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Reviewed, UniProtKB/Swiss-Prot Q05754 (DOPO_RAT)

Last modified June 16, 2009. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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- Recommended name:
            Soluble dopamine beta-hydroxylase
Gene names
Name: Dbh
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length620 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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.

Tissue specificity

Chromaffin granules of the adrenal medulla and synaptic vesicles of the sympathetic nervous system.

Sequence similarities

Belongs to the copper type II ascorbate-dependent monooxygenase family.

Contains 1 DOMON domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 620620Dopamine beta-hydroxylase
PRO_0000006358
Chain43 – 620578Soluble dopamine beta-hydroxylase Potential
PRO_0000308211

Regions

Topological domain1 – 1919Cytoplasmic Potential
Transmembrane20 – 4021Signal-anchor for type II membrane Potential
Topological domain41 – 620580Intragranular Potential
Domain60 – 176117DOMON

Sites

Active site2331 Potential
Active site4151 Potential
Metal binding2651Copper A By similarity
Metal binding2661Copper A By similarity
Metal binding3361Copper A By similarity
Metal binding4151Copper B By similarity
Metal binding4171Copper B By similarity
Metal binding4901Copper B By similarity

Amino acid modifications

Modified residue3491Phosphoserine; by CaMK Potential
Glycosylation671N-linked (GlcNAc...) Potential
Glycosylation1871N-linked (GlcNAc...) Potential
Glycosylation2741N-linked (GlcNAc...) Potential
Glycosylation4751N-linked (GlcNAc...) Potential
Glycosylation5691N-linked (GlcNAc...) Potential
Glycosylation5871N-linked (GlcNAc...) Potential
Disulfide bond157 ↔ 599 By similarity
Disulfide bond235 ↔ 286 By similarity
Disulfide bond272 ↔ 298 By similarity
Disulfide bond393 ↔ 506 By similarity
Disulfide bond397 ↔ 568 By similarity
Disulfide bond469 ↔ 491 By similarity
Disulfide bond531Interchain By similarity
Disulfide bond533Interchain By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q05754-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: FFBE26C8A4ED5776

FASTA62069,875
        10         20         30         40         50         60 
MQPHLSHQPC WSLPSPSVRE AASMYGTAVA IFLVILVAAL QGSEPPESPF PYHIPLDPEG 

        70         80         90        100        110        120 
TLELSWNVSY DQEIIHFQLQ VQGPRAGVLF GMSDRGEMEN ADLVMLWTDG DRTYFADAWS 

       130        140        150        160        170        180 
DQKGQIHLDT HQDYQLLQAQ RVSNSLSLLF KRPFVTCDPK DYVIEDDTVH LVYGILEEPF 

       190        200        210        220        230        240 
QSLEAINTSG LHTGLQQVQL LKPEVSTPAM PADVQTMDIR APDVLIPSTE TTYWCYITEL 

       250        260        270        280        290        300 
PLHFPRHHII MYEAIVTEGN EALVHHMEVF QCTNESEAFP MFNGPCDSKM KPDRLNYCRH 

       310        320        330        340        350        360 
VLAAWALGAK AFYYPEEAGV PLGSSGSSRF LRLEVHYHNP RNIQGRRDSS GIRLHYTASL 

       370        380        390        400        410        420 
RPNEAGIMEL GLVYTPLMAI PPQETTFVLT GYCTDRCTQM ALPKSGIRIF ASQLHTHLTG 

       430        440        450        460        470        480 
RKVITVLARD GQQREVVNRD NHYSPHFQEI RMLKNAVTVH QGDVLITSCT YNTENRTMAT 

       490        500        510        520        530        540 
VGGFGILEEM CVNYVHYYPK TELELCKSAV DDGFLQKYFH IVNRFGNEEV CTCPQASVPQ 

       550        560        570        580        590        600 
QFASVPWNSF NRDMLKALYN YAPISVHCNK TSAVRFPGNW NLQPLPNITS AVEEPDPRCP 

       610        620 
IRQTRGPAGP FVVITHGGRH

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References

[1]"Rat dopamine beta-hydroxylase: molecular cloning and characterization of the cDNA and regulation of the mRNA by reserpine."
McMahon A., Geertman R., Sabban E.L.
J. Neurosci. Res. 25:395-404(1990) [PubMed: 2325165] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Dopamine beta-monooxygenase signal/anchor sequence alters trafficking of peptidylglycine alpha-hydroxylating monooxygenase."
Oyarce A.M., Steveson T.C., Jin L., Eipper B.A.
J. Biol. Chem. 276:33265-33272(2001) [PubMed: 11418593] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

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Cross-references

Sequence databases

L12407 mRNA. Translation: AAA41091.1.
IPIIPI00778951.
PIRA61086.
RefSeqNP_037290.2.
UniGeneRn.87166

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1ZHBX-ray2.70C/F/I/L556-564[»]
ModBaseSearch...

Genome annotation databases

EnsemblENSRNOG00000006641. Rattus norvegicus. [Contig view]
GeneID25699.
KEGGrno:25699.

Organism-specific databases

RGD2489. Dbh.

Phylogenomic databases

HOVERGENQ05754.

Enzyme and pathway databases

BRENDA1.14.17.1. 248.

Gene expression databases

ArrayExpressQ05754.
GermOnlineENSRNOG00000006641. Rattus norvegicus.

Family and domain databases

InterProIPR014784. 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]
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.
PfamPF03712. Cu2_monoox_C. 1 hit.
PF01082. Cu2_monooxygen. 1 hit.
PF03351. DOMON. 1 hit.
[Graphical view]
PRINTSPR00767. DBMONOXGNASE.
SMARTSM00664. DoH. 1 hit.
[Graphical view]
PROSITEPS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS00085. CU2_MONOOXYGENASE_2. False negative.
PS50836. DOMON. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio607723.

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Entry information

Entry nameDOPO_RAT
AccessionPrimary (citable) accession number: Q05754
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 16, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents