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

 DOPO_MOUSE              Reviewed;         622 AA.
Q64237; Q3V1U4;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
18-SEP-2013, sequence version 2.
22-NOV-2017, entry version 142.
RecName: Full=Dopamine beta-hydroxylase;
EC=1.14.17.1 {ECO:0000269|PubMed:27148966, ECO:0000305|PubMed:7715704};
AltName: Full=Dopamine beta-monooxygenase;
Contains:
RecName: Full=Soluble dopamine beta-hydroxylase;
Name=Dbh;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=1280432; DOI=10.1016/0006-291X(92)91598-K;
Nakano T., Kobayashi K., Saito S., Fujita K., Nagatsu T.;
"Mouse dopamine beta-hydroxylase: primary structure deduced from the
cDNA sequence and exon/intron organization of the gene.";
Biochem. Biophys. Res. Commun. 189:590-599(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=7961964;
Kobayashi K., Morita S., Mizuguchi T., Sawada H., Yamada K.,
Nagatsu I., Fujita K., Nagatsu T.;
"Functional and high level expression of human dopamine beta-
hydroxylase in transgenic mice.";
J. Biol. Chem. 269:29725-29731(1994).
[7]
DISRUPTION PHENOTYPE, FUNCTION, PATHWAY, AND CATALYTIC ACTIVITY.
PubMed=7715704; DOI=10.1038/374643a0;
Thomas S.A., Matsumoto A.M., Palmiter R.D.;
"Noradrenaline is essential for mouse fetal development.";
Nature 374:643-646(1995).
[8]
DISRUPTION PHENOTYPE, FUNCTION, AND PATHWAY.
PubMed=27148966; DOI=10.1371/journal.pone.0154864;
Cubells J.F., Schroeder J.P., Barrie E.S., Manvich D.F., Sadee W.,
Berg T., Mercer K., Stowe T.A., Liles L.C., Squires K.E., Mezher A.,
Curtin P., Perdomo D.L., Szot P., Weinshenker D.;
"Human bacterial artificial chromosome (BAC) transgenesis fully
rescues noradrenergic function in dopamine beta-hydroxylase knockout
mice.";
PLoS ONE 11:E0154864-E0154864(2016).
-!- FUNCTION: Conversion of dopamine to noradrenaline.
{ECO:0000269|PubMed:27148966, ECO:0000269|PubMed:7715704}.
-!- CATALYTIC ACTIVITY: 3,4-dihydroxyphenethylamine + ascorbate + O(2)
= noradrenaline + dehydroascorbate + H(2)O.
{ECO:0000269|PubMed:27148966, ECO:0000305|PubMed:7715704}.
-!- 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:0000269|PubMed:27148966, ECO:0000269|PubMed:7715704}.
-!- SUBUNIT: Homotetramer; composed of two disulfide-linked dimers.
{ECO:0000250|UniProtKB:P09172}.
-!- SUBCELLULAR LOCATION: Soluble dopamine beta-hydroxylase:
Cytoplasmic vesicle, secretory vesicle lumen
{ECO:0000269|PubMed:7961964}. Cytoplasmic vesicle, secretory
vesicle, chromaffin granule lumen {ECO:0000269|PubMed:7961964}.
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
membrane {ECO:0000269|PubMed:7961964}; Single-pass type II
membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory
vesicle, chromaffin granule membrane {ECO:0000269|PubMed:7961964};
Single-pass type II membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Detected in adrenal gland secretory granules
(at protein level) (PubMed:7961964). Detected in adrenal gland
(PubMed:1280432). {ECO:0000269|PubMed:1280432,
ECO:0000269|PubMed:7961964}.
-!- 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}.
-!- DISRUPTION PHENOTYPE: Complete embryonic lethality in homozygous
dams, and 88% embryonic lethality for homozygous embryos in
heterozygous dams. Only 12% of the homozygous pups from
heterozygous dams are alive at birth. Mutant pups have no obvious
phenotype at birth, but nearly half of them die within 48 h, and
only 5% survive to adulthood. Three weeks after birth, mutant pups
are runted and weigh only half as much as their littermates.
