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P40936

- INMT_MOUSE

UniProt

P40936 - INMT_MOUSE

Protein

Indolethylamine N-methyltransferase

Gene

Inmt

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    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

    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

    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

    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.
    OMAiLEYSCET.
    OrthoDBiEOG7673B9.
    PhylomeDBiP40936.
    TreeFamiTF313114.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR025817. Amine_MeTrfase.
    IPR025820. NNMT/PNMT/TEMT_CS.
    IPR000940. NNMT_TEMT_trans.
    IPR029063. SAM-dependent_MTases-like.
    [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

    MEGKVYIGGE DYEKEFTPKD YLTTYYSFHS GPVAEQEIVK FSLQNLYQTF    50
    STGGVGGDVL IDIGSGPTIY QLLSACEVFR EIIVTDYTPQ NLQELQKWLK 100
    KEPGAYDWSS IVQHACELEG DRSRWQEKEA KLRRTVTRVL RCDVTKTPPL 150
    GSAQVPLADC VLTFLAMECA CPDIDTYRAA LRRLAGLLKP GGHLVTLVTL 200
    RFQHYMVGPK KFSGVYLEKE VVEKAIQDAG CQVLKCNCVS LSYSEAYCSH 250
    DGLCFVVARK GPSA 264
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M88694 mRNA. Translation: AAA62365.1 .
    AK002281 mRNA. Translation: BAB21985.1 .
    AK013010 mRNA. Translation: BAB28594.1 .
    BC013518 mRNA. Translation: AAH13518.1 .
    CCDSi CCDS20163.1.
    PIRi S52102.
    RefSeqi NP_033375.1. NM_009349.3.
    UniGenei Mm.299.

    3D structure databases

    ProteinModelPortali P40936.
    SMRi P40936. Positions 6-262.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P40936. 3 interactions.
    MINTi MINT-1869696.
    STRINGi 10090.ENSMUSP00000003569.

    PTM databases

    PhosphoSitei P40936.

    Proteomic databases

    MaxQBi P40936.
    PaxDbi P40936.
    PRIDEi P40936.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000003569 ; ENSMUSP00000003569 ; ENSMUSG00000003477 .
    GeneIDi 21743.
    KEGGi mmu:21743.
    UCSCi uc009can.1. mouse.

    Organism-specific databases

    CTDi 11185.
    MGIi MGI:102963. Inmt.

    Phylogenomic databases

    eggNOGi NOG71857.
    GeneTreei ENSGT00390000011708.
    HOGENOMi HOG000013229.
    HOVERGENi HBG000797.
    InParanoidi P40936.
    KOi K00562.
    OMAi LEYSCET.
    OrthoDBi EOG7673B9.
    PhylomeDBi P40936.
    TreeFami TF313114.

    Enzyme and pathway databases

    BRENDAi 2.1.1.96. 3474.

    Miscellaneous databases

    NextBioi 301024.
    PROi P40936.
    SOURCEi Search...

    Gene expression databases

    Bgeei P40936.
    CleanExi MM_INMT.
    Genevestigatori P40936.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR025817. Amine_MeTrfase.
    IPR025820. NNMT/PNMT/TEMT_CS.
    IPR000940. NNMT_TEMT_trans.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    PANTHERi PTHR10867. PTHR10867. 1 hit.
    Pfami PF01234. NNMT_PNMT_TEMT. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000384. PNMTase. 1 hit.
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS01100. NNMT_PNMT_TEMT. 1 hit.
    PS51681. SAM_MT_NNMT_PNMT_TEMT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 109 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