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Database: UniProt
Entry: P10632
LinkDB: P10632
Original site: P10632 
ID   CP2C8_HUMAN             Reviewed;         490 AA.
AC   P10632; A8K9N8; B0AZN2; B7Z1F6; Q5VX93; Q8WWB1; Q9UCZ9;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   29-SEP-2021, entry version 222.
DE   RecName: Full=Cytochrome P450 2C8 {ECO:0000303|PubMed:26427316};
DE            EC=1.14.14.1 {ECO:0000269|PubMed:11093772, ECO:0000269|PubMed:14559847};
DE   AltName: Full=CYPIIC8;
DE   AltName: Full=Cytochrome P450 IIC2;
DE   AltName: Full=Cytochrome P450 MP-12;
DE   AltName: Full=Cytochrome P450 MP-20;
DE   AltName: Full=Cytochrome P450 form 1;
DE   AltName: Full=S-mephenytoin 4-hydroxylase;
GN   Name=CYP2C8 {ECO:0000303|PubMed:7574697, ECO:0000312|HGNC:HGNC:2622};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-264.
RC   TISSUE=Liver;
RX   PubMed=3500169;
RA   Okino S.T., Quattrochi L.C., Pendurthi U.R., McBride O.W., Tukey R.H.;
RT   "Characterization of multiple human cytochrome P-450 1 cDNAs. The
RT   chromosomal localization of the gene and evidence for alternate RNA
RT   splicing.";
RL   J. Biol. Chem. 262:16072-16079(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=3697070; DOI=10.1093/nar/15.23.10053;
RA   Kimura S., Pastewka J., Gelboin H.V., Gonzalez F.J.;
RT   "cDNA and amino acid sequences of two members of the human P450IIC gene
RT   subfamily.";
RL   Nucleic Acids Res. 15:10053-10054(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-264.
RX   PubMed=2009263; DOI=10.1021/bi00227a012;
RA   Romkes M., Faletto M.B., Blaisdell J.A., Raucy J.L., Goldstein J.A.;
RT   "Cloning and expression of complementary DNAs for multiple members of the
RT   human cytochrome P450IIC subfamily.";
RL   Biochemistry 30:3247-3255(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP   LYS-139 AND ARG-399.
RC   TISSUE=Liver, and Mammary gland;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-139; VAL-244; MET-264;
RP   PHE-269 AND ARG-399.
RG   NIEHS SNPs program;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
RC   TISSUE=Blood;
RX   PubMed=1707679; DOI=10.1016/0167-4781(91)90138-c;
RA   Ged C., Beaune P.;
RT   "Isolation of the human cytochrome P-450 IIC8 gene: multiple glucocorticoid
RT   responsive elements in the 5' region.";
RL   Biochim. Biophys. Acta 1088:433-435(1991).
RN   [10]
RP   PROTEIN SEQUENCE OF 2-15, NUCLEOTIDE SEQUENCE [MRNA] OF 6-490, FUNCTION,
RP   CATALYTIC ACTIVITY, PATHWAY, AND VARIANT LEU-411.
RC   TISSUE=Kidney;
RX   PubMed=7574697; DOI=10.1006/abbi.1995.1438;
RA   Zeldin D.C., DuBois R.N., Falck J.R., Capdevila J.H.;
RT   "Molecular cloning, expression and characterization of an endogenous human
RT   cytochrome P450 arachidonic acid epoxygenase isoform.";
RL   Arch. Biochem. Biophys. 322:76-86(1995).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 11-490 (ISOFORM 1), AND VARIANTS ASP-154;
RP   LYS-193; ARG-249 AND LEU-411.
RC   TISSUE=Liver;
RX   PubMed=3196692; DOI=10.1021/bi00418a039;
RA   Ged C., Umbenhauer D.R., Bellew T.M., Bork R.W., Srivastava P.K.,
RA   Shinriki N., Lloyd R.S., Guengerich F.P.;
RT   "Characterization of cDNAs, mRNAs, and proteins related to human liver
RT   microsomal cytochrome P-450 (S)-mephenytoin 4'-hydroxylase.";
RL   Biochemistry 27:6929-6940(1988).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 34-382 (ISOFORM 1), AND VARIANT LYS-139.
RX   PubMed=2729895; DOI=10.1111/j.1469-1809.1989.tb01119.x;
RA   Shephard E.A., Phillips I.R., Santisteban I., Palmer C.N., Povey S.;
RT   "Cloning, expression and chromosomal localization of a member of the human
RT   cytochrome P450IIC gene sub-family.";
RL   Ann. Hum. Genet. 53:23-31(1989).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 281-490 (ISOFORM 1), AND VARIANT ARG-399.
RX   PubMed=2216732; DOI=10.1093/nar/18.18.5550;
RA   Kolyada A.Y.;
RT   "Sequence of a human liver cytochrome P-450 cDNA clone.";
RL   Nucleic Acids Res. 18:5550-5550(1990).
RN   [14]
RP   POLYMORPHISM.
RX   PubMed=15365880; DOI=10.1007/s10038-004-0188-6;
RA   Ishikawa C., Ozaki H., Nakajima T., Ishii T., Kanai S., Anjo S., Shirai K.,
RA   Inoue I.;
RT   "A frameshift variant of CYP2C8 was identified in a patient who suffered
RT   from rhabdomyolysis after administration of cerivastatin.";
RL   J. Hum. Genet. 49:582-585(2004).
RN   [15]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX   PubMed=11093772; DOI=10.1124/mol.58.6.1341;
RA   Marill J., Cresteil T., Lanotte M., Chabot G.G.;
RT   "Identification of human cytochrome P450s involved in the formation of all-
RT   trans-retinoic acid principal metabolites.";
RL   Mol. Pharmacol. 58:1341-1348(2000).
RN   [16]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=14559847;
RA   Lee A.J., Conney A.H., Zhu B.T.;
RT   "Human cytochrome P450 3A7 has a distinct high catalytic activity for the
RT   16alpha-hydroxylation of estrone but not 17beta-estradiol.";
RL   Cancer Res. 63:6532-6536(2003).
RN   [17]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
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).
