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Dopamine beta-hydroxylase (EC 1.14.17.1) (Dopamine beta-monooxygenase) [Cleaved into: Soluble dopamine beta-hydroxylase]

 DOPO_BOVIN              Reviewed;         610 AA.
P15101; Q0V8A8; Q28094; Q9TVD1;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
02-OCT-2007, sequence version 2.
30-AUG-2017, entry version 147.
RecName: Full=Dopamine beta-hydroxylase;
EC=1.14.17.1 {ECO:0000269|PubMed:2620060, ECO:0000269|PubMed:4525162};
AltName: Full=Dopamine beta-monooxygenase;
Contains:
RecName: Full=Soluble dopamine beta-hydroxylase;
Name=DBH;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS OF SOLUBLE
AND MEMBRANE-BOUND FORM, CLEAVAGE SITE, SUBCELLULAR LOCATION,
CATALYTIC ACTIVITY, FUNCTION, COFACTOR, PATHWAY, AND TISSUE
SPECIFICITY.
PubMed=2620060; DOI=10.1021/bi00452a026;
Taljanidisz J., Stewart L., Smith A.J., Klinman J.P.;
"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.";
Biochemistry 28:10054-10061(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1688549;
Lewis E.J., Allison S., Fader D., Claflin V., Baizer L.;
"Bovine dopamine beta-hydroxylase cDNA. Complete coding sequence and
expression in mammalian cells with vaccinia virus vector.";
J. Biol. Chem. 265:1021-1028(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-610.
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
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.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 14-610, AND GLYCOSYLATION.
TISSUE=Adrenal medulla;
PubMed=1693949; DOI=10.1111/j.1471-4159.1990.tb08826.x;
Wu H.J., Parmer R.J., Koop A.H., Rozansky D.J., O'Connor D.T.;
"Molecular cloning, structure, and expression of dopamine-beta-
hydroxylase from bovine adrenal medulla.";
J. Neurochem. 55:97-105(1990).
[5]
PROTEIN SEQUENCE OF 33-610, AND GLYCOSYLATION.
PubMed=2295597;
Robertson J.G., Desai P.R., Kumar A., Farrington G.K.,
Fitzpatrick P.F., Villafranca J.J.;
"Primary amino acid sequence of bovine dopamine beta-hydroxylase.";
J. Biol. Chem. 265:1029-1035(1990).
[6]
PROTEIN SEQUENCE OF 33-50, TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
TISSUE=Adrenal medulla;
PubMed=843373; DOI=10.1016/0006-291X(77)90609-X;
Skotland T., Ljones T., Flatmark T., Sletten K.;
"NH2-terminal sequence of dopamine beta-hydroxylase from bovine
adrenal medulla.";
Biochem. Biophys. Res. Commun. 74:1483-1489(1977).
[7]
PROTEIN SEQUENCE OF 33-37.
PubMed=2909511;
Taylor C.S., Kent U.M., Fleming P.J.;
"The membrane-binding segment of dopamine beta-hydroxylase is not an
uncleaved signal sequence.";
J. Biol. Chem. 264:14-16(1989).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 39-566, GLYCOSYLATION AT ASN-177 AND
ASN-559, AND LACK OF PYRROLOQUINOLINE QUINONE BINDING.
PubMed=2207088; DOI=10.1021/bi00479a019;
Wang N., Southan C., DeWolf W.E. Jr., Wells T.N., Kruse L.I.,
Leatherbarrow R.J.;
"Bovine dopamine beta-hydroxylase, primary structure determined by
cDNA cloning and amino acid sequencing.";
Biochemistry 29:6466-6474(1990).
[9]
SUBUNIT, GLYCOSYLATION, TISSUE SPECIFICITY, COFACTOR, AND CATALYTIC
ACTIVITY.
PubMed=4525162; DOI=10.1073/pnas.70.8.2253;
Wallace E.F., Krantz M.J., Lovenberg W.;
"Dopamine-beta-hydroxylase: a tetrameric glycoprotein.";
Proc. Natl. Acad. Sci. U.S.A. 70:2253-2255(1973).
[10]
LACK OF PYRROLOQUINOLINE QUINONE BINDING.
