CP4F3_HUMAN
ID CP4F3_HUMAN Reviewed; 520 AA.
AC Q08477; B7Z8Z3; O60634; Q5U740;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Cytochrome P450 4F3;
DE EC=1.14.14.1 {ECO:0000269|PubMed:11461919, ECO:0000269|PubMed:16820285, ECO:0000269|PubMed:8486631};
DE AltName: Full=20-hydroxyeicosatetraenoic acid synthase {ECO:0000303|PubMed:11461919};
DE Short=20-HETE synthase {ECO:0000303|PubMed:11461919};
DE AltName: Full=CYPIVF3;
DE AltName: Full=Cytochrome P450-LTB-omega;
DE AltName: Full=Docosahexaenoic acid omega-hydroxylase CYP4F3 {ECO:0000305|PubMed:16820285};
DE EC=1.14.14.79 {ECO:0000269|PubMed:16820285, ECO:0000269|PubMed:18577768};
DE AltName: Full=Leukotriene-B(4) 20-monooxygenase 2;
DE AltName: Full=Leukotriene-B(4) omega-hydroxylase 2;
DE EC=1.14.14.94 {ECO:0000269|PubMed:11461919, ECO:0000269|PubMed:15364545, ECO:0000269|PubMed:8486631, ECO:0000269|PubMed:9675028};
GN Name=CYP4F3 {ECO:0000303|PubMed:9539102, ECO:0000312|HGNC:HGNC:2646};
GN Synonyms=LTB4H;
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 CYP4F3A), VARIANT ASP-269, FUNCTION
RP (ISOFORM CYP4F3A), AND CATALYTIC ACTIVITY (ISOFORM CYP4F3A).
RC TISSUE=Leukocyte;
RX PubMed=8486631; DOI=10.1016/s0021-9258(18)98360-2;
RA Kikuta Y., Kusunose E., Endo K., Yamamoto S., Sogawa K., Fujii-Kuriyama Y.,
RA Kusunose M.;
RT "A novel form of cytochrome P-450 family 4 in human polymorphonuclear
RT leukocytes. cDNA cloning and expression of leukotriene B4 omega-
RT hydroxylase.";
RL J. Biol. Chem. 268:9376-9380(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM CYP4F3A), AND VARIANT
RP ASP-269.
RX PubMed=9539102; DOI=10.1089/dna.1998.17.221;
RA Kikuta Y., Kato M., Yamashita Y., Miyauchi Y., Tanaka K., Kamada N.,
RA Kusunose M.;
RT "Human leukotriene B4 omega-hydroxylase (CYP4F3) gene: molecular cloning
RT and chromosomal localization.";
RL DNA Cell Biol. 17:221-230(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYP4F3B).
RC TISSUE=Fetal liver;
RA Peng X., Morgan K., Morgan T.R.;
RT "A novel form of cytochrome P-450 family 4 in human fetal liver.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CYP4F3B).
RC TISSUE=Tongue, and Trachea;
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 ASP-269; ILE-270 AND
RP THR-271.
RG SeattleSNPs variation discovery resource;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CYP4F3B).
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 FUNCTION (ISOFORM CYP4F3A), CATALYTIC ACTIVITY (ISOFORM CYP4F3A),
RP BIOPHYSICOCHEMICAL PROPERTIES (ISOFORM CYP4F3A), ACTIVITY REGULATION, AND
RP PATHWAY (ISOFORM CYP4F3A).
RX PubMed=9675028; DOI=10.1006/abbi.1998.0724;
RA Kikuta Y., Kusunose E., Sumimoto H., Mizukami Y., Takeshige K., Sakaki T.,
RA Yabusaki Y., Kusunose M.;
RT "Purification and characterization of recombinant human neutrophil
RT leukotriene B4 omega-hydroxylase (cytochrome P450 4F3).";
RL Arch. Biochem. Biophys. 355:201-205(1998).
RN [10]
RP ALTERNATIVE SPLICING, ALTERNATIVE PROMOTER USAGE, AND SUBCELLULAR LOCATION.
RX PubMed=10409674; DOI=10.1074/jbc.274.30.21191;
RA Christmas P., Ursino S.R., Fox J.W., Soberman R.J.;
RT "Expression of the CYP4F3 gene. tissue-specific splicing and alternative
RT promoters generate high and low K(m) forms of leukotriene B(4) omega-
RT hydroxylase.";
RL J. Biol. Chem. 274:21191-21199(1999).
RN [11]
RP ALTERNATIVE SPLICING, FUNCTION (ISOFORMS CYP4F3A AND CYP4F3B), CATALYTIC
RP ACTIVITY (ISOFORMS CYP4F3A AND CYP4F3B), BIOPHYSICOCHEMICAL PROPERTIES
RP (ISOFORMS CYP4F3A AND CYP4F3B), SUBSTRATE SPECIFICITY, TISSUE SPECIFICITY
RP (ISOFORMS CYP4F3A AND CYP4F3B), AND PATHWAY.
RX PubMed=11461919; DOI=10.1074/jbc.m104818200;
RA Christmas P., Jones J.P., Patten C.J., Rock D.A., Zheng Y., Cheng S.M.,
RA Weber B.M., Carlesso N., Scadden D.T., Rettie A.E., Soberman R.J.;
RT "Alternative splicing determines the function of CYP4F3 by switching
RT substrate specificity.";
RL J. Biol. Chem. 276:38166-38172(2001).
RN [12]
RP FUNCTION (ISOFORMS CYP4F3A AND CYP4F3B), CATALYTIC ACTIVITY (ISOFORMS
RP CYP4F3A AND CYP4F3B), AND BIOPHYSICOCHEMICAL PROPERTIES (ISOFORMS CYP4F3A
RP AND CYP4F3B).
RX PubMed=15145985; DOI=10.1194/jlr.m300463-jlr200;
RA Le Quere V., Plee-Gautier E., Potin P., Madec S., Salauen J.P.;
RT "Human CYP4F3s are the main catalysts in the oxidation of fatty acid
RT epoxides.";
RL J. Lipid Res. 45:1446-1458(2004).