Still, the weight of adult males reaches 80% and that of females
88% of that of their littermates. Besides, mutant mice display
ptosis. Embryonic lethality is due to a lack of noradrenaline and
can be prevented by treatment with dihydroxyphenylserine, a
compound that can be converted into noradrenaline in the absence
of Dbh. {ECO:0000269|PubMed:27148966, ECO:0000269|PubMed:7715704}.
-!- SIMILARITY: Belongs to the copper type II ascorbate-dependent
monooxygenase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; S50200; AAB24330.1; -; mRNA.
EMBL; AK132245; BAE21055.1; -; mRNA.
EMBL; AL954801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466542; EDL08360.1; -; Genomic_DNA.
EMBL; BC141022; AAI41023.1; -; mRNA.
EMBL; BC171949; AAI71949.1; -; mRNA.
CCDS; CCDS38088.1; -.
PIR; JC1346; JC1346.
RefSeq; NP_620392.2; NM_138942.3.
UniGene; Mm.167781; -.
ProteinModelPortal; Q64237; -.
SMR; Q64237; -.
STRING; 10090.ENSMUSP00000000910; -.
PhosphoSitePlus; Q64237; -.
MaxQB; Q64237; -.
PaxDb; Q64237; -.
PRIDE; Q64237; -.
Ensembl; ENSMUST00000000910; ENSMUSP00000000910; ENSMUSG00000000889.
GeneID; 13166; -.
KEGG; mmu:13166; -.
UCSC; uc008ixe.1; mouse.
CTD; 1621; -.
MGI; MGI:94864; Dbh.
eggNOG; KOG3568; Eukaryota.
eggNOG; ENOG410XR89; LUCA.
GeneTree; ENSGT00530000063085; -.
HOGENOM; HOG000063669; -.
HOVERGEN; HBG005519; -.
InParanoid; Q64237; -.
KO; K00503; -.
OMA; CDSKMKP; -.
OrthoDB; EOG091G03XS; -.
PhylomeDB; Q64237; -.
TreeFam; TF320698; -.
Reactome; R-MMU-209905; Catecholamine biosynthesis.
UniPathway; UPA00748; UER00735.
PRO; PR:Q64237; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000000889; -.
CleanEx; MM_DBH; -.
Genevisible; Q64237; MM.
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; ISO:MGI.
GO; GO:0034774; C:secretory granule lumen; IDA:UniProtKB.
GO; GO:0030667; C:secretory granule membrane; IDA: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:0008306; P:associative learning; IMP:MGI.
GO; GO:0048149; P:behavioral response to ethanol; IMP:MGI.
GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
GO; GO:0001816; P:cytokine production; IMP:MGI.
GO; GO:0042420; P:dopamine catabolic process; IMP:UniProtKB.
GO; GO:0042596; P:fear response; IMP:MGI.
GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
GO; GO:0042309; P:homoiothermy; IMP:MGI.
GO; GO:0002443; P:leukocyte mediated immunity; IMP:MGI.
GO; GO:0050900; P:leukocyte migration; IMP:MGI.
GO; GO:0007626; P:locomotory behavior; IMP:UniProtKB.
GO; GO:0042711; P:maternal behavior; IMP:MGI.
GO; GO:0007613; P:memory; IMP:MGI.
GO; GO:0042421; P:norepinephrine biosynthetic process; IMP:UniProtKB.
GO; GO:0006589; P:octopamine biosynthetic process; IBA:GO_Central.
GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI.
GO; GO:2001236; P:regulation of extrinsic apoptotic signaling pathway; IMP:MGI.
GO; GO:0001975; P:response to amphetamine; IMP:MGI.
GO; GO:0048265; P:response to pain; IMP:MGI.
GO; GO:0008542; P:visual learning; IMP:MGI.
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; 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; 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; Disulfide bond; Glycoprotein; Membrane;
Metal-binding; Monooxygenase; Oxidoreductase; Phosphoprotein;
Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
Vitamin C.
CHAIN 1 622 Dopamine beta-hydroxylase.
/FTId=PRO_0000006357.
CHAIN 44 622 Soluble dopamine beta-hydroxylase.
{ECO:0000255}.
/FTId=PRO_0000308210.
TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.
