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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 – 2341 Reviewed prediction
Metal bindingi266 – 2661Copper A By similarity
Metal bindingi267 – 2671Copper A By similarity
Metal bindingi337 – 3371Copper A By similarity
Active sitei416 – 4161 Reviewed prediction
Metal bindingi416 – 4161Copper B By similarity
Metal bindingi418 – 4181Copper B By similarity
Metal bindingi491 – 4911Copper B By 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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2020Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei21 – 4121Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini42 – 621580Intragranular Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. chromaffin granule lumen Source: UniProtKB-SubCell
  2. chromaffin granule membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
  4. transport vesicle membrane Source: UniProtKB-SubCell
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-hydroxylase Reviewed predictionPRO_0000308210Add
BLAST

Amino acid modifications

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

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 177117DOMONAdd
BLAST

Sequence similaritiesi

Contains 1 DOMON domain.

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

MQAHLSHQPC WSSLPSPSVR EAASMYGTAV AIFLVILVAA LRGSEPPESP    50
FPYHIPLDPE GILELSWNVS YVQEIIHFQL QVQGLRAGVL FGMSDRGEME 100
NADLIMLWTD GDRAYFADAW SDRKGQIHLD SQQDYQLLQA QRTRDGLSLL 150
FKRPFVTCDP KDYVIEDDTV HLVYGILEEP FQSLEAINTS GLHTGLQRVQ 200
LLKSEVPTPS MPEDVQTMDI RAPDILIPDN ETTYWCYITE LPPRFPRHHI 250
IMYEAIVTEG NEALVHHMEV FQCAAESEDF PQFNGPCDSK MKPDRLNYCR 300
HVLAAWALGA KAFYYPKEAG VPFGGPGSSP FLRLEVHYHN PRKIQGRQDS 350
SGIRLHYTAT LRRYDAGIME LGLVYTPLMA IPPQETAFVL TGYCTDKCTQ 400
MALQDSGIHI FASQLHTHLT GRKVVTVLAR DGQERKVVNR DNHYSPHFQE 450
IRMLKKVVTV YPGDVLITSC TYNTENKTLA TVGGFGILEE MCVNYVHYYP 500
QTELELCKSA VDDGFLQKYF HMVNRFSSEE VCTCPQASVP QQFSSVPWNS 550
FNRDMLKALY DYAPISMHCN KTSAVRFPGE WNLQPLPKIT STLEEPTPRC 600
PIRQTQSPAN PTVPITTEAD AE 622
Length:622
Mass (Da):70,314
Last modified:September 18, 2013 - v2
Checksum:i7D9FA1B622F3FCA8
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1091T → S in AAB24330. 1 Publication
Sequence conflicti197 – 1971Q → L in AAB24330. 1 Publication
Sequence conflicti232 – 2321T → Q in AAB24330. 1 Publication
Sequence conflicti356 – 3561H → P in AAB24330. 1 Publication
Sequence conflicti437 – 4371V → E in AAB24330. 1 Publication
Sequence conflicti449 – 4491Q → R in AAB24330. 1 Publication
Sequence conflicti554 – 5541D → N in AAB24330. 1 Publication
Sequence conflicti618 – 6214EADA → GGRC in AAB24330. 1 Publication

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: September 3, 2014
This is version 120 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

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