Reviewed, UniProtKB/Swiss-Prot Q64237 (DOPO_MOUSE)

Names and origin

Protein names

Recommended name:
    Dopamine beta-hydroxylase
    EC=1.14.17.1
Alternative name(s):
    Dopamine beta-monooxygenase
Cleaved into the following chain:
    1- Recommended name:
            Soluble dopamine beta-hydroxylase

Gene names

Name:

Dbh

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	621 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Conversion of dopamine to noradrenaline.
Catalytic activity	3,4-dihydroxyphenethylamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O.
Cofactor	Binds 1 PQQ per subunit By similarity. Binds 2 copper ions per subunit By similarity.
Pathway	Catecholamine biosynthesis; norepinephrine biosynthesis; norepinephrine from dopamine: step 1/1.
Subunit structure	Homotetramer composed of two non-covalently bound disulfide-linked dimers By similarity.
Subcellular location	Soluble dopamine beta-hydroxylase: Cytoplasmic vesicle › secretory vesicle lumen By similarity. Cytoplasmic vesicle › secretory vesicle › chromaffin granule lumen By similarity. Cytoplasmic vesicle › secretory vesicle membrane; Single-pass type II membrane protein By similarity. Cytoplasmic vesicle › secretory vesicle › chromaffin granule membrane; Single-pass type II membrane protein By similarity.
Sequence similarities	Belongs to the copper type II ascorbate-dependent monooxygenase family. Contains 1 DOMON domain.

Ontologies

Keywords
Biological process	Catecholamine biosynthesis
Cellular component	Cytoplasmic vesicle Membrane
Domain	Signal-anchor Transmembrane
Ligand	Copper Metal-binding Vitamin C
Molecular function	Monooxygenase Oxidoreductase
PTM	Disulfide bond Glycoprotein PQQ Phosphoprotein
Gene Ontology (GO)
Biological process	associative learning Inferred from mutant phenotype. Source: MGI behavioral response to ethanol Inferred from mutant phenotype. Source: MGI blood vessel remodeling Inferred from mutant phenotype. Source: MGI cytokine production Inferred from mutant phenotype. Source: MGI dopamine catabolic process Inferred from mutant phenotype. Source: MGI fear response Inferred from mutant phenotype. Source: MGI glucose homeostasis Inferred from mutant phenotype. Source: MGI histidine catabolic process Inferred from electronic annotation. Source: InterPro homoiothermy Inferred from mutant phenotype. Source: MGI leukocyte mediated immunity Inferred from mutant phenotype. Source: MGI leukocyte migration Inferred from mutant phenotype. Source: MGI locomotory behavior Inferred from mutant phenotype. Source: MGI maternal behavior Inferred from mutant phenotype. Source: MGI memory Inferred from mutant phenotype. Source: MGI norepinephrine biosynthetic process Inferred from mutant phenotype. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of vasoconstriction Inferred from mutant phenotype. Source: MGI regulation of apoptosis Inferred from mutant phenotype. Source: MGI regulation of cell proliferation Inferred from mutant phenotype. Source: MGI response to amphetamine Inferred from mutant phenotype. Source: MGI response to pain Inferred from mutant phenotype. Source: MGI visual learning Inferred from mutant phenotype. Source: MGI
Cellular component	chromaffin granule lumen Inferred from electronic annotation. Source: UniProtKB-SubCell chromaffin granule membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW secretory granule lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW dopamine beta-monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 621	621	Dopamine beta-hydroxylase		PRO_0000006357
	Chain	44 – 621	578	Soluble dopamine beta-hydroxylase Potential		PRO_0000308210
Regions
	Topological domain	1 – 20	20	Cytoplasmic Potential
	Transmembrane	21 – 41	21	Signal-anchor for type II membrane Potential
	Topological domain	42 – 621	580	Intragranular Potential
	Domain	61 – 177	117	DOMON
Sites
	Active site	234	1	Potential
	Active site	416	1	Potential
	Metal binding	266	1	Copper A By similarity
	Metal binding	267	1	Copper A By similarity
	Metal binding	337	1	Copper A By similarity
	Metal binding	416	1	Copper B By similarity
	Metal binding	418	1	Copper B By similarity
	Metal binding	491	1	Copper B By similarity
Amino acid modifications
	Modified residue	350	1	Phosphoserine; by CaMK Potential
	Glycosylation	68	1	N-linked (GlcNAc...) Potential
	Glycosylation	188	1	N-linked (GlcNAc...) Potential
	Glycosylation	476	1	N-linked (GlcNAc...) Potential
	Glycosylation	570	1	N-linked (GlcNAc...) Potential
	Disulfide bond	158 ↔ 600		By similarity
	Disulfide bond	236 ↔ 287		By similarity
	Disulfide bond	273 ↔ 299		By similarity
	Disulfide bond	394 ↔ 507		By similarity
	Disulfide bond	398 ↔ 569		By similarity
	Disulfide bond	470 ↔ 492		By similarity
	Disulfide bond	532		Interchain By similarity
	Disulfide bond	534		Interchain By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q64237-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 1EF8B1E3149C55C4	FASTA	621	70,187
	10 20 30 40 50 60 MQAHLSHQPC WSSLPSPSVR EAASMYGTAV AIFLVILVAA LRGSEPPESP FPYHIPLDPE 70 80 90 100 110 120 GILELSWNVS YVQEIIHFQL QVQGLRAGVL FGMSDRGEME NADLIMLWSD GDRAYFADAW 130 140 150 160 170 180 SDRKGQIHLD SQQDYQLLQA QRTRDGLSLL FKRPFVTCDP KDYVIEDDTV HLVYGILEEP 190 200 210 220 230 240 FQSLEAINTS GLHTGLLRVQ LLKSEVPTPS MPEDVQTMDI RAPDILIPDN EQTYWCYITE 250 260 270 280 290 300 LPPRFPRHHI IMYEAIVTEG NEALVHHMEV FQCAAESEDF PQFNGPCDSK MKPDRLNYCR 310 320 330 340 350 360 HVLAAWALGA KAFYYPKEAG VPFGGPGSSP FLRLEVHYHN PRKIQGRQDS SGIRLPYTAT 370 380 390 400 410 420 LRRYDAGIME LGLVYTPLMA IPPQETAFVL TGYCTDKCTQ MALQDSGIHI FASQLHTHLT 430 440 450 460 470 480 GRKVVTVLAR DGQERKEVNR DNHYSPHFRE IRMLKKVVTV YPGDVLITSC TYNTENKTLA 490 500 510 520 530 540 TVGGFGILEE MCVNYVHYYP QTELELCKSA VDDGFLQKYF HMVNRFSSEE VCTCPQASVP 550 560 570 580 590 600 QQFSSVPWNS FNRNMLKALY DYAPISMHCN KTSAVRFPGE WNLQPLPKIT STLEEPTPRC 610 620 PIRQTQSPAN PTVPITTGGR C

