ID CP4F3_RAT Reviewed; 524 AA. AC Q3MID2; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2005, sequence version 1. DT 04-NOV-2008, entry version 26. DE RecName: Full=Cytochrome P450 4F3; DE EC=1.14.13.30; DE AltName: Full=CYPIVF3; DE AltName: Full=Leukotriene-B(4) omega-hydroxylase; DE AltName: Full=Leukotriene-B(4) 20-monooxygenase; DE AltName: Full=Cytochrome P450-LTB-omega; GN Name=Cyp4f3; Synonyms=Cyp4f18; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Prostate; 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, a potent chemoattractant for CC polymorphonuclear leukocytes (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 -!- ENZYME REGULATION: Inhibited by carbon monoxide (CO) (By CC similarity). CC -!- PATHWAY: Lipid metabolism; leukotriene B4 degradation. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC membrane protein (By similarity). Microsome membrane; Single-pass CC membrane protein (By similarity). CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC101918; AAI01919.1; -; mRNA. DR RefSeq; NP_001028858.1; -. DR UniGene; Rn.215683; -. DR Ensembl; ENSRNOG00000015751; Rattus norvegicus. DR GeneID; 290623; -. DR KEGG; rno:290623; -. DR RGD; 1305261; Cyp4f18. DR HOVERGEN; Q3MID2; -. DR NextBio; 631306; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. 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; Transmembrane. FT CHAIN 1 524 Cytochrome P450 4F3. FT /FTId=PRO_0000238925. FT TRANSMEM 15 35 Potential. FT METAL 468 468 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 524 AA; 59906 MW; 8DC9033E01F1A1E8 CRC64; MPLLSLSWLG LGHTAASPWL LLLLVGASCL LAYILPQVYA VFENSRRLRR FPQPPPRNWL FGHLGLIQSS EEGLLYIQSL SRTFRDVCCW WVGPWHPVIR IFHPAFIKPV ILAPASVAPK DRVFYRFLRP WLGDGLLLST GDKWSRHRRM LTPAFHFNIL KPYVKIFNDS TNIMHAKWQR LASQGSARLD MFEHISLMTL DSLQKCVFSF DSNCQEKPSE YITAILELSA LVARRHQSLL LHVDLFYHLT RDGMRFRKAC RLVHDFTDAV IRERRCTLPD QGGDDALKAK AKAKTLDFID VLLLSKDEHG EALSDEDIRA EADTFMFGGH DTTASGLSWI LYNLAKHPEY QERCRQEVRE LLRDREPEEI EWDDLAQLPF LTMCIKESLR LHPPATAISR CCTQDIMLPD GRVIPKGVIC RISIFGTHHN PAVWPDPEVY NPFRFDADNG KGRSPLAFIP FSAGPRNCIG QTFAMSEMKV ALALTLLRFR VLPDDKEPRR KPELILRAEG GLWLRVEPLS AGAH //