CP4F8_HUMAN
ID CP4F8_HUMAN Reviewed; 520 AA.
AC P98187;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Cytochrome P450 4F8 {ECO:0000303|PubMed:10791960};
DE EC=1.14.14.1 {ECO:0000269|PubMed:10791960, ECO:0000269|PubMed:15789615, ECO:0000269|PubMed:16112640};
DE AltName: Full=CYPIVF8;
GN Name=CYP4F8 {ECO:0000303|PubMed:10791960, ECO:0000312|HGNC:HGNC:2648};
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], AND TISSUE SPECIFICITY.
RC TISSUE=Seminal vesicle;
RX PubMed=10405341; DOI=10.1006/bbrc.1999.1011;
RA Bylund J., Finnstroem N., Oliw E.H.;
RT "Gene expression of a novel cytochrome P450 of the CYP4F subfamily in human
RT seminal vesicles.";
RL Biochem. Biophys. Res. Commun. 261:169-174(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=10791960; DOI=10.1074/jbc.m001712200;
RA Bylund J., Hidestrand M., Ingelman-Sundberg M., Oliw E.H.;
RT "Identification of CYP4F8 in human seminal vesicles as a prominent 19-
RT hydroxylase of prostaglandin endoperoxides.";
RL J. Biol. Chem. 275:21844-21849(2000).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=12464258; DOI=10.1016/s0003-9861(02)00511-8;
RA Stark K., Toermae H., Cristea M., Oliw E.H.;
RT "Expression of CYP4F8 (prostaglandin H 19-hydroxylase) in human epithelia
RT and prominent induction in epidermis of psoriatic lesions.";
RL Arch. Biochem. Biophys. 409:188-196(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, VARIANT PHE-125, AND MUTAGENESIS OF GLY-328.
RX PubMed=16112640; DOI=10.1016/j.abb.2005.07.003;
RA Stark K., Wongsud B., Burman R., Oliw E.H.;
RT "Oxygenation of polyunsaturated long chain fatty acids by recombinant
RT CYP4F8 and CYP4F12 and catalytic importance of Tyr-125 and Gly-328 of
RT CYP4F8.";
RL Arch. Biochem. Biophys. 441:174-181(2005).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=15789615; DOI=10.1016/j.prostaglandins.2004.09.014;
RA Stark K., Bylund J., Toermae H., Sahlen G., Oliw E.H.;
RT "On the mechanism of biosynthesis of 19-hydroxyprostaglandins of human
RT seminal fluid and expression of cyclooxygenase-2, PGH 19-hydroxylase
RT (CYP4F8) and microsomal PGE synthase-1 in seminal vesicles and vas
RT deferens.";
RL Prostaglandins Other Lipid Mediat. 75:47-64(2005).
CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of
CC endogenous polyunsaturated fatty acids (PUFAs) and their oxygenated
CC derivatives (oxylipins). Mechanistically, uses molecular oxygen
CC inserting one oxygen atom into a substrate, and reducing the second
CC into a water molecule, with two electrons provided by NADPH via
CC cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
CC Catalyzes the hydroxylation of carbon hydrogen bonds, with preference
CC for omega-1 and omega-2 positions (PubMed:10791960, PubMed:16112640,
CC PubMed:15789615). Hydroxylates (5Z,8Z,11Z,14Z)-eicosatetraenoic acid
CC (arachidonate) predominantly at omega-2 position to form (18R)-
CC hydroxyeicosatetraenoic acid (18R-HETE) (PubMed:10791960). Exhibits
CC omega-1 hydroxylase activity toward prostaglandin (PG) H1, PGH2 and
CC PGI2 (PubMed:10791960, PubMed:15789615). Catalyzes the epoxidation of
CC double bonds of PUFAs, including docosahexaenoic and docosapentaenoic
CC acids (PubMed:16112640). Shows little activity against PGD2, PGE1,
CC PGE2, PGF2alpha, and leukotriene B4. {ECO:0000269|PubMed:10791960,
CC ECO:0000269|PubMed:15789615, ECO:0000269|PubMed:16112640}.
