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UniProtKB - P15101 (DOPO_BOVIN)
Protein
Dopamine beta-hydroxylase
Gene
DBH
Organism
Bos taurus (Bovine)
Status
Functioni
Conversion of dopamine to noradrenaline.
1 PublicationCaution
Contrary to earlier results, does not contain a pyrroloquinoline quinone (PQQ) cofactor.2 Publications
Catalytic activityi
- dopamine + 2 L-ascorbate + O2 = (R)-noradrenaline + H2O + 2 monodehydro-L-ascorbate radical2 PublicationsEC:1.14.17.12 Publications
Cofactori
Cu2+2 PublicationsNote: Binds 2 copper ions per subunit.1 Publication
: (R)-noradrenaline biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes (R)-noradrenaline from dopamine.1 Publication 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 223 | Sequence analysis | 1 | |
Metal bindingi | 255 | Copper ABy similarity | 1 | |
Metal bindingi | 256 | Copper ABy similarity | 1 | |
Metal bindingi | 326 | Copper ABy similarity | 1 | |
Active sitei | 405 | Sequence analysis | 1 | |
Metal bindingi | 405 | Copper BBy similarity | 1 | |
Metal bindingi | 407 | Copper BBy similarity | 1 | |
Metal bindingi | 480 | Copper BBy similarity | 1 |
GO - Molecular functioni
- copper ion binding Source: UniProtKB
- dopamine beta-monooxygenase activity Source: UniProtKB
- L-ascorbic acid binding Source: UniProtKB-KW
GO - Biological processi
- dopamine catabolic process Source: UniProtKB
- norepinephrine biosynthetic process Source: UniProtKB
- octopamine biosynthetic process Source: GO_Central
Keywordsi
Molecular function | Monooxygenase, Oxidoreductase |
Biological process | Catecholamine biosynthesis |
Ligand | Copper, Metal-binding, Vitamin C |
Enzyme and pathway databases
SABIO-RKi | P15101 |
UniPathwayi | UPA00748;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 |
Organismi | Bos taurus (Bovine) |
Taxonomic identifieri | 9913 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Proteomesi |
|
Subcellular locationi
Other locations
- secretory vesicle lumen
- chromaffin granule lumen 1 Publication1 Publication
Other locations
Extracellular region or secreted
- extracellular space Source: UniProtKB
Other locations
- chromaffin granule lumen Source: UniProtKB-SubCell
- chromaffin granule membrane Source: UniProtKB
- integral component of membrane Source: UniProtKB-KW
- secretory granule lumen Source: UniProtKB
- secretory granule membrane Source: GO_Central
- transport vesicle membrane Source: UniProtKB-SubCell
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 9 | CytoplasmicSequence analysis | 9 | |
Transmembranei | 10 – 30 | Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST | 21 | |
Topological domaini | 31 – 610 | IntragranularSequence analysisAdd BLAST | 580 |
Keywords - Cellular componenti
Cytoplasmic vesicle, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000006355 | 1 – 610 | Dopamine beta-hydroxylaseAdd BLAST | 610 | |
ChainiPRO_0000308206 | 33 – 610 | Soluble dopamine beta-hydroxylase1 PublicationAdd BLAST | 578 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 147 ↔ 589 | 1 Publication | ||
Glycosylationi | 177 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 225 ↔ 276 | 1 Publication | ||
Disulfide bondi | 262 ↔ 288 | 1 Publication | ||
Disulfide bondi | 383 ↔ 496 | 1 Publication | ||
Disulfide bondi | 387 ↔ 558 | 1 Publication | ||
Disulfide bondi | 459 ↔ 481 | 1 Publication | ||
Disulfide bondi | 521 | Interchain1 Publication | ||
Disulfide bondi | 523 | Interchain1 Publication | ||
Glycosylationi | 559 | N-linked (GlcNAc...) asparagine1 Publication | 1 |
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 32 – 33 | Cleavage3 Publications | 2 |
Keywords - PTMi
Disulfide bond, GlycoproteinProteomic databases
PaxDbi | P15101 |
PRIDEi | P15101 |
PTM databases
iPTMneti | P15101 |
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
Bgeei | ENSBTAG00000004508, Expressed in adrenal gland and 14 other tissues |
Interactioni
Subunit structurei
Homotetramer; composed of two disulfide-linked dimers.
