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Q68CI2 (DOPO_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Cleaved into the following chain:

  1. Soluble dopamine beta-hydroxylase
Gene names
Name:DBH
OrganismCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length625 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 By similarity.

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 – 625625Dopamine beta-hydroxylase
PRO_0000305212
Chain33 – 625593Soluble dopamine beta-hydroxylase Potential
PRO_0000308207

Regions

Topological domain1 – 1313Cytoplasmic Potential
Transmembrane14 – 3421Helical; Signal-anchor for type II membrane protein; Potential
Topological domain35 – 625591Intragranular Potential
Domain50 – 166117DOMON

Sites

Active site2221 Potential
Active site4041 Potential
Metal binding2541Copper A By similarity
Metal binding2551Copper A By similarity
Metal binding3251Copper A By similarity
Metal binding4041Copper B By similarity
Metal binding4061Copper B By similarity
Metal binding4791Copper B By similarity

Amino acid modifications

Glycosylation1771N-linked (GlcNAc...) Potential
Glycosylation3151N-linked (GlcNAc...) Potential
Glycosylation5741N-linked (GlcNAc...) Potential
Disulfide bond147 ↔ 604 By similarity
Disulfide bond224 ↔ 275 By similarity
Disulfide bond261 ↔ 287 By similarity
Disulfide bond382 ↔ 495 By similarity
Disulfide bond386 ↔ 573 By similarity
Disulfide bond458 ↔ 480 By similarity
Disulfide bond520Interchain By similarity
Disulfide bond522Interchain By similarity

Natural variations

Natural variant2631N → K Frequent in Golden retrievers and Labrador retrievers. Ref.1
Natural variant6071S → G in strain: Shiba. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q68CI2 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: F78B8442F7910EE8

FASTA62569,929
        10         20         30         40         50         60 
MQVPSPSARE AASMYGTAVA VFLVLLVAVL QGLAPPESPL PYRIPLDPKG DLELSWDVSY 

        70         80         90        100        110        120 
TQKTIYFQLL VQELKAGVLF GMSDRGELEN ADLVVLWTDG DNAYFGDAWS DQRGQIHLDS 

       130        140        150        160        170        180 
QQDYQLLRAQ RTPKGLCLLF KRPFGTCDPK DYFIEDGTVH LVYGVLEEPF GSLEAINTSG 

       190        200        210        220        230        240 
LQKGLQRVQL LKPKISIPAL PEDRRTMDIQ AHNVLIPSKT TYWCHLTKLP QDFPRHHIVM 

       250        260        270        280        290        300 
YEPIITKGNE ALVHHIEIFQ CTNQFQNITS FSGSCDSKEK PQELKVCRHV LAAWALGARA 

       310        320        330        340        350        360 
FYYPEEAGLA FGGSNSSRFL LLEIHYHNPT NIRGRYDNSG IRLHYTAKLR HFNAGIMELG 

       370        380        390        400        410        420 
LVYTPVMAIP PKESAFVLTG YCTAKCTQAA LPPLGIRIFA SQLHTHLTGT KVVTMLVRDG 

       430        440        450        460        470        480 
QEIEIVNRDD HYSPNFQEIR MLKKTVYVYP GDVLITSCTY NTEDKNEATV GGLGTQEEMC 

       490        500        510        520        530        540 
VNYIHYYPQT QLELCKSHID PCFLQKYFHL VNRSNLGEYC TCPQASGTTC PQASGTTCPR 

       550        560        570        580        590        600 
ASVPEQFASV PWNSFSRVVL KALYDFIPVT VHCNKSSAVR FPGKWDLQPL PEIISKLKEP 

       610        620 
TPRCPTSRDQ SSSSLTVVNI GGGKV

« Hide

References

[1]"Canine tyrosine hydroxylase (TH) gene and dopamine beta-hydroxylase (DBH) gene: their sequences, genetic polymorphisms, and diversities among five different dog breeds."
Takeuchi Y., Hashizume C., Chon E.M.H., Momozawa Y., Masuda K., Kikusui T., Mori Y.
J. Vet. Med. Sci. 67:861-867(2005) [PubMed: 16210796] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LYS-263 AND GLY-607.
Strain: Beagle.
Tissue: Brain.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB097057 mRNA. Translation: BAD42327.1.
RefSeqNP_001005263.1. NM_001005263.1.
UniGeneCfa.15803.

3D structure databases

HSSPHSSP built from PDB template 1PHM based on UniProtKB P14925.
ProteinModelPortalQ68CI2.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ68CI2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCAFT00000031457; ENSCAFP00000029281; ENSCAFG00000019783.
GeneID448806.
KEGGcfa:448806.

Organism-specific databases

CTD1621.

Phylogenomic databases

eggNOGmaNOG05453.
GeneTreeENSGT00530000063085.
HOVERGENHBG005519.
InParanoidQ68CI2.
OMALDSQQDY.
OrthoDBEOG4SN1ND.

Family and domain databases

InterProIPR014784. Cu2_ascorb_mOase-like_C.
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.
KOK00503.
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. False negative.
PS00085. CU2_MONOOXYGENASE_2. False negative.
PS50836. DOMON. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDOPO_CANFA
AccessionPrimary (citable) accession number: Q68CI2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 11, 2004
Last modified: November 16, 2011
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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