RN   [18]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=19965576; DOI=10.1194/jlr.m003061;
RA   Lucas D., Goulitquer S., Marienhagen J., Fer M., Dreano Y., Schwaneberg U.,
RA   Amet Y., Corcos L.;
RT   "Stereoselective epoxidation of the last double bond of polyunsaturated
RT   fatty acids by human cytochromes P450.";
RL   J. Lipid Res. 51:1125-1133(2010).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 28-490.
RX   PubMed=14676196; DOI=10.1074/jbc.m312516200;
RA   Schoch G.A., Yano J.K., Wester M.R., Griffin K.J., Stout C.D.,
RA   Johnson E.F.;
RT   "Structure of human microsomal cytochrome P450 2C8. Evidence for a
RT   peripheral fatty acid binding site.";
RL   J. Biol. Chem. 279:9497-9503(2004).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 28-490 IN COMPLEX WITH
RP   INHIBITORS, AND SUBSTRATE-BINDING SITES.
RX   PubMed=18413310; DOI=10.1074/jbc.m802180200;
RA   Schoch G.A., Yano J.K., Sansen S., Dansette P.M., Stout C.D., Johnson E.F.;
RT   "Determinants of cytochrome P450 2C8 substrate binding: structures of
RT   complexes with montelukast, troglitazone, felodipine, and 9-cis-retinoic
RT   acid.";
RL   J. Biol. Chem. 283:17227-17237(2008).
RN   [22]
RP   VARIANTS LYS-139; PHE-269 AND ARG-399.
RX   PubMed=11668219; DOI=10.1097/00008571-200110000-00006;
RA   Dai D., Zeldin D.C., Blaisdell J.A., Chanas B., Coulter S.J.,
RA   Ghanayem B.I., Goldstein J.A.;
RT   "Polymorphisms in human CYP2C8 decrease metabolism of the anticancer drug
RT   paclitaxel and arachidonic acid.";
RL   Pharmacogenetics 11:597-607(2001).
RN   [23]
RP   VARIANTS LYS-139; MET-264; PHE-269; SER-390 AND ARG-399.
RX   PubMed=12429347; DOI=10.1016/s0006-2952(02)01354-0;
RA   Bahadur N., Leathart J.B., Mutch E., Steimel-Crespi D., Dunn S.A.,
RA   Gilissen R., Houdt J.V., Hendrickx J., Mannens G., Bohets H.,
RA   Williams F.M., Armstrong M., Crespi C.L., Daly A.K.;
RT   "CYP2C8 polymorphisms in Caucasians and their relationship with paclitaxel
RT   6alpha-hydroxylase activity in human liver microsomes.";
RL   Biochem. Pharmacol. 64:1579-1589(2002).
RN   [24]
RP   VARIANTS LYS-139; MET-264; PHE-269 AND ARG-399.
RX   PubMed=15469410; DOI=10.1517/14622416.5.7.895;
RA   Solus J.F., Arietta B.J., Harris J.R., Sexton D.P., Steward J.Q.,
RA   McMunn C., Ihrie P., Mehall J.M., Edwards T.L., Dawson E.P.;
RT   "Genetic variation in eleven phase I drug metabolism genes in an ethnically
RT   diverse population.";
RL   Pharmacogenomics 5:895-931(2004).
RN   [25]
RP   CHARACTERIZATION OF VARIANTS LYS-139; SER-171; GLY-186; MET-223; PRO-238;
RP   ARG-247; MET-264; PHE-269; ASN-383; ARG-399 AND VAL-461 DEL, FUNCTION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND POLYMORPHISM.
RX   PubMed=26427316; DOI=10.1016/j.dmpk.2015.07.003;
RA   Tsukada C., Saito T., Maekawa M., Mano N., Oda A., Hirasawa N.,
RA   Hiratsuka M.;
RT   "Functional characterization of 12 allelic variants of CYP2C8 by assessment
RT   of paclitaxel 6alpha-hydroxylation and amodiaquine N-deethylation.";
RL   Drug Metab. Pharmacokinet. 30:366-373(2015).
CC   -!- FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of
CC       various endogenous substrates, including fatty acids, steroid hormones
CC       and vitamins (PubMed:7574697, PubMed:11093772, PubMed:14559847,
CC       PubMed:15766564, PubMed:19965576). Mechanistically, uses molecular
CC       oxygen inserting one oxygen atom into a substrate, and reducing the
CC       second into a water molecule, with two electrons provided by NADPH via
CC       cytochrome P450 reductase (NADPH--hemoprotein reductase)
CC       (PubMed:7574697, PubMed:11093772, PubMed:14559847, PubMed:15766564,
CC       PubMed:19965576). Primarily catalyzes the epoxidation of double bonds
CC       of polyunsaturated fatty acids (PUFA) with a preference for the last
CC       double bond (PubMed:7574697, PubMed:15766564, PubMed:19965576).
CC       Catalyzes the hydroxylation of carbon-hydrogen bonds. Metabolizes all
CC       trans-retinoic acid toward its 4-hydroxylated form (PubMed:11093772).
CC       Displays 16-alpha hydroxylase activity toward estrogen steroid
CC       hormones, 17beta-estradiol (E2) and estrone (E1) (PubMed:14559847).
CC       Plays a role in the oxidative metabolism of xenobiotics. It is the
CC       principal enzyme responsible for the metabolism of the anti-cancer drug
CC       paclitaxel (taxol) (PubMed:26427316). {ECO:0000269|PubMed:11093772,
CC       ECO:0000269|PubMed:14559847, ECO:0000269|PubMed:15766564,
CC       ECO:0000269|PubMed:19965576, ECO:0000269|PubMed:26427316,
CC       ECO:0000269|PubMed:7574697}.
