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Protein

Dopamine beta-hydroxylase

Gene

DBH

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Conversion of dopamine to noradrenaline.1 Publication

Catalytic activityi

3,4-dihydroxyphenethylamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O.2 Publications

Cofactori

Cu2+2 PublicationsNote: Binds 2 copper ions per subunit.1 Publication

Pathwayi: (R)-noradrenaline biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes (R)-noradrenaline from dopamine.1 Publication
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 sitei223 – 2231Sequence analysis
Metal bindingi255 – 2551Copper ABy similarity
Metal bindingi256 – 2561Copper ABy similarity
Metal bindingi326 – 3261Copper ABy similarity
Active sitei405 – 4051Sequence analysis
Metal bindingi405 – 4051Copper BBy similarity
Metal bindingi407 – 4071Copper BBy similarity
Metal bindingi480 – 4801Copper BBy similarity

GO - Molecular functioni

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

GO - Biological processi

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-BTA-209905. Catecholamine biosynthesis.
SABIO-RKP15101.
UniPathwayiUPA00748; UER00735.

Names & Taxonomyi

Protein namesi
Recommended name:
Dopamine beta-hydroxylase (EC:1.14.17.12 Publications)
Alternative name(s):
Dopamine beta-monooxygenase
Cleaved into the following chain:
Gene namesi
Name:DBH
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 11

Subcellular locationi

Soluble dopamine beta-hydroxylase :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99CytoplasmicSequence analysis
Transmembranei10 – 3021Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini31 – 610580IntragranularSequence analysisAdd
BLAST

GO - Cellular componenti

  • chromaffin granule lumen Source: UniProtKB-SubCell
  • chromaffin granule membrane Source: UniProtKB
  • extracellular space Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • secretory granule lumen Source: UniProtKB
  • transport vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL4702.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 610610Dopamine beta-hydroxylasePRO_0000006355Add
BLAST
Chaini33 – 610578Soluble dopamine beta-hydroxylase1 PublicationPRO_0000308206Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi147 ↔ 5891 Publication
Glycosylationi177 – 1771N-linked (GlcNAc...)1 Publication
Disulfide bondi225 ↔ 2761 Publication
Disulfide bondi262 ↔ 2881 Publication
Disulfide bondi383 ↔ 4961 Publication
Disulfide bondi387 ↔ 5581 Publication
Disulfide bondi459 ↔ 4811 Publication
Disulfide bondi521 – 521Interchain1 Publication
Disulfide bondi523 – 523Interchain1 Publication
Glycosylationi559 – 5591N-linked (GlcNAc...)1 Publication

Post-translational modificationi

Proteolytic cleavage after the membrane-anchor leads to the release of the soluble form.1 Publication
N-glycosylated.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei32 – 332Cleavage3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP15101.
PRIDEiP15101.

Expressioni

Tissue specificityi

Detected in chromaffin granules in the adrenal medulla (at protein level) (PubMed:2620060, PubMed:843373, PubMed:4525162). Detected in adrenal medulla (PubMed:2620060).3 Publications

Gene expression databases

ExpressionAtlasiP15101. baseline.

Interactioni

Subunit structurei

Homotetramer; composed of two disulfide-linked dimers.2 Publications

Protein-protein interaction databases

BioGridi158157. 1 interaction.
STRINGi9913.ENSBTAP00000005924.

Chemistry

BindingDBiP15101.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 166117DOMONPROSITE-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.
InParanoidiP15101.
KOiK00503.
OMAiSYFGDAW.
OrthoDBiEOG091G03XS.
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.

P15101-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQVPSPSVRE AASMYGTAVA VFLVILVAAL QGSAPAESPF PFHIPLDPEG
60 70 80 90 100
TLELSWNISY AQETIYFQLL VRELKAGVLF GMSDRGELEN ADLVVLWTDR
110 120 130 140 150
DGAYFGDAWS DQKGQVHLDS QQDYQLLRAQ RTPEGLYLLF KRPFGTCDPN
160 170 180 190 200
DYLIEDGTVH LVYGFLEEPL RSLESINTSG LHTGLQRVQL LKPSIPKPAL
210 220 230 240 250
PADTRTMEIR APDVLIPGQQ TTYWCYVTEL PDGFPRHHIV MYEPIVTEGN
260 270 280 290 300
EALVHHMEVF QCAAEFETIP HFSGPCDSKM KPQRLNFCRH VLAAWALGAK
310 320 330 340 350
AFYYPEEAGL AFGGPGSSRF LRLEVHYHNP LVITGRRDSS GIRLYYTAAL
360 370 380 390 400
RRFDAGIMEL GLAYTPVMAI PPQETAFVLT GYCTDKCTQL ALPASGIHIF
410 420 430 440 450
ASQLHTHLTG RKVVTVLARD GRETEIVNRD NHYSPHFQEI RMLKKVVSVQ
460 470 480 490 500
PGDVLITSCT YNTEDRRLAT VGGFGILEEM CVNYVHYYPQ TQLELCKSAV
510 520 530 540 550
DPGFLHKYFR LVNRFNSEEV CTCPQASVPE QFASVPWNSF NREVLKALYG
560 570 580 590 600
FAPISMHCNR SSAVRFQGEW NRQPLPEIVS RLEEPTPHCP ASQAQSPAGP
610
TVLNISGGKG
Length:610
Mass (Da):68,141
Last modified:October 2, 2007 - v2
Checksum:i709D23860617CD3A
GO

Sequence cautioni

The sequence AAA30490 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351P → T AA sequence (PubMed:843373).Curated
Sequence conflicti40 – 401F → S in AAD09829 (PubMed:1693949).Curated
Sequence conflicti48 – 481P → T AA sequence (PubMed:843373).Curated
Sequence conflicti55 – 573SWN → RYV AA sequence (PubMed:2295597).Curated
Sequence conflicti74 – 741L → F AA sequence (PubMed:2295597).Curated
Sequence conflicti104 – 1041Y → D in AAD09829 (PubMed:1693949).Curated
Sequence conflicti205 – 2051R → C in AAA30356 (PubMed:2620060).Curated
Sequence conflicti215 – 2151L → F in ABG81467 (PubMed:16305752).Curated
Sequence conflicti267 – 2693ETI → RDH in AAA30356 (PubMed:2620060).Curated
Sequence conflicti349 – 3491A → R in AAA30491 (PubMed:2207088).Curated
Sequence conflicti376 – 3761A → P in AAD09829 (PubMed:1693949).Curated
Sequence conflicti560 – 5601R → C AA sequence (PubMed:2295597).Curated
Sequence conflicti566 – 5672FQ → LE in AAD09829 (PubMed:1693949).Curated
Sequence conflicti588 – 5881H → Q in AAA30356 (PubMed:2620060).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02890 mRNA. Translation: AAA30356.1.
J05160 mRNA. Translation: AAA30490.1. Different initiation.
BT026311 mRNA. Translation: ABG81467.1.
AF118638 mRNA. Translation: AAD09829.1.
J02909 mRNA. Translation: AAA30491.1.
PIRiA33650.
RefSeqiNP_851338.1. NM_180995.2.
UniGeneiBt.4481.

Genome annotation databases

EnsembliENSBTAT00000005924; ENSBTAP00000005924; ENSBTAG00000004508.
GeneIDi280758.
KEGGibta:280758.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02890 mRNA. Translation: AAA30356.1.
J05160 mRNA. Translation: AAA30490.1. Different initiation.
BT026311 mRNA. Translation: ABG81467.1.
AF118638 mRNA. Translation: AAD09829.1.
J02909 mRNA. Translation: AAA30491.1.
PIRiA33650.
RefSeqiNP_851338.1. NM_180995.2.
UniGeneiBt.4481.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi158157. 1 interaction.
STRINGi9913.ENSBTAP00000005924.

Chemistry

BindingDBiP15101.
ChEMBLiCHEMBL4702.

Proteomic databases

PaxDbiP15101.
PRIDEiP15101.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000005924; ENSBTAP00000005924; ENSBTAG00000004508.
GeneIDi280758.
KEGGibta:280758.

Organism-specific databases

CTDi1621.

Phylogenomic databases

eggNOGiKOG3568. Eukaryota.
ENOG410XR89. LUCA.
GeneTreeiENSGT00530000063085.
HOGENOMiHOG000063669.
HOVERGENiHBG005519.
InParanoidiP15101.
KOiK00503.
OMAiSYFGDAW.
OrthoDBiEOG091G03XS.
TreeFamiTF320698.

Enzyme and pathway databases

UniPathwayiUPA00748; UER00735.
ReactomeiR-BTA-209905. Catecholamine biosynthesis.
SABIO-RKP15101.

Miscellaneous databases

PROiP15101.

Gene expression databases

ExpressionAtlasiP15101. baseline.

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_BOVIN
AccessioniPrimary (citable) accession number: P15101
Secondary accession number(s): Q0V8A8, Q28094, Q9TVD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 2, 2007
Last modified: September 7, 2016
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Contrary to earlier results, does not contain a pyrroloquinoline quinone (PQQ) cofactor.2 Publications

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.