PubMed=2555337;
Robertson J.G., Kumar A., Mancewicz J.A., Villafranca J.J.;
"Spectral studies of bovine dopamine beta-hydroxylase. Absence of
covalently bound pyrroloquinoline quinone.";
J. Biol. Chem. 264:19916-19921(1989).
[11]
DISULFIDE BONDS.
PubMed=7918370; DOI=10.1021/bi00204a019;
Robertson J.G., Adams G.W., Medzihradszky K.F., Burlingame A.L.,
Villafranca J.J.;
"Complete assignment of disulfide bonds in bovine dopamine beta-
hydroxylase.";
Biochemistry 33:11563-11575(1994).
-!- FUNCTION: Conversion of dopamine to noradrenaline.
{ECO:0000269|PubMed:2620060}.
-!- CATALYTIC ACTIVITY: 3,4-dihydroxyphenethylamine + ascorbate + O(2)
= noradrenaline + dehydroascorbate + H(2)O.
{ECO:0000269|PubMed:2620060, ECO:0000269|PubMed:4525162}.
-!- COFACTOR:
Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
Evidence={ECO:0000269|PubMed:2620060,
ECO:0000269|PubMed:4525162};
Note=Binds 2 copper ions per subunit.
{ECO:0000269|PubMed:4525162};
-!- PATHWAY: Catecholamine biosynthesis; (R)-noradrenaline
biosynthesis; (R)-noradrenaline from dopamine: step 1/1.
{ECO:0000269|PubMed:2620060}.
-!- SUBUNIT: Homotetramer; composed of two disulfide-linked dimers.
{ECO:0000269|PubMed:4525162, ECO:0000269|PubMed:7918370}.
-!- SUBCELLULAR LOCATION: Soluble dopamine beta-hydroxylase:
Cytoplasmic vesicle, secretory vesicle lumen. Cytoplasmic vesicle,
secretory vesicle, chromaffin granule lumen
{ECO:0000269|PubMed:843373, ECO:0000305|PubMed:2620060}.
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
membrane; Single-pass type II membrane protein. Cytoplasmic
vesicle, secretory vesicle, chromaffin granule membrane
{ECO:0000269|PubMed:2620060}; Single-pass type II membrane protein
{ECO:0000305}.
-!- TISSUE SPECIFICITY: Detected in chromaffin granules in the adrenal
medulla (at protein level) (PubMed:2620060, PubMed:843373,
PubMed:4525162). Detected in adrenal medulla (PubMed:2620060).
{ECO:0000269|PubMed:2620060, ECO:0000269|PubMed:4525162,
ECO:0000269|PubMed:843373}.
-!- PTM: Proteolytic cleavage after the membrane-anchor leads to the
release of the soluble form. {ECO:0000269|PubMed:2620060}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:1693949,
ECO:0000269|PubMed:2295597, ECO:0000269|PubMed:4525162}.
-!- SIMILARITY: Belongs to the copper type II ascorbate-dependent
monooxygenase family. {ECO:0000305}.
-!- CAUTION: Contrary to earlier results, does not contain a
pyrroloquinoline quinone (PQQ) cofactor.
{ECO:0000269|PubMed:2207088, ECO:0000269|PubMed:2555337}.
-!- SEQUENCE CAUTION:
Sequence=AAA30490.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; J02890; AAA30356.1; -; mRNA.
EMBL; J05160; AAA30490.1; ALT_INIT; mRNA.
EMBL; BT026311; ABG81467.1; -; mRNA.
EMBL; AF118638; AAD09829.1; -; mRNA.
EMBL; J02909; AAA30491.1; -; mRNA.
PIR; A33650; A33650.
RefSeq; NP_851338.1; NM_180995.2.
UniGene; Bt.4481; -.
SMR; P15101; -.
BioGrid; 158157; 1.
STRING; 9913.ENSBTAP00000005924; -.
BindingDB; P15101; -.
ChEMBL; CHEMBL4702; -.
PaxDb; P15101; -.
PRIDE; P15101; -.
Ensembl; ENSBTAT00000005924; ENSBTAP00000005924; ENSBTAG00000004508.
GeneID; 280758; -.