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:11093772, ECO:0000269|PubMed:14559847};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150;
CC         Evidence={ECO:0000305|PubMed:11093772};
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:7574697,
CC         ECO:0000305|PubMed:15766564};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49881;
CC         Evidence={ECO:0000305|PubMed:7574697};
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:7574697,
CC         ECO:0000305|PubMed:15766564};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49877;
CC         Evidence={ECO:0000305|PubMed:7574697};
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:19965576,
CC         ECO:0000269|PubMed:7574697};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49861;
CC         Evidence={ECO:0000305|PubMed:19965576, ECO:0000305|PubMed:7574697};
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:19965576,
CC         ECO:0000269|PubMed:7574697};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49857;
CC         Evidence={ECO:0000305|PubMed:19965576};
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] = (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:19965576};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39780;
CC         Evidence={ECO:0000305|PubMed:19965576};
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:19965576};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39784;
CC         Evidence={ECO:0000305|PubMed:19965576};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = (19R,20S)-epoxy-(4Z,7Z,10Z,13Z,16Z)-
CC         docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:52120, 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:77016,
CC         ChEBI:CHEBI:136410; Evidence={ECO:0000269|PubMed:19965576};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52121;
CC         Evidence={ECO:0000305|PubMed:19965576};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = (19S,20R)-epoxy-(4Z,7Z,10Z,13Z,16Z)-
CC         docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:52124, 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:77016,
CC         ChEBI:CHEBI:136411; Evidence={ECO:0000269|PubMed:19965576};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52125;
CC         Evidence={ECO:0000305|PubMed:19965576};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein
CC         reductase] = all-trans-4-hydroxyretinoate + H(+) + H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51984, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:35291,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:134178;
CC         Evidence={ECO:0000269|PubMed:11093772};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51985;
CC         Evidence={ECO:0000305|PubMed:11093772};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]
CC         = 16alpha,17beta-estriol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:47332, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16469, ChEBI:CHEBI:27974, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:14559847};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47333;
CC         Evidence={ECO:0000305|PubMed:14559847};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] =
CC         16alpha-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:47204, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:776, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:14559847};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47205;
CC         Evidence={ECO:0000305|PubMed:14559847};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=50 uM for all-trans-retinoate (4-hydroxylation)
CC         {ECO:0000269|PubMed:11093772};
CC         KM=5.4 uM for (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate (epoxygenation)
CC         {ECO:0000269|PubMed:15766564};
CC         KM=6 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoate (epoxygenation)
CC         {ECO:0000269|PubMed:15766564};
CC         KM=7.18 uM for paclitaxel {ECO:0000269|PubMed:26427316};
CC         KM=1.35 uM for amodiaquine {ECO:0000269|PubMed:26427316};
CC         Vmax=1211 pmol/min/nmol enzyme toward all-trans-retinoate (4-
CC         hydroxylation) {ECO:0000269|PubMed:11093772};
CC         Vmax=6.2 nmol/min/nmol enzyme toward (5Z,8Z,11Z,14Z,17Z)-
CC         eicosapentaenoate (epoxygenation) {ECO:0000269|PubMed:15766564};
CC         Vmax=4.6 nmol/min/nmol enzyme toward (5Z,8Z,11Z,14Z)-
CC         eicosatetraenoate (epoxygenation) {ECO:0000269|PubMed:15766564};
CC         Vmax=2.18 pmol/min/pmol enzyme toward paclitaxel
CC         {ECO:0000269|PubMed:26427316};
CC         Vmax=11.30 pmol/min/pmol enzyme toward amodiaquine
CC         {ECO:0000269|PubMed:26427316};
CC   -!- PATHWAY: Steroid metabolism. {ECO:0000269|PubMed:14559847}.
CC   -!- PATHWAY: Lipid metabolism; arachidonate metabolism.
CC       {ECO:0000269|PubMed:15766564, ECO:0000269|PubMed:19965576,
CC       ECO:0000269|PubMed:7574697}.
CC   -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC       {ECO:0000269|PubMed:11093772}.
CC   -!- INTERACTION:
CC       P10632; P13473-2: LAMP2; NbExp=3; IntAct=EBI-2951522, EBI-21591415;
CC       P10632; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-2951522, EBI-5280197;
CC       P10632; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-2951522, EBI-2623095;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P10632-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P10632-2; Sequence=VSP_043306, VSP_043307;
CC   -!- INDUCTION: By phenobarbital.
CC   -!- POLYMORPHISM: Several alleles are found in the human population,
CC       contributing to interindividual variations in the therapeutic efficacy
CC       and toxicity of a myriad of drugs such as paclitaxel or amodiaquine.
CC       The allele shown here is CYP2C8*1 (PubMed:26427316). CYP2C8 genetic
CC       variations are associated with altered drug metabolism and adverse drug
CC       effects including acute rhabdomyolysis after cerivastatin use
CC       [MIM:618018]. {ECO:0000269|PubMed:15365880,
CC       ECO:0000269|PubMed:26427316}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- CAUTION: Alternative splicing has been shown to occur but the shorter
CC       forms are believed to be non-functional. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Cytochrome P450 Allele Nomenclature Committee;
CC       Note=CYP2C8 alleles;
CC       URL="http://www.cypalleles.ki.se/cyp2c8.htm";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/cyp2c8/";
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DR   EMBL; M17397; AAA35739.1; -; mRNA.
DR   EMBL; M17398; AAA35740.1; -; mRNA.
DR   EMBL; Y00498; CAA68550.1; -; mRNA.
DR   EMBL; AK292753; BAF85442.1; -; mRNA.
DR   EMBL; AK293328; BAH11492.1; -; mRNA.
DR   EMBL; AK315823; BAF98714.1; -; mRNA.
DR   EMBL; AY514490; AAR89907.1; -; Genomic_DNA.
DR   EMBL; AL359672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471066; EAW50018.1; -; Genomic_DNA.
DR   EMBL; BC020596; AAH20596.1; -; mRNA.
DR   EMBL; X54807; CAA38578.1; -; Genomic_DNA.
DR   EMBL; M21941; AAA52160.1; -; mRNA.
DR   EMBL; M21942; AAA52161.1; -; mRNA.
DR   EMBL; X51535; CAA35915.1; -; mRNA.
DR   CCDS; CCDS55721.1; -. [P10632-2]
DR   CCDS; CCDS7438.1; -. [P10632-1]
DR   PIR; A29782; A29782.
DR   RefSeq; NP_000761.3; NM_000770.3. [P10632-1]
DR   RefSeq; NP_001185782.1; NM_001198853.1.
DR   RefSeq; NP_001185783.1; NM_001198854.1. [P10632-2]
DR   RefSeq; NP_001185784.1; NM_001198855.1.
DR   PDB; 1PQ2; X-ray; 2.70 A; A/B=19-490.
DR   PDB; 2NNH; X-ray; 2.60 A; A/B=28-490.
DR   PDB; 2NNI; X-ray; 2.80 A; A=28-490.