RN [13]
RP FUNCTION (ISOFORM CYP4F3A), AND CATALYTIC ACTIVITY (ISOFORM CYP4F3A).
RX PubMed=15364545; DOI=10.1016/j.taap.2003.12.033;
RA Kalsotra A., Turman C.M., Kikuta Y., Strobel H.W.;
RT "Expression and characterization of human cytochrome P450 4F11: Putative
RT role in the metabolism of therapeutic drugs and eicosanoids.";
RL Toxicol. Appl. Pharmacol. 199:295-304(2004).
RN [14]
RP FUNCTION (ISOFORM CYP4F3B), CATALYTIC ACTIVITY (ISOFORM CYP4F3B), AND
RP BIOPHYSICOCHEMICAL PROPERTIES (ISOFORM CYP4F3B).
RX PubMed=16547005; DOI=10.1074/jbc.m513481200;
RA Sanders R.J., Ofman R., Duran M., Kemp S., Wanders R.J.;
RT "Omega-oxidation of very long-chain fatty acids in human liver microsomes.
RT Implications for X-linked adrenoleukodystrophy.";
RL J. Biol. Chem. 281:13180-13187(2006).
RN [15]
RP FUNCTION (ISOFORM CYP4F3B), AND CATALYTIC ACTIVITY (ISOFORM CYP4F3B).
RX PubMed=16820285; DOI=10.1016/j.plefa.2006.05.005;
RA Harmon S.D., Fang X., Kaduce T.L., Hu S., Raj Gopal V., Falck J.R.,
RA Spector A.A.;
RT "Oxygenation of omega-3 fatty acids by human cytochrome P450 4F3B: effect
RT on 20-hydroxyeicosatetraenoic acid production.";
RL Prostaglandins Leukot. Essent. Fatty Acids 75:169-177(2006).
RN [16]
RP FUNCTION (ISOFORMS CYP4F3A AND CYP4F3B), CATALYTIC ACTIVITY (ISOFORMS
RP CYP4F3A AND CYP4F3B), AND BIOPHYSICOCHEMICAL PROPERTIES (ISOFORMS CYP4F3A
RP AND CYP4F3B).
RX PubMed=18182499; DOI=10.1096/fj.07-099150;
RA Sanders R.J., Ofman R., Dacremont G., Wanders R.J., Kemp S.;
RT "Characterization of the human omega-oxidation pathway for omega-hydroxy-
RT very-long-chain fatty acids.";
RL FASEB J. 22:2064-2071(2008).
RN [17]
RP FUNCTION (ISOFORM CYP4F3B), AND CATALYTIC ACTIVITY (ISOFORM CYP4F3B).
RX PubMed=18065749; DOI=10.1194/jlr.m700450-jlr200;
RA Dhar M., Sepkovic D.W., Hirani V., Magnusson R.P., Lasker J.M.;
RT "Omega oxidation of 3-hydroxy fatty acids by the human CYP4F gene subfamily
RT enzyme CYP4F11.";
RL J. Lipid Res. 49:612-624(2008).
RN [18]
RP FUNCTION (ISOFORMS CYP4F3A AND CYP4F3B), AND CATALYTIC ACTIVITY (ISOFORMS
RP CYP4F3A AND CYP4F3B).
RX PubMed=18577768; DOI=10.1194/jlr.m800199-jlr200;
RA Fer M., Corcos L., Dreano Y., Plee-Gautier E., Salaun J.P., Berthou F.,
RA Amet Y.;
RT "Cytochromes P450 from family 4 are the main omega hydroxylating enzymes in
RT humans: CYP4F3B is the prominent player in PUFA metabolism.";
RL J. Lipid Res. 49:2379-2389(2008).
CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of
CC various endogenous substrates, including fatty acids and their
CC oxygenated derivatives (oxylipins) (PubMed:8486631, PubMed:9675028,
CC PubMed:11461919, PubMed:15145985, PubMed:16547005, PubMed:16820285,
CC PubMed:18182499, PubMed:18065749, PubMed:18577768). Mechanistically,
CC uses molecular oxygen inserting one oxygen atom into a substrate, and
CC reducing the second into a water molecule, with two electrons provided
CC by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein
CC reductase) (PubMed:9675028). May play a role in inactivation of pro-
CC inflammatory and anti-inflammatory oxylipins during the resolution of
CC inflammation (PubMed:8486631, PubMed:9675028, PubMed:11461919,
CC PubMed:15145985, PubMed:15364545, PubMed:16547005, PubMed:16820285,
CC PubMed:18182499, PubMed:18065749, PubMed:18577768).
CC {ECO:0000269|PubMed:11461919, ECO:0000269|PubMed:15145985,
CC ECO:0000269|PubMed:15364545, ECO:0000269|PubMed:16547005,
CC ECO:0000269|PubMed:16820285, ECO:0000269|PubMed:18065749,
CC ECO:0000269|PubMed:18182499, ECO:0000269|PubMed:18577768,
CC ECO:0000269|PubMed:8486631, ECO:0000269|PubMed:9675028}.
