Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

    • amine N-methyltransferase activity Source: UniProtKB
    • thioether S-methyltransferase activity Source: MGI

    GO - Biological processi

    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 Componenti: Chromosome 6

    Organism-specific databases

    MGIiMGI:102963. Inmt.

    Subcellular locationi

    • Cytoplasm 1 Publication

    GO - Cellular componenti

    • 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.
    GenevisibleiP40936. MM.

    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.
    GenevisibleiP40936. MM.

    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: June 24, 2015
    This is version 112 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.