DR   PDB; 2NNJ; X-ray; 2.28 A; A=28-490.
DR   PDB; 2VN0; X-ray; 2.70 A; A=28-490.
DR   PDBsum; 1PQ2; -.
DR   PDBsum; 2NNH; -.
DR   PDBsum; 2NNI; -.
DR   PDBsum; 2NNJ; -.
DR   PDBsum; 2VN0; -.
DR   SMR; P10632; -.
DR   BioGRID; 107936; 15.
DR   IntAct; P10632; 13.
DR   STRING; 9606.ENSP00000360317; -.
DR   BindingDB; P10632; -.
DR   ChEMBL; CHEMBL3721; -.
DR   DrugBank; DB08607; (5R)-5-(4-{[(2R)-6-HYDROXY-2,5,7,8-TETRAMETHYL-3,4-DIHYDRO-2H-CHROMEN-2-YL]METHOXY}BENZYL)-1,3-THIAZOLIDINE-2,4-DIONE.
DR   DrugBank; DB08496; (R)-warfarin.
DR   DrugBank; DB14055; (S)-Warfarin.
DR   DrugBank; DB12001; Abemaciclib.
DR   DrugBank; DB05812; Abiraterone.
DR   DrugBank; DB00918; Almotriptan.
DR   DrugBank; DB12015; Alpelisib.
DR   DrugBank; DB01424; Aminophenazone.
DR   DrugBank; DB01118; Amiodarone.
DR   DrugBank; DB00321; Amitriptyline.
DR   DrugBank; DB00381; Amlodipine.
DR   DrugBank; DB00613; Amodiaquine.
DR   DrugBank; DB01060; Amoxicillin.
DR   DrugBank; DB01217; Anastrozole.
DR   DrugBank; DB01435; Antipyrine.
DR   DrugBank; DB11901; Apalutamide.
DR   DrugBank; DB06605; Apixaban.
DR   DrugBank; DB00714; Apomorphine.
DR   DrugBank; DB01072; Atazanavir.
DR   DrugBank; DB01076; Atorvastatin.
DR   DrugBank; DB11995; Avatrombopag.
DR   DrugBank; DB00972; Azelastine.
DR   DrugBank; DB12781; Balaglitazone.
DR   DrugBank; DB05015; Belinostat.
DR   DrugBank; DB06770; Benzyl alcohol.
DR   DrugBank; DB05229; Beraprost.
DR   DrugBank; DB00443; Betamethasone.
DR   DrugBank; DB00307; Bexarotene.
DR   DrugBank; DB01393; Bezafibrate.
DR   DrugBank; DB13746; Bioallethrin.
DR   DrugBank; DB06616; Bosutinib.
DR   DrugBank; DB12267; Brigatinib.
DR   DrugBank; DB01222; Budesonide.
DR   DrugBank; DB00921; Buprenorphine.
DR   DrugBank; DB06772; Cabazitaxel.
DR   DrugBank; DB08875; Cabozantinib.
DR   DrugBank; DB00201; Caffeine.
DR   DrugBank; DB13919; Candesartan.
DR   DrugBank; DB00796; Candesartan cilexetil.
DR   DrugBank; DB08502; Capravirine.
DR   DrugBank; DB00564; Carbamazepine.
DR   DrugBank; DB00482; Celecoxib.
DR   DrugBank; DB06119; Cenobamate.
DR   DrugBank; DB00439; Cerivastatin.
DR   DrugBank; DB00608; Chloroquine.
DR   DrugBank; DB00169; Cholecalciferol.
DR   DrugBank; DB09201; Ciglitazone.
DR   DrugBank; DB00501; Cimetidine.
DR   DrugBank; DB00604; Cisapride.
DR   DrugBank; DB12499; Clascoterone.
DR   DrugBank; DB00845; Clofazimine.
DR   DrugBank; DB00758; Clopidogrel.
DR   DrugBank; DB00257; Clotrimazole.
DR   DrugBank; DB00363; Clozapine.
DR   DrugBank; DB00907; Cocaine.
DR   DrugBank; DB01394; Colchicine.
DR   DrugBank; DB05219; Crisaborole.
DR   DrugBank; DB00531; Cyclophosphamide.
DR   DrugBank; DB08912; Dabrafenib.
DR   DrugBank; DB00250; Dapsone.
DR   DrugBank; DB09183; Dasabuvir.
DR   DrugBank; DB01609; Deferasirox.
DR   DrugBank; DB01234; Dexamethasone.
DR   DrugBank; DB14649; Dexamethasone acetate.
DR   DrugBank; DB09213; Dexibuprofen.
DR   DrugBank; DB00829; Diazepam.
DR   DrugBank; DB00586; Diclofenac.
DR   DrugBank; DB00255; Diethylstilbestrol.
DR   DrugBank; DB00343; Diltiazem.
DR   DrugBank; DB01184; Domperidone.
DR   DrugBank; DB00625; Efavirenz.
DR   DrugBank; DB11979; Elagolix.
DR   DrugBank; DB15444; Elexacaftor.
DR   DrugBank; DB06210; Eltrombopag.
DR   DrugBank; DB13874; Enasidenib.
DR   DrugBank; DB08899; Enzalutamide.
DR   DrugBank; DB00530; Erlotinib.
DR   DrugBank; DB00783; Estradiol.
DR   DrugBank; DB13952; Estradiol acetate.
DR   DrugBank; DB13953; Estradiol benzoate.
DR   DrugBank; DB13954; Estradiol cypionate.
DR   DrugBank; DB13955; Estradiol dienanthate.
DR   DrugBank; DB13956; Estradiol valerate.
DR   DrugBank; DB00402; Eszopiclone.
DR   DrugBank; DB00977; Ethinylestradiol.
DR   DrugBank; DB00973; Ezetimibe.
DR   DrugBank; DB12466; Favipiravir.
DR   DrugBank; DB01023; Felodipine.
DR   DrugBank; DB01039; Fenofibrate.
DR   DrugBank; DB00544; Fluorouracil.
DR   DrugBank; DB13867; Fluticasone.
DR   DrugBank; DB08906; Fluticasone furoate.
DR   DrugBank; DB00588; Fluticasone propionate.
DR   DrugBank; DB01095; Fluvastatin.
