CP2CB_RAT
ID CP2CB_RAT Reviewed; 500 AA.
AC P08683; Q63141; Q64554;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Cytochrome P450 2C11;
DE EC=1.14.14.1 {ECO:0000269|PubMed:10491410, ECO:0000269|PubMed:2434473};
DE AltName: Full=CYPIIC11;
DE AltName: Full=Cytochrome P-450(M-1) {ECO:0000303|PubMed:2434473};
DE AltName: Full=Cytochrome P450-UT-2;
DE AltName: Full=Cytochrome P450-UT-A;
DE AltName: Full=Cytochrome P450H;
GN Name=Cyp2c11; Synonyms=Cyp2c, Cyp2c-11;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3805049; DOI=10.1016/s0021-9258(19)75695-6;
RA Yoshioka H., Morohashi K., Sogawa K., Miyata T., Kawajiri K., Hirose T.,
RA Inayama S., Fujii-Kuriyama Y., Omura T.;
RT "Structural analysis and specific expression of microsomal cytochrome P-
RT 450(M-1) mRNA in male rat livers.";
RL J. Biol. Chem. 262:1706-1711(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2894840; DOI=10.1021/bi00399a039;
RA Morishima N., Yoshioka H., Higashi Y., Sogawa K., Fujii-Kuriyama Y.;
RT "Gene structure of cytochrome P-450(M-1) specifically expressed in male rat
RT liver.";
RL Biochemistry 26:8279-8285(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2455430; DOI=10.1530/acta.0.1180314;
RA Stroem A., Mode A., Zaphiropoulos P.G., Nilsson A.G., Morgan E.,
RA Gustafsson J.-A.;
RT "Cloning and pretranslational hormonal regulation of testosterone 16 alpha-
RT hydroxylase (P-45016 alpha) in male rat liver.";
RL Acta Endocrinol. 118:314-320(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ALA-4; SER-116 AND LEU-187.
RC STRAIN=Wistar Gunn; TISSUE=Liver;
RX PubMed=8611037; DOI=10.1006/abbi.1996.0079;
RA Biagini C., Celier C.;
RT "cDNA-directed expression of two allelic variants of cytochrome P450 2C11
RT using COS1 and SF21 insect cells.";
RL Arch. Biochem. Biophys. 326:298-305(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3164963;
RA Zaphiropoulos P.G., Mode A., Stroem A., Husman B., Andersson G.,
RA Gustafsson J.-A.;
RT "Sequence and regulation of two growth-hormone-controlled, sex-specific
RT isozymes of cytochrome P-450 in rat liver, P-450(15)beta and P-
RT 450(16)alpha.";
RL Acta Med. Scand. Suppl. 723:161-167(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8068205; DOI=10.1089/dna.1994.13.805;
RA Stroem A., Eguchi H., Mode A., Legraverend C., Tollet P.,
RA Stroemstedt P.-E., Gustafsson J.-A.;
RT "Characterization of the proximal promoter and two silencer elements in the
RT CYP2C11 gene expressed in rat liver.";
RL DNA Cell Biol. 13:805-819(1994).
RN [8]
RP SEQUENCE REVISION TO 12.
RA Stroem A.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PROTEIN SEQUENCE OF 1-30, FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=2434473; DOI=10.1093/oxfordjournals.jbchem.a121842;
RA Matsumoto T., Emi Y., Kawabata S., Omura T.;
RT "Purification and characterization of three male-specific and one female-
RT specific forms of cytochrome P-450 from rat liver microsomes.";
RL J. Biochem. 100:1359-1371(1986).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND TISSUE SPECIFICITY.