CC -!- FUNCTION: [Isoform CYP4F3A]: Catalyzes predominantly the oxidation of
CC the terminal carbon (omega-oxidation) of oxylipins in myeloid cells,
CC displaying higher affinity for arachidonate metabolite leukotriene B4
CC (LTB4) (PubMed:8486631, PubMed:9675028, PubMed:11461919,
CC PubMed:15364545). Inactivates LTB4 via three successive oxidative
CC transformations to 20-hydroxy-LTB4, then to 20-oxo-LTB4 and to 20-
CC carboxy-LTB4 (PubMed:9675028). Has omega-hydroxylase activity toward
CC long-chain fatty acid epoxides with preference for 8,9-epoxy-
CC (5Z,11Z,14Z)-eicosatrienoate (EET) and 9,10-epoxyoctadecanoate
CC (PubMed:15145985). Omega-hydroxylates monohydroxy polyunsaturated fatty
CC acids (PUFAs), including hydroxyeicosatetraenoates (HETEs) and
CC hydroxyeicosapentaenoates (HEPEs), to dihydroxy compounds
CC (PubMed:15364545, PubMed:9675028). Contributes to the degradation of
CC saturated very long-chain fatty acids (VLCFAs) such as docosanoic acid,
CC by catalyzing successive omega-oxidations to the corresponding
CC dicarboxylic acid, thereby initiating chain shortening
CC (PubMed:18182499). Has low hydroxylase activity toward PUFAs
CC (PubMed:18577768, PubMed:11461919). {ECO:0000269|PubMed:11461919,
CC ECO:0000269|PubMed:15145985, ECO:0000269|PubMed:15364545,
CC ECO:0000269|PubMed:18182499, ECO:0000269|PubMed:18577768,
CC ECO:0000269|PubMed:8486631, ECO:0000269|PubMed:9675028}.
CC -!- FUNCTION: [Isoform CYP4F3B]: Catalyzes predominantly the oxidation of
CC the terminal carbon (omega-oxidation) of polyunsaturated fatty acids
CC (PUFAs) (PubMed:11461919, PubMed:16820285, PubMed:18577768).
CC Participates in the conversion of arachidonic acid to 20-
CC hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting
CC both as vasoconstrictive and natriuretic with overall effect on
CC arterial blood pressure (PubMed:11461919, PubMed:16820285,
CC PubMed:18577768). Has high omega-hydroxylase activity toward other
CC PUFAs, including eicosatrienoic acid (ETA), eicosapentaenoic acid (EPA)
CC and docosahexaenoic acid (DHA) (PubMed:16820285, PubMed:18577768). Can
CC also catalyze the oxidation of the penultimate carbon (omega-1
CC oxidation) of PUFAs with lower efficiency (PubMed:18577768).
CC Contributes to the degradation of saturated very long-chain fatty acids
CC (VLCFAs) such as docosanoic acid and hexacosanoic acid, by catalyzing
CC successive omega-oxidations to the corresponding dicarboxylic acids,
CC thereby initiating chain shortening (PubMed:16547005, PubMed:18182499).
CC Omega-hydroxylates long-chain 3-hydroxy fatty acids, likely initiating
CC the oxidative conversion to the corresponding 3-hydroxydicarboxylic
CC fatty acids (PubMed:18065749). Has omega-hydroxylase activity toward
CC long-chain fatty acid epoxides with preference for 8,9-epoxy-
CC (5Z,11Z,14Z)-eicosatrienoate (EET) and 9,10-epoxyoctadecanoate
CC (PubMed:15145985). {ECO:0000269|PubMed:11461919,
CC ECO:0000269|PubMed:15145985, ECO:0000269|PubMed:16547005,
CC ECO:0000269|PubMed:16820285, ECO:0000269|PubMed:18065749,
CC ECO:0000269|PubMed:18182499, ECO:0000269|PubMed:18577768}.
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:11461919, ECO:0000269|PubMed:16820285,
CC ECO:0000269|PubMed:8486631};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17151;
CC Evidence={ECO:0000305|PubMed:11461919, ECO:0000305|PubMed:16820285,
CC ECO:0000305|PubMed:8486631};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=leukotriene B4 + O2 + reduced [NADPH--hemoprotein reductase] =
CC 20-hydroxy-leukotriene B4 + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:22176, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57460, ChEBI:CHEBI:57461, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.94;
CC Evidence={ECO:0000269|PubMed:11461919, ECO:0000269|PubMed:15364545,
CC ECO:0000269|PubMed:8486631, ECO:0000269|PubMed:9675028};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22177;
CC Evidence={ECO:0000305|PubMed:11461919, ECO:0000305|PubMed:15364545,
CC ECO:0000305|PubMed:8486631, ECO:0000305|PubMed:9675028};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=20-hydroxy-leukotriene B4 + O2 + reduced [NADPH--hemoprotein
CC reductase] = 20-oxo-leukotriene B4 + H(+) + 2 H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:48668, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57460, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:90720;
CC Evidence={ECO:0000269|PubMed:9675028};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48669;
CC Evidence={ECO:0000305|PubMed:9675028};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=20-oxo-leukotriene B4 + O2 + reduced [NADPH--hemoprotein
CC reductase] = 20-carboxy-leukotriene B4 + 2 H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:48672, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:90720, ChEBI:CHEBI:90722;
CC Evidence={ECO:0000269|PubMed:9675028};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48673;
CC Evidence={ECO:0000305|PubMed:9675028};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=(5Z,8Z,11Z)-eicosatrienoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 20-hydroxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50164,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:78043, ChEBI:CHEBI:132026;
CC Evidence={ECO:0000269|PubMed:18577768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50165;
CC Evidence={ECO:0000305|PubMed:18577768};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:39755, 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:76624; Evidence={ECO:0000269|PubMed:11461919,
CC ECO:0000269|PubMed:15364545, ECO:0000269|PubMed:18577768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39756;
CC Evidence={ECO:0000305|PubMed:11461919, ECO:0000305|PubMed:15364545,
CC ECO:0000305|PubMed:18577768};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z,17Z)-
CC eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:39787, 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:76636; Evidence={ECO:0000269|PubMed:18577768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39788;
CC Evidence={ECO:0000305|PubMed:18577768};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z,14Z,17Z)-
CC eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:39791, 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:76639; Evidence={ECO:0000269|PubMed:18577768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39792;
CC Evidence={ECO:0000305|PubMed:18577768};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 21-hydroxy-(4Z,7Z,10Z,13Z,16Z,19Z)-
CC docosahexaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:50088, 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:132025; Evidence={ECO:0000269|PubMed:18577768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50089;
CC Evidence={ECO:0000305|PubMed:18577768};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 22-hydroxy-(4Z,7Z,10Z,13Z,16Z,19Z)-
CC docosahexaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:40155, 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:77015,
CC ChEBI:CHEBI:77016; EC=1.14.14.79;
CC Evidence={ECO:0000269|PubMed:18577768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40156;
CC Evidence={ECO:0000305|PubMed:18577768};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 20-hydroxy-8,9-epoxy-(5Z,11Z,14Z)-
CC eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:53572, 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:84025,
CC ChEBI:CHEBI:137474; Evidence={ECO:0000269|PubMed:15145985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53573;
CC Evidence={ECO:0000305|PubMed:15145985};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 20-hydroxy-11,12-epoxy-(5Z,8Z,14Z)-
CC eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:53576, 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:76625,
