Dopamine beta-hydroxylase - Bos taurus (Bovine)

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P15101 (DOPO_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 104. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Dopamine beta-hydroxylase
EC=1.14.17.1

Alternative name(s):
Dopamine beta-monooxygenase

Cleaved into the following chain:

Soluble dopamine beta-hydroxylase

Gene names

Name:

DBH

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	610 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Conversion of dopamine to noradrenaline.
Catalytic activity	3,4-dihydroxyphenethylamine + ascorbate + O₂ = noradrenaline + dehydroascorbate + H₂O.
Cofactor	Binds 1 PQQ per subunit. Binds 2 copper ions per subunit.
Pathway	Catecholamine biosynthesis; (R)-noradrenaline biosynthesis; (R)-noradrenaline from dopamine: step 1/1.
Subunit structure	Homotetramer composed of two non-covalently bound disulfide-linked dimers. Ref.9
Subcellular location	Soluble dopamine beta-hydroxylase: Cytoplasmic vesicle › secretory vesicle lumen. Cytoplasmic vesicle › secretory vesicle › chromaffin granule lumen. Cytoplasmic vesicle › secretory vesicle membrane; Single-pass type II membrane protein. Cytoplasmic vesicle › secretory vesicle › chromaffin granule membrane; Single-pass type II membrane protein Potential.
Sequence similarities	Belongs to the copper type II ascorbate-dependent monooxygenase family. Contains 1 DOMON domain.
Sequence caution	The sequence AAA30490.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Catecholamine biosynthesis
Cellular component	Cytoplasmic vesicle Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Copper Metal-binding PQQ Vitamin C
Molecular function	Monooxygenase Oxidoreductase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	chromaffin granule lumen Inferred from electronic annotation. Source: UniProtKB-SubCell chromaffin granule membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW transport vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW copper ion binding Inferred from electronic annotation. Source: InterPro dopamine beta-monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 610

610

Dopamine beta-hydroxylase

PRO_0000006355

Chain

33 – 610

578

Soluble dopamine beta-hydroxylase Potential

PRO_0000308206

Regions

Topological domain

1 – 9

Cytoplasmic Potential

Transmembrane

10 – 30

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

31 – 610

580

Intragranular Potential

Domain

50 – 166

117

DOMON

Sites

Active site

223

Potential

Active site

405

Potential

Metal binding

255

Copper A By similarity

Metal binding

256

Copper A By similarity

Metal binding

326

Copper A By similarity

Metal binding

405

Copper B By similarity

Metal binding

407

Copper B By similarity

Metal binding

480

Copper B By similarity

Amino acid modifications

Glycosylation

177

N-linked (GlcNAc...)

Glycosylation

559

N-linked (GlcNAc...)

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Interchain Ref.9

Disulfide bond

523

Interchain Ref.9

Experimental info

Sequence conflict

P → T AA sequence Ref.6

Sequence conflict

F → S in AAD09829. Ref.4

Sequence conflict

P → T AA sequence Ref.6

Sequence conflict

55 – 57

SWN → RYV AA sequence Ref.5

Sequence conflict

L → F AA sequence Ref.5

Sequence conflict

104

Y → D in AAD09829. Ref.4

Sequence conflict

205

R → C in AAA30356. Ref.1

Sequence conflict

215

L → F in ABG81467. Ref.3

Sequence conflict

267 – 269

ETI → RDH in AAA30356. Ref.1

Sequence conflict

349

A → R in AAA30491. Ref.8

Sequence conflict

376

A → P in AAD09829. Ref.4

Sequence conflict

560

R → C AA sequence Ref.5

Sequence conflict

566 – 567

FQ → LE in AAD09829. Ref.4

Sequence conflict

588

H → Q in AAA30356. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P15101 [UniParc].

Last modified October 2, 2007. Version 2.
Checksum: 709D23860617CD3A
Show »

FASTA

610

68,141

        10         20         30         40         50         60 
MQVPSPSVRE AASMYGTAVA VFLVILVAAL QGSAPAESPF PFHIPLDPEG TLELSWNISY 

        70         80         90        100        110        120 
AQETIYFQLL VRELKAGVLF GMSDRGELEN ADLVVLWTDR DGAYFGDAWS DQKGQVHLDS 

       130        140        150        160        170        180 
QQDYQLLRAQ RTPEGLYLLF KRPFGTCDPN DYLIEDGTVH LVYGFLEEPL RSLESINTSG 

       190        200        210        220        230        240 
LHTGLQRVQL LKPSIPKPAL PADTRTMEIR APDVLIPGQQ TTYWCYVTEL PDGFPRHHIV 

       250        260        270        280        290        300 
MYEPIVTEGN EALVHHMEVF QCAAEFETIP HFSGPCDSKM KPQRLNFCRH VLAAWALGAK 

       310        320        330        340        350        360 
AFYYPEEAGL AFGGPGSSRF LRLEVHYHNP LVITGRRDSS GIRLYYTAAL RRFDAGIMEL 

       370        380        390        400        410        420 
GLAYTPVMAI PPQETAFVLT GYCTDKCTQL ALPASGIHIF ASQLHTHLTG RKVVTVLARD 

