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   02-SEP-2026, entry version 163.
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 a 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 + S-adenosyl-L-homocysteine + H(+);
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 + S-adenosyl-L-homocysteine + H(+);
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 + S-adenosyl-L-homocysteine + H(+);
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 =
CC         trimethylsulfonium + S-adenosyl-L-homocysteine; 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 uM for dimethyl sulfide;
CC         KM=1 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   FunCoup; P40936; 346.
DR   IntAct; P40936; 2.
DR   MINT; P40936; -.
DR   STRING; 10090.ENSMUSP00000003569; -.
DR   GlyGen; P40936; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P40936; -.
DR   PhosphoSitePlus; P40936; -.
DR   SwissPalm; P40936; -.
DR   jPOST; P40936; -.
DR   PaxDb; 10090-ENSMUSP00000003569; -.
DR   PeptideAtlas; P40936; -.
DR   ProteomicsDB; 267338; -.
DR   DNASU; 21743; -.
DR   Ensembl; ENSMUST00000003569.6; ENSMUSP00000003569.6; ENSMUSG00000003477.6.
DR   GeneID; 21743; -.
DR   KEGG; mmu:21743; -.
DR   UCSC; uc009can.1; mouse.
DR   AGR; MGI:102963; -.
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; RSQHYMV; -.
DR   OrthoDB; 10050085at2759; -.
DR   PhylomeDB; P40936; -.
DR   BRENDA; 2.1.1.96; 3474.
DR   BioGRID-ORCS; 21743; 1 hit in 79 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 cell types or tissues.
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; IDA:MGI.
DR   GO; GO:0098613; F:methaneselenol methyltransferase activity; ISO:MGI.
DR   GO; GO:0008170; F:N-methyltransferase activity; IBA:GO_Central.
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:0001887; P:selenium compound metabolic process; IDA:MGI.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   FunFam; 3.40.50.150:FF:000065; Phenylethanolamine N-methyltransferase; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR025820; NNMT/PNMT/TEMT_CS.
DR   InterPro; IPR000940; NNMT_TEMT_trans.
DR   InterPro; IPR053384; SAM-dep_methyltransferase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; NF041360; GntF_guanitoxin; 1.
DR   PANTHER; PTHR10867:SF33; INDOLETHYLAMINE N-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10867; NNMT/PNMT/TEMT FAMILY MEMBER; 1.
DR   Pfam; PF01234; NNMT_PNMT_TEMT; 1.
DR   PIRSF; PIRSF000384; PNMTase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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
//