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Indolethylamine N-methyltransferase (Indolamine N-methyltransferase) (EC 2.1.1.49) (EC 2.1.1.96) (Aromatic alkylamine N-methyltransferase) (Amine N-methyltransferase) (Arylamine N-methyltransferase) (Thioether S-methyltransferase) (TEMT)

 INMT_MOUSE              Reviewed;         264 AA.
P40936; Q9CZ50;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
12-SEP-2018, entry version 130.
RecName: Full=Indolethylamine N-methyltransferase;
Short=Indolamine N-methyltransferase;
EC=2.1.1.49;
EC=2.1.1.96;
AltName: Full=Aromatic alkylamine N-methyltransferase;
Short=Amine N-methyltransferase;
Short=Arylamine N-methyltransferase;
AltName: Full=Thioether S-methyltransferase;
Short=TEMT;
Name=Inmt; Synonyms=Temt;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Lung;
PubMed=7819283; DOI=10.1016/0167-4838(94)00186-K;
Warner D.R., Mozier N.M., Pearson J.D., Hoffman J.L.;
"Cloning and base sequence analysis of a cDNA encoding mouse lung
thioether S-methyltransferase.";
Biochim. Biophys. Acta 1246:160-166(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, ACTIVITY
REGULATION, AND TISSUE SPECIFICITY.
PubMed=3350800;
Mozier N.M., McConnell K.P., Hoffman J.L.;
"S-adenosyl-L-methionine:thioether S-methyltransferase, a new enzyme
in sulfur and selenium metabolism.";
J. Biol. Chem. 263:4527-4531(1988).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Liver, Lung, and Pancreas;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-14 AND LYS-97, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Catalyzes the N-methylation of tryptamine and
structurally related compounds (By similarity). Functions as
thioether S-methyltransferase and is active with a variety of
thioethers and the corresponding selenium and tellurium compounds,
including 3-methylthiopropionaldehyde, dimethyl selenide, dimethyl
telluride, 2-methylthioethylamine, 2-methylthioethanol, methyl-n-
propyl sulfide and diethyl sulfide. Plays an important role in the
detoxification of selenium compounds. {ECO:0000250,
ECO:0000269|PubMed:3350800}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + an amine = S-
adenosyl-L-homocysteine + a methylated amine.
{ECO:0000269|PubMed:3350800}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + dimethyl sulfide =
S-adenosyl-L-homocysteine + trimethylsulfonium.
{ECO:0000269|PubMed:3350800}.
-!- ACTIVITY REGULATION: Inhibited by the S-adenosyl-L-methionine
analog sinefungin and by the product S-adenosyl-L-homocysteine.
{ECO:0000269|PubMed:3350800}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.4 uM for dimethyl selenide;
KM=1.0 uM for dimethyl sulfide;
KM=1.0 uM for S-adenosyl-L-methionine;
pH dependence:
Optimum pH is 6.3.;
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:3350800}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:3350800}.
-!- TISSUE SPECIFICITY: Detected in lung and liver (at protein level).
{ECO:0000269|PubMed:3350800}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. NNMT/PNMT/TEMT family.
{ECO:0000305}.
-!- CAUTION: Was originally thought to be a thioether S-
methyltransferase but appears to be the ortholog of human INMT.
{ECO:0000305|PubMed:7819283}.
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EMBL; M88694; AAA62365.1; -; mRNA.
EMBL; AK002281; BAB21985.1; -; mRNA.
EMBL; AK013010; BAB28594.1; -; mRNA.
EMBL; BC013518; AAH13518.1; -; mRNA.
CCDS; CCDS20163.1; -.
PIR; S52102; S52102.
RefSeq; NP_033375.1; NM_009349.3.
UniGene; Mm.299; -.
ProteinModelPortal; P40936; -.
SMR; P40936; -.
BioGrid; 204112; 1.
IntAct; P40936; 3.
MINT; P40936; -.
STRING; 10090.ENSMUSP00000003569; -.
iPTMnet; P40936; -.
PhosphoSitePlus; P40936; -.
SwissPalm; P40936; -.
MaxQB; P40936; -.
PaxDb; P40936; -.
PeptideAtlas; P40936; -.
PRIDE; P40936; -.
Ensembl; ENSMUST00000003569; ENSMUSP00000003569; ENSMUSG00000003477.
GeneID; 21743; -.
KEGG; mmu:21743; -.
UCSC; uc009can.1; mouse.
CTD; 11185; -.
MGI; MGI:102963; Inmt.
eggNOG; ENOG410IFTZ; Eukaryota.
eggNOG; ENOG41128ZR; LUCA.
GeneTree; ENSGT00390000011708; -.
HOGENOM; HOG000013229; -.
HOVERGEN; HBG000797; -.
InParanoid; P40936; -.
KO; K00562; -.
OMA; YSALCFR; -.
OrthoDB; EOG091G0EF7; -.
PhylomeDB; P40936; -.
TreeFam; TF313114; -.
BRENDA; 2.1.1.96; 3474.
PRO; PR:P40936; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000003477; Expressed in 188 organ(s), highest expression level in lung.
CleanEx; MM_INMT; -.
Genevisible; P40936; MM.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0030748; F:amine N-methyltransferase activity; ISS:UniProtKB.
GO; GO:0098615; F:dimethyl selenide methyltransferase activity; TAS:Reactome.
GO; GO:0102707; F:S-adenosyl-L-methionine:beta-alanine N-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0004790; F:thioether S-methyltransferase activity; IDA:MGI.
GO; GO:0009308; P:amine metabolic process; ISS:UniProtKB.
GO; GO:0032259; P:methylation; ISS:UniProtKB.
GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
InterPro; IPR025820; NNMT/PNMT/TEMT_CS.
InterPro; IPR000940; NNMT_TEMT_trans.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR10867; PTHR10867; 1.
Pfam; PF01234; NNMT_PNMT_TEMT; 1.
PIRSF; PIRSF000384; PNMTase; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS01100; NNMT_PNMT_TEMT; 1.
PROSITE; PS51681; SAM_MT_NNMT_PNMT_TEMT; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Detoxification;
Direct protein sequencing; Methyltransferase; Reference proteome;
S-adenosyl-L-methionine; Transferase.
CHAIN 1 264 Indolethylamine N-methyltransferase.
/FTId=PRO_0000159713.
REGION 64 65 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 143 144 S-adenosyl-L-methionine binding.
{ECO:0000250}.
BINDING 21 21 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 26 26 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 70 70 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 86 86 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 91 91 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 164 164 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250}.
MOD_RES 14 14 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 97 97 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
CONFLICT 92 92 L -> M (in Ref. 2; BAB28594).
{ECO:0000305}.
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


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