2 PublicationsProtein-protein interaction databases
BioGRIDi | 158157, 1 interactor |
STRINGi | 9913.ENSBTAP00000005924 |
Chemistry databases
BindingDBi | P15101 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 50 – 166 | DOMONPROSITE-ProRule annotationAdd BLAST | 117 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 585 – 610 | DisorderedSequence analysisAdd BLAST | 26 |
Sequence similaritiesi
Belongs to the copper type II ascorbate-dependent monooxygenase family.Curated
Keywords - Domaini
Signal-anchor, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG3568, Eukaryota |
InParanoidi | P15101 |
OrthoDBi | 1472750at2759 |
TreeFami | TF320698 |
Family and domain databases
CDDi | cd09631, DOMON_DOH, 1 hit |
Gene3Di | 2.60.120.230, 1 hit 2.60.120.310, 1 hit |
InterProi | View protein in InterPro IPR014784, Cu2_ascorb_mOase-like_C IPR020611, Cu2_ascorb_mOase_CS-1 IPR014783, Cu2_ascorb_mOase_CS-2 IPR000323, Cu2_ascorb_mOase_N IPR036939, Cu2_ascorb_mOase_N_sf IPR024548, Cu2_monoox_C IPR000945, DBH-like IPR045266, DOH_DOMON IPR005018, DOMON_domain IPR008977, PHM/PNGase_F_dom_sf IPR028460, Tbh/DBH |
PANTHERi | PTHR10157, PTHR10157, 1 hit |
Pfami | View protein in Pfam PF03712, Cu2_monoox_C, 1 hit PF01082, Cu2_monooxygen, 1 hit |
PRINTSi | PR00767, DBMONOXGNASE |
SMARTi | View protein in SMART SM00664, DoH, 1 hit |
SUPFAMi | SSF49742, SSF49742, 2 hits |
PROSITEi | View protein in PROSITE PS00084, CU2_MONOOXYGENASE_1, 1 hit PS00085, CU2_MONOOXYGENASE_2, 1 hit PS50836, DOMON, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P15101-1 [UniParc]FASTAAdd to basket
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
Sequence cautioni
The sequence AAA30490 differs from that shown. Reason: Erroneous initiation.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 35 | P → T AA sequence (PubMed:843373).Curated | 1 | |
Sequence conflicti | 40 | F → S in AAD09829 (PubMed:1693949).Curated | 1 | |
Sequence conflicti | 48 | P → T AA sequence (PubMed:843373).Curated | 1 | |
Sequence conflicti | 55 – 57 | SWN → RYV AA sequence (PubMed:2295597).Curated | 3 | |
Sequence conflicti | 74 | L → F AA sequence (PubMed:2295597).Curated | 1 | |
Sequence conflicti | 104 | Y → D in AAD09829 (PubMed:1693949).Curated | 1 | |
Sequence conflicti | 205 | R → C in AAA30356 (PubMed:2620060).Curated | 1 | |
Sequence conflicti | 215 | L → F in ABG81467 (PubMed:16305752).Curated | 1 | |
Sequence conflicti | 267 – 269 | ETI → RDH in AAA30356 (PubMed:2620060).Curated | 3 | |
Sequence conflicti | 349 | A → R in AAA30491 (PubMed:2207088).Curated | 1 | |
Sequence conflicti | 376 | A → P in AAD09829 (PubMed:1693949).Curated | 1 | |
Sequence conflicti | 560 | R → C AA sequence (PubMed:2295597).Curated | 1 | |
Sequence conflicti | 566 – 567 | FQ → LE in AAD09829 (PubMed:1693949).Curated | 2 | |
Sequence conflicti | 588 | H → Q in AAA30356 (PubMed:2620060).Curated | 1 |
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 |
PIRi | A33650 |
RefSeqi | NP_851338.1, NM_180995.2 |
Genome annotation databases
GeneIDi | 280758 |
KEGGi | bta:280758 |
Similar proteinsi
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 |
PIRi | A33650 |
RefSeqi | NP_851338.1, NM_180995.2 |
3D structure databases
SMRi | P15101 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 158157, 1 interactor |
STRINGi | 9913.ENSBTAP00000005924 |
Chemistry databases
BindingDBi | P15101 |
ChEMBLi | CHEMBL4702 |
DrugCentrali | P15101 |
PTM databases
iPTMneti | P15101 |
Proteomic databases
PaxDbi | P15101 |
PRIDEi | P15101 |
Genome annotation databases
GeneIDi | 280758 |
KEGGi | bta:280758 |
Organism-specific databases
CTDi | 1621 |
Phylogenomic databases
eggNOGi | KOG3568, Eukaryota |
InParanoidi | P15101 |
OrthoDBi | 1472750at2759 |
TreeFami | TF320698 |
Enzyme and pathway databases
UniPathwayi | UPA00748;UER00735 |
SABIO-RKi | P15101 |
Miscellaneous databases
PROi | PR:P15101 |
Gene expression databases
Bgeei | ENSBTAG00000004508, Expressed in adrenal gland and 14 other tissues |
Family and domain databases
CDDi | cd09631, DOMON_DOH, 1 hit |
Gene3Di | 2.60.120.230, 1 hit 2.60.120.310, 1 hit |
InterProi | View protein in InterPro IPR014784, Cu2_ascorb_mOase-like_C IPR020611, Cu2_ascorb_mOase_CS-1 IPR014783, Cu2_ascorb_mOase_CS-2 IPR000323, Cu2_ascorb_mOase_N IPR036939, Cu2_ascorb_mOase_N_sf IPR024548, Cu2_monoox_C IPR000945, DBH-like IPR045266, DOH_DOMON IPR005018, DOMON_domain IPR008977, PHM/PNGase_F_dom_sf IPR028460, Tbh/DBH |
PANTHERi | PTHR10157, PTHR10157, 1 hit |
Pfami | View protein in Pfam PF03712, Cu2_monoox_C, 1 hit PF01082, Cu2_monooxygen, 1 hit |
PRINTSi | PR00767, DBMONOXGNASE |
SMARTi | View protein in SMART SM00664, DoH, 1 hit |
SUPFAMi | SSF49742, SSF49742, 2 hits |
PROSITEi | View protein in PROSITE PS00084, CU2_MONOOXYGENASE_1, 1 hit PS00085, CU2_MONOOXYGENASE_2, 1 hit PS50836, DOMON, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | DOPO_BOVIN | |
Accessioni | P15101Primary (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: | February 23, 2022 | |
This is version 173 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families