ID   CP2DF_CANLF             Reviewed;         500 AA.
AC   Q29473; O02859;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Cytochrome P450 2D15;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIID15;
DE   AltName: Full=Cytochrome P450 DUT2;
GN   Name=CYP2D15;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   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 microsomes:
RT   purification, cDNA cloning, and enzyme characterization.";
RL   Arch. Biochem. Biophys. 319:372-382(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Beagle;
RX   PubMed=9504424; DOI=10.1093/oxfordjournals.jbchem.a021905;
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   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:
CC       Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC         reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:142491; EC=1.14.14.1;
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- TISSUE SPECIFICITY: Liver. Also detected in several other tissues.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; D17397; BAA04220.1; -; mRNA.
DR   EMBL; AB004268; BAA20357.1; -; mRNA.
DR   PIR; JC4157; JC4157.
DR   RefSeq; NP_001003333.1; NM_001003333.1.
DR   AlphaFoldDB; Q29473; -.
DR   SMR; Q29473; -.
DR   ChEMBL; CHEMBL1795137; -.
DR   GeneID; 415120; -.
DR   KEGG; cfa:415120; -.
DR   CTD; 415120; -.
DR   InParanoid; Q29473; -.
DR   OrthoDB; 702827at2759; -.
DR   PRO; PR:Q29473; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR   GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR   GO; GO:0019369; P:arachidonic acid metabolic process; IBA:GO_Central.
DR   GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR008069; Cyt_P450_E_grp-I_CYP2D-like.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR01686; EP450ICYP2D.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane;
KW   Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..500
FT                   /note="Cytochrome P450 2D15"
FT                   /id="PRO_0000051739"
FT   BINDING         446
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   500 AA;  56432 MW;  E7E352A01FABAED5 CRC64;
     MGLLTGDTLG PLAVAVAIFL LLVDLMHRRR RWATRYPPGP TPVPMVGNLL QMDFQEPICY
     FSQLQGRFGN VFSLELAWTP VVVLNGLEAV REALVHRSED TADRPPMPIY DHLGLGPESQ
     GLFLARYGRA WREQRRFSLS TLRNFGLGRK SLEQWVTEEA SCLCAAFAEQ AGRPFGPGAL
     LNKAVSNVIS SLTYGRRFEY DDPRLLQLLE LTQQALKQDS GFLREALNSI PVLLHIPGLA
     SKVFSAQKAI ITLTNEMIQE HRKTRDPTQP PRHLIDAFVD EIEKAKGNPK TSFNEENLCM
     VTSDLFIAGM VSTSITLTWA LLLMILHPDV QRRVQQEIDE VIGREQLPEM GDQTRMPFTV
     AVIHEVQRFG DIVPLGVPHM TSRDTEVQGF LIPKGTTLIT NLSSVLKDEK VWKKPFRFYP
     EHFLDAQGHF VKHEAFMPFS AGRRVCLGEP LARMELFLFF TCLLQRFSFS VPAGQPRPSD
     HGVFTFLKVP APFQLCVEPR