A0A0A0AWZ0 · A0A0A0AWZ0_CHAVO
- ProteinDopamine beta-hydroxylase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids570 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the hydroxylation of dopamine to noradrenaline (also known as norepinephrine), and is thus vital for regulation of these neurotransmitters.
Catalytic activity
- dopamine + 2 L-ascorbate + O2 = (R)-noradrenaline + H2O + 2 monodehydro-L-ascorbate radicalThis reaction proceeds in the forward direction.
Cofactor
Pathway
Catecholamine biosynthesis; (R)-noradrenaline biosynthesis; (R)-noradrenaline from dopamine: step 1/1.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromaffin granule lumen | |
Cellular Component | chromaffin granule membrane | |
Cellular Component | transport vesicle membrane | |
Molecular Function | copper ion binding | |
Molecular Function | dopamine beta-monooxygenase activity | |
Biological Process | norepinephrine biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDopamine beta-hydroxylase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Charadriiformes > Charadriidae > Charadrius
Accessions
- Primary accessionA0A0A0AWZ0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cytoplasmic vesicle, secretory vesicle membrane ; Single-pass type II membrane protein
Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane ; Single-pass type II membrane protein
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Interaction
Subunit
Homotetramer; composed of two disulfide-linked dimers.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 10-126 | DOMON | ||||
Sequence: GLLQLSWNVSYPEQVVHFQLLVRDLRFGLLFGMSDRGEFENADLAVLWSDGHNSYFGDAWSDAKGQLHMDSQQDYQLLGARKAPEGLYLLFRRAFSTCDPKDYLIEDGTVHLIYGIL | ||||||
Region | 543-570 | Disordered | ||||
Sequence: REPVPHCPPAPGPRPSAPVPLNLGELRR | ||||||
Compositional bias | 546-560 | Pro residues | ||||
Sequence: VPHCPPAPGPRPSAP |
Sequence similarities
Belongs to the copper type II ascorbate-dependent monooxygenase family.
Family and domain databases
Sequence
- Sequence statusFragment
- Length570
- Mass (Da)64,457
- Last updated2015-01-07 v1
- Checksum5D7B16631FF992AC
Features
Showing features for non-terminal residue, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: P | ||||||
Compositional bias | 546-560 | Pro residues | ||||
Sequence: VPHCPPAPGPRPSAP | ||||||
Non-terminal residue | 570 | |||||
Sequence: R |
Keywords
- Technical term