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Q64237 (DOPO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dopamine beta-hydroxylase
EC=1.14.17.1
Alternative name(s):
Dopamine beta-monooxygenase

Cleaved into the following chain:

  1. Soluble dopamine beta-hydroxylase
Gene names
Name:Dbh
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length621 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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; (R)-noradrenaline biosynthesis; (R)-noradrenaline 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 621621Dopamine beta-hydroxylase
PRO_0000006357
Chain44 – 621578Soluble dopamine beta-hydroxylase Potential
PRO_0000308210

Regions

Topological domain1 – 2020Cytoplasmic Potential
Transmembrane21 – 4121Helical; Signal-anchor for type II membrane protein; Potential
Topological domain42 – 621580Intragranular Potential
Domain61 – 177117DOMON

Sites

Active site2341 Potential
Active site4161 Potential
Metal binding2661Copper A By similarity
Metal binding2671Copper A By similarity
Metal binding3371Copper A By similarity
Metal binding4161Copper B By similarity
Metal binding4181Copper B By similarity
Metal binding4911Copper B By similarity

Amino acid modifications

Modified residue3501Phosphoserine; by CaMK Potential
Glycosylation681N-linked (GlcNAc...) Potential
Glycosylation1881N-linked (GlcNAc...) Potential
Glycosylation4761N-linked (GlcNAc...) Potential
Glycosylation5701N-linked (GlcNAc...) Potential
Disulfide bond158 ↔ 600 By similarity
Disulfide bond236 ↔ 287 By similarity
Disulfide bond273 ↔ 299 By similarity
Disulfide bond394 ↔ 507 By similarity
Disulfide bond398 ↔ 569 By similarity
Disulfide bond470 ↔ 492 By similarity
Disulfide bond532Interchain By similarity
Disulfide bond534Interchain By similarity

Sequences

Sequence LengthMass (Da)Tools
Q64237 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 1EF8B1E3149C55C4

FASTA62170,187
        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

« Hide

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

EMBL
GenBank
DDBJ		S50200 mRNA. Translation: AAB24330.1.
IPIIPI00132202.
PIRJC1346.
UniGeneMm.167781.

3D structure databases

ProteinModelPortalQ64237.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ64237.

PTM databases

PhosphoSiteQ64237.

Proteomic databases

PRIDEQ64237.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:94864. Dbh.

Phylogenomic databases

GeneTreeENSGT00530000063085.
HOVERGENHBG005519.
InParanoidQ64237.
OrthoDBEOG4SN1ND.

Gene expression databases

ArrayExpressQ64237.
BgeeQ64237.
CleanExMM_DBH.
GenevestigatorQ64237.
GermOnlineENSMUSG00000000889. Mus musculus.

Family and domain databases

InterProIPR014784. Cu2_ascorb_mOase-like_C.
IPR020611. Cu2_ascorb_mOase_CS-1.
IPR014783. Cu2_ascorb_mOase_CS-2.
IPR000323. Cu2_ascorb_mOase_N.
IPR005018. DOMON_domain.
IPR000945. Dopamine_b_mOase.
IPR008977. PHM/PNGase_F_dom.
[Graphical view]
Gene3DG3DSA:2.60.120.230. Cu2_ascorb_mOase_core. 1 hit.
G3DSA:2.60.120.310. Cu2_ascorb_mOase_core. 1 hit.
PANTHERPTHR10157. Dopamine_b_mOase. 1 hit.
PfamPF01082. Cu2_monooxygen. 1 hit.
PF03351. DOMON. 1 hit.
[Graphical view]
PRINTSPR00767. DBMONOXGNASE.
SMARTSM00664. DoH. 1 hit.
[Graphical view]
SUPFAMSSF49742. PHM_PNGase_F. 2 hits.
PROSITEPS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS00085. CU2_MONOOXYGENASE_2. 1 hit.
PS50836. DOMON. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry nameDOPO_MOUSE
AccessionPrimary (citable) accession number: Q64237
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 19, 2011
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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