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Q64237

- DOPO_MOUSE

UniProt

Q64237 - DOPO_MOUSE

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Protein

Dopamine beta-hydroxylase

Gene

Dbh

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Conversion of dopamine to noradrenaline.

Catalytic activityi

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

Cofactori

Binds 1 PQQ per subunit.By similarity
Binds 2 copper ions per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei234 – 2341Sequence Analysis
Metal bindingi266 – 2661Copper ABy similarity
Metal bindingi267 – 2671Copper ABy similarity
Metal bindingi337 – 3371Copper ABy similarity
Active sitei416 – 4161Sequence Analysis
Metal bindingi416 – 4161Copper BBy similarity
Metal bindingi418 – 4181Copper BBy similarity
Metal bindingi491 – 4911Copper BBy similarity

GO - Molecular functioni

  1. copper ion binding Source: InterPro
  2. dopamine beta-monooxygenase activity Source: UniProtKB-EC
  3. L-ascorbic acid binding Source: UniProtKB-KW

GO - Biological processi

  1. associative learning Source: MGI
  2. behavioral response to ethanol Source: MGI
  3. blood vessel remodeling Source: MGI
  4. cytokine production Source: MGI
  5. dopamine catabolic process Source: MGI
  6. fear response Source: MGI
  7. glucose homeostasis Source: MGI
  8. homoiothermy Source: MGI
  9. leukocyte mediated immunity Source: MGI
  10. leukocyte migration Source: MGI
  11. locomotory behavior Source: MGI
  12. maternal behavior Source: MGI
  13. memory Source: MGI
  14. norepinephrine biosynthetic process Source: MGI
  15. positive regulation of vasoconstriction Source: MGI
  16. regulation of cell proliferation Source: MGI
  17. regulation of extrinsic apoptotic signaling pathway Source: MGI
  18. response to amphetamine Source: MGI
  19. response to pain Source: MGI
  20. visual learning Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Catecholamine biosynthesis

Keywords - Ligandi

Copper, Metal-binding, PQQ, Vitamin C

Enzyme and pathway databases

ReactomeiREACT_217777. Catecholamine biosynthesis.
UniPathwayiUPA00748; UER00735.

Names & Taxonomyi

Protein namesi
Recommended name:
Dopamine beta-hydroxylase (EC:1.14.17.1)
Alternative name(s):
Dopamine beta-monooxygenase
Cleaved into the following chain:
Gene namesi
Name:Dbh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:94864. Dbh.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasmic vesicle Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 622622Dopamine beta-hydroxylasePRO_0000006357Add
BLAST
Chaini44 – 622579Soluble dopamine beta-hydroxylaseSequence AnalysisPRO_0000308210Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi68 – 681N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi158 ↔ 600By similarity
Glycosylationi188 – 1881N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi236 ↔ 287By similarity
Disulfide bondi273 ↔ 299By similarity
Modified residuei350 – 3501Phosphoserine; by CaMKSequence Analysis
Disulfide bondi394 ↔ 507By similarity
Disulfide bondi398 ↔ 569By similarity
Disulfide bondi470 ↔ 492By similarity
Glycosylationi476 – 4761N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi532 – 532InterchainBy similarity
Disulfide bondi534 – 534InterchainBy similarity
Glycosylationi570 – 5701N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ64237.
PRIDEiQ64237.

PTM databases

PhosphoSiteiQ64237.

Expressioni

Gene expression databases

CleanExiMM_DBH.
GenevestigatoriQ64237.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000000910.

Structurei

3D structure databases

ProteinModelPortaliQ64237.
SMRiQ64237. Positions 209-506.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2020CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini42 – 621580IntragranularSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei21 – 4121Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 177117DOMONPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 DOMON domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG286384.
GeneTreeiENSGT00530000063085.
HOVERGENiHBG005519.
InParanoidiQ64237.
KOiK00503.
OMAiSYFGDAW.
OrthoDBiEOG78WKR4.
PhylomeDBiQ64237.
TreeFamiTF320698.