CC ChEBI:CHEBI:137475; Evidence={ECO:0000269|PubMed:15145985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53577;
CC Evidence={ECO:0000305|PubMed:15145985};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 20-hydroxy-14,15-epoxy-(5Z,8Z,11Z)-
CC eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:53580, 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:84024,
CC ChEBI:CHEBI:137476; Evidence={ECO:0000269|PubMed:15145985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53581;
CC Evidence={ECO:0000305|PubMed:15145985};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=12,13-epoxy-(9Z)-octadecenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 18-hydroxy-12,13-epoxy-(9Z)-octadecenoate +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:53568, 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:84026,
CC ChEBI:CHEBI:137469; Evidence={ECO:0000269|PubMed:15145985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53569;
CC Evidence={ECO:0000305|PubMed:15145985};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=9,10-epoxy-(12Z)-octadecenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 18-hydroxy-9,10-epoxy-(12Z)-octadecenoate +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:53564, 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:84023,
CC ChEBI:CHEBI:137467; Evidence={ECO:0000269|PubMed:15145985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53565;
CC Evidence={ECO:0000305|PubMed:15145985};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=9,10-epoxyoctadecanoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 18-hydroxy-9,10-epoxy-octadecanoate + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53560,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:85195, ChEBI:CHEBI:137457;
CC Evidence={ECO:0000269|PubMed:15145985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53561;
CC Evidence={ECO:0000305|PubMed:15145985};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=(12R)-hydroxy-(9Z)-octadecenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (12R),18-dihydroxy-(9Z)-octadecenoate + H(+)
CC + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49384, 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:91295,
CC ChEBI:CHEBI:91300; Evidence={ECO:0000269|PubMed:9675028};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49385;
CC Evidence={ECO:0000305|PubMed:9675028};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=12-hydroxyoctadecanoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 12,18-dihydroxyoctadecanoate + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49376, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:84201, ChEBI:CHEBI:91294;
CC Evidence={ECO:0000269|PubMed:9675028};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49377;
CC Evidence={ECO:0000305|PubMed:9675028};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 5,20-dihydroxy-(6E,8Z,11Z,14Z)-
CC eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:48656, 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:65341,
CC ChEBI:CHEBI:90715; Evidence={ECO:0000269|PubMed:15364545,
CC ECO:0000269|PubMed:9675028};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48657;
CC Evidence={ECO:0000305|PubMed:15364545, ECO:0000305|PubMed:9675028};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=8-hydroxy-(5Z,9E,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 8,20-dihydroxy-(5Z,9E,11Z,14Z)-
CC eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:48660, 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:90716,
CC ChEBI:CHEBI:90717; Evidence={ECO:0000269|PubMed:15364545,
CC ECO:0000269|PubMed:9675028};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48661;
CC Evidence={ECO:0000305|PubMed:15364545, ECO:0000305|PubMed:9675028};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 12,20-dihydroxy-(5Z,8Z,10E,14Z)-
CC eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:48664, 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:90718,
CC ChEBI:CHEBI:90719; Evidence={ECO:0000269|PubMed:15364545};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48665;
CC Evidence={ECO:0000305|PubMed:9675028};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=5-hydroxy-(6E,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 5,20-dihydroxy-(6E,8Z,11Z,14Z,17Z)-
CC eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:49380, 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:90737,
CC ChEBI:CHEBI:91301; Evidence={ECO:0000269|PubMed:9675028};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49381;
CC Evidence={ECO:0000305|PubMed:9675028};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=lipoxin A4 + O2 + reduced [NADPH--hemoprotein reductase] = 20-
CC hydroxy-lipoxin A4 + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:48648, 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:67026,
CC ChEBI:CHEBI:90707; Evidence={ECO:0000269|PubMed:15364545};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48649;
CC Evidence={ECO:0000305|PubMed:15364545};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=lipoxin B4 + O2 + reduced [NADPH--hemoprotein reductase] = 20-
CC hydroxy-lipoxin B4 + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:48652, 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:67031,
CC ChEBI:CHEBI:90711; Evidence={ECO:0000269|PubMed:15364545,
CC ECO:0000269|PubMed:9675028};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48653;
CC Evidence={ECO:0000305|PubMed:15364545, ECO:0000305|PubMed:9675028};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=22-hydroxydocosanoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 22-oxodocosanoate + H(+) + 2 H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:39055, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:76298, ChEBI:CHEBI:76304;
CC Evidence={ECO:0000269|PubMed:18182499};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39056;
CC Evidence={ECO:0000305|PubMed:18182499};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3A]:
CC Reaction=22-oxodocosanoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = docosanedioate + 2 H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:39043, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:76298, ChEBI:CHEBI:76299;
CC Evidence={ECO:0000269|PubMed:18182499};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39044;
CC Evidence={ECO:0000305|PubMed:18182499};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3B]:
CC Reaction=(5Z,8Z,11Z)-eicosatrienoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 20-hydroxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50164,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:78043, ChEBI:CHEBI:132026;
CC Evidence={ECO:0000269|PubMed:18577768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50165;
CC Evidence={ECO:0000305|PubMed:18577768};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3B]:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:39755, 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:76624; Evidence={ECO:0000269|PubMed:11461919,
CC ECO:0000269|PubMed:16820285, ECO:0000269|PubMed:18577768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39756;
CC Evidence={ECO:0000305|PubMed:11461919, ECO:0000305|PubMed:16820285,
CC ECO:0000305|PubMed:18577768};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3B]:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z,17Z)-
CC eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:39787, 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:76636; Evidence={ECO:0000269|PubMed:18577768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39788;
CC Evidence={ECO:0000305|PubMed:18577768};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3B]:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z,14Z,17Z)-
CC eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:39791, 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:76639; Evidence={ECO:0000269|PubMed:16820285,
