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Q64237

- DOPO_MOUSE

UniProt

Q64237 - DOPO_MOUSE

Protein

Dopamine beta-hydroxylase

Gene

Dbh

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (18 Sep 2013)
      Previous versions | rss
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    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

    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. 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

    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

    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

    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

    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 1, 2014
    This is version 121 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