References

[1]	"Mouse dopamine beta-hydroxylase: primary structure deduced from the cDNA sequence and exon/intron organization of the gene." Nakano T., Kobayashi K., Saito S., Fujita K., Nagatsu T. Biochem. Biophys. Res. Commun. 189:590-599(1992) [PubMed: 1280432] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	S50200 mRNA. Translation: AAB24330.1.
IPI	IPI00132202.
PIR	JC1346.
UniGene	Mm.167781
3D structure databases
HSSP	HSSP built from PDB template 1PHM based on UniProtKB P14925.
ModBase	Search...
Genome annotation databases
Ensembl	ENSMUSG00000000889. Mus musculus. [Contig view]
Organism-specific databases
MGI	MGI:94864. Dbh.
Phylogenomic databases
HOVERGEN	Q64237.
Enzyme and pathway databases
BRENDA	1.14.17.1. 244.
Gene expression databases
ArrayExpress	Q64237.
Bgee	Q64237.
CleanEx	MM_DBH.
GermOnline	ENSMUSG00000000889. Mus musculus.
Family and domain databases
InterPro	IPR014784. Cu2_ascorb_mOase-like_C. IPR014783. Cu2_ascorb_mOase_C. IPR000323. Cu2_ascorb_mOase_N. IPR013050. DOMON. IPR005018. DOMON_rel. IPR000945. Dopamine_b_mOase. [Graphical view]
Gene3D	G3DSA:2.60.120.230. Cu2_ascorb_mOase_core. 1 hit. G3DSA:2.60.120.310. Cu2_ascorb_mOase_core. 1 hit.
PANTHER	PTHR10157. Dopamine_b_mOase. 1 hit.
Pfam	PF03712. Cu2_monoox_C. 1 hit. PF01082. Cu2_monooxygen. 1 hit. PF03351. DOMON. 1 hit. [Graphical view]
PRINTS	PR00767. DBMONOXGNASE.
SMART	SM00664. DoH. 1 hit. [Graphical view]
PROSITE	PS00084. CU2_MONOOXYGENASE_1. 1 hit. PS00085. CU2_MONOOXYGENASE_2. 1 hit. PS50836. DOMON. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

DOPO_MOUSE

Accession

Primary (citable) accession number: Q64237

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)