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UniProtKB/Swiss-Prot entry P15101


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DOPO_BOVIN
Primary accession number P15101
Secondary accession numbers Q0V8A8 Q28094 Q9TVD1
Integrated into Swiss-Prot on April 1, 1990
Sequence was last modified on October 2, 2007 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 81)
Name and origin of the protein
Protein name Dopamine beta-hydroxylase
Synonyms EC 1.14.17.1
Dopamine beta-monooxygenase
Contains Soluble dopamine beta-hydroxylase
Gene name
Name: DBH
From
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1021/bi00452a026; PubMed=2620060 [NCBI, ExPASy, EBI, Israel, Japan]
Taljanidisz J., Stewart L., Smith A.J., Klinman J.P.;
"Structure of bovine adrenal dopamine beta-monooxygenase, as deduced from cDNA and protein sequencing: evidence that the membrane-bound form of the enzyme is anchored by an uncleaved signal peptide.";
Biochemistry 28:10054-10061(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1688549 [NCBI, ExPASy, EBI, Israel, Japan]
Lewis E.J., Allison S., Fader D., Claflin V., Baizer L.;
"Bovine dopamine beta-hydroxylase cDNA. Complete coding sequence and expression in mammalian cells with vaccinia virus vector.";
J. Biol. Chem. 265:1021-1028(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-610.
DOI=10.1186/1471-2164-6-166; PubMed=16305752 [NCBI, ExPASy, EBI, Israel, Japan]
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 14-610.
TISSUE=Adrenal medulla;
DOI=10.1111/j.1471-4159.1990.tb08826.x; PubMed=1693949 [NCBI, ExPASy, EBI, Israel, Japan]
Wu H.J., Parmer R.J., Koop A.H., Rozansky D.J., O'Connor D.T.;
"Molecular cloning, structure, and expression of dopamine-beta-hydroxylase from bovine adrenal medulla.";
J. Neurochem. 55:97-105(1990).
[5]
PARTIAL PROTEIN SEQUENCE OF 33-610.
PubMed=2295597 [NCBI, ExPASy, EBI, Israel, Japan]
Robertson J.G., Desai P.R., Kumar A., Farrington G.K., Fitzpatrick P.F., Villafranca J.J.;
"Primary amino acid sequence of bovine dopamine beta-hydroxylase.";
J. Biol. Chem. 265:1029-1035(1990).
[6]
PROTEIN SEQUENCE OF 33-50.
TISSUE=Adrenal medulla;
DOI=10.1016/0006-291X(77)90609-X; PubMed=843373 [NCBI, ExPASy, EBI, Israel, Japan]
Skotland T., Ljones T., Flatmark T., Sletten K.;
"NH2-terminal sequence of dopamine beta-hydroxylase from bovine adrenal medulla.";
Biochem. Biophys. Res. Commun. 74:1483-1489(1977).
[7]
PROTEIN SEQUENCE OF 33-37.
PubMed=2909511 [NCBI, ExPASy, EBI, Israel, Japan]
Taylor C.S., Kent U.M., Fleming P.J.;
"The membrane-binding segment of dopamine beta-hydroxylase is not an uncleaved signal sequence.";
J. Biol. Chem. 264:14-16(1989).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 39-566.
DOI=10.1021/bi00479a019; PubMed=2207088 [NCBI, ExPASy, EBI, Israel, Japan]
Wang N., Southan C., DeWolf W.E. Jr., Wells T.N., Kruse L.I., Leatherbarrow R.J.;
"Bovine dopamine beta-hydroxylase, primary structure determined by cDNA cloning and amino acid sequencing.";
Biochemistry 29:6466-6474(1990).
[9]
DISULFIDE BONDS.
DOI=10.1021/bi00204a019; PubMed=7918370 [NCBI, ExPASy, EBI, Israel, Japan]
Robertson J.G., Adams G.W., Medzihradszky K.F., Burlingame A.L., Villafranca J.J.;
"Complete assignment of disulfide bonds in bovine dopamine beta-hydroxylase.";
Biochemistry 33:11563-11575(1994).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J02890; AAA30356.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J05160; AAA30490.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT026311; ABG81467.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF118638; AAD09829.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J02909; AAA30491.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00698276; -.
PIR A33650; A33650.
RefSeq NP_851338.1; -.
UniGene Bt.4481
3D structure databases
HSSP P14925; 1PHM. [HSSP ENTRY / PDB]
ModBase P15101.
Enzyme and pathway databases
BRENDA 1.14.17.1; 251.
Ontologies
GO
GO:0034466; Cellular component: chromaffin granule lumen (inferred from electronic annotation from UniProtKB-SubCell).
GO:0042584; Cellular component: chromaffin granule membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0034774; Cellular component: secretory granule lumen (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005507; Molecular function: copper ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004500; Molecular function: dopamine beta-monooxygenase activity (inferred from electronic annotation from EC).
GO:0031418; Molecular function: L-ascorbic acid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0042423; Biological process: catecholamine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0006548; Biological process: histidine catabolic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR014784; Cu2_ascorb_mOase-like_C.
IPR014783; Cu2_ascorb_mOase_C.
IPR000323; Cu2_ascorb_mOase_N.
IPR013050; DOMON.
IPR005018; DOMON_rel.
IPR000945; Dopamine_b_mOase.
Graphical view of domain structure.
Gene3D G3DSA:2.60.120.230; Cu2_ascorb_mOase_core; 1.
G3DSA:2.60.120.310; Cu2_ascorb_mOase_core; 1.
PANTHER PTHR10157; Dopamine_b_mOase; 1.
Pfam PF03712; Cu2_monoox_C; 1.
PF01082; Cu2_monooxygen; 1.
PF03351; DOMON; 1.
Pfam graphical view of domain structure.
PRINTS PR00767; DBMONOXGNASE.
SMART SM00664; DoH; 1.
SMART graphical view of domain structure.
PROSITE PS00084; CU2_MONOOXYGENASE_1; 1.
PS00085; CU2_MONOOXYGENASE_2; 1.
PS50836; DOMON; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
Ensembl ENSBTAG00000004508; Bos taurus. [Contig view]
GeneID 280758; -.
KEGG bta:280758; -.
Phylogenomic databases
HOVERGEN P15101; -.
Other
ProtoNet P15101.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Catecholamine biosynthesis; Copper; Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond; Glycoprotein; Membrane; Metal-binding; Monooxygenase; Oxidoreductase; PQQ; Signal-anchor; Transmembrane; Vitamin C.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   610  610     Dopamine beta-hydroxylase. PRO_0000006355
CHAIN   33   610  578     Soluble dopamine beta-hydroxylase (Potential). PRO_0000308206
TOPO_DOM   1     9  9     Cytoplasmic (Potential). 
TRANSMEM   10    30  21     Signal-anchor for type II membrane (Potential). 
TOPO_DOM   31   610  580     Intragranular (Potential). 
DOMAIN   50   166  117     DOMON. 
ACT_SITE   223   223        Potential. 
ACT_SITE   405   405        Potential. 
METAL   255   255        Copper A (By similarity). 
METAL   256   256        Copper A (By similarity). 
METAL   326   326        Copper A (By similarity). 
METAL   405   405        Copper B (By similarity). 
METAL   407   407        Copper B (By similarity). 
METAL   480   480        Copper B (By similarity). 
CARBOHYD   177   177        N-linked (GlcNAc...). 
CARBOHYD   559   559        N-linked (GlcNAc...). 
DISULFID   147   589         
DISULFID   225   276         
DISULFID   262   288         
DISULFID   383   496         
DISULFID   387   558         
DISULFID   459   481         
DISULFID   521   521        Interchain. 
DISULFID   523   523        Interchain. 
CONFLICT   35    35        P -> T (in Ref. 6; AA sequence). 
CONFLICT   40    40        F -> S (in Ref. 4; AAD09829). 
CONFLICT   48    48        P -> T (in Ref. 6; AA sequence). 
CONFLICT   55    57        SWN -> RYV (in Ref. 5; AA sequence). 
CONFLICT   74    74        L -> F (in Ref. 5; AA sequence). 
CONFLICT   104   104        Y -> D (in Ref. 4; AAD09829). 
CONFLICT   205   205        R -> C (in Ref. 1; AAA30356). 
CONFLICT   215   215        L -> F (in Ref. 3; ABG81467). 
CONFLICT   267   269        ETI -> RDH (in Ref. 1; AAA30356). 
CONFLICT   349   349        A -> R (in Ref. 8; AAA30491). 
CONFLICT   376   376        A -> P (in Ref. 4; AAD09829). 
CONFLICT   560   560        R -> C (in Ref. 5; AA sequence). 
CONFLICT   566   567        FQ -> LE (in Ref. 4; AAD09829). 
CONFLICT   588   588        H -> Q (in Ref. 1; AAA30356). 
Sequence information
Length: 610 AA [This is the length of the unprocessed precursor] Molecular weight: 68141 Da [This is the MW of the unprocessed precursor] CRC64: 709D23860617CD3A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQVPSPSVRE AASMYGTAVA VFLVILVAAL QGSAPAESPF PFHIPLDPEG TLELSWNISY 