RX PubMed=10491410; DOI=10.1172/jci7013;
RA Holla V.R., Makita K., Zaphiropoulos P.G., Capdevila J.H.;
RT "The kidney cytochrome P-450 2C23 arachidonic acid epoxygenase is
RT upregulated during dietary salt loading.";
RL J. Clin. Invest. 104:751-760(1999).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15766564; DOI=10.1016/j.bbrc.2005.02.103;
RA Barbosa-Sicard E., Markovic M., Honeck H., Christ B., Muller D.N.,
RA Schunck W.H.;
RT "Eicosapentaenoic acid metabolism by cytochrome P450 enzymes of the CYP2C
RT subfamily.";
RL Biochem. Biophys. Res. Commun. 329:1275-1281(2005).
CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of
CC steroid hormones and fatty acids. Catalyzes the hydroxylation of
CC carbon-hydrogen bonds. Metabolizes testosterone to 2alpha- and 16alpha-
CC hydroxytestosterone (PubMed:2434473). Catalyzes the epoxidation of
CC double bonds of polyunsaturated fatty acids (PUFAs) (PubMed:10491410,
CC PubMed:15766564). Converts arachidonic acid (ARA, C20:4(n-6)) primarily
CC to epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and
CC 14,15-EET, with both R,S and S,R stereochemistry (PubMed:10491410).
CC Preferentially produces 11R,12S-EET enantiomer. To a lesser extent,
CC catalyzes the hydroxylation of arachidonic acid producing
CC hydroxyeicosatetraenoates (HETEs) (PubMed:10491410). Metabolizes
CC eicosapentaenoic acid (EPA, C20:5(n-3)) to epoxyeicosatetraenoic acid
CC (EETeTr) regioisomers, 8,9-, 11,12-, 14,15-, and 17,18-EETeTr,
CC preferentially producing 17R,18S-EETeTr enantiomer (PubMed:15766564).
CC Mechanistically, uses molecular oxygen inserting one oxygen atom into a
CC substrate, and reducing the second into a water molecule, with two
CC electrons provided by NADPH via cytochrome P450 reductase (NADPH--
CC hemoprotein reductase) (PubMed:2434473, PubMed:15766564).
CC {ECO:0000269|PubMed:10491410, ECO:0000269|PubMed:15766564,
CC ECO:0000269|PubMed:2434473}.
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 Evidence={ECO:0000269|PubMed:10491410, ECO:0000269|PubMed:2434473};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150;
CC Evidence={ECO:0000305|PubMed:10491410, ECO:0000305|PubMed:2434473};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + reduced [NADPH--hemoprotein reductase] + testosterone =
CC 2alpha,17beta-dihydroxyandrost-4-en-3-one + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:65276, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17347,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:83025;
CC Evidence={ECO:0000269|PubMed:2434473};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65277;
CC Evidence={ECO:0000305|PubMed:2434473};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + reduced [NADPH--hemoprotein reductase] + testosterone =
CC 16alpha,17beta-dihydroxyandrost-4-en-3-one + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53196, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17347,
CC ChEBI:CHEBI:34172, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:2434473};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53197;
CC Evidence={ECO:0000305|PubMed:2434473};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (8R,9S)-epoxy-(5Z,11Z,14Z)-eicosatrienoate +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49884, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:131975; Evidence={ECO:0000269|PubMed:10491410};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49885;
CC Evidence={ECO:0000305|PubMed:10491410};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (8S,9R)-epoxy-(5Z,11Z,14Z)-eicosatrienoate +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49928, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:131974; Evidence={ECO:0000269|PubMed:10491410};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49929;
CC Evidence={ECO:0000305|PubMed:10491410};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (11R,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49880, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:131970; Evidence={ECO:0000269|PubMed:10491410};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49881;
CC Evidence={ECO:0000305|PubMed:10491410};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (11S,12R)-epoxy-(5Z,8Z,14Z)-eicosatrienoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49876, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:131969; Evidence={ECO:0000269|PubMed:10491410};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49877;
CC Evidence={ECO:0000305|PubMed:10491410};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49860, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:131965; Evidence={ECO:0000269|PubMed:10491410};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49861;
CC Evidence={ECO:0000305|PubMed:10491410};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49856, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:131964; Evidence={ECO:0000269|PubMed:10491410};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49857;
CC Evidence={ECO:0000305|PubMed:10491410};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 8,9-epoxy-(5Z,11Z,14Z,17Z)-eicosatetraenoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:52168, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562,
CC ChEBI:CHEBI:136439; Evidence={ECO:0000269|PubMed:15766564};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52169;
CC Evidence={ECO:0000305|PubMed:15766564};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 11,12-epoxy-(5Z,8Z,14Z,17Z)-
CC eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:52172, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562,
CC ChEBI:CHEBI:136441; Evidence={ECO:0000269|PubMed:15766564};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52173;
CC Evidence={ECO:0000305|PubMed:15766564};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 14,15-epoxy-(5Z,8Z,11Z,17Z)-
CC eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:52176, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562,
CC ChEBI:CHEBI:136443; Evidence={ECO:0000269|PubMed:15766564};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52177;
CC Evidence={ECO:0000305|PubMed:15766564};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (17S,18R)-epoxy-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:39783, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562,
CC ChEBI:CHEBI:76635; Evidence={ECO:0000269|PubMed:15766564};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39784;
CC Evidence={ECO:0000305|PubMed:15766564};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (17R,18S)-epoxy-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:39779, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562,
CC ChEBI:CHEBI:76634; Evidence={ECO:0000269|PubMed:15766564};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39780;
CC Evidence={ECO:0000305|PubMed:15766564};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P33261};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.5 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoate (total epoxygenase
CC activity) {ECO:0000269|PubMed:15766564};
CC KM=9.5 uM for (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate (total
CC epoxygenase activity) {ECO:0000269|PubMed:15766564};
CC Vmax=5.8 nmol/min/nmol enzyme toward (5Z,8Z,11Z,14Z)-
CC eicosatetraenoate (total epoxygenase activity)
CC {ECO:0000269|PubMed:15766564};
CC Vmax=14.6 nmol/min/nmol enzyme toward (5Z,8Z,11Z,14Z,17Z)-
CC eicosapentaenoate (total epoxygenase activity)
CC {ECO:0000269|PubMed:15766564};
CC -!- PATHWAY: Lipid metabolism; arachidonate metabolism.
CC {ECO:0000305|PubMed:10491410}.
CC -!- PATHWAY: Steroid metabolism. {ECO:0000305|PubMed:2434473}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:2434473}; Peripheral membrane protein. Microsome
CC membrane {ECO:0000269|PubMed:2434473}; Peripheral membrane protein.
CC -!- TISSUE SPECIFICITY: Liver and kidney; male-specific.
CC {ECO:0000269|PubMed:10491410, ECO:0000269|PubMed:2434473}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; J02657; AAA41062.1; -; mRNA.
DR EMBL; M18363; AAA41007.1; -; Genomic_DNA.
DR EMBL; M18356; AAA41007.1; JOINED; Genomic_DNA.
DR EMBL; M18357; AAA41007.1; JOINED; Genomic_DNA.
DR EMBL; M18359; AAA41007.1; JOINED; Genomic_DNA.
DR EMBL; M18360; AAA41007.1; JOINED; Genomic_DNA.
DR EMBL; M18361; AAA41007.1; JOINED; Genomic_DNA.
DR EMBL; M18362; AAA41007.1; JOINED; Genomic_DNA.
DR EMBL; U33173; AAB02144.1; -; mRNA.
DR EMBL; BC088146; AAH88146.1; -; mRNA.
DR EMBL; X79081; CAA55686.3; -; Genomic_DNA.
DR PIR; A26685; A26685.
DR PIR; S62785; S62785.
DR RefSeq; NP_062057.2; NM_019184.2.
DR AlphaFoldDB; P08683; -.
DR SMR; P08683; -.
DR STRING; 10116.ENSRNOP00000017310; -.
