ID   CP4FE_MOUSE             Reviewed;         524 AA.
AC   Q9EP75; Q52L93;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   04-NOV-2008, entry version 52.
DE   RecName: Full=Cytochrome P450 4F14;
DE            EC=1.14.13.30;
DE   AltName: Full=Leukotriene-B4 omega-hydroxylase;
DE   AltName: Full=Leukotriene-B4 20-monooxygenase;
DE   AltName: Full=Cytochrome P450-LTB-omega;
DE   AltName: Full=Cyp4f-14;
GN   Name=Cyp4f14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Liver;
RA   Kikuta Y., Kasyu H., Kusunose E., Kusunose M.;
RT   "Mouse liver leukotriene B4 omega-hydroxylase.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/Sv; TISSUE=Brain;
RA   Antonovic L., Kawashima H., Strobel H.;
RT   "Protein expression and catalytic activity assessment of mouse 4F
RT   clones.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cecum, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate
CC       monooxygenases. This enzyme requires molecular oxygen and NADPH
CC       for the omega-hydroxylation of LTB4 (By similarity).
CC   -!- CATALYTIC ACTIVITY: (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-
CC       6,8,10,14-tetraenoate + NADPH + O(2) = (6Z,8E,10E,14Z)-(5S,12R)-
CC       5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + NADP(+) + H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- PATHWAY: Lipid metabolism; leukotriene B4 degradation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein (By similarity). Microsome membrane; Peripheral
CC       membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; AB037541; BAB12564.1; -; mRNA.
DR   EMBL; AB037540; BAB12563.1; -; mRNA.
DR   EMBL; AF233644; AAK15010.1; -; mRNA.
DR   EMBL; AK005007; BAB23740.1; -; mRNA.
DR   EMBL; AK018676; BAB31338.1; -; mRNA.
DR   EMBL; BC011228; AAH11228.1; -; mRNA.
DR   EMBL; BC094016; AAH94016.1; -; mRNA.
DR   RefSeq; NP_071879.1; -.
DR   UniGene; Mm.426027; -.
DR   Ensembl; ENSMUSG00000024292; Mus musculus.
DR   GeneID; 64385; -.
DR   KEGG; mmu:64385; -.
DR   MGI; MGI:1927669; Cyp4f14.
DR   HOGENOM; Q9EP75; -.
DR   HOVERGEN; Q9EP75; -.
DR   NextBio; 320067; -.
DR   ArrayExpress; Q9EP75; -.
DR   GermOnline; ENSMUSG00000024292; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005792; C:microsome; IEA:UniProtKB-KW.
DR   GO; GO:0050051; F:leukotriene-B4 20-monooxygenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1.
DR   PANTHER; PTHR19383; Cyt_P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; NADP; Oxidoreductase.
FT   CHAIN         1    524       Cytochrome P450 4F14.
FT                                /FTId=PRO_0000051858.
FT   METAL       468    468       Iron (heme axial ligand) (By similarity).
FT   BINDING     328    328       Heme (covalent; via 1 link) (By
FT                                similarity).
SQ   SEQUENCE   524 AA;  59800 MW;  A89F80E10925E9F4 CRC64;
     MSQLSLSWLG LGPEVAFPWK TLLLLGASWI LARILIQIYA AYRNYRHLHG FPQPPKRNWL
     MGHVGMVTPT EQGLKELTRL VGTYPQGFLM WIGPMVPVIT LCHSDIVRSI LNASAAVALK
     DVIFYSILKP WLGDGLLVSA GDKWSRHRRM LTPAFHFNIL KPYVKIFNDS TNIMHAKWQR
     LISDGSARLD MFEHVSLMTL DSLQKCVFSF DSNCQEKSSE YIAAILELSA LVAKRHQQPL
     MFMDLLYNLT PDGMRFRKAC NVVHEFTDAV IRERHRTLPD QGLDDFLKSK AKSKTLDFID
     VLLLSKDEDG KELSDEDIRA EADTFMFEGH DTTASGLSWI LYNLARHPEY QERCRQEVQE
     LLRGREPEEI EWDDLAQLPF LTMCIKESLR LHPPVTVISR CCTQDILLPD GRTIPKGIIC
     LISIFGIHHN PSVWPDPEVY DPFRFDPENI KDSSPLAFIP FSAGPRNCIG QTFAMSEMKV
     ALALTLLRFR LLPDDKEPRR QPELILRAEG GLWLRVEPLS AGAH
//