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Q64237 (DOPO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dopamine beta-hydroxylase

EC=1.14.17.1
Alternative name(s):
Dopamine beta-monooxygenase

Cleaved into the following chain:

  1. Soluble dopamine beta-hydroxylase
Gene names
Name:Dbh
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length622 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Conversion of dopamine to noradrenaline.

Catalytic activity

3,4-dihydroxyphenethylamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O.

Cofactor

Binds 1 PQQ per subunit By similarity.

Binds 2 copper ions per subunit By similarity.

Pathway

Catecholamine biosynthesis; (R)-noradrenaline biosynthesis; (R)-noradrenaline from dopamine: step 1/1.

Subunit structure

Homotetramer composed of two non-covalently bound disulfide-linked dimers By similarity.

Subcellular location

Soluble dopamine beta-hydroxylase: Cytoplasmic vesiclesecretory vesicle lumen By similarity. Cytoplasmic vesiclesecretory vesiclechromaffin granule lumen By similarity.

Cytoplasmic vesiclesecretory vesicle membrane; Single-pass type II membrane protein By similarity. Cytoplasmic vesiclesecretory vesiclechromaffin granule membrane; Single-pass type II membrane protein By similarity.

Sequence similarities

Belongs to the copper type II ascorbate-dependent monooxygenase family.

Contains 1 DOMON domain.

Ontologies

Keywords
   Biological processCatecholamine biosynthesis
   Cellular componentCytoplasmic vesicle
Membrane
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandCopper
Metal-binding
PQQ
Vitamin C
   Molecular functionMonooxygenase
Oxidoreductase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processassociative learning

Inferred from mutant phenotype PubMed 9189272. Source: MGI

behavioral response to ethanol

Inferred from mutant phenotype PubMed 10777779. Source: MGI

blood vessel remodeling

Inferred from mutant phenotype PubMed 15231500PubMed 15849236. Source: MGI

cytokine production

Inferred from mutant phenotype PubMed 10051631. Source: MGI

dopamine catabolic process

Inferred from mutant phenotype PubMed 10051631. Source: MGI

fear response

Inferred from mutant phenotype PubMed 15066288. Source: MGI

glucose homeostasis

Inferred from mutant phenotype PubMed 12959968. Source: MGI

homoiothermy

Inferred from mutant phenotype PubMed 9139828. Source: MGI

leukocyte mediated immunity

Inferred from mutant phenotype PubMed 10051631. Source: MGI

leukocyte migration

Inferred from mutant phenotype PubMed 15849236. Source: MGI

locomotory behavior

Inferred from mutant phenotype PubMed 9189272. Source: MGI

maternal behavior

Inferred from mutant phenotype PubMed 9393852. Source: MGI

memory

Inferred from mutant phenotype PubMed 15066288PubMed 9189272. Source: MGI

norepinephrine biosynthetic process

Inferred from mutant phenotype PubMed 10051631PubMed 9603211. Source: MGI

positive regulation of vasoconstriction

Inferred from mutant phenotype PubMed 9139828. Source: MGI

regulation of cell proliferation

Inferred from mutant phenotype PubMed 15849236. Source: MGI

regulation of extrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 15849236. Source: MGI

response to amphetamine

Inferred from mutant phenotype PubMed 12370425. Source: MGI

response to pain

Inferred from mutant phenotype PubMed 11805341. Source: MGI

synaptic transmission

Inferred from electronic annotation. Source: InterPro

visual learning

Inferred from mutant phenotype PubMed 9189272. Source: MGI

   Cellular_componentchromaffin granule lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

chromaffin granule membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

transport vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionL-ascorbic acid binding

Inferred from electronic annotation. Source: UniProtKB-KW

copper ion binding

Inferred from electronic annotation. Source: InterPro

dopamine beta-monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 622622Dopamine beta-hydroxylase
PRO_0000006357
Chain44 – 622579Soluble dopamine beta-hydroxylase Potential
PRO_0000308210

Regions

Topological domain1 – 2020Cytoplasmic Potential
Transmembrane21 – 4121Helical; Signal-anchor for type II membrane protein; Potential
Topological domain42 – 621580Intragranular Potential
Domain61 – 177117DOMON

Sites

Active site2341 Potential
Active site4161 Potential
Metal binding2661Copper A By similarity
Metal binding2671Copper A By similarity
Metal binding3371Copper A By similarity
Metal binding4161Copper B By similarity
Metal binding4181Copper B By similarity
Metal binding4911Copper B By similarity

Amino acid modifications

Modified residue3501Phosphoserine; by CaMK Potential
Glycosylation681N-linked (GlcNAc...) Potential
Glycosylation1881N-linked (GlcNAc...) Potential
Glycosylation4761N-linked (GlcNAc...) Potential
Glycosylation5701N-linked (GlcNAc...) Potential
Disulfide bond158 ↔ 600 By similarity
Disulfide bond236 ↔ 287 By similarity
Disulfide bond273 ↔ 299 By similarity
Disulfide bond394 ↔ 507 By similarity
Disulfide bond398 ↔ 569 By similarity
Disulfide bond470 ↔ 492 By similarity
Disulfide bond532Interchain By similarity
Disulfide bond534Interchain By similarity

Experimental info

Sequence conflict1091T → S in AAB24330. Ref.1
Sequence conflict1971Q → L in AAB24330. Ref.1
Sequence conflict2321T → Q in AAB24330. Ref.1
Sequence conflict3561H → P in AAB24330. Ref.1
Sequence conflict4371V → E in AAB24330. Ref.1
Sequence conflict4491Q → R in AAB24330. Ref.1
Sequence conflict5541D → N in AAB24330. Ref.1
Sequence conflict618 – 6214EADA → GGRC in AAB24330. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q64237 [UniParc].

