INMT_MOUSE
ID INMT_MOUSE Reviewed; 264 AA.
AC P40936; Q9CZ50;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Indolethylamine N-methyltransferase;
DE Short=Indolamine N-methyltransferase;
DE EC=2.1.1.49;
DE EC=2.1.1.96;
DE AltName: Full=Aromatic alkylamine N-methyltransferase;
DE Short=Amine N-methyltransferase;
DE Short=Arylamine N-methyltransferase;
DE AltName: Full=Thioether S-methyltransferase;
DE Short=TEMT;
GN Name=Inmt; Synonyms=Temt;
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 PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Lung;
RX PubMed=7819283; DOI=10.1016/0167-4838(94)00186-k;
RA Warner D.R., Mozier N.M., Pearson J.D., Hoffman J.L.;
RT "Cloning and base sequence analysis of a cDNA encoding mouse lung thioether
RT S-methyltransferase.";
RL Biochim. Biophys. Acta 1246:160-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
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 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 [4]
RP CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, ACTIVITY
RP REGULATION, AND TISSUE SPECIFICITY.
RX PubMed=3350800; DOI=10.1016/s0021-9258(18)68814-3;
RA Mozier N.M., McConnell K.P., Hoffman J.L.;
RT "S-adenosyl-L-methionine:thioether S-methyltransferase, a new enzyme in
RT sulfur and selenium metabolism.";
RL J. Biol. Chem. 263:4527-4531(1988).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, and Pancreas;
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).
RN [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-14 AND LYS-97, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Catalyzes the N-methylation of tryptamine and structurally
CC related compounds (By similarity). Functions as thioether S-
CC methyltransferase and is active with a variety of thioethers and the
CC corresponding selenium and tellurium compounds, including 3-
CC methylthiopropionaldehyde, dimethyl selenide, dimethyl telluride, 2-
CC methylthioethylamine, 2-methylthioethanol, methyl-n-propyl sulfide and
CC diethyl sulfide. Plays an important role in the detoxification of
CC selenium compounds. {ECO:0000250, ECO:0000269|PubMed:3350800}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tertiary amine + S-adenosyl-L-methionine = a methylated
CC tertiary amine + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:53928, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:137982, ChEBI:CHEBI:137983;
CC EC=2.1.1.49; Evidence={ECO:0000269|PubMed:3350800};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary amine + S-adenosyl-L-methionine = a methylated
CC secondary amine + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:53924, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:137419, ChEBI:CHEBI:137984;
CC EC=2.1.1.49; Evidence={ECO:0000269|PubMed:3350800};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary amine + S-adenosyl-L-methionine = a methylated
CC primary amine + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:23136, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:65296, ChEBI:CHEBI:131823;
CC EC=2.1.1.49; Evidence={ECO:0000269|PubMed:3350800};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethyl sulfide + S-adenosyl-L-methionine = S-adenosyl-L-
CC homocysteine + trimethylsulfonium; Xref=Rhea:RHEA:19613,
CC ChEBI:CHEBI:17434, ChEBI:CHEBI:17437, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789; EC=2.1.1.96;
CC Evidence={ECO:0000269|PubMed:3350800};
CC -!- ACTIVITY REGULATION: Inhibited by the S-adenosyl-L-methionine analog
CC sinefungin and by the product S-adenosyl-L-homocysteine.
CC {ECO:0000269|PubMed:3350800}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 uM for dimethyl selenide;
CC KM=1.0 uM for dimethyl sulfide;
CC KM=1.0 uM for S-adenosyl-L-methionine;
CC pH dependence:
CC Optimum pH is 6.3.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:3350800}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:3350800}.
CC -!- TISSUE SPECIFICITY: Detected in lung and liver (at protein level).
CC {ECO:0000269|PubMed:3350800}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. NNMT/PNMT/TEMT family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a thioether S-methyltransferase
CC but appears to be the ortholog of human INMT.
CC {ECO:0000305|PubMed:7819283}.
