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Protein

Dopamine beta-hydroxylase

Gene

Dbh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Conversion of dopamine to noradrenaline.2 Publications

Catalytic activityi

3,4-dihydroxyphenethylamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O.1 Publication1 Publication

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.2 Publications
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 sitei234 – 2341Sequence analysis
Metal bindingi266 – 2661Copper ABy similarity
Metal bindingi267 – 2671Copper ABy similarity
Metal bindingi337 – 3371Copper ABy similarity
Active sitei416 – 4161Sequence analysis
Metal bindingi416 – 4161Copper BBy similarity
Metal bindingi418 – 4181Copper BBy similarity
Metal bindingi491 – 4911Copper BBy similarity

GO - Molecular functioni

GO - Biological processi

  • associative learning Source: MGI
  • behavioral response to ethanol Source: MGI
  • blood vessel remodeling Source: MGI
  • cytokine production Source: MGI
  • dopamine catabolic process Source: UniProtKB
  • fear response Source: MGI
  • glucose homeostasis Source: MGI
  • homoiothermy Source: MGI
  • leukocyte mediated immunity Source: MGI
  • leukocyte migration Source: MGI
  • locomotory behavior Source: UniProtKB
  • maternal behavior Source: MGI
  • memory Source: MGI
  • norepinephrine biosynthetic process Source: UniProtKB
  • positive regulation of vasoconstriction Source: MGI
  • regulation of cell proliferation Source: MGI
  • regulation of extrinsic apoptotic signaling pathway Source: MGI
  • response to amphetamine Source: MGI
  • response to pain Source: MGI
  • visual learning Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Catecholamine biosynthesis

Keywords - Ligandi

Copper, Metal-binding, Vitamin C

Enzyme and pathway databases

ReactomeiR-MMU-209905. Catecholamine biosynthesis.
UniPathwayiUPA00748; UER00735.

Names & Taxonomyi

Protein namesi
Recommended name:
Dopamine beta-hydroxylase (EC:1.14.17.11 Publication1 Publication)
Alternative name(s):
Dopamine beta-monooxygenase
Cleaved into the following chain:
Gene namesi
Name:Dbh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:94864. Dbh.

Subcellular locationi

Soluble dopamine beta-hydroxylase :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2020CytoplasmicSequence analysisAdd
BLAST
Transmembranei21 – 4121Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini42 – 621580IntragranularSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Disruption phenotypei

Complete embryonic lethality in homozygous dams, and 88% embryonic lethality for homozygous embryos in heterozygous dams. Only 12% of the homozygous pups from heterozygous dams are alive at birth. Mutant pups have no obvious phenotype at birth, but nearly half of them die within 48 h, and only 5% survive to adulthood. Three weeks after birth, mutant pups are runted and weigh only half as much as their littermates. Still, the weight of adult males reaches 80% and that of females 88% of that of their littermates. Besides, mutant mice display ptosis. Embryonic lethality is due to a lack of noradrenaline and can be prevented by treatment with dihydroxyphenylserine, a compound that can be converted into noradrenaline in the absence of Dbh.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 622622Dopamine beta-hydroxylasePRO_0000006357Add
BLAST
Chaini44 – 622579Soluble dopamine beta-hydroxylaseSequence analysisPRO_0000308210Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi68 – 681N-linked (GlcNAc...)Sequence analysis
Disulfide bondi158 ↔ 600By similarity
Glycosylationi188 – 1881N-linked (GlcNAc...)Sequence analysis
Disulfide bondi236 ↔ 287By similarity
Disulfide bondi273 ↔ 299By similarity
Modified residuei350 – 3501Phosphoserine; by CaMKSequence analysis
Disulfide bondi394 ↔ 507By similarity
Disulfide bondi398 ↔ 569By similarity
Disulfide bondi470 ↔ 492By similarity
Glycosylationi476 – 4761N-linked (GlcNAc...)Sequence analysis
Disulfide bondi532 – 532InterchainBy similarity
Disulfide bondi534 – 534InterchainBy similarity
Glycosylationi570 – 5701N-linked (GlcNAc...)Sequence analysis

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)LengthDescriptionGraphical viewFeature identifierActions
Sitei43 – 442CleavageBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ64237.
PaxDbiQ64237.
PRIDEiQ64237.

PTM databases

PhosphoSiteiQ64237.

Expressioni

Tissue specificityi

Detected in adrenal gland secretory granules (at protein level) (PubMed:7961964). Detected in adrenal gland (PubMed:1280432).2 Publications

Gene expression databases

BgeeiENSMUSG00000000889.
CleanExiMM_DBH.
GenevisibleiQ64237. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000000910.

Structurei

3D structure databases

ProteinModelPortaliQ64237.
SMRiQ64237. Positions 209-506.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 177117DOMONPROSITE-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.
GeneTreeiENSGT00530000063085.
HOGENOMiHOG000063669.
HOVERGENiHBG005519.
InParanoidiQ64237.
KOiK00503.
OMAiSYFGDAW.
OrthoDBiEOG091G03XS.
PhylomeDBiQ64237.
TreeFamiTF320698.

