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O88587

- COMT_MOUSE

UniProt

O88587 - COMT_MOUSE

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Protein

Catechol O-methyltransferase

Gene
Comt, Comt1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 nitrogen By similarity
Binding sitei107 – 1071S-adenosyl-L-methionine By similarity
Binding sitei115 – 1151S-adenosyl-L-methionine By similarity
Binding sitei133 – 1331S-adenosyl-L-methionine By similarity
Binding sitei134 – 1341S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding sitei162 – 1621S-adenosyl-L-methionine; via amide nitrogen By similarity
Metal bindingi184 – 1841Magnesium By similarity
Binding sitei184 – 1841S-adenosyl-L-methionine By similarity
Binding sitei187 – 1871Substrate By similarity
Metal bindingi212 – 2121Magnesium By similarity
Metal bindingi213 – 2131Magnesium By similarity
Binding sitei213 – 2131Substrate By similarity
Binding sitei242 – 2421Substrate By 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
Complete GO annotation...

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

Topology

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

GO - Cellular componenti

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

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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni160 – 1634S-adenosyl-L-methionine binding By similarity

Sequence similaritiesi

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4343Missing in isoform Soluble. VSP_018779Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti162 – 1621S → P in AAC33334. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 125 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

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