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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.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: UniProtKB
  • 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: UniProtKB
  • 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
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Catecholamine biosynthesis

Keywords - Ligandi

Copper, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2489. Dbh.

Subcellular locationi

Soluble dopamine beta-hydroxylase :

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

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
  • extracellular space Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • neuronal cell body Source: RGD
  • secretory granule lumen Source: UniProtKB
  • secretory granule membrane Source: UniProtKB
  • 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, 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...)Sequence analysis1
Disulfide bondi157 ↔ 599By similarity
Glycosylationi187N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi235 ↔ 286By similarity
Disulfide bondi272 ↔ 298By similarity
Glycosylationi274N-linked (GlcNAc...)Sequence analysis1
Modified residuei349Phosphoserine; by CaMKSequence analysis1
Disulfide bondi393 ↔ 506By similarity
Disulfide bondi397 ↔ 568By similarity
Disulfide bondi469 ↔ 491By similarity
Glycosylationi475N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi531InterchainBy similarity
Disulfide bondi533InterchainBy similarity
Glycosylationi569N-linked (GlcNAc...)Sequence analysis1
Glycosylationi587N-linked (GlcNAc...)Sequence 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

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZHBX-ray2.70C/F/I/L556-564[»]
ProteinModelPortaliQ05754.
SMRiQ05754.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000057915.

Chemistry databases

BindingDBiQ05754.
ChEMBLiCHEMBL2992.

PTM databases

PhosphoSitePlusiQ05754.

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.
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...

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: November 2, 2016
This is version 137 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.