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.
IPR014783. Cu2_ascorb_mOase_CS-2.
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.
PS00085. CU2_MONOOXYGENASE_2. 1 hit.
PS50836. DOMON. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q64237-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQAHLSHQPC WSSLPSPSVR EAASMYGTAV AIFLVILVAA LRGSEPPESP
60 70 80 90 100
FPYHIPLDPE GILELSWNVS YVQEIIHFQL QVQGLRAGVL FGMSDRGEME
110 120 130 140 150
NADLIMLWTD GDRAYFADAW SDRKGQIHLD SQQDYQLLQA QRTRDGLSLL
160 170 180 190 200
FKRPFVTCDP KDYVIEDDTV HLVYGILEEP FQSLEAINTS GLHTGLQRVQ
210 220 230 240 250
LLKSEVPTPS MPEDVQTMDI RAPDILIPDN ETTYWCYITE LPPRFPRHHI
260 270 280 290 300
IMYEAIVTEG NEALVHHMEV FQCAAESEDF PQFNGPCDSK MKPDRLNYCR
310 320 330 340 350
HVLAAWALGA KAFYYPKEAG VPFGGPGSSP FLRLEVHYHN PRKIQGRQDS
360 370 380 390 400
SGIRLHYTAT LRRYDAGIME LGLVYTPLMA IPPQETAFVL TGYCTDKCTQ
410 420 430 440 450
MALQDSGIHI FASQLHTHLT GRKVVTVLAR DGQERKVVNR DNHYSPHFQE
460 470 480 490 500
IRMLKKVVTV YPGDVLITSC TYNTENKTLA TVGGFGILEE MCVNYVHYYP
510 520 530 540 550
QTELELCKSA VDDGFLQKYF HMVNRFSSEE VCTCPQASVP QQFSSVPWNS
560 570 580 590 600
FNRDMLKALY DYAPISMHCN KTSAVRFPGE WNLQPLPKIT STLEEPTPRC
610 620
PIRQTQSPAN PTVPITTEAD AE
Length:622
Mass (Da):70,314
Last modified:September 18, 2013 - v2
Checksum:i7D9FA1B622F3FCA8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1091T → S in AAB24330 (PubMed:1280432).Curated
Sequence conflicti197 – 1971Q → L in AAB24330 (PubMed:1280432).Curated
Sequence conflicti232 – 2321T → Q in AAB24330 (PubMed:1280432).Curated
Sequence conflicti356 – 3561H → P in AAB24330 (PubMed:1280432).Curated
Sequence conflicti437 – 4371V → E in AAB24330 (PubMed:1280432).Curated
Sequence conflicti449 – 4491Q → R in AAB24330 (PubMed:1280432).Curated
Sequence conflicti554 – 5541D → N in AAB24330 (PubMed:1280432).Curated
Sequence conflicti618 – 6214EADA → GGRC in AAB24330 (PubMed:1280432).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S50200 mRNA. Translation: AAB24330.1.
AK132245 mRNA. Translation: BAE21055.1.
AL954801 Genomic DNA. No translation available.
CH466542 Genomic DNA. Translation: EDL08360.1.
BC141022 mRNA. Translation: AAI41023.1.
BC171949 mRNA. Translation: AAI71949.1.
CCDSiCCDS38088.1.
PIRiJC1346.
RefSeqiNP_620392.2. NM_138942.3.
UniGeneiMm.167781.

Genome annotation databases

EnsembliENSMUST00000000910; ENSMUSP00000000910; ENSMUSG00000000889.
GeneIDi13166.
KEGGimmu:13166.
UCSCiuc008ixe.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S50200 mRNA. Translation: AAB24330.1.
AK132245 mRNA. Translation: BAE21055.1.
AL954801 Genomic DNA. No translation available.
CH466542 Genomic DNA. Translation: EDL08360.1.
BC141022 mRNA. Translation: AAI41023.1.
BC171949 mRNA. Translation: AAI71949.1.
CCDSiCCDS38088.1.
PIRiJC1346.
RefSeqiNP_620392.2. NM_138942.3.
UniGeneiMm.167781.

3D structure databases

ProteinModelPortaliQ64237.
SMRiQ64237. Positions 209-506.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000000910.

PTM databases

PhosphoSiteiQ64237.

Proteomic databases

MaxQBiQ64237.
PaxDbiQ64237.
PRIDEiQ64237.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000000910; ENSMUSP00000000910; ENSMUSG00000000889.
GeneIDi13166.
KEGGimmu:13166.
UCSCiuc008ixe.1. mouse.

Organism-specific databases

CTDi1621.
MGIiMGI:94864. Dbh.

Phylogenomic databases

eggNOGiKOG3568. Eukaryota.
ENOG410XR89. LUCA.
GeneTreeiENSGT00530000063085.
HOGENOMiHOG000063669.
HOVERGENiHBG005519.
InParanoidiQ64237.
KOiK00503.
OMAiSYFGDAW.
OrthoDBiEOG091G03XS.
PhylomeDBiQ64237.
TreeFamiTF320698.

Enzyme and pathway databases

UniPathwayiUPA00748; UER00735.
ReactomeiR-MMU-209905. Catecholamine biosynthesis.

Miscellaneous databases

PROiQ64237.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000000889.
CleanExiMM_DBH.
GenevisibleiQ64237. MM.

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.
IPR014783. Cu2_ascorb_mOase_CS-2.
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.
PS00085. CU2_MONOOXYGENASE_2. 1 hit.
PS50836. DOMON. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDOPO_MOUSE
AccessioniPrimary (citable) accession number: Q64237
Secondary accession number(s): Q3V1U4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 18, 2013
Last modified: September 7, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.