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Protein

Dopamine beta-hydroxylase

Gene

Dbh

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Conversion of dopamine to noradrenaline.

Catalytic activityi

3,4-dihydroxyphenethylamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O.

Cofactori

Protein has several cofactor binding sites:
  • pyrroloquinoline quinoneBy similarityNote: Binds 1 PQQ per subunit.By similarity
  • Cu2+By similarityNote: Binds 2 copper ions per subunit.By similarity

Pathwayi: (R)-noradrenaline biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes (R)-noradrenaline from dopamine.
Proteins known to be involved in this subpathway in this organism are:
  1. Dopamine beta-hydroxylase (Dbh)
This subpathway is part of the pathway (R)-noradrenaline biosynthesis, which is itself part of Catecholamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-noradrenaline from dopamine, the pathway (R)-noradrenaline biosynthesis and in Catecholamine biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei233 – 2331Sequence analysis
Metal bindingi265 – 2651Copper ABy similarity
Metal bindingi266 – 2661Copper ABy similarity
Metal bindingi336 – 3361Copper ABy similarity
Active sitei415 – 4151Sequence analysis
Metal bindingi415 – 4151Copper BBy similarity
Metal bindingi417 – 4171Copper BBy similarity
Metal bindingi490 – 4901Copper BBy similarity

GO - Molecular functioni

  • copper ion binding Source: RGD
  • dopamine beta-monooxygenase activity Source: RGD
  • L-ascorbic acid binding Source: UniProtKB-KW

GO - Biological processi

  • bone development Source: RGD
  • catecholamine metabolic process Source: RGD
  • cellular response to manganese ion Source: RGD
  • cellular response to nicotine Source: RGD
  • glucose homeostasis Source: RGD
  • multicellular organism aging Source: RGD
  • norepinephrine biosynthetic process Source: RGD
  • octopamine metabolic process Source: RGD
  • response to copper ion Source: RGD
  • response to drug Source: RGD
  • response to estradiol Source: RGD
  • response to ethanol Source: RGD
  • response to immobilization stress Source: RGD
  • response to iron ion Source: RGD
  • response to isolation stress Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to ozone Source: RGD
  • response to peptide hormone Source: RGD
  • sensory perception of taste Source: RGD
  • social behavior Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Catecholamine biosynthesis

Keywords - Ligandi

Copper, Metal-binding, PQQ, Vitamin C

Enzyme and pathway databases

UniPathwayiUPA00748; UER00735.

Names & Taxonomyi

Protein namesi
Recommended name:
Dopamine beta-hydroxylase (EC:1.14.17.1)
Alternative name(s):
Dopamine beta-monooxygenase
Cleaved into the following chain:
Gene namesi
Name:Dbh
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2489. Dbh.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1919CytoplasmicSequence analysisAdd
BLAST
Transmembranei20 – 4021Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini41 – 620580IntragranularSequence analysisAdd
BLAST

GO - Cellular componenti

  • apical part of cell Source: RGD
  • axon Source: RGD
  • chromaffin granule lumen Source: UniProtKB-SubCell
  • chromaffin granule membrane Source: UniProtKB-SubCell
  • cytoplasm Source: RGD
  • cytoplasmic, membrane-bounded vesicle Source: RGD
  • dendrite Source: RGD
  • integral component of membrane Source: UniProtKB-KW
  • neuronal cell body Source: RGD
  • synapse Source: RGD
  • terminal bouton Source: RGD
  • transport vesicle membrane Source: UniProtKB-SubCell
  • varicosity Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2992.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 620620Dopamine beta-hydroxylasePRO_0000006358Add
BLAST
Chaini43 – 620578Soluble dopamine beta-hydroxylaseSequence analysisPRO_0000308211Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi67 – 671N-linked (GlcNAc...)Sequence analysis
Disulfide bondi157 ↔ 599By similarity
Glycosylationi187 – 1871N-linked (GlcNAc...)Sequence analysis
Disulfide bondi235 ↔ 286By similarity
Disulfide bondi272 ↔ 298By similarity
Glycosylationi274 – 2741N-linked (GlcNAc...)Sequence analysis
Modified residuei349 – 3491Phosphoserine; by CaMKSequence analysis
Disulfide bondi393 ↔ 506By similarity
Disulfide bondi397 ↔ 568By similarity
Disulfide bondi469 ↔ 491By similarity
Glycosylationi475 – 4751N-linked (GlcNAc...)Sequence analysis
Disulfide bondi531 – 531InterchainBy similarity
Disulfide bondi533 – 533InterchainBy similarity
Glycosylationi569 – 5691N-linked (GlcNAc...)Sequence analysis
Glycosylationi587 – 5871N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ05754.
PRIDEiQ05754.

PTM databases

PhosphoSiteiQ05754.

Expressioni

Tissue specificityi

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

Interactioni

Subunit structurei

Homotetramer composed of two non-covalently bound disulfide-linked dimers.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000057915.

Chemistry

BindingDBiQ05754.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZHBX-ray2.70C/F/I/L556-564[»]
ProteinModelPortaliQ05754.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05754.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini60 – 176117DOMONPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 DOMON domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3568. Eukaryota.
ENOG410XR89. LUCA.
HOGENOMiHOG000063669.
HOVERGENiHBG005519.
InParanoidiQ05754.
KOiK00503.
PhylomeDBiQ05754.