       430        440        450        460        470        480 
GRETEIVNRD NHYSPHFQEI RMLKKVVSVQ PGDVLITSCT YNTEDRRLAT VGGFGILEEM 

       490        500        510        520        530        540 
CVNYVHYYPQ TQLELCKSAV DPGFLHKYFR LVNRFNSEEV CTCPQASVPE QFASVPWNSF 

       550        560        570        580        590        600 
NREVLKALYG FAPISMHCNR SSAVRFQGEW NRQPLPEIVS RLEEPTPHCP ASQAQSPAGP 

       610 
TVLNISGGKG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of bovine adrenal dopamine beta-monooxygenase, as deduced from cDNA and protein sequencing: evidence that the membrane-bound form of the enzyme is anchored by an uncleaved signal peptide." Taljanidisz J., Stewart L., Smith A.J., Klinman J.P. Biochemistry 28:10054-10061(1989) [PubMed: 2620060] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Bovine dopamine beta-hydroxylase cDNA. Complete coding sequence and expression in mammalian cells with vaccinia virus vector." Lewis E.J., Allison S., Fader D., Claflin V., Baizer L. J. Biol. Chem. 265:1021-1028(1990) [PubMed: 1688549] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-610.
[4]	"Molecular cloning, structure, and expression of dopamine-beta-hydroxylase from bovine adrenal medulla." Wu H.J., Parmer R.J., Koop A.H., Rozansky D.J., O'Connor D.T. J. Neurochem. 55:97-105(1990) [PubMed: 1693949] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-610. Tissue: Adrenal medulla.
[5]	"Primary amino acid sequence of bovine dopamine beta-hydroxylase." Robertson J.G., Desai P.R., Kumar A., Farrington G.K., Fitzpatrick P.F., Villafranca J.J. J. Biol. Chem. 265:1029-1035(1990) [PubMed: 2295597] [Abstract] Cited for: PROTEIN SEQUENCE OF 33-610.
[6]	"NH2-terminal sequence of dopamine beta-hydroxylase from bovine adrenal medulla." Skotland T., Ljones T., Flatmark T., Sletten K. Biochem. Biophys. Res. Commun. 74:1483-1489(1977) [PubMed: 843373] [Abstract] Cited for: PROTEIN SEQUENCE OF 33-50. Tissue: Adrenal medulla.
[7]	"The membrane-binding segment of dopamine beta-hydroxylase is not an uncleaved signal sequence." Taylor C.S., Kent U.M., Fleming P.J. J. Biol. Chem. 264:14-16(1989) [PubMed: 2909511] [Abstract] Cited for: PROTEIN SEQUENCE OF 33-37.
[8]	"Bovine dopamine beta-hydroxylase, primary structure determined by cDNA cloning and amino acid sequencing." Wang N., Southan C., DeWolf W.E. Jr., Wells T.N., Kruse L.I., Leatherbarrow R.J. Biochemistry 29:6466-6474(1990) [PubMed: 2207088] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 39-566.
[9]	"Complete assignment of disulfide bonds in bovine dopamine beta-hydroxylase." Robertson J.G., Adams G.W., Medzihradszky K.F., Burlingame A.L., Villafranca J.J. Biochemistry 33:11563-11575(1994) [PubMed: 7918370] [Abstract] Cited for: DISULFIDE BONDS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00698276.
PIR	A33650.
RefSeq	NP_851338.1. NM_180995.2.
UniGene	Bt.4481.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P15101.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000005924; ENSBTAP00000005924; ENSBTAG00000004508.
GeneID	280758.
KEGG	bta:280758.
Organism-specific databases
CTD	1621.
Phylogenomic databases
eggNOG	maNOG05453.
GeneTree	ENSGT00530000063085.
HOVERGEN	HBG005519.
InParanoid	P15101.
OrthoDB	EOG4SN1ND.
PhylomeDB	P15101.
Family and domain databases
InterPro	IPR014784. Cu2_ascorb_mOase-like_C. IPR020611. Cu2_ascorb_mOase_CS-1. IPR014783. Cu2_ascorb_mOase_CS-2. IPR000323. Cu2_ascorb_mOase_N. IPR005018. DOMON_domain. IPR000945. Dopamine_b_mOase. IPR008977. PHM/PNGase_F_dom. [Graphical view]
Gene3D	G3DSA:2.60.120.230. Cu2_ascorb_mOase_core. 1 hit. G3DSA:2.60.120.310. Cu2_ascorb_mOase_core. 1 hit.
KO	K00503.
PANTHER	PTHR10157. Dopamine_b_mOase. 1 hit.
Pfam	PF01082. Cu2_monooxygen. 1 hit. PF03351. DOMON. 1 hit. [Graphical view]
PRINTS	PR00767. DBMONOXGNASE.
SMART	SM00664. DoH. 1 hit. [Graphical view]
SUPFAM	SSF49742. PHM_PNGase_F. 2 hits.
PROSITE	PS00084. CU2_MONOOXYGENASE_1. 1 hit. PS00085. CU2_MONOOXYGENASE_2. 1 hit. PS50836. DOMON. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DOPO_BOVIN

Accession

Primary (citable) accession number: P15101
Secondary accession number(s): Q0V8A8, Q28094, Q9TVD1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	October 2, 2007
Last modified:	January 25, 2012
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following chain:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents