ID   CP2DF_CANFA    STANDARD;      PRT;   499 AA.
AC   Q29473; O02859;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   16-MAY-2006, entry version 45.
DE   Cytochrome P450 2D15 (EC 1.14.14.1) (CYPIID15) (P450 DUT2).
GN   Name=CYP2D15;
OS   Canis familiaris (Dog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   MEDLINE=95305574; PubMed=7786018; DOI=10.1006/abbi.1995.1307;
RA   Sakamoto K., Kirita S., Baba T., Nakamura Y., Yamazoe Y., Kato R.,
RA   Takanaka A., Matsubara T.;
RT   "A new cytochrome P450 form belonging to the CYP2D in dog liver
RT   microsomes: purification, cDNA cloning, and enzyme characterization.";
RL   Arch. Biochem. Biophys. 319:372-382(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Beagle;
RX   MEDLINE=98162950; PubMed=9504424;
RA   Tasaki T., Nakamura A., Itoh S., Ohashi K., Yamamoto Y., Masuda M.,
RA   Iwata H., Kazusaka A., Kamataki T., Fujita S.;
RT   "Expression and characterization of dog CYP2D15 using baculovirus
RT   expression system.";
RL   J. Biochem. 123:162-168(1998).
RN   [3]
RP   CHARACTERIZATION.
RX   MEDLINE=98389575; PubMed=9721180; DOI=10.1006/abbi.1998.0801;
RA   Roussel F., Duignan D.B., Lawton M.P., Obach R.S., Strick C.A.,
RA   Tweedie D.J.;
RT   "Expression and characterization of canine cytochrome P450 2D15.";
RL   Arch. Biochem. Biophys. 357:27-36(1998).
CC   -!- FUNCTION: High activity for the hydroxylation of bunitrolol and
CC       imipramine; low activity on debrisoquine.
CC   -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH +
CC       oxidized flavoprotein + H(2)O.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum
CC       membrane; peripheral membrane protein.
CC   -!- TISSUE SPECIFICITY: Liver. Also detected in several other tissues.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; D17397; BAA04220.1; -; mRNA.
DR   EMBL; AB004268; BAA20357.1; -; mRNA.
DR   PIR; JC4157; JC4157.
DR   UniGene; Cfa.15290; -.
DR   HSSP; P00179; 1DT6.
DR   Ensembl; ENSCAFG00000000980; Canis familiaris.
DR   InterPro; IPR001128; Cytochrome_P450.
DR   InterPro; IPR008069; EP450_CYP2D.
DR   InterPro; IPR002401; EP450I.
DR   PANTHER; PTHR19383; Cytochrome_P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR01686; EP450ICYP2D.
DR   PRINTS; PR00385; P450.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
KW   Direct protein sequencing; Endoplasmic reticulum; Heme; Iron;
KW   Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase.
FT   INIT_MET      0      0
FT   CHAIN         1    499       Cytochrome P450 2D15.
FT                                /FTId=PRO_0000051739.
FT   METAL       445    445       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   499 AA;  56301 MW;  27E352B5B309E7F1 CRC64;
     GLLTGDTLGP LAVAVAIFLL LVDLMHRRRR WATRYPPGPT PVPMVGNLLQ MDFQEPICYF
     SQLQGRFGNV FSLELAWTPV VVLNGLEAVR EALVHRSEDT ADRPPMPIYD HLGLGPESQG
     LFLARYGRAW REQRRFSLST LRNFGLGRKS LEQWVTEEAS CLCAAFAEQA GRPFGPGALL
     NKAVSNVISS LTYGRRFEYD DPRLLQLLEL TQQALKQDSG FLREALNSIP VLLHIPGLAS
     KVFSAQKAII TLTNEMIQEH RKTRDPTQPP RHLIDAFVDE IEKAKGNPKT SFNEENLCMV
     TSDLFIAGMV STSITLTWAL LLMILHPDVQ RRVQQEIDEV IGREQLPEMG DQTRMPFTVA
     VIHEVQRFGD IVPLGVPHMT SRDTEVQGFL IPKGTTLITN LSSVLKDEKV WKKPFRFYPE
     HFLDAQGHFV KHEAFMPFSA GRRVCLGEPL ARMELFLFFT CLLQRFSFSV PAGQPRPSDH
     GVFTFLKVPA PFQLCVEPR
//