TRANSMEM 21 41 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 42 621 Intragranular. {ECO:0000255}.
DOMAIN 61 177 DOMON. {ECO:0000255|PROSITE-
ProRule:PRU00246}.
ACT_SITE 234 234 {ECO:0000255}.
ACT_SITE 416 416 {ECO:0000255}.
METAL 266 266 Copper A. {ECO:0000250}.
METAL 267 267 Copper A. {ECO:0000250}.
METAL 337 337 Copper A. {ECO:0000250}.
METAL 416 416 Copper B. {ECO:0000250|UniProtKB:P09172}.
METAL 418 418 Copper B. {ECO:0000250|UniProtKB:P09172}.
METAL 491 491 Copper B. {ECO:0000250|UniProtKB:P09172}.
SITE 43 44 Cleavage. {ECO:0000250|UniProtKB:P15101}.
MOD_RES 350 350 Phosphoserine; by CaMK. {ECO:0000255}.
CARBOHYD 68 68 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 188 188 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 476 476 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 570 570 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 158 600 {ECO:0000250|UniProtKB:P09172}.
DISULFID 236 287 {ECO:0000250|UniProtKB:P09172}.
DISULFID 273 299 {ECO:0000250|UniProtKB:P09172}.
DISULFID 394 507 {ECO:0000250|UniProtKB:P09172}.
DISULFID 398 569 {ECO:0000250|UniProtKB:P09172}.
DISULFID 470 492 {ECO:0000250|UniProtKB:P09172}.
DISULFID 532 532 Interchain.
{ECO:0000250|UniProtKB:P09172}.
DISULFID 534 534 Interchain.
{ECO:0000250|UniProtKB:P09172}.
CONFLICT 109 109 T -> S (in Ref. 1; AAB24330).
{ECO:0000305}.
CONFLICT 197 197 Q -> L (in Ref. 1; AAB24330).
{ECO:0000305}.
CONFLICT 232 232 T -> Q (in Ref. 1; AAB24330).
{ECO:0000305}.
CONFLICT 356 356 H -> P (in Ref. 1; AAB24330).
{ECO:0000305}.
CONFLICT 437 437 V -> E (in Ref. 1; AAB24330).
{ECO:0000305}.
CONFLICT 449 449 Q -> R (in Ref. 1; AAB24330).
{ECO:0000305}.
CONFLICT 554 554 D -> N (in Ref. 1; AAB24330).
{ECO:0000305}.
CONFLICT 618 621 EADA -> GGRC (in Ref. 1; AAB24330).
{ECO:0000305}.
SEQUENCE 622 AA; 70314 MW; 7D9FA1B622F3FCA8 CRC64;
MQAHLSHQPC WSSLPSPSVR EAASMYGTAV AIFLVILVAA LRGSEPPESP FPYHIPLDPE
GILELSWNVS YVQEIIHFQL QVQGLRAGVL FGMSDRGEME NADLIMLWTD GDRAYFADAW
SDRKGQIHLD SQQDYQLLQA QRTRDGLSLL FKRPFVTCDP KDYVIEDDTV HLVYGILEEP
FQSLEAINTS GLHTGLQRVQ LLKSEVPTPS MPEDVQTMDI RAPDILIPDN ETTYWCYITE
LPPRFPRHHI IMYEAIVTEG NEALVHHMEV FQCAAESEDF PQFNGPCDSK MKPDRLNYCR
HVLAAWALGA KAFYYPKEAG VPFGGPGSSP FLRLEVHYHN PRKIQGRQDS SGIRLHYTAT
LRRYDAGIME LGLVYTPLMA IPPQETAFVL TGYCTDKCTQ MALQDSGIHI FASQLHTHLT
GRKVVTVLAR DGQERKVVNR DNHYSPHFQE IRMLKKVVTV YPGDVLITSC TYNTENKTLA
TVGGFGILEE MCVNYVHYYP QTELELCKSA VDDGFLQKYF HMVNRFSSEE VCTCPQASVP
QQFSSVPWNS FNRDMLKALY DYAPISMHCN KTSAVRFPGE WNLQPLPKIT STLEEPTPRC
PIRQTQSPAN PTVPITTEAD AE


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