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O88587

- COMT_MOUSE

UniProt

O88587 - COMT_MOUSE

Protein

Catechol O-methyltransferase

Gene

Comt

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (03 Oct 2012)
      Previous versions | rss
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    Functioni

    Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol.

    Catalytic activityi

    S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol.

    Cofactori

    Binds 1 magnesium ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei85 – 851S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
    Binding sitei107 – 1071S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei115 – 1151S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei133 – 1331S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei134 – 1341S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
    Binding sitei162 – 1621S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
    Metal bindingi184 – 1841MagnesiumBy similarity
    Binding sitei184 – 1841S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei187 – 1871SubstrateBy similarity
    Metal bindingi212 – 2121MagnesiumBy similarity
    Metal bindingi213 – 2131MagnesiumBy similarity
    Binding sitei213 – 2131SubstrateBy similarity
    Binding sitei242 – 2421SubstrateBy similarity

    GO - Molecular functioni

    1. catechol O-methyltransferase activity Source: MGI
    2. magnesium ion binding Source: InterPro

    GO - Biological processi

    1. catechol-containing compound metabolic process Source: MGI
    2. cellular response to phosphate starvation Source: MGI
    3. dopamine catabolic process Source: MGI
    4. dopamine metabolic process Source: MGI
    5. estrogen metabolic process Source: Ensembl
    6. female pregnancy Source: Ensembl
    7. learning Source: Ensembl
    8. multicellular organismal reproductive process Source: Ensembl
    9. negative regulation of dopamine metabolic process Source: Ensembl
    10. negative regulation of smooth muscle cell proliferation Source: Ensembl
    11. neurotransmitter catabolic process Source: UniProtKB-KW
    12. positive regulation of homocysteine metabolic process Source: Ensembl
    13. response to drug Source: Ensembl
    14. response to lipopolysaccharide Source: Ensembl
    15. response to organic cyclic compound Source: Ensembl
    16. response to pain Source: Ensembl

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Catecholamine metabolism, Neurotransmitter degradation

    Keywords - Ligandi

    Magnesium, Metal-binding, S-adenosyl-L-methionine

    Enzyme and pathway databases

    SABIO-RKO88587.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Catechol O-methyltransferase (EC:2.1.1.6)
    Gene namesi
    Name:Comt
    Synonyms:Comt1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 16

    Organism-specific databases

    MGIiMGI:88470. Comt.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. mitochondrion Source: MGI
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi51 – 511R → L: Reduces methyltransferase activity against norepinephrine. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 265265Catechol O-methyltransferasePRO_0000020973Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei261 – 2611Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiO88587.
    PRIDEiO88587.

    PTM databases

    PhosphoSiteiO88587.

    Expressioni

    Gene expression databases

    ArrayExpressiO88587.
    GenevestigatoriO88587.

    Interactioni

    Protein-protein interaction databases

    IntActiO88587. 3 interactions.
    MINTiMINT-1854931.
    STRINGi10090.ENSMUSP00000111272.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4P7FX-ray1.37A44-265[»]
    ProteinModelPortaliO88587.
    SMRiO88587. Positions 47-258.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei3 – 1917Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni160 – 1634S-adenosyl-L-methionine bindingPROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG4122.
    GeneTreeiENSGT00390000011316.
    HOGENOMiHOG000046392.
    HOVERGENiHBG005376.
    InParanoidiO88587.
    KOiK00545.
    OMAiCTHYSSY.
    OrthoDBiEOG7PZRZJ.
    TreeFamiTF329140.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR025782. Catechol_O-MeTrfase.
    IPR017128. Catechol_O-MeTrfase_euk.
    IPR002935. O-MeTrfase_3.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PANTHERiPTHR10509. PTHR10509. 1 hit.
    PfamiPF01596. Methyltransf_3. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037177. Catechol_O-mtfrase_euk. 1 hit.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS51682. SAM_OMT_I. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform Membrane-bound (identifier: O88587-1) [UniParc]FASTAAdd to Basket

    Also known as: MB-COMT

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLLAAVSLGL LLLAFLLLLR HLGWGLVAIG WFEFVQQPVH NLLMGGTKEQ    50
    RILRHVQQHA KPGDPQSVLE AIDTYCSEKE WAMNVGDAKG QIMDAVIREY 100
    RPSLVLELGA YCGYSAVRMA RLLPPGARLL TMEINPDYAA ITQQMLDFAG 150
    LQDKVSILIG ASQDLIPQLK KKYDVDTLDM VFLDHWKDRY LPDTLLLEEC 200
    GLLRKGTVLL ADNVIVPGTP DFLAYVRGSS SFECTHYSSY LEYMKVVDGL 250
    EKAVYQGPGS SPVKS 265
    Length:265
    Mass (Da):29,486
    Last modified:October 3, 2012 - v2
    Checksum:iE82E9307F6D8A6CF
    GO
    Isoform Soluble (identifier: O88587-2) [UniParc]FASTAAdd to Basket

    Also known as: S-COMT

    The sequence of this isoform differs from the canonical sequence as follows:
         1-43: Missing.