Last modified September 18, 2013. Version 2.
Checksum: 7D9FA1B622F3FCA8

FASTA62270,314
        10         20         30         40         50         60 
MQAHLSHQPC WSSLPSPSVR EAASMYGTAV AIFLVILVAA LRGSEPPESP FPYHIPLDPE 

        70         80         90        100        110        120 
GILELSWNVS YVQEIIHFQL QVQGLRAGVL FGMSDRGEME NADLIMLWTD GDRAYFADAW 

       130        140        150        160        170        180 
SDRKGQIHLD SQQDYQLLQA QRTRDGLSLL FKRPFVTCDP KDYVIEDDTV HLVYGILEEP 

       190        200        210        220        230        240 
FQSLEAINTS GLHTGLQRVQ LLKSEVPTPS MPEDVQTMDI RAPDILIPDN ETTYWCYITE 

       250        260        270        280        290        300 
LPPRFPRHHI IMYEAIVTEG NEALVHHMEV FQCAAESEDF PQFNGPCDSK MKPDRLNYCR 

       310        320        330        340        350        360 
HVLAAWALGA KAFYYPKEAG VPFGGPGSSP FLRLEVHYHN PRKIQGRQDS SGIRLHYTAT 

       370        380        390        400        410        420 
LRRYDAGIME LGLVYTPLMA IPPQETAFVL TGYCTDKCTQ MALQDSGIHI FASQLHTHLT 

       430        440        450        460        470        480 
GRKVVTVLAR DGQERKVVNR DNHYSPHFQE IRMLKKVVTV YPGDVLITSC TYNTENKTLA 

       490        500        510        520        530        540 
TVGGFGILEE MCVNYVHYYP QTELELCKSA VDDGFLQKYF HMVNRFSSEE VCTCPQASVP 

       550        560        570        580        590        600 
QQFSSVPWNS FNRDMLKALY DYAPISMHCN KTSAVRFPGE WNLQPLPKIT STLEEPTPRC 

       610        620 
PIRQTQSPAN PTVPITTEAD AE 

« Hide

References

« Hide 'large scale' references
[1]"Mouse dopamine beta-hydroxylase: primary structure deduced from the cDNA sequence and exon/intron organization of the gene."
Nakano T., Kobayashi K., Saito S., Fujita K., Nagatsu T.
Biochem. Biophys. Res. Commun. 189:590-599(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
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. expand/collapse author list , 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.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S50200 mRNA. Translation: AAB24330.1.
AK132245 mRNA. Translation: BAE21055.1.
AL954801 Genomic DNA. No translation available.
CH466542 Genomic DNA. Translation: EDL08360.1.
BC141022 mRNA. Translation: AAI41023.1.
BC171949 mRNA. Translation: AAI71949.1.
PIRJC1346.
RefSeqNP_620392.2. NM_138942.3.
UniGeneMm.167781.

3D structure databases

ProteinModelPortalQ64237.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000000910.

PTM databases

PhosphoSiteQ64237.

Proteomic databases

PRIDEQ64237.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000000910; ENSMUSP00000000910; ENSMUSG00000000889.
GeneID13166.
KEGGmmu:13166.
UCSCuc008ixe.1. mouse.

Organism-specific databases

CTD1621.
MGIMGI:94864. Dbh.

Phylogenomic databases

eggNOGNOG286384.
GeneTreeENSGT00530000063085.
HOVERGENHBG005519.
InParanoidQ64237.
KOK00503.
OMAGAKAFYY.
OrthoDBEOG78WKR4.
PhylomeDBQ64237.
TreeFamTF320698.

Enzyme and pathway databases

UniPathwayUPA00748; UER00735.

Gene expression databases

CleanExMM_DBH.
GenevestigatorQ64237.

Family and domain databases

Gene3D2.60.120.230. 1 hit.
2.60.120.310. 1 hit.
InterProIPR014784. Cu2_ascorb_mOase-like_C.
IPR020611. Cu2_ascorb_mOase_CS-1.
IPR014783. Cu2_ascorb_mOase_CS-2.
IPR000323. Cu2_ascorb_mOase_N.
IPR028461. DBH.
IPR000945. DBH-rel.
IPR005018. DOMON_domain.
IPR008977. PHM/PNGase_F_dom.
[Graphical view]
PANTHERPTHR10157. PTHR10157. 1 hit.
PTHR10157:SF16. PTHR10157:SF16. 1 hit.
PfamPF01082. Cu2_monooxygen. 1 hit.
PF03351. DOMON. 1 hit.
[Graphical view]
PRINTSPR00767. DBMONOXGNASE.
SMARTSM00664. DoH. 1 hit.
[Graphical view]
SUPFAMSSF49742. SSF49742. 2 hits.
PROSITEPS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS00085. CU2_MONOOXYGENASE_2. 1 hit.
PS50836. DOMON. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio283246.
PROQ64237.
SOURCESearch...

Entry information

Entry nameDOPO_MOUSE
AccessionPrimary (citable) accession number: Q64237
Secondary accession number(s): Q3V1U4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 18, 2013
Last modified: April 16, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot