
DR EMBL; AK162087; BAE36716.1; -; mRNA.
DR EMBL; AL646055; CAI25424.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL646055; CAI25422.1; -; Genomic_DNA.
DR EMBL; AL646055; CAI25423.1; -; Genomic_DNA.
DR EMBL; BC003457; AAH03457.1; -; mRNA.
DR CCDS; CCDS24547.1; -. [Q99LB6-1]
DR CCDS; CCDS56767.1; -. [Q99LB6-2]
DR RefSeq; NP_001186203.1; NM_001199274.1. [Q99LB6-2]
DR RefSeq; NP_598778.1; NM_134017.2. [Q99LB6-1]
DR AlphaFoldDB; Q99LB6; -.
DR SMR; Q99LB6; -.
DR BioGRID; 224352; 18.
DR IntAct; Q99LB6; 1.
DR STRING; 10090.ENSMUSP00000048222; -.
DR iPTMnet; Q99LB6; -.
DR PhosphoSitePlus; Q99LB6; -.
DR REPRODUCTION-2DPAGE; IPI00649402; -.
DR REPRODUCTION-2DPAGE; Q99LB6; -.
DR EPD; Q99LB6; -.
DR jPOST; Q99LB6; -.
DR MaxQB; Q99LB6; -.
DR PaxDb; Q99LB6; -.
DR PeptideAtlas; Q99LB6; -.
DR PRIDE; Q99LB6; -.
DR ProteomicsDB; 293413; -. [Q99LB6-1]
DR ProteomicsDB; 293414; -. [Q99LB6-2]
DR Antibodypedia; 28655; 244 antibodies from 30 providers.
DR DNASU; 108645; -.
DR Ensembl; ENSMUST00000040167; ENSMUSP00000048222; ENSMUSG00000042032. [Q99LB6-1]
DR Ensembl; ENSMUST00000101347; ENSMUSP00000098901; ENSMUSG00000042032. [Q99LB6-2]
DR GeneID; 108645; -.
DR KEGG; mmu:108645; -.
DR UCSC; uc007ilp.2; mouse. [Q99LB6-1]
DR UCSC; uc007ilq.2; mouse. [Q99LB6-2]
DR CTD; 27430; -.
DR MGI; MGI:1913667; Mat2b.
DR VEuPathDB; HostDB:ENSMUSG00000042032; -.
DR eggNOG; KOG1430; Eukaryota.
DR GeneTree; ENSGT00390000006721; -.
DR HOGENOM; CLU_045518_0_0_1; -.
DR InParanoid; Q99LB6; -.
DR OMA; AGETTWH; -.
DR OrthoDB; 1007850at2759; -.
DR PhylomeDB; Q99LB6; -.
DR TreeFam; TF332849; -.
DR Reactome; R-MMU-156581; Methylation.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR UniPathway; UPA00315; UER00080.
DR BioGRID-ORCS; 108645; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Mat2b; mouse.
DR PRO; PR:Q99LB6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q99LB6; protein.
DR Bgee; ENSMUSG00000042032; Expressed in animal zygote and 253 other tissues.
DR ExpressionAtlas; Q99LB6; baseline and differential.
DR Genevisible; Q99LB6; MM.
DR GO; GO:0048269; C:methionine adenosyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0048270; F:methionine adenosyltransferase regulator activity; ISS:UniProtKB.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029903; RmlD-like-bd.
DR PANTHER; PTHR10491; PTHR10491; 1.
DR Pfam; PF04321; RmlD_sub_bind; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; NADP; One-carbon metabolism; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..334
FT /note="Methionine adenosyltransferase 2 subunit beta"
FT /id="PRO_0000287521"
FT REGION 319..334
FT /note="Required for interaction with MAT2A"
FT /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT BINDING 37..40
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT BINDING 60..62
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT BINDING 71..72
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT BINDING 93
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT BINDING 97
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT BINDING 159
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT BINDING 185
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT MOD_RES 309
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT VAR_SEQ 1..21
FT /note="MVGREKELSIHFVPGCCQLVE -> MPEMPEAMEQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025541"
FT CONFLICT 97
FT /note="R -> G (in Ref. 1; BAD06938)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="F -> L (in Ref. 1; BAD06938)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="V -> A (in Ref. 1; BAD06938)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 37393 MW; 0B209731D713BD02 CRC64;
MVGREKELSI HFVPGCCQLV EEEVNIPSRR VLITGATGLL GRAVYKEFQQ SNWHTVGCGF
RRARPKFEQV NLLDSEAVHH LIHDFQPHVI VHCAAERRPD VVESQPDAAS QLNVGASGNL
AKEAAAIGAF LIYISSDYVF DGTNPPYTEE DIPSPLNLYG KTKLDGEKAV LENNLGAAVL
RIPVLYGEVE KLEESAVTVM FDKVQFSNKS ANMDHWQQRF PTHVKDVASV CRQLAEKRML
DPSIKGTFHW SGNEQMTKYE MACAIADAFN LPSSHLRPIT DSPVIGAQRP KNAQLDCSKL
ETLGIGQRTP FRTGIKESLW PFLIDKRWRQ TVFH
