ID   CP4F2_HUMAN    STANDARD;      PRT;   520 AA.
AC   P78329; Q16677; Q6NWT4; Q6NWT6; Q9NNZ0; Q9UIU8;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   16-MAY-2006, entry version 59.
DE   Cytochrome P450 4F2 (EC 1.14.13.30) (CYPIVF2) (Leukotriene-B(4) omega-
DE   hydroxylase) (Leukotriene-B(4) 20-monooxygenase) (Cytochrome P450-LTB-
DE   omega).
GN   Name=CYP4F2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Liver;
RX   MEDLINE=94298958; PubMed=8026587; DOI=10.1016/0014-5793(94)00587-7;
RA   Kikuta Y., Kusunose E., Kondo T., Yamamoto S., Kinoshita H.,
RA   Kusunose M.;
RT   "Cloning and expression of a novel form of leukotriene B4 omega-
RT   hydroxylase from human liver.";
RL   FEBS Lett. 348:70-74(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Liver;
RA   Chen L., Hardwick J.P.;
RT   "The human liver CYP4F2 cDNA sequence and expression in baculovirus-
RT   infected insect cells.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=99420152; PubMed=10492403; DOI=10.1089/104454999315006;
RA   Kikuta Y., Miyauchi Y., Kusunose E., Kusunose M.;
RT   "Expression and molecular cloning of human liver leukotriene B4 omega-
RT   hydroxylase (CYP4F2) gene.";
RL   DNA Cell Biol. 18:723-730(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TYR-7; GLY-12;
RP   VAL-185; MET-433 AND MET-519.
RA   Rieder M.J., Armel T.Z., Carrington D.P., Chung M.-W., Lee K.L.,
RA   Ozuna M., Poel C.L., Toth E.J., Yi Q., Nickerson D.A.;
RT   "SeattleSNPs. NHLBI HL66682 program for genomic applications,
RT   UW-FHCRC, Seattle, WA (URL: http://pga.gs.washington.edu).";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLY-12 AND
RP   MET-433.
RX   MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA   Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA   Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA   Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA   Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA   Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA   Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA   Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA   Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA   Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA   Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA   Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA   Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA   Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA   Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA   Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA   Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA   Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT   "Generation and initial analysis of more than 15,000 full-length human
RT   and mouse cDNA sequences.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN   [7]
RP   NUCLEOTIDE SEQUENCE OF 1-175.
RC   TISSUE=Liver;
RX   MEDLINE=20318331; PubMed=10860554; DOI=10.1006/abbi.2000.1836;
RA   Zhang X., Chen L., Hardwick J.P.;
RT   "Promoter activity and regulation of the CYP4F2 leukotriene B4 omega
RT   hydroxylase gene by peroxisomal proliferators and retinoic acid in
RT   HepG2 cells.";
RL   Arch. Biochem. Biophys. 378:364-376(2000).
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:
CC       (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate
CC       + NADPH + O(2) =
CC       (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-
CC       tetraenoate + NADP(+) + H(2)O.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum; endoplasmic reticulum
CC       membrane; peripheral membrane protein.
CC   -!- TISSUE SPECIFICITY: Liver.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; D26480; BAA05490.1; -; mRNA.
DR   EMBL; U02388; AAC50052.2; -; mRNA.
DR   EMBL; AB015306; BAA75823.1; -; Genomic_DNA.
DR   EMBL; AF467894; AAL67578.1; -; Genomic_DNA.
DR   EMBL; AC005336; AAC27730.1; -; Genomic_DNA.
DR   EMBL; BC067437; AAH67437.1; -; mRNA.
DR   EMBL; BC067439; AAH67439.1; -; mRNA.
DR   EMBL; BC067440; AAH67440.1; -; mRNA.
DR   EMBL; AF221943; AAF86378.1; -; Genomic_DNA.
DR   PIR; S45702; S45702.
DR   UniGene; Hs.558423; -.
DR   HSSP; P14779; 1JME.
DR   Ensembl; ENSG00000186115; Homo sapiens.
DR   HGNC; HGNC:2645; CYP4F2.
DR   MIM; 604426; gene.
DR   LinkHub; P78329; -.
DR   GO; GO:0004497; F:monooxygenase activity; TAS.
DR   GO; GO:0006691; P:leukotriene metabolism; TAS.
DR   InterPro; IPR001128; Cytochrome_P450.
DR   InterPro; IPR002401; EP450I.
DR   PANTHER; PTHR19383; Cytochrome_P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; NADP; Oxidoreductase; Polymorphism.
FT   CHAIN         1    520       Cytochrome P450 4F2.
FT                                /FTId=PRO_0000051850.
FT   METAL       468    468       Iron (heme axial ligand) (By similarity).
FT   BINDING     328    328       Heme (covalent; via 1 link) (By
FT                                similarity).
FT   VARIANT       7      7       S -> Y (in dbSNP:3093104).
FT                                /FTId=VAR_013116.
FT   VARIANT      12     12       W -> G (in dbSNP:3093105).
FT                                /FTId=VAR_013117.
FT   VARIANT     185    185       G -> V (in dbSNP:3093153).
FT                                /FTId=VAR_013118.
FT   VARIANT     269    269       A -> D (in dbSNP:1805040).
FT                                /FTId=VAR_020125.
FT   VARIANT     433    433       V -> M (in dbSNP:2108622).
FT                                /FTId=VAR_013119.
FT   VARIANT     519    519       L -> M (in dbSNP:3093200).
FT                                /FTId=VAR_013120.
FT   CONFLICT     12     13       WP -> CR (in Ref. 2 and 7).
FT   CONFLICT     25     25       V -> A (in Ref. 6; AAH67437).
FT   CONFLICT    169    169       E -> D (in Ref. 6; AAH67440).
FT   CONFLICT    336    336       G -> V (in Ref. 2).
FT   CONFLICT    391    391       L -> V (in Ref. 2).
SQ   SEQUENCE   520 AA;  59853 MW;  1791F9E6EECB59B5 CRC64;
     MSQLSLSWLG LWPVAASPWL LLLLVGASWL LAHVLAWTYA FYDNCRRLRC FPQPPRRNWF
     WGHQGMVNPT EEGMRVLTQL VATYPQGFKV WMGPISPLLS LCHPDIIRSV INASAAIAPK
     DKFFYSFLEP WLGDGLLLSA GDKWSRHRRM LTPAFHFNIL KPYMKIFNES VNIMHAKWQL
     LASEGSACLD MFEHISLMTL DSLQKCVFSF DSHCQEKPSE YIAAILELSA LVSKRHHEIL
     LHIDFLYYLT PDGQRFRRAC RLVHDFTDAV IQERRRTLPS QGVDDFLQAK AKSKTLDFID
     VLLLSKDEDG KKLSDEDIRA EADTFMFEGH DTTASGLSWV LYHLAKHPEY QERCRQEVQE
     LLKDREPKEI EWDDLAHLPF LTMCMKESLR LHPPVPVISR HVTQDIVLPD GRVIPKGIIC
     LISVFGTHHN PAVWPDPEVY DPFRFDPENI KERSPLAFIP FSAGPRNCIG QTFAMAEMKV
     VLALTLLRFR VLPDHTEPRR KPELVLRAEG GLWLRVEPLS
//