DR   DrugBank; DB01241; Gemfibrozil.
DR   DrugBank; DB01645; Genistein.
DR   DrugBank; DB11978; Glasdegib.
DR   DrugBank; DB01218; Halofantrine.
DR   DrugBank; DB00741; Hydrocortisone.
DR   DrugBank; DB14538; Hydrocortisone aceponate.
DR   DrugBank; DB14539; Hydrocortisone acetate.
DR   DrugBank; DB14540; Hydrocortisone butyrate.
DR   DrugBank; DB14541; Hydrocortisone cypionate.
DR   DrugBank; DB14542; Hydrocortisone phosphate.
DR   DrugBank; DB14543; Hydrocortisone probutate.
DR   DrugBank; DB14545; Hydrocortisone succinate.
DR   DrugBank; DB14544; Hydrocortisone valerate.
DR   DrugBank; DB01611; Hydroxychloroquine.
DR   DrugBank; DB01050; Ibuprofen.
DR   DrugBank; DB09054; Idelalisib.
DR   DrugBank; DB01181; Ifosfamide.
DR   DrugBank; DB00619; Imatinib.
DR   DrugBank; DB01029; Irbesartan.
DR   DrugBank; DB11633; Isavuconazole.
DR   DrugBank; DB00951; Isoniazid.
DR   DrugBank; DB11757; Istradefylline.
DR   DrugBank; DB14568; Ivosidenib.
DR   DrugBank; DB09570; Ixazomib.
DR   DrugBank; DB01221; Ketamine.
DR   DrugBank; DB06738; Ketobemidone.
DR   DrugBank; DB01026; Ketoconazole.
DR   DrugBank; DB01009; Ketoprofen.
DR   DrugBank; DB00465; Ketorolac.
DR   DrugBank; DB00448; Lansoprazole.
DR   DrugBank; DB01259; Lapatinib.
DR   DrugBank; DB09078; Lenvatinib.
DR   DrugBank; DB12070; Letermovir.
DR   DrugBank; DB08918; Levomilnacipran.
DR   DrugBank; DB00451; Levothyroxine.
DR   DrugBank; DB04725; Licofelone.
DR   DrugBank; DB00281; Lidocaine.
DR   DrugBank; DB01583; Liotrix.
DR   DrugBank; DB09198; Lobeglitazone.
DR   DrugBank; DB06448; Lonafarnib.
DR   DrugBank; DB00836; Loperamide.
DR   DrugBank; DB00455; Loratadine.
DR   DrugBank; DB12130; Lorlatinib.
DR   DrugBank; DB00678; Losartan.
DR   DrugBank; DB00227; Lovastatin.
DR   DrugBank; DB09280; Lumacaftor.
DR   DrugBank; DB15935; Lumasiran.
DR   DrugBank; DB06077; Lumateperone.
DR   DrugBank; DB00603; Medroxyprogesterone acetate.
DR   DrugBank; DB00784; Mefenamic acid.
DR   DrugBank; DB00814; Meloxicam.
DR   DrugBank; DB00532; Mephenytoin.
DR   DrugBank; DB01357; Mestranol.
DR   DrugBank; DB00333; Methadone.
DR   DrugBank; DB09241; Methylene blue.
DR   DrugBank; DB00959; Methylprednisolone.
DR   DrugBank; DB00916; Metronidazole.
DR   DrugBank; DB01110; Miconazole.
DR   DrugBank; DB06595; Midostaurin.
DR   DrugBank; DB00834; Mifepristone.
DR   DrugBank; DB00764; Mometasone.
DR   DrugBank; DB14512; Mometasone furoate.
DR   DrugBank; DB00471; Montelukast.
DR   DrugBank; DB00295; Morphine.
DR   DrugBank; DB06510; Muraglitazar.
DR   DrugBank; DB00688; Mycophenolate mofetil.
DR   DrugBank; DB00486; Nabilone.
DR   DrugBank; DB00788; Naproxen.
DR   DrugBank; DB09199; Netoglitazone.
DR   DrugBank; DB00622; Nicardipine.
DR   DrugBank; DB00184; Nicotine.
DR   DrugBank; DB01115; Nifedipine.
DR   DrugBank; DB04868; Nilotinib.
DR   DrugBank; DB06712; Nilvadipine.
DR   DrugBank; DB06670; Odanacatib.
DR   DrugBank; DB09080; Olodaterol.
DR   DrugBank; DB09296; Ombitasvir.
DR   DrugBank; DB00338; Omeprazole.
DR   DrugBank; DB11632; Opicapone.
DR   DrugBank; DB01062; Oxybutynin.
DR   DrugBank; DB12612; Ozanimod.
DR   DrugBank; DB01229; Paclitaxel.
DR   DrugBank; DB03796; Palmitic Acid.
DR   DrugBank; DB00617; Paramethadione.
DR   DrugBank; DB06589; Pazopanib.
DR   DrugBank; DB08922; Perospirone.
DR   DrugBank; DB00850; Perphenazine.
DR   DrugBank; DB00780; Phenelzine.
DR   DrugBank; DB01174; Phenobarbital.
DR   DrugBank; DB00946; Phenprocoumon.
DR   DrugBank; DB00252; Phenytoin.
DR   DrugBank; DB01132; Pioglitazone.
DR   DrugBank; DB00554; Piroxicam.
DR   DrugBank; DB08860; Pitavastatin.
DR   DrugBank; DB08901; Ponatinib.
DR   DrugBank; DB15822; Pralsetinib.
DR   DrugBank; DB14631; Prednisolone phosphate.
DR   DrugBank; DB00635; Prednisone.
DR   DrugBank; DB01032; Probenecid.
DR   DrugBank; DB00818; Propofol.
DR   DrugBank; DB00205; Pyrimethamine.
DR   DrugBank; DB04216; Quercetin.
DR   DrugBank; DB00908; Quinidine.
DR   DrugBank; DB00468; Quinine.
DR   DrugBank; DB01129; Rabeprazole.
DR   DrugBank; DB00481; Raloxifene.
DR   DrugBank; DB08896; Regorafenib.
DR   DrugBank; DB11853; Relugolix.
DR   DrugBank; DB14761; Remdesivir.
DR   DrugBank; DB00912; Repaglinide.
DR   DrugBank; DB00615; Rifabutin.