CC ECO:0000269|PubMed:18577768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39792;
CC Evidence={ECO:0000305|PubMed:16820285, ECO:0000305|PubMed:18577768};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3B]:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 21-hydroxy-(4Z,7Z,10Z,13Z,16Z,19Z)-
CC docosahexaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:50088, 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:132025; Evidence={ECO:0000269|PubMed:18577768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50089;
CC Evidence={ECO:0000305|PubMed:18577768};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3B]:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 22-hydroxy-(4Z,7Z,10Z,13Z,16Z,19Z)-
CC docosahexaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:40155, 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:77015,
CC ChEBI:CHEBI:77016; EC=1.14.14.79;
CC Evidence={ECO:0000269|PubMed:16820285, ECO:0000269|PubMed:18577768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40156;
CC Evidence={ECO:0000305|PubMed:16820285, ECO:0000305|PubMed:18577768};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3B]:
CC Reaction=8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 20-hydroxy-8,9-epoxy-(5Z,11Z,14Z)-
CC eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:53572, 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:84025,
CC ChEBI:CHEBI:137474; Evidence={ECO:0000269|PubMed:15145985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53573;
CC Evidence={ECO:0000305|PubMed:15145985};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3B]:
CC Reaction=14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 20-hydroxy-14,15-epoxy-(5Z,8Z,11Z)-
CC eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:53580, 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:84024,
CC ChEBI:CHEBI:137476; Evidence={ECO:0000269|PubMed:15145985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53581;
CC Evidence={ECO:0000305|PubMed:15145985};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3B]:
CC Reaction=12,13-epoxy-(9Z)-octadecenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 18-hydroxy-12,13-epoxy-(9Z)-octadecenoate +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:53568, 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:84026,
CC ChEBI:CHEBI:137469; Evidence={ECO:0000269|PubMed:15145985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53569;
CC Evidence={ECO:0000305|PubMed:15145985};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3B]:
CC Reaction=9,10-epoxy-(12Z)-octadecenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 18-hydroxy-9,10-epoxy-(12Z)-octadecenoate +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:53564, 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:84023,
CC ChEBI:CHEBI:137467; Evidence={ECO:0000269|PubMed:15145985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53565;
CC Evidence={ECO:0000305|PubMed:15145985};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3B]:
CC Reaction=9,10-epoxyoctadecanoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 18-hydroxy-9,10-epoxy-octadecanoate + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53560,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:85195, ChEBI:CHEBI:137457;
CC Evidence={ECO:0000269|PubMed:15145985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53561;
CC Evidence={ECO:0000305|PubMed:15145985};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3B]:
CC Reaction=docosanoate + O2 + reduced [NADPH--hemoprotein reductase] =
CC 22-hydroxydocosanoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:40079, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:23858, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:76304; Evidence={ECO:0000269|PubMed:16547005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40080;
CC Evidence={ECO:0000305|PubMed:16547005};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3B]:
CC Reaction=22-hydroxydocosanoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 22-oxodocosanoate + H(+) + 2 H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:39055, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:76298, ChEBI:CHEBI:76304;
CC Evidence={ECO:0000269|PubMed:18182499};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39056;
CC Evidence={ECO:0000305|PubMed:18182499};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3B]:
CC Reaction=22-oxodocosanoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = docosanedioate + 2 H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:39043, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:76298, ChEBI:CHEBI:76299;
CC Evidence={ECO:0000269|PubMed:18182499};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39044;
CC Evidence={ECO:0000305|PubMed:18182499};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3B]:
CC Reaction=O2 + reduced [NADPH--hemoprotein reductase] + tetracosanoate =
CC 24-hydroxytetracosanoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:39719, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:31014, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:76610; Evidence={ECO:0000269|PubMed:16547005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39720;
CC Evidence={ECO:0000305|PubMed:16547005};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3B]:
CC Reaction=hexacosanoate + O2 + reduced [NADPH--hemoprotein reductase] =
CC 26-hydroxyhexacosanoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:40083, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:31013, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:76305; Evidence={ECO:0000269|PubMed:16547005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40084;
CC Evidence={ECO:0000305|PubMed:16547005};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3B]:
CC Reaction=26-hydroxyhexacosanoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 26-oxohexacosanoate + H(+) + 2 H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:39059, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:76305, ChEBI:CHEBI:76311;
CC Evidence={ECO:0000269|PubMed:16547005, ECO:0000269|PubMed:18182499};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39060;
CC Evidence={ECO:0000305|PubMed:16547005, ECO:0000305|PubMed:18182499};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3B]:
CC Reaction=26-oxohexacosanoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 2 H(+) + H2O + hexacosanedioate + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:39047, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:76311, ChEBI:CHEBI:76312;
CC Evidence={ECO:0000269|PubMed:16547005, ECO:0000269|PubMed:18182499};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39048;
CC Evidence={ECO:0000305|PubMed:16547005, ECO:0000305|PubMed:18182499};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3B]:
CC Reaction=3-hydroxyoctadecanoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 3,18-dihydroxyoctadecanoate + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39735, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:76614, ChEBI:CHEBI:76615;
CC Evidence={ECO:0000269|PubMed:18065749};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39736;
CC Evidence={ECO:0000305|PubMed:18065749};
CC -!- CATALYTIC ACTIVITY: [Isoform CYP4F3B]:
CC Reaction=3-hydroxyhexadecanoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 3,16-dihydroxyhexadecanoate + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39731, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:63904, ChEBI:CHEBI:76613;
CC Evidence={ECO:0000269|PubMed:18065749};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39732;
CC Evidence={ECO:0000305|PubMed:18065749};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P51869};
CC -!- ACTIVITY REGULATION: Inhibited by carbon monoxide (CO).
