DOPO_HORSE
ID DOPO_HORSE Reviewed; 610 AA.
AC Q9XTA0;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 114.
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 Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12592705; DOI=10.1080/1042517021000013553;
RA Sato F., Hasegawa T., Katayama Y., Ishida N.;
RT "Molecular cloning, nucleotide sequence and presence of multiple functional
RT polyadenylation signals in the 3'-untranslated region of equine dopamine
RT beta-hydroxylase cDNA.";
RL DNA Seq. 13:257-262(2002).
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 -!- TISSUE SPECIFICITY: Detected in adrenal medulla chromaffin cells.
CC {ECO:0000269|PubMed:12592705}.
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}.
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DR EMBL; AB029430; BAA82274.1; -; mRNA.
DR RefSeq; NP_001075239.2; NM_001081770.2.
DR AlphaFoldDB; Q9XTA0; -.
DR SMR; Q9XTA0; -.
DR STRING; 9796.ENSECAP00000017330; -.
DR PaxDb; Q9XTA0; -.
DR GeneID; 791247; -.
DR KEGG; ecb:791247; -.
DR CTD; 1621; -.
DR InParanoid; Q9XTA0; -.
DR OrthoDB; 1472750at2759; -.
DR UniPathway; UPA00748; UER00735.
DR Proteomes; UP000002281; Unplaced.
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 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; IPR020611; Cu2_ascorb_mOase_CS-1.
DR InterPro; IPR014783; Cu2_ascorb_mOase_CS-2.
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; PS00084; CU2_MONOOXYGENASE_1; 1.
DR PROSITE; PS00085; CU2_MONOOXYGENASE_2; 1.
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..610
FT /note="Dopamine beta-hydroxylase"
FT /id="PRO_0000305213"
FT CHAIN 33..610
FT /note="Soluble dopamine beta-hydroxylase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000308208"
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..610
FT /note="Intragranular"
FT /evidence="ECO:0000255"
FT DOMAIN 50..166
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT REGION 586..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 223
FT /evidence="ECO:0000255"
FT ACT_SITE 405
FT /evidence="ECO:0000255"
FT BINDING 255
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P09172"
FT BINDING 407
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P09172"
FT BINDING 480
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 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 147..589
FT /evidence="ECO:0000250|UniProtKB:P09172"
FT DISULFID 225..276
FT /evidence="ECO:0000250|UniProtKB:P09172"
FT DISULFID 262..288
FT /evidence="ECO:0000250|UniProtKB:P09172"
FT DISULFID 383..496
FT /evidence="ECO:0000250|UniProtKB:P09172"
FT DISULFID 387..558
FT /evidence="ECO:0000250|UniProtKB:P09172"
FT DISULFID 459..481
FT /evidence="ECO:0000250|UniProtKB:P09172"
FT DISULFID 521
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P09172"
FT DISULFID 523
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P09172"
SQ SEQUENCE 610 AA; 68229 MW; 09B6095DD0551D8D CRC64;
MKVPSPSVRE AASMYGTAVA IFLVILVAAL QGSEPPESPF PYRIPLDPEG TLELSWNVSY
VQETIHFQLL VRELKAGVLF GMSDRGELEN ADLVVLWTDG DSAYFGDAWS DQKGWIHLDA
QQDYQLLRAQ RTPEGLSLLF KRPFGTCDPK DYLIEDGTVH LVYGILEEPF WSLEAINTSA
LHTGLQRVQL LKPNVSVPAL PADMRTMEVR APDVLVPGQE TTYWCYITEL PDGFPRHHIV
MYEPIVTEGN EALVHHMEVF QCAAEFESFP QFNGPCDSKM KPSRLNYCRN VLAAWALGAK
AFYYPEEAGL AFGGAGSSRF LRLEVHYHNP LKIEGRRDSS GIRLYYTATL RRFDAGIMEL
GLVYTPVMAI PPQETAFVLT GYCTDKCTQL ALPPSGIHIF ASQLHTHLTG RKVVTVLARD
GREREVVNRD DHYSPHFQEI RMLKKVVSVH PGDVLITSCT YNTEDRKLAT VGGFGILEEM
CVNYVHYYPQ TQLELCKSAV DPGFLQKYFH FVNRFNGEEV CTCPQASVPE QFATVPWNSF
NRQVLSALYG FAPISMHCNR SSAVRFQGDW NLQPLPEIIS KLEEPTPRCP ASRGRSPAGP
TVVDIGGGKG