KEGG; bta:280758; -.
CTD; 1621; -.
eggNOG; KOG3568; Eukaryota.
eggNOG; ENOG410XR89; LUCA.
GeneTree; ENSGT00530000063085; -.
HOGENOM; HOG000063669; -.
HOVERGEN; HBG005519; -.
InParanoid; P15101; -.
KO; K00503; -.
OMA; CDSKMKP; -.
OrthoDB; EOG091G03XS; -.
TreeFam; TF320698; -.
Reactome; R-BTA-209905; Catecholamine biosynthesis.
SABIO-RK; P15101; -.
UniPathway; UPA00748; UER00735.
PRO; PR:P15101; -.
Proteomes; UP000009136; Chromosome 11.
Bgee; ENSBTAG00000004508; -.
ExpressionAtlas; P15101; baseline.
GO; GO:0034466; C:chromaffin granule lumen; IEA:UniProtKB-SubCell.
GO; GO:0042584; C:chromaffin granule membrane; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
GO; GO:0034774; C:secretory granule lumen; ISS:UniProtKB.
GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
GO; GO:0004500; F:dopamine beta-monooxygenase activity; IDA:UniProtKB.
GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
GO; GO:0048149; P:behavioral response to ethanol; IEA:Ensembl.
GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
GO; GO:0001816; P:cytokine production; IEA:Ensembl.
GO; GO:0042420; P:dopamine catabolic process; IDA:UniProtKB.
GO; GO:0042596; P:fear response; IEA:Ensembl.
GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
GO; GO:0042309; P:homoiothermy; IEA:Ensembl.
GO; GO:0002443; P:leukocyte mediated immunity; IEA:Ensembl.
GO; GO:0050900; P:leukocyte migration; IEA:Ensembl.
GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
GO; GO:0042711; P:maternal behavior; IEA:Ensembl.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:0042421; P:norepinephrine biosynthetic process; ISS:UniProtKB.
GO; GO:0006589; P:octopamine biosynthetic process; IBA:GO_Central.
GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:2001236; P:regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
GO; GO:0048265; P:response to pain; IEA:Ensembl.
GO; GO:0008542; P:visual learning; IEA:Ensembl.
Gene3D; 2.60.120.230; -; 1.
Gene3D; 2.60.120.310; -; 1.
InterPro; IPR014784; Cu2_ascorb_mOase-like_C.
InterPro; IPR020611; Cu2_ascorb_mOase_CS-1.
InterPro; IPR014783; Cu2_ascorb_mOase_CS-2.
InterPro; IPR000323; Cu2_ascorb_mOase_N.
InterPro; IPR024548; Cu2_monoox_C.
InterPro; IPR000945; DBH-rel.
InterPro; IPR005018; DOMON_domain.
InterPro; IPR008977; PHM/PNGase_F_dom.
InterPro; IPR028460; Tbh/DBH.
PANTHER; PTHR10157:SF31; PTHR10157:SF31; 1.
Pfam; PF03712; Cu2_monoox_C; 1.
Pfam; PF01082; Cu2_monooxygen; 1.
Pfam; PF03351; DOMON; 1.
PRINTS; PR00767; DBMONOXGNASE.
SMART; SM00664; DoH; 1.
SUPFAM; SSF49742; SSF49742; 2.
PROSITE; PS00084; CU2_MONOOXYGENASE_1; 1.
PROSITE; PS00085; CU2_MONOOXYGENASE_2; 1.
PROSITE; PS50836; DOMON; 1.
1: Evidence at protein level;
Catecholamine biosynthesis; Complete proteome; Copper;
Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond;
Glycoprotein; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
Vitamin C.
CHAIN 1 610 Dopamine beta-hydroxylase.
/FTId=PRO_0000006355.
CHAIN 33 610 Soluble dopamine beta-hydroxylase.
{ECO:0000269|PubMed:2295597}.
/FTId=PRO_0000308206.
TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}.
TRANSMEM 10 30 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 31 610 Intragranular. {ECO:0000255}.
DOMAIN 50 166 DOMON. {ECO:0000255|PROSITE-
ProRule:PRU00246}.
ACT_SITE 223 223 {ECO:0000255}.