CC {ECO:0000269|PubMed:9675028}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform CYP4F3A]:
CC Kinetic parameters:
CC KM=0.64 uM for leukotriene B4 {ECO:0000269|PubMed:9675028};
CC KM=6.5 uM for 20-hydroxy-leukotriene B4 {ECO:0000269|PubMed:9675028};
CC KM=0.68 uM for leukotriene B4 {ECO:0000269|PubMed:11461919};
CC KM=185.6 uM for arachidonate {ECO:0000269|PubMed:11461919};
CC KM=17.9 uM for lipoxin B4 {ECO:0000269|PubMed:9675028};
CC KM=25.7 uM for 5-HETE {ECO:0000269|PubMed:9675028};
CC KM=40.9 uM for 12-HETE {ECO:0000269|PubMed:9675028};
CC KM=49.5 uM for 5-HEPE {ECO:0000269|PubMed:9675028};
CC KM=14.2 uM for 12-hydroxyoctadecanoate {ECO:0000269|PubMed:9675028};
CC KM=22.8 uM for (12R)-hydroxy-(9Z)-octadecenoate
CC {ECO:0000269|PubMed:9675028};
CC KM=6.3 uM for 9(10)-epoxyoctadecanoate {ECO:0000269|PubMed:15145985};
CC KM=46.6 uM for 9(10)-epoxy-(12Z)-octadecenoate
CC {ECO:0000269|PubMed:15145985};
CC KM=61.8 uM for 12(13)-epoxy-(9Z)-octadecenoate
CC {ECO:0000269|PubMed:15145985};
CC KM=0.6 uM for 22-hydroxydocosanoate {ECO:0000269|PubMed:18182499};
CC Vmax=34.0 nmol/min/nmol enzyme toward leukotriene B4
CC {ECO:0000269|PubMed:9675028};
CC Vmax=66.7 nmol/min/nmol enzyme toward 20-hydroxy-leukotriene B4
CC {ECO:0000269|PubMed:9675028};
CC Vmax=32.8 pmol/min/pmol enzyme toward leukotriene B4
CC {ECO:0000269|PubMed:11461919};
CC Vmax=11.5 pmol/min/pmol enzyme toward arachidonate
CC {ECO:0000269|PubMed:11461919};
CC Vmax=38.5 nmol/min/nmol enzyme toward lipoxin B4
CC {ECO:0000269|PubMed:9675028};
CC Vmax=21.6 nmol/min/nmol enzyme toward 5-HETE
CC {ECO:0000269|PubMed:9675028};
CC Vmax=43.2 nmol/min/nmol enzyme toward 12-HETE
CC {ECO:0000269|PubMed:9675028};
CC Vmax=95.1 nmol/min/nmol enzyme toward 5-HEPE
CC {ECO:0000269|PubMed:9675028};
CC Vmax=54.5 nmol/min/nmol enzyme toward 12-hydroxyoctadecanoate
CC {ECO:0000269|PubMed:9675028};
CC Vmax=19.0 nmol/min/nmol enzyme toward (12R)-hydroxy-(9Z)-
CC octadecenoate {ECO:0000269|PubMed:9675028};
CC Vmax=10.8 nmol/min/nmol enzyme toward 9(10)-epoxyoctadecanoate
CC {ECO:0000269|PubMed:15145985};
CC Vmax=21.2 nmol/min/nmol enzyme toward 9(10)-epoxy-(12Z)-octadecenoate
CC {ECO:0000269|PubMed:15145985};
CC Vmax=3 nmol/min/nmol enzyme toward 12(13)-epoxy-(9Z)-octadecenoate
CC {ECO:0000269|PubMed:15145985};
CC Vmax=0.2 pmol/min/pmol enzyme toward 22-hydroxydocosanoate
CC {ECO:0000269|PubMed:18182499};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:9675028};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform CYP4F3B]:
CC Kinetic parameters:
CC KM=20.6 uM for leukotriene B4 {ECO:0000269|PubMed:11461919};
CC KM=22.0 uM for arachidonate {ECO:0000269|PubMed:11461919};
CC KM=35.7 uM for 9(10)-epoxyoctadecanoate
CC {ECO:0000269|PubMed:15145985};
CC KM=108.1 uM for 9(10)-epoxy-(12Z)-octadecenoate
CC {ECO:0000269|PubMed:15145985};
CC KM=100.6 uM for 12(13)-epoxy-(9Z)-octadecenoate
CC {ECO:0000269|PubMed:15145985};
CC KM=1.6 uM for docosanoate {ECO:0000269|PubMed:16547005};
CC KM=3.8 uM for tetracosanoate {ECO:0000269|PubMed:16547005};
CC KM=1.3 uM for hexacosanoate {ECO:0000269|PubMed:16547005};
CC KM=13.1 uM for 22-hydroxydocosanoate {ECO:0000269|PubMed:18182499};
CC KM=5.2 uM for 26-hydroxyhexacosanoate {ECO:0000269|PubMed:18182499};
CC Vmax=23.3 pmol/min/pmol enzyme toward leukotriene B4
CC {ECO:0000269|PubMed:11461919};
CC Vmax=13.3 pmol/min/pmol enzyme toward arachidonate
CC {ECO:0000269|PubMed:11461919};
CC Vmax=13.2 nmol/min/nmol enzyme toward 9(10)-epoxyoctadecanoate
CC {ECO:0000269|PubMed:15145985};
CC Vmax=15.02 nmol/min/nmol enzyme toward 9(10)-epoxy-(12Z)-
CC octadecenoate {ECO:0000269|PubMed:15145985};
CC Vmax=3.93 nmol/min/nmol enzyme toward 12(13)-epoxy-(9Z)-octadecenoate
CC {ECO:0000269|PubMed:15145985};
CC Vmax=5.0 pmol/min/pmol enzyme toward docosanoate
CC {ECO:0000269|PubMed:16547005};
CC Vmax=9.8 pmol/min/pmol enzyme toward tetracosanoate
CC {ECO:0000269|PubMed:16547005};
CC Vmax=2.2 pmol/min/pmol enzyme toward hexacosanoate
CC {ECO:0000269|PubMed:16547005};
CC Vmax=0.3 pmol/min/pmol enzyme toward 22-hydroxydocosanoate
CC {ECO:0000269|PubMed:18182499};
CC Vmax=0.8 pmol/min/pmol enzyme toward 26-hydroxyhexacosanoate
CC {ECO:0000269|PubMed:18182499};
CC Note=The omega-hydroxylation of VLCFAs follows dual-enzyme Michaelis-
CC Menten kinetics, suggesting simultaneous binding of two substrate
CC molecules. The high affinity Michaelis-Menten constants are shown.