DR   DrugBank; DB01045; Rifampicin.
DR   DrugBank; DB11753; Rifamycin.
DR   DrugBank; DB01201; Rifapentine.
DR   DrugBank; DB01220; Rifaximin.
DR   DrugBank; DB08931; Riociguat.
DR   DrugBank; DB14840; Ripretinib.
DR   DrugBank; DB00503; Ritonavir.
DR   DrugBank; DB09200; Rivoglitazone.
DR   DrugBank; DB00533; Rofecoxib.
DR   DrugBank; DB00412; Rosiglitazone.
DR   DrugBank; DB12332; Rucaparib.
DR   DrugBank; DB00938; Salmeterol.
DR   DrugBank; DB01232; Saquinavir.
DR   DrugBank; DB00418; Secobarbital.
DR   DrugBank; DB01037; Selegiline.
DR   DrugBank; DB11362; Selexipag.
DR   DrugBank; DB15685; Selpercatinib.
DR   DrugBank; DB11689; Selumetinib.
DR   DrugBank; DB06739; Seratrodast.
DR   DrugBank; DB00641; Simvastatin.
DR   DrugBank; DB01261; Sitagliptin.
DR   DrugBank; DB00398; Sorafenib.
DR   DrugBank; DB00421; Spironolactone.
DR   DrugBank; DB00359; Sulfadiazine.
DR   DrugBank; DB06729; Sulfaphenazole.
DR   DrugBank; DB01138; Sulfinpyrazone.
DR   DrugBank; DB00675; Tamoxifen.
DR   DrugBank; DB00799; Tazarotene.
DR   DrugBank; DB09256; Tegafur.
DR   DrugBank; DB01079; Tegaserod.
DR   DrugBank; DB00857; Terbinafine.
DR   DrugBank; DB00342; Terfenadine.
DR   DrugBank; DB08880; Teriflunomide.
DR   DrugBank; DB00624; Testosterone.
DR   DrugBank; DB13943; Testosterone cypionate.
DR   DrugBank; DB13944; Testosterone enanthate.
DR   DrugBank; DB13946; Testosterone undecanoate.
DR   DrugBank; DB00208; Ticlopidine.
DR   DrugBank; DB06137; Tirbanibulin.
DR   DrugBank; DB01124; Tolbutamide.
DR   DrugBank; DB01685; Topiroxostat.
DR   DrugBank; DB00214; Torasemide.
DR   DrugBank; DB08911; Trametinib.
DR   DrugBank; DB00755; Tretinoin.
DR   DrugBank; DB00897; Triazolam.
DR   DrugBank; DB12245; Triclabendazole.
DR   DrugBank; DB12808; Trifarotene.
DR   DrugBank; DB00347; Trimethadione.
DR   DrugBank; DB00440; Trimethoprim.
DR   DrugBank; DB00197; Troglitazone.
DR   DrugBank; DB13179; Troleandomycin.
DR   DrugBank; DB11652; Tucatinib.
DR   DrugBank; DB15328; Ubrogepant.
DR   DrugBank; DB11613; Velpatasvir.
DR   DrugBank; DB08881; Vemurafenib.
DR   DrugBank; DB00661; Verapamil.
DR   DrugBank; DB08828; Vismodegib.
DR   DrugBank; DB09068; Vortioxetine.
DR   DrugBank; DB12026; Voxilaprevir.
DR   DrugBank; DB00682; Warfarin.
DR   DrugBank; DB00549; Zafirlukast.
DR   DrugBank; DB01198; Zopiclone.
DR   DrugCentral; P10632; -.
DR   GuidetoPHARMACOLOGY; 1325; -.
DR   SwissLipids; SLP:000001548; -.
DR   SwissLipids; SLP:000001616; -. [P10632-1]
DR   iPTMnet; P10632; -.
DR   PhosphoSitePlus; P10632; -.
DR   BioMuta; CYP2C8; -.
DR   DMDM; 117225; -.
DR   MassIVE; P10632; -.
DR   PaxDb; P10632; -.
DR   PeptideAtlas; P10632; -.
DR   PRIDE; P10632; -.
DR   ProteomicsDB; 52621; -. [P10632-1]
DR   ProteomicsDB; 52622; -. [P10632-2]
DR   Antibodypedia; 3013; 218 antibodies.
DR   DNASU; 1558; -.
DR   Ensembl; ENST00000371270; ENSP00000360317; ENSG00000138115. [P10632-1]
DR   Ensembl; ENST00000535898; ENSP00000445062; ENSG00000138115. [P10632-2]
DR   GeneID; 1558; -.
DR   KEGG; hsa:1558; -.
DR   UCSC; uc001kkb.4; human. [P10632-1]
DR   CTD; 1558; -.
DR   DisGeNET; 1558; -.
DR   GeneCards; CYP2C8; -.
DR   HGNC; HGNC:2622; CYP2C8.
DR   HPA; ENSG00000138115; Tissue enriched (liver).
DR   MalaCards; CYP2C8; -.
DR   MIM; 601129; gene.
DR   MIM; 618018; phenotype.
DR   neXtProt; NX_P10632; -.
DR   OpenTargets; ENSG00000138115; -.
DR   Orphanet; 529828; Enzalutamide toxicity.
DR   PharmGKB; PA125; -.
DR   VEuPathDB; HostDB:ENSG00000138115; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   GeneTree; ENSGT00940000163696; -.
DR   HOGENOM; CLU_001570_22_2_1; -.
DR   InParanoid; P10632; -.
DR   OMA; FVPLSWA; -.
DR   OrthoDB; 702827at2759; -.
DR   PhylomeDB; P10632; -.
DR   TreeFam; TF352043; -.
DR   BRENDA; 1.14.14.1; 2681.
DR   PathwayCommons; P10632; -.
DR   Reactome; R-HSA-211981; Xenobiotics.
DR   Reactome; R-HSA-211999; CYP2E1 reactions.
DR   Reactome; R-HSA-2142670; Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
DR   Reactome; R-HSA-2142816; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
DR   Reactome; R-HSA-9027307; Biosynthesis of maresin-like SPMs.
DR   SABIO-RK; P10632; -.
DR   UniPathway; UPA00383; -.
DR   UniPathway; UPA00912; -.