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:10791960, ECO:0000269|PubMed:15789615};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150;
CC Evidence={ECO:0000305|PubMed:10791960};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (18R)-hydroxy-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:48736, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:90790; Evidence={ECO:0000269|PubMed:10791960};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48737;
CC Evidence={ECO:0000305|PubMed:10791960};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 20-hydroxy-(4Z,7Z,10Z,13Z,16Z)-
CC docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:51112, 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:77226,
CC ChEBI:CHEBI:133939; Evidence={ECO:0000269|PubMed:16112640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51113;
CC Evidence={ECO:0000305|PubMed:16112640};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + prostaglandin H1 + reduced [NADPH--hemoprotein reductase]
CC = 19-hydroxyprostaglandin H1 + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:48796, 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:90793, ChEBI:CHEBI:90801;
CC Evidence={ECO:0000269|PubMed:10791960};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48797;
CC Evidence={ECO:0000305|PubMed:10791960};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + prostaglandin H2 + reduced [NADPH--hemoprotein reductase]
CC = 19-hydroxyprostaglandin H2 + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:48776, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57405, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:90797;
CC Evidence={ECO:0000269|PubMed:10791960};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48777;
CC Evidence={ECO:0000305|PubMed:10791960};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + prostaglandin I2 + reduced [NADPH--hemoprotein reductase]
CC = 19-hydroxy-prostaglandin I2 + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:53932, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57403, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:137987;
CC Evidence={ECO:0000269|PubMed:15789615};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53933;
CC Evidence={ECO:0000305|PubMed:15789615};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 10,11-epoxy-(4Z,7Z,13Z,16Z,19Z)-
CC docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:51092, 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:133934; Evidence={ECO:0000269|PubMed:16112640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51093;
CC Evidence={ECO:0000305|PubMed:16112640};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 13,14-epoxy-(4Z,7Z,10Z,16Z,19Z)-
CC docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:51088, 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:133933; Evidence={ECO:0000269|PubMed:16112640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51089;
CC Evidence={ECO:0000305|PubMed:16112640};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 16,17-epoxy-(4Z,7Z,10Z,13Z,19Z)-
CC docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:51084, 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:133932; Evidence={ECO:0000269|PubMed:16112640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51085;
CC Evidence={ECO:0000305|PubMed:16112640};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 19,20-epoxy-(4Z,7Z,10Z,13Z,16Z)-
CC docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:51080, 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:133931; Evidence={ECO:0000269|PubMed:16112640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51081;
CC Evidence={ECO:0000305|PubMed:16112640};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7Z,10Z,13Z,16Z,19Z)-docosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 10,11-epoxy-(7Z,13Z,16Z,19Z)-
CC docosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:51108, 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:77224,
CC ChEBI:CHEBI:133938; Evidence={ECO:0000269|PubMed:16112640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51109;
CC Evidence={ECO:0000305|PubMed:16112640};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7Z,10Z,13Z,16Z,19Z)-docosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 13,14-epoxy-(7Z,10Z,16Z,19Z)-
CC docosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:51104, 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:77224,
CC ChEBI:CHEBI:133937; Evidence={ECO:0000269|PubMed:16112640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51105;
CC Evidence={ECO:0000305|PubMed:16112640};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7Z,10Z,13Z,16Z,19Z)-docosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 16,17-epoxy-(7Z,10Z,13Z,19Z)-
CC docosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:51100, 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:77224,
CC ChEBI:CHEBI:133936; Evidence={ECO:0000269|PubMed:16112640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51101;
CC Evidence={ECO:0000305|PubMed:16112640};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7Z,10Z,13Z,16Z,19Z)-docosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 19,20-epoxy-(7Z,10Z,13Z,16Z)-
CC docosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:51096, 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:77224,
CC ChEBI:CHEBI:133935; Evidence={ECO:0000269|PubMed:16112640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51097;
CC Evidence={ECO:0000305|PubMed:16112640};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q02928};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7 uM for 9-alpha,11-alpha-epoxymethano-PGH2 (U-44069)
CC {ECO:0000269|PubMed:10791960};
CC KM=40 uM for 6,9-alpha-methylene-PGI2 {ECO:0000269|PubMed:15789615};
CC Vmax=260 pmol/min/pmol enzyme with 9-alpha,11-alpha-epoxymethano-PGH2
CC (U-44069) {ECO:0000269|PubMed:10791960};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000269|PubMed:10791960}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9HBI6}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9HBI6}. Microsome membrane
CC {ECO:0000250|UniProtKB:Q9HBI6}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9HBI6}.
CC -!- TISSUE SPECIFICITY: Expressed in the epithelium of seminal vesicles, in
CC renal cortex, in adult and fetal liver, in epidermis, in corneal
CC epithelium, in sweat glands, hair follicles, epithelial linings of the
CC ampulla of vas deferens and of the stomach and small intestine, as well
CC as in the transitional epithelium of the bladder and ureter (at protein
CC level). In the epidermis, expressed from the basal cell to the granular
CC cell layers. In the corneal epithelium, expressed in all cell layers.
CC Also detected in prostate. Up-regulated in the epidermis of psoriatic
CC lesions. {ECO:0000269|PubMed:10405341, ECO:0000269|PubMed:12464258,
CC ECO:0000269|PubMed:15789615}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF133298; AAD49566.1; -; mRNA.
