DOPO_CANLF
ID DOPO_CANLF Reviewed; 625 AA.
AC Q68CI2;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Dopamine beta-hydroxylase;
DE EC=1.14.17.1 {ECO:0000250|UniProtKB:P09172};
DE Contains:
DE RecName: Full=Soluble dopamine beta-hydroxylase;
GN Name=DBH;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS LYS-263 AND GLY-607.
RC STRAIN=Beagle; TISSUE=Brain;
RX PubMed=16210796; DOI=10.1292/jvms.67.861;
RA Takeuchi Y., Hashizume C., Chon E.M.H., Momozawa Y., Masuda K., Kikusui T.,
RA Mori Y.;
RT "Canine tyrosine hydroxylase (TH) gene and dopamine beta-hydroxylase (DBH)
RT gene: their sequences, genetic polymorphisms, and diversities among five
RT different dog breeds.";
RL J. Vet. Med. Sci. 67:861-867(2005).
CC -!- FUNCTION: Conversion of dopamine to noradrenaline.
CC {ECO:0000250|UniProtKB:P09172}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dopamine + 2 L-ascorbate + O2 = (R)-noradrenaline + H2O + 2
CC monodehydro-L-ascorbate radical; Xref=Rhea:RHEA:19117,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:38290,
CC ChEBI:CHEBI:59513, ChEBI:CHEBI:59905, ChEBI:CHEBI:72587;
CC EC=1.14.17.1; Evidence={ECO:0000250|UniProtKB:P09172};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:P09172};
CC Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:P09172};
CC -!- PATHWAY: Catecholamine biosynthesis; (R)-noradrenaline biosynthesis;
CC (R)-noradrenaline from dopamine: step 1/1.
CC {ECO:0000250|UniProtKB:P09172}.
CC -!- SUBUNIT: Homotetramer; composed of two disulfide-linked dimers.
CC {ECO:0000250|UniProtKB:P09172}.
CC -!- SUBCELLULAR LOCATION: [Soluble dopamine beta-hydroxylase]: Cytoplasmic
CC vesicle, secretory vesicle lumen {ECO:0000250|UniProtKB:P09172}.
CC Cytoplasmic vesicle, secretory vesicle, chromaffin granule lumen
CC {ECO:0000250|UniProtKB:P09172}. Secreted
CC {ECO:0000250|UniProtKB:P09172}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000250|UniProtKB:P09172}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P09172}. Cytoplasmic vesicle, secretory vesicle,
CC chromaffin granule membrane {ECO:0000250|UniProtKB:P09172}; Single-pass
CC type II membrane protein {ECO:0000250|UniProtKB:P09172}.
CC -!- PTM: Proteolytic cleavage after the membrane-anchor leads to the
CC release of the soluble form. {ECO:0000250|UniProtKB:P15101}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P09172}.
CC -!- SIMILARITY: Belongs to the copper type II ascorbate-dependent
CC monooxygenase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB097057; BAD42327.1; -; mRNA.
DR RefSeq; NP_001005263.1; NM_001005263.1.
DR AlphaFoldDB; Q68CI2; -.
DR SMR; Q68CI2; -.
DR STRING; 9612.ENSCAFP00000029281; -.
DR PaxDb; Q68CI2; -.
DR GeneID; 448806; -.
DR KEGG; cfa:448806; -.
DR CTD; 1621; -.
DR eggNOG; KOG3568; Eukaryota.
DR HOGENOM; CLU_017939_3_0_1; -.
DR InParanoid; Q68CI2; -.
DR OMA; CAPEMDN; -.
DR OrthoDB; 1472750at2759; -.
DR TreeFam; TF320698; -.
DR BRENDA; 1.14.16.2; 1153.
DR Reactome; R-CFA-209905; Catecholamine biosynthesis.
DR UniPathway; UPA00748; UER00735.
DR Proteomes; UP000002254; Chromosome 9.
DR Bgee; ENSCAFG00000019783; Expressed in adrenal cortex and 16 other tissues.
DR GO; GO:0034466; C:chromaffin granule lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0034774; C:secretory granule lumen; ISS:UniProtKB.
DR GO; GO:0030667; C:secretory granule membrane; ISS:UniProtKB.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0004500; F:dopamine beta-monooxygenase activity; ISS:UniProtKB.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0042420; P:dopamine catabolic process; ISS:UniProtKB.
DR GO; GO:0042421; P:norepinephrine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006589; P:octopamine biosynthetic process; IBA:GO_Central.
DR CDD; cd09631; DOMON_DOH; 1.
DR Gene3D; 2.60.120.230; -; 1.
DR Gene3D; 2.60.120.310; -; 1.
DR InterPro; IPR014784; Cu2_ascorb_mOase-like_C.
DR InterPro; IPR000323; Cu2_ascorb_mOase_N.
DR InterPro; IPR036939; Cu2_ascorb_mOase_N_sf.
DR InterPro; IPR024548; Cu2_monoox_C.
DR InterPro; IPR000945; DBH-like.
DR InterPro; IPR045266; DOH_DOMON.
DR InterPro; IPR005018; DOMON_domain.
DR InterPro; IPR008977; PHM/PNGase_F_dom_sf.
DR InterPro; IPR028460; Tbh/DBH.
DR PANTHER; PTHR10157; PTHR10157; 1.
DR Pfam; PF03712; Cu2_monoox_C; 1.
DR Pfam; PF01082; Cu2_monooxygen; 1.
DR PRINTS; PR00767; DBMONOXGNASE.
DR SMART; SM00664; DoH; 1.
DR SUPFAM; SSF49742; SSF49742; 2.
DR PROSITE; PS50836; DOMON; 1.
PE 2: Evidence at transcript level;
KW Catecholamine biosynthesis; Copper; Cytoplasmic vesicle; Disulfide bond;
KW Glycoprotein; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Secreted; Signal-anchor; Transmembrane;
KW Transmembrane helix; Vitamin C.
FT CHAIN 1..625
FT /note="Dopamine beta-hydroxylase"
FT /id="PRO_0000305212"
FT CHAIN 33..625
FT /note="Soluble dopamine beta-hydroxylase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000308207"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..625
FT /note="Intragranular"
FT /evidence="ECO:0000255"
FT DOMAIN 50..166
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT ACT_SITE 222
FT /evidence="ECO:0000255"
FT ACT_SITE 404
FT /evidence="ECO:0000255"
FT BINDING 254
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P09172"
FT BINDING 406
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P09172"
FT BINDING 479
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P09172"
FT SITE 32..33
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P15101"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 147..604
FT /evidence="ECO:0000250|UniProtKB:P09172"
FT DISULFID 224..275
FT /evidence="ECO:0000250|UniProtKB:P09172"
FT DISULFID 261..287
FT /evidence="ECO:0000250|UniProtKB:P09172"
FT DISULFID 382..495
FT /evidence="ECO:0000250|UniProtKB:P09172"
FT DISULFID 386..573
FT /evidence="ECO:0000250|UniProtKB:P09172"
FT DISULFID 458..480
FT /evidence="ECO:0000250|UniProtKB:P09172"
FT DISULFID 520
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P09172"
FT DISULFID 522
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P09172"
FT VARIANT 263
FT /note="N -> K (frequent in Golden retrievers and Labrador
FT retrievers)"
FT /evidence="ECO:0000269|PubMed:16210796"
FT VARIANT 607
FT /note="S -> G (in strain: Shiba)"
FT /evidence="ECO:0000269|PubMed:16210796"
SQ 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
