ID   G3V9S4_RAT              Unreviewed;       621 AA.
AC   G3V9S4;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=Dopamine beta-hydroxylase {ECO:0000256|ARBA:ARBA00020179};
DE            EC=1.14.17.1 {ECO:0000256|ARBA:ARBA00012686};
GN   Name=Dbh {ECO:0000313|Ensembl:ENSRNOP00000057915.1,
GN   ECO:0000313|RGD:2489};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000057915.1, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000057915.1, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000057915.1,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000057915.1}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000057915.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the hydroxylation of dopamine to noradrenaline
CC       (also known as norepinephrine), and is thus vital for regulation of
CC       these neurotransmitters. {ECO:0000256|ARBA:ARBA00037327}.
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:0000256|ARBA:ARBA00035782};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19118;
CC         Evidence={ECO:0000256|ARBA:ARBA00035782};
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|ARBA:ARBA00001973};
CC   -!- PATHWAY: Catecholamine biosynthesis; (R)-noradrenaline biosynthesis;
CC       (R)-noradrenaline from dopamine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005223}.
CC   -!- SUBUNIT: Homotetramer; composed of two disulfide-linked dimers.
CC       {ECO:0000256|ARBA:ARBA00011406}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle lumen
CC       {ECO:0000256|ARBA:ARBA00004263}. Cytoplasmic vesicle, secretory vesicle
CC       membrane {ECO:0000256|ARBA:ARBA00004213}; Single-pass type II membrane
CC       protein {ECO:0000256|ARBA:ARBA00004213}. Cytoplasmic vesicle, secretory
CC       vesicle, chromaffin granule lumen {ECO:0000256|ARBA:ARBA00004553}.
CC       Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane
CC       {ECO:0000256|ARBA:ARBA00004351}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004351}.
CC   -!- SIMILARITY: Belongs to the copper type II ascorbate-dependent
CC       monooxygenase family. {ECO:0000256|ARBA:ARBA00010676}.
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DR   AlphaFoldDB; G3V9S4; -.
DR   SMR; G3V9S4; -.
DR   Ensembl; ENSRNOT00000061201.4; ENSRNOP00000057915.1; ENSRNOG00000006641.9.
DR   RGD; 2489; Dbh.
DR   GeneTree; ENSGT00530000063085; -.
DR   OMA; FPHFSGP; -.
DR   OrthoDB; 37880at2759; -.
DR   TreeFam; TF320698; -.
DR   UniPathway; UPA00748; UER00735.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000006641; Expressed in heart and 8 other cell types or tissues.
DR   ExpressionAtlas; G3V9S4; baseline and differential.
DR   GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
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:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:Ensembl.
DR   GO; GO:0004500; F:dopamine beta-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0048149; P:behavioral response to ethanol; IEA:Ensembl.
DR   GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
DR   GO; GO:0042420; P:dopamine catabolic process; IEA:Ensembl.
DR   GO; GO:0042596; P:fear response; IEA:Ensembl.
DR   GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR   GO; GO:0042309; P:homoiothermy; IEA:Ensembl.
DR   GO; GO:0002443; P:leukocyte mediated immunity; IEA:Ensembl.
DR   GO; GO:0050900; P:leukocyte migration; IEA:Ensembl.
DR   GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR   GO; GO:0042711; P:maternal behavior; IEA:Ensembl.
DR   GO; GO:0007613; P:memory; IEA:Ensembl.
DR   GO; GO:0042421; P:norepinephrine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
DR   GO; GO:2001236; P:regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:1904705; P:regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:1905562; P:regulation of vascular endothelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR   GO; GO:0048265; P:response to pain; IEA:Ensembl.
DR   GO; GO:0042310; P:vasoconstriction; IEA:Ensembl.
DR   GO; GO:0008542; P:visual learning; IEA:Ensembl.
DR   CDD; cd09631; DOMON_DOH; 1.
DR   Gene3D; 2.60.120.230; -; 1.
DR   Gene3D; 2.60.120.310; Copper type II, ascorbate-dependent monooxygenase, N-terminal domain; 1.
DR   InterPro; IPR014784; Cu2_ascorb_mOase-like_C.
DR   InterPro; IPR020611; Cu2_ascorb_mOase_CS-1.
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; DOPAMINE BETA HYDROXYLASE RELATED; 1.
DR   PANTHER; PTHR10157:SF29; DOPAMINE BETA-HYDROXYLASE; 1.
DR   Pfam; PF03712; Cu2_monoox_C; 1.
DR   Pfam; PF01082; Cu2_monooxygen; 1.
DR   Pfam; PF03351; DOMON; 1.
DR   PRINTS; PR00767; DBMONOXGNASE.
DR   SMART; SM00664; DoH; 1.
DR   SUPFAM; SSF49742; PHM/PNGase F; 2.
DR   PROSITE; PS00084; CU2_MONOOXYGENASE_1; 1.
DR   PROSITE; PS50836; DOMON; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023033};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
SQ   SEQUENCE   621 AA;  69996 MW;  AC8213A9291902C6 CRC64;
     MQPHLSHQPC WSLPSPSVRE AASMYGTAVA IFLVILVAAL QGSEPPESPF PYHIPLDPEG
     TLELSWNVSY DQEIIHFQLQ VQGPRAGVLF GMSDRGEMEN ADLVMLWTDG DRTYFADAWS
     DQKGQIHLDT HQDYQLLQAQ RVSNSLSLLF KRPFVTCDPK DYVIEDDTVH LVYGILEEPF
     QSLEAINTSG LHTGLQQVQL LKPEVSTPAM PADVQTMDIR APDVLIPSTE TTYWCYITEL
     PLHFPRHHII MYEAIVTEGN EALVHHMEVF QCTNESEAFP MFNGPCDSKM KPDRLNYCRH
     VLAAWALGAK AFYYPEEAGV PFGGSGSSRF LRLEVHYHNP RNIQGRRDSS GIRLHYTASL
     RPNEAGIMEL GLVYTPLMAI PPQETTFVLT GYCTDRCTQM ALPKSGIRIF ASQLHTHLTG
     RKVITVLARD GQQREVVNRD NHYSPHFQEI RMLKNAVTVH QGDVLITSCT YNTENRTMAT
     VGGFGILEEM CVNYVHYYPK TELELCKSAV DDGFLQKYFH IVNRFGNEEV CTCPQASVPQ
     QFASVPWNSF NRDMLKALYN YAPISVHCNK TSAVRFPGNW NLQPLPKITS AVEEPDPRCP
     IRQTRGPAGP FVVITTEADT E
//