Family and domain databases

Gene3Di2.60.120.230. 1 hit.
2.60.120.310. 1 hit.
InterProiIPR014784. Cu2_ascorb_mOase-like_C.
IPR020611. Cu2_ascorb_mOase_CS-1.
IPR014783. Cu2_ascorb_mOase_CS-2.
IPR000323. Cu2_ascorb_mOase_N.
IPR000945. DBH-rel.
IPR005018. DOMON_domain.
IPR008977. PHM/PNGase_F_dom.
IPR028460. Tbh/DBH.
[Graphical view]
PANTHERiPTHR10157. PTHR10157. 1 hit.
PTHR10157:SF4. PTHR10157:SF4. 1 hit.
PfamiPF01082. Cu2_monooxygen. 1 hit.
PF03351. DOMON. 1 hit.
[Graphical view]
PRINTSiPR00767. DBMONOXGNASE.
SMARTiSM00664. DoH. 1 hit.
[Graphical view]
SUPFAMiSSF49742. SSF49742. 2 hits.
PROSITEiPS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS00085. CU2_MONOOXYGENASE_2. 1 hit.
PS50836. DOMON. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q64237-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQAHLSHQPC WSSLPSPSVR EAASMYGTAV AIFLVILVAA LRGSEPPESP
60 70 80 90 100
FPYHIPLDPE GILELSWNVS YVQEIIHFQL QVQGLRAGVL FGMSDRGEME
110 120 130 140 150
NADLIMLWTD GDRAYFADAW SDRKGQIHLD SQQDYQLLQA QRTRDGLSLL
160 170 180 190 200
FKRPFVTCDP KDYVIEDDTV HLVYGILEEP FQSLEAINTS GLHTGLQRVQ
210 220 230 240 250
LLKSEVPTPS MPEDVQTMDI RAPDILIPDN ETTYWCYITE LPPRFPRHHI
260 270 280 290 300
IMYEAIVTEG NEALVHHMEV FQCAAESEDF PQFNGPCDSK MKPDRLNYCR
310 320 330 340 350
HVLAAWALGA KAFYYPKEAG VPFGGPGSSP FLRLEVHYHN PRKIQGRQDS
360 370 380 390 400
SGIRLHYTAT LRRYDAGIME LGLVYTPLMA IPPQETAFVL TGYCTDKCTQ
410 420 430 440 450
MALQDSGIHI FASQLHTHLT GRKVVTVLAR DGQERKVVNR DNHYSPHFQE
460 470 480 490 500
IRMLKKVVTV YPGDVLITSC TYNTENKTLA TVGGFGILEE MCVNYVHYYP
510 520 530 540 550
QTELELCKSA VDDGFLQKYF HMVNRFSSEE VCTCPQASVP QQFSSVPWNS
560 570 580 590 600
FNRDMLKALY DYAPISMHCN KTSAVRFPGE WNLQPLPKIT STLEEPTPRC
610 620
PIRQTQSPAN PTVPITTEAD AE
Length:622
Mass (Da):70,314
Last modified:September 18, 2013 - v2
Checksum:i7D9FA1B622F3FCA8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1091T → S in AAB24330. (PubMed:1280432)Curated
Sequence conflicti197 – 1971Q → L in AAB24330. (PubMed:1280432)Curated
Sequence conflicti232 – 2321T → Q in AAB24330. (PubMed:1280432)Curated
Sequence conflicti356 – 3561H → P in AAB24330. (PubMed:1280432)Curated
Sequence conflicti437 – 4371V → E in AAB24330. (PubMed:1280432)Curated
Sequence conflicti449 – 4491Q → R in AAB24330. (PubMed:1280432)Curated
Sequence conflicti554 – 5541D → N in AAB24330. (PubMed:1280432)Curated
Sequence conflicti618 – 6214EADA → GGRC in AAB24330. (PubMed:1280432)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS38088.1.
PIRiJC1346.
RefSeqiNP_620392.2. NM_138942.3.
UniGeneiMm.167781.

Genome annotation databases

EnsembliENSMUST00000000910; ENSMUSP00000000910; ENSMUSG00000000889.
GeneIDi13166.
KEGGimmu:13166.
UCSCiuc008ixe.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS38088.1.
PIRi JC1346.
RefSeqi NP_620392.2. NM_138942.3.
UniGenei Mm.167781.

3D structure databases

ProteinModelPortali Q64237.
SMRi Q64237. Positions 209-506.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000000910.

PTM databases

PhosphoSitei Q64237.

Proteomic databases

MaxQBi Q64237.
PRIDEi Q64237.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000000910 ; ENSMUSP00000000910 ; ENSMUSG00000000889 .
GeneIDi 13166.
KEGGi mmu:13166.
UCSCi uc008ixe.1. mouse.

Organism-specific databases

CTDi 1621.
MGIi MGI:94864. Dbh.

Phylogenomic databases

eggNOGi NOG286384.
GeneTreei ENSGT00530000063085.
HOVERGENi HBG005519.
InParanoidi Q64237.
KOi K00503.
OMAi SYFGDAW.
OrthoDBi EOG78WKR4.
PhylomeDBi Q64237.
TreeFami TF320698.

Enzyme and pathway databases

UniPathwayi UPA00748 ; UER00735 .
Reactomei REACT_217777. Catecholamine biosynthesis.

Miscellaneous databases

NextBioi 283246.
PROi Q64237.
SOURCEi Search...

Gene expression databases

CleanExi MM_DBH.
Genevestigatori Q64237.

Family and domain databases

Gene3Di 2.60.120.230. 1 hit.
2.60.120.310. 1 hit.
InterProi IPR014784. Cu2_ascorb_mOase-like_C.
IPR020611. Cu2_ascorb_mOase_CS-1.
IPR014783. Cu2_ascorb_mOase_CS-2.
IPR000323. Cu2_ascorb_mOase_N.
IPR000945. DBH-rel.
IPR005018. DOMON_domain.
IPR008977. PHM/PNGase_F_dom.
IPR028460. Tbh/DBH.
[Graphical view ]
PANTHERi PTHR10157. PTHR10157. 1 hit.
PTHR10157:SF4. PTHR10157:SF4. 1 hit.
Pfami PF01082. Cu2_monooxygen. 1 hit.
PF03351. DOMON. 1 hit.
[Graphical view ]
PRINTSi PR00767. DBMONOXGNASE.
SMARTi SM00664. DoH. 1 hit.
[Graphical view ]
SUPFAMi SSF49742. SSF49742. 2 hits.
PROSITEi PS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS00085. CU2_MONOOXYGENASE_2. 1 hit.
PS50836. DOMON. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiDOPO_MOUSE
AccessioniPrimary (citable) accession number: Q64237
Secondary accession number(s): Q3V1U4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 18, 2013
Last modified: October 29, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3