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DBH dopamine beta-hydroxylase [ Bos taurus (domestic cattle) ]

Gene ID: 280758, updated on 4-Oct-2024

Summary

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Official Symbol
DBHprovided by VGNC
Official Full Name
dopamine beta-hydroxylaseprovided by VGNC
Primary source
VGNC:VGNC:27888
See related
BGD:BT11121; Ensembl:ENSBTAG00000004508
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Bos taurus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos
Orthologs
human mouse all
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Genomic context

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See DBH in Genome Data Viewer
Location:
chromosome: 11
Exon count:
12
Annotation release Status Assembly Chr Location
RS_2023_09 current ARS-UCD2.0 (GCF_002263795.3) 11 NC_037338.1 (104498730..104516525)

Chromosome 11 - NC_037338.1Genomic Context describing neighboring genes Neighboring gene ADAMTS like 2 Neighboring gene family with sequence similarity 163 member B Neighboring gene uncharacterized LOC132346649 Neighboring gene sarcosine dehydrogenase Neighboring gene uncharacterized LOC132346651 Neighboring gene vav guanine nucleotide exchange factor 2

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_037338.1 Chromosome 11 Reference ARS-UCD2.0 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Evidence that dioxygen and substrate activation are tightly coupled in dopamine beta-monooxygenase. Implications for the reactive oxygen species. Evans JP, et al. J Biol Chem, 2003 Dec 12. PMID 12966104
  2. Anion- and pH-dependent activation of the soluble form of dopamine beta-hydroxylase. Terland O, et al. Biochem J, 2003 Feb 1. PMID 12379149, Free PMC Article
  3. The membrane-binding segment of dopamine beta-hydroxylase is not an uncleaved signal sequence. Taylor CS, et al. J Biol Chem, 1989 Jan 5. PMID 2909511
  4. Structure of bovine adrenal dopamine beta-monooxygenase, as deduced from cDNA and protein sequencing: evidence that the membrane-bound form of the enzyme is anchored by an uncleaved signal peptide. Taljanidisz J, et al. Biochemistry, 1989 Dec 26. PMID 2620060
  5. Primary amino acid sequence of bovine dopamine beta-hydroxylase. Robertson JG, et al. J Biol Chem, 1990 Jan 15. PMID 2295597

See all (16) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. The present study presents evidence for the conclusion that the catalytic activity of dopamine beta-hydroxylase (DBH; dopamine beta-mono-oxygenase, EC 1.14.17.1) is regulated independently by pH and by anions
    Title: Anion- and pH-dependent activation of the soluble form of dopamine beta-hydroxylase.
  2. dioxygen and substrate activation are tightly coupled in dopamine beta-monooxygenase
    Title: Evidence that dioxygen and substrate activation are tightly coupled in dopamine beta-monooxygenase. Implications for the reactive oxygen species.
Submit: New GeneRIF Correction

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Markers

Homology

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables copper ion binding IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables dopamine beta-monooxygenase activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
Process Evidence Code Pubs
involved_in dopamine catabolic process IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in norepinephrine biosynthetic process IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in octopamine biosynthetic process IEA
Inferred from Electronic Annotation
more info
 PubMed 
Component Evidence Code Pubs
located_in extracellular space IEA
Inferred from Electronic Annotation
more info
 PubMed 
located_in secretory granule membrane IEA
Inferred from Electronic Annotation
more info
 PubMed 

General protein information

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Preferred Names
dopamine beta-hydroxylase
Names
dopamine beta-monooxygenase
NP_851338.1

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_180995.2 → NP_851338.1  dopamine beta-hydroxylase precursor

    See identical proteins and their annotated locations for NP_851338.1

    Status: PROVISIONAL

    Source sequence(s)
    J02890
    UniProtKB/Swiss-Prot
    P15101, Q0V8A8, Q28094, Q9TVD1
    Related
    ENSBTAP00000047899.3, ENSBTAT00000055221.3
    Conserved Domains (3) summary
    pfam01082
    Location:206 → 330
    Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain
    pfam03351
    Location:50 → 163
    DOMON; DOMON domain
    pfam03712
    Location:354 → 509
    Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain

RefSeqs of Annotated Genomes: GCF_002263795.3-RS_2023_09

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference ARS-UCD2.0 Primary Assembly

Genomic

  1. NC_037338.1 Reference ARS-UCD2.0 Primary Assembly

    Range
    104498730..104516525
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)
Nucleotide Protein Strain
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P15101.2 GenPept UniProtKB/Swiss-Prot:P15101

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

Molecular Biology Databases
Research Materials