COMTB_DANRE
ID COMTB_DANRE Reviewed; 264 AA.
AC A4IG53; Q7SZX0;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Catechol O-methyltransferase B {ECO:0000303|PubMed:28844929};
DE EC=2.1.1.6 {ECO:0000250|UniProtKB:P21964};
DE Flags: Precursor;
GN Name=comtb {ECO:0000303|PubMed:28844929};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN [1] {ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2] {ECO:0000312|EMBL:AAI34932.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:AAI34932.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=28844929; DOI=10.1016/j.bcp.2017.08.017;
RA Semenova S., Rozov S., Panula P.;
RT "Distribution, properties, and inhibitor sensitivity of zebrafish catechol-
RT O-methyl transferases (COMT).";
RL Biochem. Pharmacol. 145:147-157(2017).
CC -!- FUNCTION: Catalyzes the O-methylation, and thereby the inactivation, of
CC catecholamine neurotransmitters and catechol hormones.
CC {ECO:0000250|UniProtKB:P21964}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a catechol + S-adenosyl-L-methionine = a guaiacol + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:17877, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33566, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:134251; EC=2.1.1.6;
CC Evidence={ECO:0000250|UniProtKB:P21964};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PIRSR:PIRSR037177-3};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|PIRSR:PIRSR037177-3};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in eye, diencephalon, spinal
CC cord, hindbrain, liver, kidney and telencephalon. Also detected at very
CC low levels in muscle, spleen, anterior gut and heart. In eye, expressed
CC strongly in retina. In brain, expressed in the central part of the
CC telencephalon, the periventricular gray zone of the optic tectum, the
CC periglomerular nucleus, the olfactory bulb, and the region adjacent to
CC the diencephalic ventricle in the hypothalamus. Expressed in gill, with
CC strongest expression in gill filaments nearest the gill arch, and in
CC esophageal epithelium. {ECO:0000269|PubMed:28844929}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-dependent O-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01019}.
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DR EMBL; AL844847; CAE30427.1; -; Genomic_DNA.
DR EMBL; CR933820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC134931; AAI34932.1; -; mRNA.
DR RefSeq; NP_001077312.1; NM_001083843.1.
DR RefSeq; XP_009304313.1; XM_009306038.2.
DR AlphaFoldDB; A4IG53; -.
DR SMR; A4IG53; -.
DR STRING; 7955.ENSDARP00000038939; -.
DR PaxDb; A4IG53; -.
DR PeptideAtlas; A4IG53; -.
DR Ensembl; ENSDART00000033702; ENSDARP00000038939; ENSDARG00000025679.
DR GeneID; 565370; -.
DR KEGG; dre:565370; -.
DR CTD; 565370; -.
DR ZFIN; ZDB-GENE-040724-164; comtb.
DR eggNOG; KOG1663; Eukaryota.
DR GeneTree; ENSGT00940000155317; -.
DR HOGENOM; CLU_050461_5_0_1; -.
DR InParanoid; A4IG53; -.
DR OMA; HEYSDLK; -.
DR OrthoDB; 1274244at2759; -.
DR PhylomeDB; A4IG53; -.
DR TreeFam; TF329140; -.
DR PRO; PR:A4IG53; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 11.
DR Bgee; ENSDARG00000025679; Expressed in retina and 14 other tissues.
DR ExpressionAtlas; A4IG53; baseline.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016206; F:catechol O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0102084; F:L-dopa O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0102938; F:orcinol O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042424; P:catecholamine catabolic process; IBA:GO_Central.
DR GO; GO:0032502; P:developmental process; IBA:GO_Central.
DR GO; GO:0042417; P:dopamine metabolic process; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR017128; Catechol_O-MeTrfase_euk.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002935; SAM_O-MeTrfase.
DR Pfam; PF01596; Methyltransf_3; 1.
DR PIRSF; PIRSF037177; Catechol_O-mtfrase_euk; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51682; SAM_OMT_I; 1.
PE 2: Evidence at transcript level;
KW Catecholamine metabolism; Glycoprotein; Magnesium; Metal-binding;
KW Methyltransferase; Neurotransmitter degradation; Reference proteome;
KW S-adenosyl-L-methionine; Secreted; Signal; Transferase.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..264
FT /note="Catechol O-methyltransferase B"
FT /evidence="ECO:0000255"
FT /id="PRO_0000444754"
FT BINDING 92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PIRSR:PIRSR037177-1"
FT BINDING 122
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PIRSR:PIRSR037177-1"
FT BINDING 140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PIRSR:PIRSR037177-1"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PIRSR:PIRSR037177-3"
FT BINDING 191
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PIRSR:PIRSR037177-1"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR037177-2"
FT BINDING 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PIRSR:PIRSR037177-3"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PIRSR:PIRSR037177-3"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR037177-2"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR037177-2"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 207
FT /note="C -> W (in Ref. 1; CAE30427)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 264 AA; 29872 MW; 5EDA6771526447FA CRC64;
MLGVLLCWCL GASVLLYVLY SWLIPAAVQF NGSLALLWHD VIVERALDSL TRSTRPQRLL
KAVKQHATRG DPQSVISAID HFCRHREWAM NVGDEKGCIL DSVVSELNPE KVLELGTYCG
YSTVRIARLL PPGARLITLE FNPDYAVIAR QVIAWAGIED KVQLVEGASE DWIPRMKEHF
GIETFDLVFL DHWKDHYLPD TKLMEGCGLL RKGTVLLADN VICPGVPDYL EYVRNSRSYK
SCYFKSHLEY TRAEDGLEKS VFLG