DR   BioGRID-ORCS; 1558; 7 hits in 1006 CRISPR screens.
DR   ChiTaRS; CYP2C8; human.
DR   EvolutionaryTrace; P10632; -.
DR   GeneWiki; CYP2C8; -.
DR   GenomeRNAi; 1558; -.
DR   Pharos; P10632; Tchem.
DR   PRO; PR:P10632; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; P10632; protein.
DR   Bgee; ENSG00000138115; Expressed in liver and 134 other tissues.
DR   ExpressionAtlas; P10632; baseline and differential.
DR   Genevisible; P10632; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0008392; F:arachidonic acid epoxygenase activity; IDA:UniProtKB.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034875; F:caffeine oxidase activity; IDA:BHF-UCL.
DR   GO; GO:0101020; F:estrogen 16-alpha-hydroxylase activity; IDA:BHF-UCL.
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:0008401; F:retinoic acid 4-hydroxylase activity; IDA:UniProtKB.
DR   GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR   GO; GO:0017144; P:drug metabolic process; IDA:BHF-UCL.
DR   GO; GO:0019373; P:epoxygenase P450 pathway; IDA:UniProtKB.
DR   GO; GO:0008210; P:estrogen metabolic process; IDA:UniProtKB.
DR   GO; GO:0042738; P:exogenous drug catabolic process; IDA:BHF-UCL.
DR   GO; GO:0046456; P:icosanoid biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0002933; P:lipid hydroxylation; IDA:BHF-UCL.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; TAS:Reactome.
DR   GO; GO:0097267; P:omega-hydroxylase P450 pathway; TAS:Reactome.
DR   GO; GO:0006082; P:organic acid metabolic process; IDA:BHF-UCL.
DR   GO; GO:0070989; P:oxidative demethylation; IDA:BHF-UCL.
DR   GO; GO:0042573; P:retinoic acid metabolic process; IDA:UniProtKB.
DR   GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008202; P:steroid metabolic process; IDA:BHF-UCL.
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   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing;
KW   Endoplasmic reticulum; Heme; Iron; Lipid metabolism; Membrane;
KW   Metal-binding; Microsome; Monooxygenase; Oxidoreductase; Phosphoprotein;
KW   Reference proteome; Steroid metabolism.
FT   CHAIN           1..490
FT                   /note="Cytochrome P450 2C8"
FT                   /id="PRO_0000051699"
FT   METAL           435
FT                   /note="Iron (heme axial ligand)"
FT   BINDING         100
FT                   /note="Substrate"
FT   BINDING         204
FT                   /note="Substrate"
FT   BINDING         241
FT                   /note="Substrate"
FT   MOD_RES         100
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         1..8
FT                   /note="MEPFVVLV -> MFLQPIAK (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_043306"
FT   VAR_SEQ         9..110
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_043307"
FT   VARIANT         139
FT                   /note="R -> K (in allele CYP2C8*3; reduces enzymatic
FT                   activity with paclitaxel as substrate; decreases intrinsic
FT                   clearance of paclitaxel; reduces enzymatic activity with
FT                   amodiaquine as substrate; dbSNP:rs11572080)"
FT                   /evidence="ECO:0000269|PubMed:11668219,
FT                   ECO:0000269|PubMed:12429347, ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15469410, ECO:0000269|PubMed:26427316,
FT                   ECO:0000269|PubMed:2729895, ECO:0000269|Ref.5"
FT                   /id="VAR_012238"
FT   VARIANT         154
FT                   /note="E -> D"
FT                   /evidence="ECO:0000269|PubMed:3196692"
FT                   /id="VAR_001250"
FT   VARIANT         171
FT                   /note="G -> S (in allele CYP2C8*6; no effect on affinity or
FT                   enzymatic activity with paclitaxel as substrate; decreases
FT                   affinity for amodiaquine; reduces enzymatic activity with
FT                   amodiaquine as substrate; decreases intrinsic clearance of
FT                   amodiaquine; dbSNP:rs142886225)"
FT                   /evidence="ECO:0000269|PubMed:26427316"
FT                   /id="VAR_075541"
FT   VARIANT         186
FT                   /note="R -> G (in allele CYP2C8*8; increases affinity for
FT                   paclitaxel; reduces enzymatic activity with paclitaxel as
FT                   substrate; decreases intrinsic clearance of paclitaxel;
FT                   reduces enzymatic activity with amodiaquine as substrate;
FT                   decreases intrinsic clearance of amodiaquine;
FT                   dbSNP:rs72558195)"
FT                   /evidence="ECO:0000269|PubMed:26427316"
FT                   /id="VAR_075542"
FT   VARIANT         193
FT                   /note="N -> K"
FT                   /evidence="ECO:0000269|PubMed:3196692"
FT                   /id="VAR_001251"
FT   VARIANT         223
FT                   /note="I -> M (in allele CYP2C8*13; reduces enzymatic
FT                   activity with paclitaxel as substrate; decreases intrinsic
FT                   clearance of paclitaxel; reduces enzymatic activity with
FT                   amodiaquine as substrate; decreases intrinsic clearance of
FT                   amodiaquine)"
FT                   /evidence="ECO:0000269|PubMed:26427316"
FT                   /id="VAR_075543"
FT   VARIANT         238
FT                   /note="A -> P (in allele CYP2C8*14; reduces enzymatic
FT                   activity with paclitaxel as substrate; decreases intrinsic
FT                   clearance of paclitaxel; dbSNP:rs188934928)"
FT                   /evidence="ECO:0000269|PubMed:26427316"
FT                   /id="VAR_075544"
FT   VARIANT         244
FT                   /note="I -> V (in dbSNP:rs11572102)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_018958"
FT   VARIANT         247
FT                   /note="K -> R (in allele CYP2C8*9; increases enzymatic
FT                   activity with paclitaxel as substrate; reduces enzymatic
FT                   activity with amodiaquine as substrate; decreases intrinsic
FT                   clearance of amodiaquine; dbSNP:rs769460274)"
FT                   /evidence="ECO:0000269|PubMed:26427316"
FT                   /id="VAR_075545"
FT   VARIANT         249
FT                   /note="K -> R"
FT                   /evidence="ECO:0000269|PubMed:3196692"
FT                   /id="VAR_001252"
FT   VARIANT         264
FT                   /note="I -> M (in allele CYP2C8*4; reduces enzymatic
FT                   activity with paclitaxel as substrate; decreases affinity
FT                   for amodiaquine; dbSNP:rs1058930)"
FT                   /evidence="ECO:0000269|PubMed:12429347,
FT                   ECO:0000269|PubMed:15469410, ECO:0000269|PubMed:2009263,
FT                   ECO:0000269|PubMed:26427316, ECO:0000269|PubMed:3500169,
FT                   ECO:0000269|Ref.5"
FT                   /id="VAR_011754"
FT   VARIANT         269
FT                   /note="I -> F (in allele CYP2C8*2; only found in African-
FT                   Americans; increases intrinsic clearance of paclitaxel;
FT                   decreases affinity for amodiaquine; increases enzymatic
