Skip Header

Contribute Send feedback
Read comments (?) or add your own

P40936 (INMT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Indolethylamine N-methyltransferase
Short name=Indolamine N-methyltransferase
EC=2.1.1.49
EC=2.1.1.96
Alternative name(s):
Aromatic alkylamine N-methyltransferase
Short name=Amine N-methyltransferase
Short name=Arylamine N-methyltransferase
Thioether S-methyltransferase
Short name=TEMT
Gene names
Name:Inmt
Synonyms:Temt
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.4

Catalytic activity

S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine. Ref.4

S-adenosyl-L-methionine + dimethyl sulfide = S-adenosyl-L-homocysteine + trimethylsulfonium. Ref.4

Enzyme regulation

Inhibited by the S-adenosyl-L-methionine analog sinefungin and by the product S-adenosyl-L-homocysteine. Ref.4

Subunit structure

Monomer. Ref.4

Subcellular location

Cytoplasm Ref.4.

Tissue specificity

Detected in lung and liver (at protein level). Ref.4

Sequence similarities

Belongs to the NNMT/PNMT/TEMT family.

Caution

Was originally (Ref.1) thought to be a thioether S-methyltransferase but appears to be the ortholog of human INMT.

Biophysicochemical properties

Kinetic parameters:

KM=0.4 µM for dimethyl selenide

KM=1.0 µM for dimethyl sulfide

KM=1.0 µM for S-adenosyl-L-methionine

pH dependence:

Optimum pH is 6.3.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 264264Indolethylamine N-methyltransferase
PRO_0000159713

Regions

Region64 – 652S-adenosyl-L-methionine binding By similarity
Region143 – 1442S-adenosyl-L-methionine binding By similarity

Sites

Binding site211S-adenosyl-L-methionine By similarity
Binding site261S-adenosyl-L-methionine By similarity
Binding site701S-adenosyl-L-methionine By similarity
Binding site861S-adenosyl-L-methionine By similarity
Binding site911S-adenosyl-L-methionine By similarity
Binding site1641S-adenosyl-L-methionine; via carbonyl oxygen By similarity

Experimental info

Sequence conflict921L → M in BAB28594. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P40936 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 58AC5BA580AFB2EE

FASTA26429,460
        10         20         30         40         50         60 
MEGKVYIGGE DYEKEFTPKD YLTTYYSFHS GPVAEQEIVK FSLQNLYQTF STGGVGGDVL 

        70         80         90        100        110        120 
IDIGSGPTIY QLLSACEVFR EIIVTDYTPQ NLQELQKWLK KEPGAYDWSS IVQHACELEG 

       130        140        150        160        170        180 
DRSRWQEKEA KLRRTVTRVL RCDVTKTPPL GSAQVPLADC VLTFLAMECA CPDIDTYRAA 

       190        200        210        220        230        240 
LRRLAGLLKP GGHLVTLVTL RFQHYMVGPK KFSGVYLEKE VVEKAIQDAG CQVLKCNCVS 

       250        260 
LSYSEAYCSH DGLCFVVARK GPSA

« Hide

References

« Hide 'large scale' references
[1]"Cloning and base sequence analysis of a cDNA encoding mouse lung thioether S-methyltransferase."
Warner D.R., Mozier N.M., Pearson J.D., Hoffman J.L.
Biochim. Biophys. Acta 1246:160-166(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Lung.
[2]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo and Kidney.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney.
[4]"S-adenosyl-L-methionine:thioether S-methyltransferase, a new enzyme in sulfur and selenium metabolism."
Mozier N.M., McConnell K.P., Hoffman J.L.
J. Biol. Chem. 263:4527-4531(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, ENZYME REGULATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M88694 mRNA. Translation: AAA62365.1.
AK002281 mRNA. Translation: BAB21985.1.
AK013010 mRNA. Translation: BAB28594.1.
BC013518 mRNA. Translation: AAH13518.1.
IPIIPI00114628.
PIRS52102.
RefSeqNP_033375.1. NM_009349.3.
UniGeneMm.299.

3D structure databases

ProteinModelPortalP40936.
SMRP40936. Positions 6-262.
ModBaseSearch...

Protein-protein interaction databases

IntActP40936. 1 interaction.
STRING10090.ENSMUSP00000003569.

PTM databases

PhosphoSiteP40936.

Proteomic databases

PaxDbP40936.
PRIDEP40936.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000003569; ENSMUSP00000003569; ENSMUSG00000003477.
GeneID21743.
KEGGmmu:21743.
UCSCuc009can.1. mouse.

Organism-specific databases

CTD11185.
MGIMGI:102963. Inmt.

Phylogenomic databases

eggNOGNOG71857.
GeneTreeENSGT00390000011708.
HOGENOMHOG000013229.
HOVERGENHBG000797.
InParanoidP40936.
KOK00562.
OMALEYSCET.
OrthoDBEOG49079M.

Enzyme and pathway databases

BRENDA2.1.1.96. 3474.

Gene expression databases

BgeeP40936.
CleanExMM_INMT.
GenevestigatorP40936.
GermOnlineENSMUSG00000003477. Mus musculus.

Family and domain databases

InterProIPR025817. Amine_MeTrfase.
IPR025820. NNMT/PNMT/TEMT_CS.
IPR000940. NNMT_TEMT_trans.
[Graphical view]
PANTHERPTHR10867. PTHR10867. 1 hit.
PfamPF01234. NNMT_PNMT_TEMT. 1 hit.
[Graphical view]
PIRSFPIRSF000384. PNMTase. 1 hit.
PROSITEPS01100. NNMT_PNMT_TEMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio301024.
SOURCESearch...

Entry information

Entry nameINMT_MOUSE
AccessionPrimary (citable) accession number: P40936
Secondary accession number(s): Q9CZ50
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents