AS3MT_MOUSE
ID AS3MT_MOUSE Reviewed; 376 AA.
AC Q91WU5; A6H5W4; E9QLU6; Q9QZT1;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Arsenite methyltransferase;
DE EC=2.1.1.137 {ECO:0000250|UniProtKB:Q8VHT6};
DE AltName: Full=Methylarsonite methyltransferase;
DE AltName: Full=S-adenosyl-L-methionine:arsenic(III) methyltransferase;
GN Name=As3mt; Synonyms=Cyt19;
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].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Phillips R.L., Ernst R.E., Dosil M., Wesley C.K., Moore K.A.,
RA Kingsley P.D., Sykes S., Palis J., Lemischka I.R.;
RT "Identification of novel hematopoietic stem cell regulatory genes.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, and Colon;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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: Catalyzes the transfer of a methyl group from AdoMet to
CC trivalent arsenicals producing methylated and dimethylated arsenicals.
CC It methylates arsenite to form methylarsonate, Me-AsO(3)H(2), which is
CC reduced by methylarsonate reductase to methylarsonite, Me-As(OH)2.
CC Methylarsonite is also a substrate and it is converted into the much
CC less toxic compound dimethylarsinate (cacodylate), Me(2)As(O)-OH.
CC {ECO:0000250|UniProtKB:Q8VHT6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + arsenic triglutathione + 2 H2O + S-
CC adenosyl-L-methionine = [thioredoxin]-disulfide + 3 glutathione +
CC H(+) + methylarsonous acid + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:69460, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17826,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:59789, ChEBI:CHEBI:183640;
CC EC=2.1.1.137; Evidence={ECO:0000250|UniProtKB:Q8VHT6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 [thioredoxin]-dithiol + arsenic triglutathione + H2O + 2 S-
CC adenosyl-L-methionine = 2 [thioredoxin]-disulfide + dimethylarsinous
CC acid + 3 glutathione + 2 H(+) + 2 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:69464, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:23808,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:59789, ChEBI:CHEBI:183640;
CC EC=2.1.1.137; Evidence={ECO:0000250|UniProtKB:Q8VHT6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 [thioredoxin]-dithiol + arsenic triglutathione + 3 S-
CC adenosyl-L-methionine = 3 [thioredoxin]-disulfide + 3 glutathione + 3
CC H(+) + 3 S-adenosyl-L-homocysteine + trimethylarsine;
CC Xref=Rhea:RHEA:69432, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27130, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:50058, ChEBI:CHEBI:57856, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:183640; EC=2.1.1.137;
CC Evidence={ECO:0000250|UniProtKB:Q8VHT6};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8VHT6}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Arsenite
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; AF166383; AAF00618.1; -; mRNA.
DR EMBL; AC161865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC145663; AAI45664.1; -; mRNA.
DR EMBL; BC013468; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS50458.1; -.
DR PIR; T44795; T44795.
DR RefSeq; NP_065602.2; NM_020577.2.
DR AlphaFoldDB; Q91WU5; -.
DR SMR; Q91WU5; -.
DR BioGRID; 208264; 1.
DR STRING; 10090.ENSMUSP00000003655; -.
DR iPTMnet; Q91WU5; -.
DR PhosphoSitePlus; Q91WU5; -.
DR SwissPalm; Q91WU5; -.
DR EPD; Q91WU5; -.
DR jPOST; Q91WU5; -.
DR MaxQB; Q91WU5; -.
DR PaxDb; Q91WU5; -.
DR PeptideAtlas; Q91WU5; -.
DR PRIDE; Q91WU5; -.
DR ProteomicsDB; 281808; -.
DR Antibodypedia; 2804; 144 antibodies from 32 providers.
DR DNASU; 57344; -.
DR Ensembl; ENSMUST00000003655; ENSMUSP00000003655; ENSMUSG00000003559.
DR GeneID; 57344; -.
DR KEGG; mmu:57344; -.
DR UCSC; uc008huc.1; mouse.
DR CTD; 57412; -.
DR MGI; MGI:1929882; As3mt.
DR VEuPathDB; HostDB:ENSMUSG00000003559; -.
DR eggNOG; ENOG502QQD6; Eukaryota.
DR GeneTree; ENSGT00390000001742; -.
DR HOGENOM; CLU_052868_0_1_1; -.
DR InParanoid; Q91WU5; -.
DR OMA; PVCGNTW; -.
DR OrthoDB; 1025394at2759; -.
DR PhylomeDB; Q91WU5; -.
DR TreeFam; TF343797; -.
DR BRENDA; 2.1.1.137; 3474.
DR Reactome; R-MMU-156581; Methylation.
DR BioGRID-ORCS; 57344; 0 hits in 59 CRISPR screens.
DR ChiTaRS; As3mt; mouse.
DR PRO; PR:Q91WU5; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q91WU5; protein.
DR Bgee; ENSMUSG00000003559; Expressed in yolk sac and 230 other tissues.
DR ExpressionAtlas; Q91WU5; baseline and differential.
DR Genevisible; Q91WU5; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0030791; F:arsenite methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0030792; F:methylarsonite methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0018872; P:arsonoacetate metabolic process; ISS:UniProtKB.
DR GO; GO:0032259; P:methylation; ISO:MGI.
DR GO; GO:0046685; P:response to arsenic-containing substance; ISO:MGI.
DR GO; GO:0009404; P:toxin metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR026669; Arsenite_MeTrfase-like.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43675; PTHR43675; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..376
FT /note="Arsenite methyltransferase"
FT /id="PRO_0000204448"
FT REGION 354..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHT6"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBK9"
FT CONFLICT 106
FT /note="E -> K (in Ref. 3; AAI45664)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="D -> G (in Ref. 1; AAF00618)"
FT /evidence="ECO:0000305"
FT CONFLICT 335..346
FT /note="Missing (in Ref. 1; AAF00618)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 41794 MW; 9421A663FCC825E5 CRC64;
MAASRDADEI HKDVQNYYGN VLKTSADLQT NACVTRAKPV PSYIRESLQN VHEDVSSRYY
GCGLTVPERL ENCRILDLGS GSGRDCYVLS QLVGEKGHVT GIDMTEVQVE VAKTYLEHHM
EKFGFQAPNV TFLHGRIEKL AEAGIQSESY DIVISNCVIN LVPDKQQVLQ EVYRVLKHGG
ELYFSDVYAS LEVPEDIKSH KVLWGECLGG ALYWKDLAII AQKIGFCPPR LVTADIITVE
NKELEGVLGD CRFVSATFRL FKLPKTEPAE RCRVVYNGGI KGHEKELIFD ANFTFKEGEA
VAVDEETAAV LKNSRFAPDF LFTPVDASLP APQGRSELET KVLIRDPFKL AEDSDKMKPR
HAPEGTGGCC GKRKNC
