ID   CP241_CANLF             Reviewed;         489 AA.
AC   O62671;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Cytochrome P450 2C41;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIC41;
GN   Name=CYP2C41;
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].
RC   TISSUE=Liver;
RX   PubMed=9492393;
RA   Blaisdell J., Goldstein J.A., Bai S.A.;
RT   "Isolation of a new canine cytochrome P450 cDNA from the cytochrome P450 2C
RT   subfamily (CYP2C41) and evidence for polymorphic differences in its
RT   expression.";
RL   Drug Metab. Dispos. 26:278-283(1998).
CC   -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases.
CC       In liver microsomes, this enzyme is involved in an NADPH-dependent
CC       electron transport pathway. It oxidizes a variety of structurally
CC       unrelated compounds, including steroids, fatty acids, and xenobiotics.
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   -!- INDUCTION: P450 can be induced to high levels in liver and other
CC       tissues by various foreign compounds, including drugs, pesticides, and
CC       carcinogens.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF016248; AAC08738.1; -; mRNA.
DR   RefSeq; NP_001003334.1; NM_001003334.1.
DR   AlphaFoldDB; O62671; -.
DR   SMR; O62671; -.
DR   GeneID; 415123; -.
DR   KEGG; ag:AAC08738; -.
DR   CTD; 415123; -.
DR   InParanoid; O62671; -.
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:0008392; F:arachidonic acid epoxygenase activity; 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:0019373; P:epoxygenase P450 pathway; 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; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..489
FT                   /note="Cytochrome P450 2C41"
FT                   /id="PRO_0000051724"
FT   BINDING         434
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   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