CC {ECO:0000269|PubMed:16547005};
CC -!- PATHWAY: [Isoform CYP4F3A]: Lipid metabolism; leukotriene B4
CC degradation. {ECO:0000269|PubMed:9675028}.
CC -!- PATHWAY: Lipid metabolism; arachidonate metabolism.
CC {ECO:0000269|PubMed:11461919}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:10409674}; Single-pass membrane protein
CC {ECO:0000255}. Microsome membrane {ECO:0000305|PubMed:10409674};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=2;
CC Name=CYP4F3A;
CC IsoId=Q08477-1; Sequence=Displayed;
CC Name=CYP4F3B;
CC IsoId=Q08477-2; Sequence=VSP_047193;
CC -!- TISSUE SPECIFICITY: [Isoform CYP4F3A]: Selectively expressed in blood
CC neutrophils and bone marrow cells. Coexpressed with CYP4F3B in
CC prostate, ileum and trachea. {ECO:0000269|PubMed:11461919}.
CC -!- TISSUE SPECIFICITY: [Isoform CYP4F3B]: Selectively expressed in liver
CC and kidney. It is also the predominant CYP4F isoform in trachea and
CC tissues of the gastrointestinal tract. {ECO:0000269|PubMed:11461919}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/cyp4f3/";
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DR EMBL; D12620; BAA02144.1; -; mRNA.
DR EMBL; D12621; BAA02145.1; -; mRNA.
DR EMBL; AB002454; BAA25990.1; -; mRNA.
DR EMBL; AB002461; BAA25991.1; -; Genomic_DNA.
DR EMBL; AF054821; AAC08589.1; -; mRNA.
DR EMBL; AK304200; BAH14129.1; -; mRNA.
DR EMBL; AK316136; BAH14507.1; -; mRNA.
DR EMBL; AY792513; AAV40834.1; -; Genomic_DNA.
DR EMBL; AD000685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84489.1; -; Genomic_DNA.
DR EMBL; BC136299; AAI36300.1; -; mRNA.
DR CCDS; CCDS12332.1; -. [Q08477-1]
DR CCDS; CCDS59362.1; -. [Q08477-2]
DR PIR; A46661; A46661.
DR RefSeq; NP_000887.2; NM_000896.2. [Q08477-1]
DR RefSeq; NP_001186137.1; NM_001199208.1. [Q08477-2]
DR RefSeq; NP_001186138.1; NM_001199209.1. [Q08477-2]
DR RefSeq; XP_016882303.1; XM_017026814.1.
DR AlphaFoldDB; Q08477; -.
DR SMR; Q08477; -.
DR BioGRID; 110229; 7.
DR IntAct; Q08477; 4.
DR STRING; 9606.ENSP00000221307; -.
DR BindingDB; Q08477; -.
DR ChEMBL; CHEMBL3508692; -.
DR DrugBank; DB12016; Ponesimod.
DR SwissLipids; SLP:000000422; -. [Q08477-1]
DR SwissLipids; SLP:000000423; -. [Q08477-2]
DR iPTMnet; Q08477; -.
DR PhosphoSitePlus; Q08477; -.
DR BioMuta; CYP4F3; -.
DR DMDM; 56757430; -.
DR EPD; Q08477; -.
DR jPOST; Q08477; -.
DR MassIVE; Q08477; -.
DR MaxQB; Q08477; -.
DR PaxDb; Q08477; -.
DR PeptideAtlas; Q08477; -.
DR PRIDE; Q08477; -.
DR ProteomicsDB; 58614; -. [Q08477-1]
DR Antibodypedia; 27108; 138 antibodies from 27 providers.
DR DNASU; 4051; -.
DR Ensembl; ENST00000221307.13; ENSP00000221307.6; ENSG00000186529.16. [Q08477-1]
DR Ensembl; ENST00000585846.1; ENSP00000468105.1; ENSG00000186529.16. [Q08477-2]
DR Ensembl; ENST00000586182.6; ENSP00000466395.1; ENSG00000186529.16. [Q08477-2]
DR Ensembl; ENST00000591058.5; ENSP00000466988.1; ENSG00000186529.16. [Q08477-2]
DR GeneID; 4051; -.
DR KEGG; hsa:4051; -.
DR MANE-Select; ENST00000221307.13; ENSP00000221307.6; NM_000896.3; NP_000887.2.
DR UCSC; uc002nbj.4; human. [Q08477-1]
DR CTD; 4051; -.
DR DisGeNET; 4051; -.
DR GeneCards; CYP4F3; -.
DR HGNC; HGNC:2646; CYP4F3.
DR HPA; ENSG00000186529; Group enriched (bone marrow, liver).
DR MIM; 601270; gene.
DR neXtProt; NX_Q08477; -.
DR OpenTargets; ENSG00000186529; -.
DR PharmGKB; PA234; -.