DR BindingDB; P08683; -.
DR ChEMBL; CHEMBL4971; -.
DR DrugBank; DB13746; Bioallethrin.
DR DrugBank; DB00266; Dicoumarol.
DR SwissLipids; SLP:000001687; -.
DR iPTMnet; P08683; -.
DR PhosphoSitePlus; P08683; -.
DR PaxDb; P08683; -.
DR PRIDE; P08683; -.
DR Ensembl; ENSRNOT00000088853; ENSRNOP00000074503; ENSRNOG00000052810.
DR GeneID; 29277; -.
DR KEGG; rno:29277; -.
DR CTD; 29277; -.
DR RGD; 2469; Cyp2c11.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000162913; -.
DR InParanoid; P08683; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; P08683; -.
DR TreeFam; TF352043; -.
DR BRENDA; 1.14.14.1; 5301.
DR BRENDA; 1.14.14.24; 5301.
DR SABIO-RK; P08683; -.
DR UniPathway; UPA00383; -.
DR PRO; PR:P08683; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0008405; F:arachidonic acid 11,12-epoxygenase activity; IDA:UniProtKB.
DR GO; GO:0008404; F:arachidonic acid 14,15-epoxygenase activity; IDA:UniProtKB.
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:0004497; F:monooxygenase activity; IDA:UniProtKB.
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:0008390; F:testosterone 16-alpha-hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0019373; P:epoxygenase P450 pathway; IDA:UniProtKB.
DR GO; GO:0046456; P:icosanoid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
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; IPR008068; Cyt_P450_E_grp-I_CYP2B-like.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR01685; EP450ICYP2B.
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; Fatty acid metabolism;
KW Heme; Iron; Lipid metabolism; Membrane; Metal-binding; Microsome;
KW Monooxygenase; Oxidoreductase; Reference proteome; Steroid metabolism.
FT CHAIN 1..500
FT /note="Cytochrome P450 2C11"
FT /id="PRO_0000051701"
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"
FT /evidence="ECO:0000250|UniProtKB:P33261"
FT VARIANT 4
FT /note="V -> A (in strain: Wistar Gunn)"
FT /evidence="ECO:0000269|PubMed:8611037"
FT VARIANT 116
FT /note="N -> S (in strain: Wistar Gunn)"
FT /evidence="ECO:0000269|PubMed:8611037"
FT VARIANT 187
FT /note="F -> L (in strain: Wistar Gunn)"
FT /evidence="ECO:0000269|PubMed:8611037"
FT CONFLICT 329
FT /note="R -> H (in Ref. 2; AAA41007)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 57181 MW; 8DCE0E356D8A5AC3 CRC64;
MDPVLVLVLT LSSLLLLSLW RQSFGRGKLP PGPTPLPIIG NTLQIYMKDI GQSIKKFSKV
YGPIFTLYLG MKPFVVLHGY EAVKEALVDL GEEFSGRGSF PVSERVNKGL GVIFSNGMQW
KEIRRFSIMT LRTFGMGKRT IEDRIQEEAQ CLVEELRKSK GAPFDPTFIL GCAPCNVICS
IIFQNRFDYK DPTFLNLMHR FNENFRLFSS PWLQVCNTFP AIIDYFPGSH NQVLKNFFYI
KNYVLEKVKE HQESLDKDNP RDFIDCFLNK MEQEKHNPQS EFTLESLVAT VTDMFGAGTE
TTSTTLRYGL LLLLKHVDVT AKVQEEIERV IGRNRSPCMK DRSQMPYTDA VVHEIQRYID
LVPTNLPHLV TRDIKFRNYF IPKGTNVIVS LSSILHDDKE FPNPEKFDPG HFLDERGNFK
KSDYFMPFSA GKRICAGEAL ARTELFLFFT TILQNFNLKS LVDVKDIDTT PAISGFGHLP
PFYEACFIPV QRADSLSSHL