        70         80         90        100        110        120 
AQETIYFQLL VRELKAGVLF GMSDRGELEN ADLVVLWTDR DGAYFGDAWS DQKGQVHLDS 

       130        140        150        160        170        180 
QQDYQLLRAQ RTPEGLYLLF KRPFGTCDPN DYLIEDGTVH LVYGFLEEPL RSLESINTSG 

       190        200        210        220        230        240 
LHTGLQRVQL LKPSIPKPAL PADTRTMEIR APDVLIPGQQ TTYWCYVTEL PDGFPRHHIV 

       250        260        270        280        290        300 
MYEPIVTEGN EALVHHMEVF QCAAEFETIP HFSGPCDSKM KPQRLNFCRH VLAAWALGAK 

       310        320        330        340        350        360 
AFYYPEEAGL AFGGPGSSRF LRLEVHYHNP LVITGRRDSS GIRLYYTAAL RRFDAGIMEL 

       370        380        390        400        410        420 
GLAYTPVMAI PPQETAFVLT GYCTDKCTQL ALPASGIHIF ASQLHTHLTG RKVVTVLARD 

       430        440        450        460        470        480 
GRETEIVNRD NHYSPHFQEI RMLKKVVSVQ PGDVLITSCT YNTEDRRLAT VGGFGILEEM 

       490        500        510        520        530        540 
CVNYVHYYPQ TQLELCKSAV DPGFLHKYFR LVNRFNSEEV CTCPQASVPE QFASVPWNSF 

       550        560        570        580        590        600 
NREVLKALYG FAPISMHCNR SSAVRFQGEW NRQPLPEIVS RLEEPTPHCP ASQAQSPAGP 

       610 
TVLNISGGKG 

P15101 in FASTA format

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