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

 DOPO_CANLF              Reviewed;         625 AA.
Q68CI2;
02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
22-NOV-2017, entry version 97.
RecName: Full=Dopamine beta-hydroxylase;
EC=1.14.17.1 {ECO:0000250|UniProtKB:P09172};
Contains:
RecName: Full=Soluble dopamine beta-hydroxylase;
Name=DBH;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS LYS-263 AND GLY-607.
STRAIN=Beagle; TISSUE=Brain;
PubMed=16210796; DOI=10.1292/jvms.67.861;
Takeuchi Y., Hashizume C., Chon E.M.H., Momozawa Y., Masuda K.,
Kikusui T., Mori Y.;
"Canine tyrosine hydroxylase (TH) gene and dopamine beta-hydroxylase
(DBH) gene: their sequences, genetic polymorphisms, and diversities
among five different dog breeds.";
J. Vet. Med. Sci. 67:861-867(2005).
-!- FUNCTION: Conversion of dopamine to noradrenaline.
{ECO:0000250|UniProtKB:P09172}.
-!- CATALYTIC ACTIVITY: 3,4-dihydroxyphenethylamine + ascorbate + O(2)
= noradrenaline + dehydroascorbate + H(2)O.
{ECO:0000250|UniProtKB:P09172}.
-!- COFACTOR:
Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
Evidence={ECO:0000250|UniProtKB:P09172};
Note=Binds 2 copper ions per subunit.
{ECO:0000250|UniProtKB:P09172};
-!- PATHWAY: Catecholamine biosynthesis; (R)-noradrenaline
biosynthesis; (R)-noradrenaline from dopamine: step 1/1.
{ECO:0000250|UniProtKB:P09172}.
-!- SUBUNIT: Homotetramer; composed of two disulfide-linked dimers.
{ECO:0000250|UniProtKB:P09172}.
-!- SUBCELLULAR LOCATION: Soluble dopamine beta-hydroxylase:
Cytoplasmic vesicle, secretory vesicle lumen
{ECO:0000250|UniProtKB:P09172}. Cytoplasmic vesicle, secretory
vesicle, chromaffin granule lumen {ECO:0000250|UniProtKB:P09172}.
Secreted {ECO:0000250|UniProtKB:P09172}.
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
membrane {ECO:0000250|UniProtKB:P09172}; Single-pass type II
membrane protein {ECO:0000250|UniProtKB:P09172}. Cytoplasmic
vesicle, secretory vesicle, chromaffin granule membrane
{ECO:0000250|UniProtKB:P09172}; Single-pass type II membrane
protein {ECO:0000250|UniProtKB:P09172}.
-!- PTM: Proteolytic cleavage after the membrane-anchor leads to the
release of the soluble form. {ECO:0000250|UniProtKB:P15101}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P09172}.
-!- SIMILARITY: Belongs to the copper type II ascorbate-dependent
monooxygenase family. {ECO:0000305}.
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EMBL; AB097057; BAD42327.1; -; mRNA.
RefSeq; NP_001005263.1; NM_001005263.1.
UniGene; Cfa.15803; -.
ProteinModelPortal; Q68CI2; -.
SMR; Q68CI2; -.
STRING; 9615.ENSCAFP00000029281; -.
PaxDb; Q68CI2; -.
Ensembl; ENSCAFT00000031457; ENSCAFP00000029281; ENSCAFG00000019783.
GeneID; 448806; -.
KEGG; cfa:448806; -.
CTD; 1621; -.
eggNOG; KOG3568; Eukaryota.
eggNOG; ENOG410XR89; LUCA.
GeneTree; ENSGT00530000063085; -.
HOGENOM; HOG000063669; -.
HOVERGEN; HBG005519; -.
InParanoid; Q68CI2; -.
KO; K00503; -.
OMA; CDSKMKP; -.
OrthoDB; EOG091G03XS; -.
TreeFam; TF320698; -.
Reactome; R-CFA-209905; Catecholamine biosynthesis.
UniPathway; UPA00748; UER00735.
Proteomes; UP000002254; Chromosome 9.
Bgee; ENSCAFG00000019783; -.
GO; GO:0034466; C:chromaffin granule lumen; IEA:UniProtKB-SubCell.
GO; GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; ISS: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:0030667; C:secretory granule membrane; ISS:UniProtKB.
GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
GO; GO:0004500; F:dopamine beta-monooxygenase activity; ISS: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; ISS: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; IPR000323; Cu2_ascorb_mOase_N.
InterPro; IPR036939; Cu2_ascorb_mOase_N_sf.
InterPro; IPR024548; Cu2_monoox_C.
InterPro; IPR005018; DOMON_domain.
InterPro; IPR008977; PHM/PNGase_F_dom_sf.
InterPro; IPR028460; Tbh/DBH.
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; PS50836; DOMON; 1.
2: Evidence at transcript level;
Catecholamine biosynthesis; Complete proteome; Copper;
Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Membrane;
Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome;
Secreted; Signal-anchor; Transmembrane; Transmembrane helix;
Vitamin C.
CHAIN 1 625 Dopamine beta-hydroxylase.
/FTId=PRO_0000305212.
CHAIN 33 625 Soluble dopamine beta-hydroxylase.
{ECO:0000255}.
/FTId=PRO_0000308207.
TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}.
TRANSMEM 10 30 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 31 625 Intragranular. {ECO:0000255}.
DOMAIN 50 166 DOMON. {ECO:0000255|PROSITE-
ProRule:PRU00246}.
ACT_SITE 222 222 {ECO:0000255}.
ACT_SITE 404 404 {ECO:0000255}.
METAL 254 254 Copper A. {ECO:0000250}.
METAL 255 255 Copper A. {ECO:0000250}.
METAL 325 325 Copper A. {ECO:0000250}.
METAL 404 404 Copper B. {ECO:0000250|UniProtKB:P09172}.
METAL 406 406 Copper B. {ECO:0000250|UniProtKB:P09172}.
METAL 479 479 Copper B. {ECO:0000250|UniProtKB:P09172}.
SITE 32 33 Cleavage. {ECO:0000250|UniProtKB:P15101}.
CARBOHYD 177 177 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 315 315 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 574 574 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 147 604 {ECO:0000250|UniProtKB:P09172}.
DISULFID 224 275 {ECO:0000250|UniProtKB:P09172}.
DISULFID 261 287 {ECO:0000250|UniProtKB:P09172}.
DISULFID 382 495 {ECO:0000250|UniProtKB:P09172}.
DISULFID 386 573 {ECO:0000250|UniProtKB:P09172}.
DISULFID 458 480 {ECO:0000250|UniProtKB:P09172}.
DISULFID 520 520 Interchain.
{ECO:0000250|UniProtKB:P09172}.
DISULFID 522 522 Interchain.
{ECO:0000250|UniProtKB:P09172}.
VARIANT 263 263 N -> K (frequent in Golden retrievers and
Labrador retrievers).
{ECO:0000269|PubMed:16210796}.
VARIANT 607 607 S -> G (in strain: Shiba).
{ECO:0000269|PubMed:16210796}.
SEQUENCE 625 AA; 69929 MW; F78B8442F7910EE8 CRC64;
MQVPSPSARE AASMYGTAVA VFLVLLVAVL QGLAPPESPL PYRIPLDPKG DLELSWDVSY
TQKTIYFQLL VQELKAGVLF GMSDRGELEN ADLVVLWTDG DNAYFGDAWS DQRGQIHLDS
QQDYQLLRAQ RTPKGLCLLF KRPFGTCDPK DYFIEDGTVH LVYGVLEEPF GSLEAINTSG
LQKGLQRVQL LKPKISIPAL PEDRRTMDIQ AHNVLIPSKT TYWCHLTKLP QDFPRHHIVM
YEPIITKGNE ALVHHIEIFQ CTNQFQNITS FSGSCDSKEK PQELKVCRHV LAAWALGARA
FYYPEEAGLA FGGSNSSRFL LLEIHYHNPT NIRGRYDNSG IRLHYTAKLR HFNAGIMELG
LVYTPVMAIP PKESAFVLTG YCTAKCTQAA LPPLGIRIFA SQLHTHLTGT KVVTMLVRDG
QEIEIVNRDD HYSPNFQEIR MLKKTVYVYP GDVLITSCTY NTEDKNEATV GGLGTQEEMC
VNYIHYYPQT QLELCKSHID PCFLQKYFHL VNRSNLGEYC TCPQASGTTC PQASGTTCPR
ASVPEQFASV PWNSFSRVVL KALYDFIPVT VHCNKSSAVR FPGKWDLQPL PEIISKLKEP
TPRCPTSRDQ SSSSLTVVNI GGGKV


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