    Show »
    Length:222
    Mass (Da):24,707
    Checksum:iC7D5BB1ADC5B40B2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti162 – 1621S → P in AAC33334. (PubMed:9707588)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4343Missing in isoform Soluble. CuratedVSP_018779Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF076156 mRNA. Translation: AAC33334.1.
    AK148311 mRNA. Translation: BAE28473.1.
    AC133487 Genomic DNA. No translation available.
    BC010402 mRNA. Translation: AAH10402.1.
    CCDSiCCDS28021.1. [O88587-1]
    RefSeqiNP_001104532.1. NM_001111062.1. [O88587-1]
    NP_001104533.1. NM_001111063.1. [O88587-1]
    NP_031770.2. NM_007744.3. [O88587-1]
    UniGeneiMm.100940.

    Genome annotation databases

    EnsembliENSMUST00000000335; ENSMUSP00000000335; ENSMUSG00000000326. [O88587-1]
    ENSMUST00000115609; ENSMUSP00000111272; ENSMUSG00000000326. [O88587-1]
    ENSMUST00000165430; ENSMUSP00000130077; ENSMUSG00000000326. [O88587-1]
    ENSMUST00000183626; ENSMUSP00000138930; ENSMUSG00000098892. [O88587-1]
    ENSMUST00000185030; ENSMUSP00000139196; ENSMUSG00000098892. [O88587-1]
    GeneIDi12846.
    KEGGimmu:12846.
    UCSCiuc007ynu.2. mouse.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF076156 mRNA. Translation: AAC33334.1 .
    AK148311 mRNA. Translation: BAE28473.1 .
    AC133487 Genomic DNA. No translation available.
    BC010402 mRNA. Translation: AAH10402.1 .
    CCDSi CCDS28021.1. [O88587-1 ]
    RefSeqi NP_001104532.1. NM_001111062.1. [O88587-1 ]
    NP_001104533.1. NM_001111063.1. [O88587-1 ]
    NP_031770.2. NM_007744.3. [O88587-1 ]
    UniGenei Mm.100940.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4P7F X-ray 1.37 A 44-265 [» ]
    ProteinModelPortali O88587.
    SMRi O88587. Positions 47-258.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O88587. 3 interactions.
    MINTi MINT-1854931.
    STRINGi 10090.ENSMUSP00000111272.

    PTM databases

    PhosphoSitei O88587.

    Proteomic databases

    PaxDbi O88587.
    PRIDEi O88587.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000000335 ; ENSMUSP00000000335 ; ENSMUSG00000000326 . [O88587-1 ]
    ENSMUST00000115609 ; ENSMUSP00000111272 ; ENSMUSG00000000326 . [O88587-1 ]
    ENSMUST00000165430 ; ENSMUSP00000130077 ; ENSMUSG00000000326 . [O88587-1 ]
    ENSMUST00000183626 ; ENSMUSP00000138930 ; ENSMUSG00000098892 . [O88587-1 ]
    ENSMUST00000185030 ; ENSMUSP00000139196 ; ENSMUSG00000098892 . [O88587-1 ]
    GeneIDi 12846.
    KEGGi mmu:12846.
    UCSCi uc007ynu.2. mouse.

    Organism-specific databases

    CTDi 1312.
    MGIi MGI:88470. Comt.

    Phylogenomic databases

    eggNOGi COG4122.
    GeneTreei ENSGT00390000011316.
    HOGENOMi HOG000046392.
    HOVERGENi HBG005376.
    InParanoidi O88587.
    KOi K00545.
    OMAi CTHYSSY.
    OrthoDBi EOG7PZRZJ.
    TreeFami TF329140.

    Enzyme and pathway databases

    SABIO-RK O88587.

    Miscellaneous databases

    NextBioi 282388.
    PROi O88587.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O88587.
    Genevestigatori O88587.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR025782. Catechol_O-MeTrfase.
    IPR017128. Catechol_O-MeTrfase_euk.
    IPR002935. O-MeTrfase_3.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    PANTHERi PTHR10509. PTHR10509. 1 hit.
    Pfami PF01596. Methyltransf_3. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037177. Catechol_O-mtfrase_euk. 1 hit.
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS51682. SAM_OMT_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Catechol-O-methyltransferase-deficient mice exhibit sexually dimorphic changes in catecholamine levels and behavior."
      Gogos J.A., Morgan M., Luine V., Santha M., Ogawa S., Pfaff D., Karayiorgou M.
      Proc. Natl. Acad. Sci. U.S.A. 95:9991-9996(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "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: Liver.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. Cited for: MUTAGENESIS OF ARG-51.
    7. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiCOMT_MOUSE
    AccessioniPrimary (citable) accession number: O88587
    Secondary accession number(s): Q91XH4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: October 3, 2012
    Last modified: October 1, 2014
    This is version 126 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3