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Protein

Dopamine beta-hydroxylase

Gene

Dbh

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

Functioni

Conversion of dopamine to noradrenaline.By similarity

Catalytic activityi

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

Cofactori

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.By similarity
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)DescriptionActionsGraphical viewLength
Active sitei233Sequence analysis1
Metal bindingi265Copper ABy similarity1
Metal bindingi266Copper ABy similarity1
Metal bindingi336Copper ABy similarity1
Active sitei415Sequence analysis1
Metal bindingi415Copper BBy similarity1
Metal bindingi417Copper BBy similarity1
Metal bindingi490Copper BBy similarity1

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
  • dopamine catabolic process Source: UniProtKB
  • glucose homeostasis Source: RGD
  • multicellular organism aging Source: RGD
  • norepinephrine biosynthetic process Source: RGD
  • octopamine biosynthetic process Source: GO_Central
  • 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

Keywordsi

Molecular functionMonooxygenase, Oxidoreductase
Biological processCatecholamine biosynthesis
LigandCopper, Metal-binding, Vitamin C

Enzyme and pathway databases

UniPathwayiUPA00748; UER00735

Names & Taxonomyi

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

Organism-specific databases

RGDi2489 Dbh

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 19CytoplasmicSequence analysisAdd BLAST19
Transmembranei20 – 40Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini41 – 620IntragranularSequence analysisAdd BLAST580

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane, Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2992

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000063581 – 620Dopamine beta-hydroxylaseAdd BLAST620
ChainiPRO_000030821143 – 620Soluble dopamine beta-hydroxylaseSequence analysisAdd BLAST578

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi67N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi157 ↔ 599By similarity
Glycosylationi187N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi235 ↔ 286By similarity
Disulfide bondi272 ↔ 298By similarity
Glycosylationi274N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei349Phosphoserine; by CaMKSequence analysis1
Disulfide bondi393 ↔ 506By similarity
Disulfide bondi397 ↔ 568By similarity
Disulfide bondi469 ↔ 491By similarity
Glycosylationi475N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi531InterchainBy similarity
Disulfide bondi533InterchainBy similarity
Glycosylationi569N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi587N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

Proteolytic cleavage after the membrane-anchor leads to the release of the soluble form.By similarity
N-glycosylated.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei42 – 43CleavageBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ05754
PRIDEiQ05754

PTM databases

PhosphoSitePlusiQ05754

Expressioni

Tissue specificityi

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

Interactioni

Subunit structurei

Homotetramer; composed of two disulfide-linked dimers.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000057915

Chemistry databases

BindingDBiQ05754

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZHBX-ray2.70C/F/I/L556-564[»]
ProteinModelPortaliQ05754
SMRiQ05754
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05754

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini60 – 176DOMONPROSITE-ProRule annotationAdd BLAST117

Sequence similaritiesi

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
InterProiView protein in InterPro
IPR014784 Cu2_ascorb_mOase-like_C
IPR020611 Cu2_ascorb_mOase_CS-1
IPR000323 Cu2_ascorb_mOase_N
IPR036939 Cu2_ascorb_mOase_N_sf
IPR024548 Cu2_monoox_C
IPR005018 DOMON_domain
IPR008977 PHM/PNGase_F_dom_sf
IPR028460 Tbh/DBH
PfamiView protein in Pfam
PF03712 Cu2_monoox_C, 1 hit
PF01082 Cu2_monooxygen, 1 hit
PF03351 DOMON, 1 hit
PRINTSiPR00767 DBMONOXGNASE
SMARTiView protein in SMART
SM00664 DoH, 1 hit
SUPFAMiSSF49742 SSF49742, 2 hits
PROSITEiView protein in PROSITE
PS00084 CU2_MONOOXYGENASE_1, 1 hit
PS50836 DOMON, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiDOPO_RAT
AccessioniPrimary (citable) accession number: Q05754
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 23, 2018
This is version 144 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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