ID   CP241_CANFA             Reviewed;         489 AA.
AC   O62671;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Cytochrome P450 2C41;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIC41;
GN   Name=CYP2C41;
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].
RC   TISSUE=Liver;
RX   MEDLINE=98160435; PubMed=9492393;
RA   Blaisdell J., Goldstein J.A., Bai S.A.;
RT   "Isolation of a new canine cytochrome P450 cDNA from the cytochrome
RT   P450 2C subfamily (CYP2C41) and evidence for polymorphic differences
RT   in its expression.";
RL   Drug Metab. Dispos. 26:278-283(1998).
CC   -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate
CC       monooxygenases. In liver microsomes, this enzyme is involved in an
CC       NADPH-dependent electron transport pathway. It oxidizes a variety
CC       of structurally unrelated compounds, including steroids, fatty
CC       acids, and xenobiotics.
CC   -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH +
CC       oxidized flavoprotein + H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- INDUCTION: P450 can be induced to high levels in liver and other
CC       tissues by various foreign compounds, including drugs, pesticides,
CC       and carcinogens.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; AF016248; AAC08738.1; -; mRNA.
DR   RefSeq; NP_001003334.1; -.
DR   UniGene; Cfa.3499; -.
DR   HSSP; P11712; 1OG2.
DR   SMR; O62671; 47-489.
DR   GeneID; 415123; -.
DR   KEGG; cfa:415123; -.
DR   HOVERGEN; O62671; -.
DR   BRENDA; 1.14.14.1; 463.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005792; C:microsome; IEA:UniProtKB-SubCell.
DR   GO; GO:0070330; F:aromatase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017973; Cyt_P450_C.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1.
DR   PANTHER; PTHR19383; Cyt_P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase.
FT   CHAIN         1    489       Cytochrome P450 2C41.
FT                                /FTId=PRO_0000051724.
FT   METAL       434    434       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   489 AA;  55499 MW;  BDAA6739BAAA8E15 CRC64;
     MDPVVVLVLC LSCCLLLSLW KQSSRKGKLP PGPTPLPFIG NILQLDKDIN KSLSNLSKAY
     GPVFTLYFGM KPTVVLHGYD AVKETLIDLG EEFSARGRFP IAEKVSGGHG IIFTSGNRWK
     EMRRFALTTL RNLGMGKSDL ESRVQEEACY LVEELRKTNA LPCDPTFVLG CASCNVICSI
     IFQNRFDYTD QTLIGFLEKL NENFRILSSP WIQAYNSFPA LLHYLPGSHN TIFKNFAFIK
     SYILEKIKEH QESFDVNNPR DFIDYFLIKM EQEKHNQPLE FTFENLKTIA TDLFGAGTET
     TSTTLRYGLL LLLKHPEVTV KVQEEIDRVI GRHQSPHMQD RSRMPYTNAV LHEIQRYIDL
     VPNSLPHAVT CDVKFRNYVI PKGTTILISL SSVLSDEKEF PRPEIFDPAH FLDDSGNFKK
     SDYFMAFSAG KRICVGEGLA RMELFLFLTT ILQKFTLKPL VDPKDIDTTP LASGFGHVPP
     TYQLCFIPV
//