ID   CP2CE_RABIT             Reviewed;         490 AA.
AC   P17666;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Cytochrome P450 2C14;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIC14;
DE   AltName: Full=Cytochrome P450 PHP3;
GN   Name=CYP2C14;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2820951; DOI=10.1093/oxfordjournals.jbchem.a121977;
RA   Imai Y.;
RT   "Cytochrome P-450 related to P-4504 from phenobarbital-treated rabbit
RT   liver: molecular cloning of cDNA and characterization of cytochrome P-450
RT   obtained by its expression in yeast cells.";
RL   J. Biochem. 101:1129-1139(1987).
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; D00190; BAA00130.1; -; mRNA.
DR   PIR; A26921; A26921.
DR   RefSeq; NP_001164591.1; NM_001171120.1.
DR   AlphaFoldDB; P17666; -.
DR   SMR; P17666; -.
DR   STRING; 9986.ENSOCUP00000020330; -.
DR   GeneID; 100328936; -.
DR   KEGG; ocu:100328936; -.
DR   CTD; 100328936; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   InParanoid; P17666; -.
DR   OrthoDB; 702827at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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..490
FT                   /note="Cytochrome P450 2C14"
FT                   /id="PRO_0000051704"
FT   BINDING         435
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"
SQ   SEQUENCE   490 AA;  55721 MW;  2572163B0AAA076E CRC64;
     MDPVVVLVLC LSCLLLLSLW KQSHGGGKLP PGPTPLPILG NILQIDFKDI SKSLQNLSKV
     YGNVFTVYMG MKPTVVMYGY EAVKEALVDL GEEFSGRNLS PINKKVNKGL GVIFSNGKRW
     KEIRRFSLMT LRNFGMGKRS IEDRVQEEAR CLVEELRKTN GSPCDPTFIL GAAPCNVICS
     VIFQNRFDYK DETFLNLMGK FNENFRILNS PWLQVCNIFP ILMDYLPGTH KTVFENFDYV
     RNFVLEKTKE HQESLDINNP RDFIDCFLIK MKQEKHNQQS EFTIENLMAT VTDVFAAGTE
     TTSTTLRYGL LLLMKHPEVT AKVQEEIERV IGRHRSPCMQ DRSRMPYTDA TVHEIQRYIN
     LVPNNVPHAT TCNVKFRNYF IPKGTAVLTS LTSVLHDNQE FLKPDKFDPG HFLDASGNFK
     KSDYFMPFST GKRVCMGEAL ARMELFLFLT AILQNFTLKP LVDPKDIDTT PLVSGARSCA
     TLYQLSFIPA