FT                   activity with amodiaquine as substrate; dbSNP:rs11572103)"
FT                   /evidence="ECO:0000269|PubMed:11668219,
FT                   ECO:0000269|PubMed:12429347, ECO:0000269|PubMed:15469410,
FT                   ECO:0000269|PubMed:26427316, ECO:0000269|Ref.5"
FT                   /id="VAR_012239"
FT   VARIANT         383
FT                   /note="K -> N (in allele CYP2C8*10; reduces enzymatic
FT                   activity with paclitaxel as substrate; reduces enzymatic
FT                   activity with amodiaquine as substrate; decreases intrinsic
FT                   clearance of amodiaquine)"
FT                   /evidence="ECO:0000269|PubMed:26427316"
FT                   /id="VAR_075546"
FT   VARIANT         390
FT                   /note="L -> S (in dbSNP:rs72558194)"
FT                   /evidence="ECO:0000269|PubMed:12429347"
FT                   /id="VAR_016947"
FT   VARIANT         399
FT                   /note="K -> R (in allele CYP2C8*3; reduces enzymatic
FT                   activity with paclitaxel as substrate; decreases intrinsic
FT                   clearance of paclitaxel; reduces enzymatic activity with
FT                   amodiaquine as substrate; dbSNP:rs10509681)"
FT                   /evidence="ECO:0000269|PubMed:11668219,
FT                   ECO:0000269|PubMed:12429347, ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15469410, ECO:0000269|PubMed:2216732,
FT                   ECO:0000269|PubMed:26427316, ECO:0000269|Ref.5"
FT                   /id="VAR_012240"
FT   VARIANT         411
FT                   /note="H -> L"
FT                   /evidence="ECO:0000269|PubMed:3196692,
FT                   ECO:0000269|PubMed:7574697"
FT                   /id="VAR_001253"
FT   VARIANT         461
FT                   /note="Missing (in allele CYP2C8*12; increases enzymatic
FT                   activity with paclitaxel as substrate; reduces enzymatic
FT                   activity with amodiaquine as substrate; decreases intrinsic
FT                   clearance of amodiaquine)"
FT                   /evidence="ECO:0000269|PubMed:26427316"
FT                   /id="VAR_075547"
FT   CONFLICT        54
FT                   /note="F -> L (in Ref. 12; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        67
FT                   /note="V -> L (in Ref. 12; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        76
FT                   /note="V -> C (in Ref. 12; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        82
FT                   /note="A -> S (in Ref. 8; AAH20596)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130
FT                   /note="T -> N (in Ref. 1; AAA35739/AAA35740 and 3; no
FT                   nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        209
FT                   /note="N -> S (in Ref. 12; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        384..393
FT                   /note="GTTIMALLTS -> SFDNKIMLAA (in Ref. 1; AAA35740)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        386
FT                   /note="T -> A (in Ref. 4; BAF85442)"
FT                   /evidence="ECO:0000305"
FT   TURN            37..39
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:1PQ2"
FT   HELIX           50..61
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   STRAND          63..69
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   STRAND          72..77
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   HELIX           80..87
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   TURN            88..94
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   HELIX           101..107
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   TURN            111..113
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   HELIX           117..130
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   TURN            133..136
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   STRAND          137..139
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   HELIX           141..157
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   TURN            158..161
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   HELIX           167..182
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   STRAND          183..185
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   HELIX           192..208
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   HELIX           212..218
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   HELIX           220..225
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   HELIX           227..252
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   HELIX           263..273
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   HELIX           284..298
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   HELIX           300..315
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   HELIX           317..330
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   STRAND          333..335
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   HELIX           339..344
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   HELIX           346..359
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   STRAND          374..376
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   STRAND          379..381
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   STRAND          386..389
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   HELIX           391..395
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   TURN            398..400
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   STRAND          401..403
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   HELIX           409..412
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   HELIX           431..433
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   HELIX           438..455
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   STRAND          456..459
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   HELIX           464..466
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   STRAND          472..479
FT                   /evidence="ECO:0007829|PDB:2NNJ"
FT   STRAND          485..489
FT                   /evidence="ECO:0007829|PDB:2NNJ"
SQ   SEQUENCE   490 AA;  55825 MW;  E920EB2084F477E1 CRC64;
     MEPFVVLVLC LSFMLLFSLW RQSCRRRKLP PGPTPLPIIG NMLQIDVKDI CKSFTNFSKV
     YGPVFTVYFG MNPIVVFHGY EAVKEALIDN GEEFSGRGNS PISQRITKGL GIISSNGKRW
     KEIRRFSLTT LRNFGMGKRS IEDRVQEEAH CLVEELRKTK ASPCDPTFIL GCAPCNVICS
     VVFQKRFDYK DQNFLTLMKR FNENFRILNS PWIQVCNNFP LLIDCFPGTH NKVLKNVALT
     RSYIREKVKE HQASLDVNNP RDFIDCFLIK MEQEKDNQKS EFNIENLVGT VADLFVAGTE
     TTSTTLRYGL LLLLKHPEVT AKVQEEIDHV IGRHRSPCMQ DRSHMPYTDA VVHEIQRYSD
     LVPTGVPHAV TTDTKFRNYL IPKGTTIMAL LTSVLHDDKE FPNPNIFDPG HFLDKNGNFK
     KSDYFMPFSA GKRICAGEGL ARMELFLFLT TILQNFNLKS VDDLKNLNTT AVTKGIVSLP
     PSYQICFIPV
//
DBGET integrated database retrieval system