Family and domain databases

Gene3Di2.60.120.230. 1 hit.
2.60.120.310. 1 hit.
InterProiIPR014784. Cu2_ascorb_mOase-like_C.
IPR020611. Cu2_ascorb_mOase_CS-1.
IPR000323. Cu2_ascorb_mOase_N.
IPR024548. Cu2_monoox_C.
IPR000945. DBH-rel.
IPR005018. DOMON_domain.
IPR008977. PHM/PNGase_F_dom.
IPR028460. Tbh/DBH.
[Graphical view]
PANTHERiPTHR10157. PTHR10157. 1 hit.
PTHR10157:SF29. PTHR10157:SF29. 1 hit.
PfamiPF03712. Cu2_monoox_C. 1 hit.
PF01082. Cu2_monooxygen. 1 hit.
PF03351. DOMON. 1 hit.
[Graphical view]
PRINTSiPR00767. DBMONOXGNASE.
SMARTiSM00664. DoH. 1 hit.
[Graphical view]
SUPFAMiSSF49742. SSF49742. 2 hits.
PROSITEiPS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS50836. DOMON. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q05754-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQPHLSHQPC WSLPSPSVRE AASMYGTAVA IFLVILVAAL QGSEPPESPF
60 70 80 90 100
PYHIPLDPEG TLELSWNVSY DQEIIHFQLQ VQGPRAGVLF GMSDRGEMEN
110 120 130 140 150
ADLVMLWTDG DRTYFADAWS DQKGQIHLDT HQDYQLLQAQ RVSNSLSLLF
160 170 180 190 200
KRPFVTCDPK DYVIEDDTVH LVYGILEEPF QSLEAINTSG LHTGLQQVQL
210 220 230 240 250
LKPEVSTPAM PADVQTMDIR APDVLIPSTE TTYWCYITEL PLHFPRHHII
260 270 280 290 300
MYEAIVTEGN EALVHHMEVF QCTNESEAFP MFNGPCDSKM KPDRLNYCRH
310 320 330 340 350
VLAAWALGAK AFYYPEEAGV PLGSSGSSRF LRLEVHYHNP RNIQGRRDSS
360 370 380 390 400
GIRLHYTASL RPNEAGIMEL GLVYTPLMAI PPQETTFVLT GYCTDRCTQM
410 420 430 440 450
ALPKSGIRIF ASQLHTHLTG RKVITVLARD GQQREVVNRD NHYSPHFQEI
460 470 480 490 500
RMLKNAVTVH QGDVLITSCT YNTENRTMAT VGGFGILEEM CVNYVHYYPK
510 520 530 540 550
TELELCKSAV DDGFLQKYFH IVNRFGNEEV CTCPQASVPQ QFASVPWNSF
560 570 580 590 600
NRDMLKALYN YAPISVHCNK TSAVRFPGNW NLQPLPNITS AVEEPDPRCP
610 620
IRQTRGPAGP FVVITHGGRH
Length:620
Mass (Da):69,875
Last modified:February 1, 1995 - v1
Checksum:iFFBE26C8A4ED5776
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12407 mRNA. Translation: AAA41091.1.
PIRiA61086.
RefSeqiNP_037290.2. NM_013158.2.
UniGeneiRn.87166.

Genome annotation databases

GeneIDi25699.
KEGGirno:25699.
UCSCiRGD:2489. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12407 mRNA. Translation: AAA41091.1.
PIRiA61086.
RefSeqiNP_037290.2. NM_013158.2.
UniGeneiRn.87166.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZHBX-ray2.70C/F/I/L556-564[»]
ProteinModelPortaliQ05754.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000057915.

Chemistry

BindingDBiQ05754.
ChEMBLiCHEMBL2992.

PTM databases

PhosphoSiteiQ05754.

Proteomic databases

PaxDbiQ05754.
PRIDEiQ05754.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25699.
KEGGirno:25699.
UCSCiRGD:2489. rat.

Organism-specific databases

CTDi1621.
RGDi2489. Dbh.

Phylogenomic databases

eggNOGiKOG3568. Eukaryota.
ENOG410XR89. LUCA.
HOGENOMiHOG000063669.
HOVERGENiHBG005519.
InParanoidiQ05754.
KOiK00503.
PhylomeDBiQ05754.

Enzyme and pathway databases

UniPathwayiUPA00748; UER00735.

Miscellaneous databases

EvolutionaryTraceiQ05754.
NextBioi607723.
PROiQ05754.

Family and domain databases

Gene3Di2.60.120.230. 1 hit.
2.60.120.310. 1 hit.
InterProiIPR014784. Cu2_ascorb_mOase-like_C.
IPR020611. Cu2_ascorb_mOase_CS-1.
IPR000323. Cu2_ascorb_mOase_N.
IPR024548. Cu2_monoox_C.
IPR000945. DBH-rel.
IPR005018. DOMON_domain.
IPR008977. PHM/PNGase_F_dom.
IPR028460. Tbh/DBH.
[Graphical view]
PANTHERiPTHR10157. PTHR10157. 1 hit.
PTHR10157:SF29. PTHR10157:SF29. 1 hit.
PfamiPF03712. Cu2_monoox_C. 1 hit.
PF01082. Cu2_monooxygen. 1 hit.
PF03351. DOMON. 1 hit.
[Graphical view]
PRINTSiPR00767. DBMONOXGNASE.
SMARTiSM00664. DoH. 1 hit.
[Graphical view]
SUPFAMiSSF49742. SSF49742. 2 hits.
PROSITEiPS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS50836. DOMON. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiDOPO_RAT
AccessioniPrimary (citable) accession number: Q05754
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 11, 2016
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.