DR VEuPathDB; HostDB:ENSG00000186529; -.
DR eggNOG; KOG0157; Eukaryota.
DR GeneTree; ENSGT00940000163407; -.
DR InParanoid; Q08477; -.
DR OMA; WVFPNQK; -.
DR PhylomeDB; Q08477; -.
DR TreeFam; TF105088; -.
DR BRENDA; 1.14.14.79; 2681.
DR BRENDA; 1.14.14.94; 2681.
DR PathwayCommons; Q08477; -.
DR Reactome; R-HSA-211935; Fatty acids.
DR Reactome; R-HSA-211958; Miscellaneous substrates.
DR Reactome; R-HSA-211979; Eicosanoids.
DR Reactome; R-HSA-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR SABIO-RK; Q08477; -.
DR SignaLink; Q08477; -.
DR UniPathway; UPA00383; -.
DR UniPathway; UPA00883; -.
DR BioGRID-ORCS; 4051; 9 hits in 1072 CRISPR screens.
DR ChiTaRS; CYP4F3; human.
DR GeneWiki; CYP4F3; -.
DR GenomeRNAi; 4051; -.
DR Pharos; Q08477; Tbio.
DR PRO; PR:Q08477; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q08477; protein.
DR Bgee; ENSG00000186529; Expressed in right lobe of liver and 119 other tissues.
DR ExpressionAtlas; Q08477; baseline and differential.
DR Genevisible; Q08477; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0097259; F:20-aldehyde-leukotriene B4 20-monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0097258; F:20-hydroxy-leukotriene B4 omega oxidase activity; IDA:UniProtKB.
DR GO; GO:0008391; F:arachidonic acid monooxygenase activity; IBA:GO_Central.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0102207; F:docosanoate omega-hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0050051; F:leukotriene-B4 20-monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0120319; F:long-chain fatty acid omega-1 hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0102033; F:long-chain fatty acid omega-hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0004497; F:monooxygenase activity; TAS:Reactome.
DR GO; GO:0140692; F:very long-chain fatty acid omega-hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IBA:GO_Central.
DR GO; GO:0010430; P:fatty acid omega-oxidation; IDA:UniProtKB.
DR GO; GO:0006690; P:icosanoid metabolic process; TAS:Reactome.
DR GO; GO:0036101; P:leukotriene B4 catabolic process; IDA:UniProtKB.
DR GO; GO:0006691; P:leukotriene metabolic process; TAS:Reactome.
DR GO; GO:2001302; P:lipoxin A4 metabolic process; IDA:UniProtKB.
DR GO; GO:2001304; P:lipoxin B4 metabolic process; IDA:UniProtKB.
DR GO; GO:0042361; P:menaquinone catabolic process; IBA:GO_Central.
DR GO; GO:0097267; P:omega-hydroxylase P450 pathway; IDA:UniProtKB.
DR GO; GO:0042376; P:phylloquinone catabolic 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 Alternative promoter usage; Alternative splicing; Endoplasmic reticulum;
KW Fatty acid metabolism; Heme; Iron; Lipid metabolism; Membrane;
KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..520
FT /note="Cytochrome P450 4F3"
FT /id="PRO_0000051851"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 328
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P51869"
FT BINDING 468
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:P51869"
FT VAR_SEQ 67..114
FT /note="IHSSEEGLLYTQSLACTFGDMCCWWVGPWHAIVRIFHPTYIKPVLFAP ->
FT VTPTEQGMRVLTQLVATYPQGFKVWMGPIFPVIRFCHPNIIRSVINAS (in
FT isoform CYP4F3B)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_047193"
FT VARIANT 96
FT /note="H -> Q (in dbSNP:rs34923393)"
FT /id="VAR_048457"
FT VARIANT 106
FT /note="Y -> C (in dbSNP:rs35888783)"
FT /id="VAR_048458"
FT VARIANT 269
FT /note="A -> D (in dbSNP:rs1805040)"
FT /evidence="ECO:0000269|PubMed:8486631,
FT ECO:0000269|PubMed:9539102, ECO:0000269|Ref.5"
FT /id="VAR_001258"
FT VARIANT 270
FT /note="V -> I (in dbSNP:rs28371536)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_020664"
FT VARIANT 271
FT /note="I -> T (in dbSNP:rs28371479)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_020665"
FT CONFLICT 184..186
FT /note="EGS -> KGY (in Ref. 3; AAC08589)"
FT /evidence="ECO:0000305"
FT CONFLICT 488
FT /note="R -> A (in Ref. 1; BAA02144 and 2; BAA25990/
FT BAA25991)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="L -> I (in Ref. 3; AAC08589)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 59847 MW; 2519D875280CF9DC CRC64;
MPQLSLSSLG LWPMAASPWL LLLLVGASWL LARILAWTYT FYDNCCRLRC FPQPPKRNWF
LGHLGLIHSS EEGLLYTQSL ACTFGDMCCW WVGPWHAIVR IFHPTYIKPV LFAPAAIVPK
DKVFYSFLKP WLGDGLLLSA GEKWSRHRRM LTPAFHFNIL KPYMKIFNES VNIMHAKWQL
LASEGSARLD MFEHISLMTL DSLQKCVFSF DSHCQEKPSE YIAAILELSA LVTKRHQQIL
LYIDFLYYLT PDGQRFRRAC RLVHDFTDAV IQERRRTLPS QGVDDFLQAK AKSKTLDFID
VLLLSKDEDG KKLSDEDIRA EADTFMFEGH DTTASGLSWV LYHLAKHPEY QERCRQEVQE
LLKDREPKEI EWDDLAQLPF LTMCIKESLR LHPPVPAVSR CCTQDIVLPD GRVIPKGIIC
LISVFGTHHN PAVWPDPEVY DPFRFDPKNI KERSPLAFIP FSAGPRNCIG QAFAMAEMKV
VLGLTLLRFR VLPDHTEPRR KPELVLRAEG GLWLRVEPLS