ACT_SITE 405 405 {ECO:0000255}.
METAL 255 255 Copper A. {ECO:0000250}.
METAL 256 256 Copper A. {ECO:0000250}.
METAL 326 326 Copper A. {ECO:0000250}.
METAL 405 405 Copper B. {ECO:0000250|UniProtKB:P09172}.
METAL 407 407 Copper B. {ECO:0000250|UniProtKB:P09172}.
METAL 480 480 Copper B. {ECO:0000250|UniProtKB:P09172}.
SITE 32 33 Cleavage. {ECO:0000269|PubMed:2295597,
ECO:0000269|PubMed:2620060,
ECO:0000269|PubMed:843373}.
CARBOHYD 177 177 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:2207088}.
CARBOHYD 559 559 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:2207088}.
DISULFID 147 589 {ECO:0000269|PubMed:7918370}.
DISULFID 225 276 {ECO:0000269|PubMed:7918370}.
DISULFID 262 288 {ECO:0000269|PubMed:7918370}.
DISULFID 383 496 {ECO:0000269|PubMed:7918370}.
DISULFID 387 558 {ECO:0000269|PubMed:7918370}.
DISULFID 459 481 {ECO:0000269|PubMed:7918370}.
DISULFID 521 521 Interchain. {ECO:0000269|PubMed:7918370}.
DISULFID 523 523 Interchain. {ECO:0000269|PubMed:7918370}.
CONFLICT 35 35 P -> T (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 40 40 F -> S (in Ref. 4; AAD09829).
{ECO:0000305}.
CONFLICT 48 48 P -> T (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 55 57 SWN -> RYV (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 74 74 L -> F (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 104 104 Y -> D (in Ref. 4; AAD09829).
{ECO:0000305}.
CONFLICT 205 205 R -> C (in Ref. 1; AAA30356).
{ECO:0000305}.
CONFLICT 215 215 L -> F (in Ref. 3; ABG81467).
{ECO:0000305}.
CONFLICT 267 269 ETI -> RDH (in Ref. 1; AAA30356).
{ECO:0000305}.
CONFLICT 349 349 A -> R (in Ref. 8; AAA30491).
{ECO:0000305}.
CONFLICT 376 376 A -> P (in Ref. 4; AAD09829).
{ECO:0000305}.
CONFLICT 560 560 R -> C (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 566 567 FQ -> LE (in Ref. 4; AAD09829).
{ECO:0000305}.
CONFLICT 588 588 H -> Q (in Ref. 1; AAA30356).
{ECO:0000305}.
SEQUENCE 610 AA; 68141 MW; 709D23860617CD3A CRC64;
MQVPSPSVRE AASMYGTAVA VFLVILVAAL QGSAPAESPF PFHIPLDPEG TLELSWNISY
AQETIYFQLL VRELKAGVLF GMSDRGELEN ADLVVLWTDR DGAYFGDAWS DQKGQVHLDS
QQDYQLLRAQ RTPEGLYLLF KRPFGTCDPN DYLIEDGTVH LVYGFLEEPL RSLESINTSG
LHTGLQRVQL LKPSIPKPAL PADTRTMEIR APDVLIPGQQ TTYWCYVTEL PDGFPRHHIV
MYEPIVTEGN EALVHHMEVF QCAAEFETIP HFSGPCDSKM KPQRLNFCRH VLAAWALGAK
AFYYPEEAGL AFGGPGSSRF LRLEVHYHNP LVITGRRDSS GIRLYYTAAL RRFDAGIMEL
GLAYTPVMAI PPQETAFVLT GYCTDKCTQL ALPASGIHIF ASQLHTHLTG RKVVTVLARD
GRETEIVNRD NHYSPHFQEI RMLKKVVSVQ PGDVLITSCT YNTEDRRLAT VGGFGILEEM
CVNYVHYYPQ TQLELCKSAV DPGFLHKYFR LVNRFNSEEV CTCPQASVPE QFASVPWNSF
NREVLKALYG FAPISMHCNR SSAVRFQGEW NRQPLPEIVS RLEEPTPHCP ASQAQSPAGP
TVLNISGGKG


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