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DR EMBL; M88694; AAA62365.1; -; mRNA.
DR EMBL; AK002281; BAB21985.1; -; mRNA.
DR EMBL; AK013010; BAB28594.1; -; mRNA.
DR EMBL; BC013518; AAH13518.1; -; mRNA.
DR CCDS; CCDS20163.1; -.
DR PIR; S52102; S52102.
DR RefSeq; NP_033375.1; NM_009349.3.
DR AlphaFoldDB; P40936; -.
DR SMR; P40936; -.
DR BioGRID; 204112; 1.
DR IntAct; P40936; 2.
DR MINT; P40936; -.
DR STRING; 10090.ENSMUSP00000003569; -.
DR iPTMnet; P40936; -.
DR PhosphoSitePlus; P40936; -.
DR SwissPalm; P40936; -.
DR jPOST; P40936; -.
DR MaxQB; P40936; -.
DR PaxDb; P40936; -.
DR PeptideAtlas; P40936; -.
DR PRIDE; P40936; -.
DR ProteomicsDB; 267338; -.
DR DNASU; 21743; -.
DR Ensembl; ENSMUST00000003569; ENSMUSP00000003569; ENSMUSG00000003477.
DR GeneID; 21743; -.
DR KEGG; mmu:21743; -.
DR UCSC; uc009can.1; mouse.
DR CTD; 11185; -.
DR MGI; MGI:102963; Inmt.
DR VEuPathDB; HostDB:ENSMUSG00000003477; -.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00390000011708; -.
DR HOGENOM; CLU_082526_1_1_1; -.
DR InParanoid; P40936; -.
DR OMA; CFVVARK; -.
DR OrthoDB; 1054662at2759; -.
DR PhylomeDB; P40936; -.
DR TreeFam; TF313114; -.
DR BRENDA; 2.1.1.96; 3474.
DR BioGRID-ORCS; 21743; 1 hit in 74 CRISPR screens.
DR PRO; PR:P40936; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P40936; protein.
DR Bgee; ENSMUSG00000003477; Expressed in right lung lobe and 146 other tissues.
DR Genevisible; P40936; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0030748; F:amine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0098615; F:dimethyl selenide methyltransferase activity; TAS:Reactome.
DR GO; GO:0008170; F:N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0102707; F:S-adenosyl-L-methionine:beta-alanine N-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004790; F:thioether S-methyltransferase activity; IDA:MGI.
DR GO; GO:0009308; P:amine metabolic process; ISS:UniProtKB.
DR GO; GO:0032259; P:methylation; ISS:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025820; NNMT/PNMT/TEMT_CS.
DR InterPro; IPR000940; NNMT_TEMT_trans.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10867; PTHR10867; 1.
DR Pfam; PF01234; NNMT_PNMT_TEMT; 1.
DR PIRSF; PIRSF000384; PNMTase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS01100; NNMT_PNMT_TEMT; 1.
DR PROSITE; PS51681; SAM_MT_NNMT_PNMT_TEMT; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Detoxification; Direct protein sequencing; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..264
FT /note="Indolethylamine N-methyltransferase"
FT /id="PRO_0000159713"
FT BINDING 21
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 26
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 64..65
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 143..144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 14
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 97
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 92
FT /note="L -> M (in Ref. 2; BAB28594)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 264 AA; 29460 MW; 58AC5BA580AFB2EE CRC64;
MEGKVYIGGE DYEKEFTPKD YLTTYYSFHS GPVAEQEIVK FSLQNLYQTF STGGVGGDVL
IDIGSGPTIY QLLSACEVFR EIIVTDYTPQ NLQELQKWLK KEPGAYDWSS IVQHACELEG
DRSRWQEKEA KLRRTVTRVL RCDVTKTPPL GSAQVPLADC VLTFLAMECA CPDIDTYRAA
LRRLAGLLKP GGHLVTLVTL RFQHYMVGPK KFSGVYLEKE VVEKAIQDAG CQVLKCNCVS
LSYSEAYCSH DGLCFVVARK GPSA
