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Protein

Indolethylamine N-methyltransferase

Gene

Inmt

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

Catalytic activityi

S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine.1 Publication
S-adenosyl-L-methionine + dimethyl sulfide = S-adenosyl-L-homocysteine + trimethylsulfonium.1 Publication

Enzyme regulationi

Inhibited by the S-adenosyl-L-methionine analog sinefungin and by the product S-adenosyl-L-homocysteine.1 Publication

Kineticsi

  1. KM=0.4 µM for dimethyl selenide
  2. KM=1.0 µM for dimethyl sulfide
  3. KM=1.0 µM for S-adenosyl-L-methionine

pH dependencei

Optimum pH is 6.3.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei21 – 211S-adenosyl-L-methionineBy similarity
Binding sitei26 – 261S-adenosyl-L-methionineBy similarity
Binding sitei70 – 701S-adenosyl-L-methionineBy similarity
Binding sitei86 – 861S-adenosyl-L-methionineBy similarity
Binding sitei91 – 911S-adenosyl-L-methionineBy similarity
Binding sitei164 – 1641S-adenosyl-L-methionine; via carbonyl oxygenBy similarity

GO - Molecular functioni

  1. amine N-methyltransferase activity Source: UniProtKB
  2. thioether S-methyltransferase activity Source: MGI

GO - Biological processi

  1. amine metabolic process Source: UniProtKB
  2. methylation Source: UniProtKB
  3. response to toxic substance Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Detoxification

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.96. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Indolethylamine N-methyltransferase (EC:2.1.1.49, EC:2.1.1.96)
Short name:
Indolamine N-methyltransferase
Alternative name(s):
Aromatic alkylamine N-methyltransferase
Short name:
Amine N-methyltransferase
Short name:
Arylamine N-methyltransferase
Thioether S-methyltransferase
Short name:
TEMT
Gene namesi
Name:Inmt
Synonyms:Temt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:102963. Inmt.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytosol Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 264264Indolethylamine N-methyltransferasePRO_0000159713Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141N6-succinyllysine1 Publication
Modified residuei97 – 971N6-succinyllysine1 Publication

Proteomic databases

MaxQBiP40936.
PaxDbiP40936.
PRIDEiP40936.

PTM databases

PhosphoSiteiP40936.

Expressioni

Tissue specificityi

Detected in lung and liver (at protein level).1 Publication

Gene expression databases

BgeeiP40936.
CleanExiMM_INMT.
GenevestigatoriP40936.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi204112. 1 interaction.
IntActiP40936. 3 interactions.
MINTiMINT-1869696.
STRINGi10090.ENSMUSP00000003569.

Structurei

3D structure databases

ProteinModelPortaliP40936.
SMRiP40936. Positions 6-262.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni64 – 652S-adenosyl-L-methionine bindingBy similarity
Regioni143 – 1442S-adenosyl-L-methionine bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG71857.
GeneTreeiENSGT00390000011708.
HOGENOMiHOG000013229.
HOVERGENiHBG000797.
InParanoidiP40936.
KOiK00562.
OMAiRWVNNES.
OrthoDBiEOG7673B9.
PhylomeDBiP40936.
TreeFamiTF313114.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025820. NNMT/PNMT/TEMT_CS.
IPR000940. NNMT_TEMT_trans.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10867. PTHR10867. 1 hit.
PfamiPF01234. NNMT_PNMT_TEMT. 1 hit.
[Graphical view]
PIRSFiPIRSF000384. PNMTase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS01100. NNMT_PNMT_TEMT. 1 hit.
PS51681. SAM_MT_NNMT_PNMT_TEMT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40936-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEGKVYIGGE DYEKEFTPKD YLTTYYSFHS GPVAEQEIVK FSLQNLYQTF
60 70 80 90 100
STGGVGGDVL IDIGSGPTIY QLLSACEVFR EIIVTDYTPQ NLQELQKWLK
110 120 130 140 150
KEPGAYDWSS IVQHACELEG DRSRWQEKEA KLRRTVTRVL RCDVTKTPPL
160 170 180 190 200
GSAQVPLADC VLTFLAMECA CPDIDTYRAA LRRLAGLLKP GGHLVTLVTL
210 220 230 240 250
RFQHYMVGPK KFSGVYLEKE VVEKAIQDAG CQVLKCNCVS LSYSEAYCSH
260
DGLCFVVARK GPSA
Length:264
Mass (Da):29,460
Last modified:February 1, 1995 - v1
Checksum:i58AC5BA580AFB2EE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921L → M in BAB28594. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88694 mRNA. Translation: AAA62365.1.
AK002281 mRNA. Translation: BAB21985.1.
AK013010 mRNA. Translation: BAB28594.1.
BC013518 mRNA. Translation: AAH13518.1.
CCDSiCCDS20163.1.
PIRiS52102.
RefSeqiNP_033375.1. NM_009349.3.
UniGeneiMm.299.

Genome annotation databases

EnsembliENSMUST00000003569; ENSMUSP00000003569; ENSMUSG00000003477.
GeneIDi21743.
KEGGimmu:21743.
UCSCiuc009can.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88694 mRNA. Translation: AAA62365.1.
AK002281 mRNA. Translation: BAB21985.1.
AK013010 mRNA. Translation: BAB28594.1.
BC013518 mRNA. Translation: AAH13518.1.
CCDSiCCDS20163.1.
PIRiS52102.
RefSeqiNP_033375.1. NM_009349.3.
UniGeneiMm.299.

3D structure databases

ProteinModelPortaliP40936.
SMRiP40936. Positions 6-262.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204112. 1 interaction.
IntActiP40936. 3 interactions.
MINTiMINT-1869696.
STRINGi10090.ENSMUSP00000003569.

PTM databases

PhosphoSiteiP40936.

Proteomic databases

MaxQBiP40936.
PaxDbiP40936.
PRIDEiP40936.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003569; ENSMUSP00000003569; ENSMUSG00000003477.
GeneIDi21743.
KEGGimmu:21743.
UCSCiuc009can.1. mouse.

Organism-specific databases

CTDi11185.
MGIiMGI:102963. Inmt.

Phylogenomic databases

eggNOGiNOG71857.
GeneTreeiENSGT00390000011708.
HOGENOMiHOG000013229.
HOVERGENiHBG000797.
InParanoidiP40936.
KOiK00562.
OMAiRWVNNES.
OrthoDBiEOG7673B9.
PhylomeDBiP40936.
TreeFamiTF313114.

Enzyme and pathway databases

BRENDAi2.1.1.96. 3474.

Miscellaneous databases

NextBioi301024.
PROiP40936.
SOURCEiSearch...

Gene expression databases

BgeeiP40936.
CleanExiMM_INMT.
GenevestigatoriP40936.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025820. NNMT/PNMT/TEMT_CS.
IPR000940. NNMT_TEMT_trans.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10867. PTHR10867. 1 hit.
PfamiPF01234. NNMT_PNMT_TEMT. 1 hit.
[Graphical view]
PIRSFiPIRSF000384. PNMTase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS01100. NNMT_PNMT_TEMT. 1 hit.
PS51681. SAM_MT_NNMT_PNMT_TEMT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    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.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-14 AND LYS-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiINMT_MOUSE
AccessioniPrimary (citable) accession number: P40936
Secondary accession number(s): Q9CZ50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 4, 2015
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.