DR CCDS; CCDS74303.1; -.
DR RefSeq; NP_009184.1; NM_007253.3.
DR AlphaFoldDB; P98187; -.
DR SMR; P98187; -.
DR BioGRID; 116439; 10.
DR IntAct; P98187; 5.
DR MINT; P98187; -.
DR STRING; 9606.ENSP00000477567; -.
DR BindingDB; P98187; -.
DR ChEMBL; CHEMBL4523270; -.
DR SwissLipids; SLP:000001467; -.
DR iPTMnet; P98187; -.
DR PhosphoSitePlus; P98187; -.
DR BioMuta; CYP4F8; -.
DR DMDM; 10719963; -.
DR EPD; P98187; -.
DR jPOST; P98187; -.
DR MassIVE; P98187; -.
DR MaxQB; P98187; -.
DR PeptideAtlas; P98187; -.
DR PRIDE; P98187; -.
DR ProteomicsDB; 57819; -.
DR Antibodypedia; 43609; 56 antibodies from 24 providers.
DR DNASU; 11283; -.
DR Ensembl; ENST00000612078.5; ENSP00000477567.1; ENSG00000186526.13.
DR GeneID; 11283; -.
DR KEGG; hsa:11283; -.
DR MANE-Select; ENST00000612078.5; ENSP00000477567.1; NM_007253.4; NP_009184.1.
DR UCSC; uc032hoh.2; human.
DR CTD; 11283; -.
DR DisGeNET; 11283; -.
DR GeneCards; CYP4F8; -.
DR HGNC; HGNC:2648; CYP4F8.
DR HPA; ENSG00000186526; Tissue enriched (seminal).
DR MIM; 611545; gene.
DR neXtProt; NX_P98187; -.
DR OpenTargets; ENSG00000186526; -.
DR PharmGKB; PA405; -.
DR VEuPathDB; HostDB:ENSG00000186526; -.
DR eggNOG; KOG0157; Eukaryota.
DR GeneTree; ENSGT00940000155021; -.
DR HOGENOM; CLU_001570_5_1_1; -.
DR InParanoid; P98187; -.
DR OMA; QRFEIRT; -.
DR OrthoDB; 1247045at2759; -.
DR PhylomeDB; P98187; -.
DR BRENDA; 1.14.14.B9; 2681.
DR PathwayCommons; P98187; -.
DR Reactome; R-HSA-211935; Fatty acids.
DR Reactome; R-HSA-211979; Eicosanoids.
DR Reactome; R-HSA-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR SABIO-RK; P98187; -.
DR SignaLink; P98187; -.
DR UniPathway; UPA00199; -.
DR BioGRID-ORCS; 11283; 9 hits in 210 CRISPR screens.
DR ChiTaRS; CYP4F8; human.
DR GeneWiki; CYP4F8; -.
DR GenomeRNAi; 11283; -.
DR Pharos; P98187; Tbio.
DR PRO; PR:P98187; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P98187; protein.
DR Bgee; ENSG00000186526; Expressed in seminal vesicle and 98 other tissues.
DR ExpressionAtlas; P98187; baseline and differential.
DR Genevisible; P98187; 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:0018685; F:alkane 1-monooxygenase activity; TAS:ProtInc.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; TAS:Reactome.
DR GO; GO:0006690; P:icosanoid metabolic process; TAS:Reactome.
DR GO; GO:0006693; P:prostaglandin metabolic process; TAS:ProtInc.
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 Endoplasmic reticulum; Fatty acid metabolism; Heme; Iron; Lipid metabolism;
KW Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..520
FT /note="Cytochrome P450 4F8"
FT /id="PRO_0000051855"
FT TRANSMEM 15..37
FT /note="Helical"
FT /evidence="ECO:0000255"
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"
FT VARIANT 125
FT /note="Y -> F (no effect on U-44069 and 9,11-diazo-
FT prostadienoic acid (U-51605) hydroxylation; loss of 20:4n-6
FT or 22:5n-6 oxidation; dbSNP:rs2072600)"
FT /evidence="ECO:0000269|PubMed:16112640"
FT /id="VAR_038347"
FT VARIANT 447
FT /note="P -> Q (in dbSNP:rs2056822)"
FT /id="VAR_038348"
FT MUTAGEN 328
FT /note="G->E: No effect on U-44069 and U-51605
FT hydroxylation. 20:4n-6 hydroxylation shifted from C-18 to
FT C-19."
FT /evidence="ECO:0000269|PubMed:16112640"
SQ SEQUENCE 520 AA; 59995 MW; 6839640CF4E9EB86 CRC64;
MSLLSLSWLG LRPVAASPWL LLLVVGASWL LARILAWTYA FYHNGRRLRC FPQPRKQNWF
LGHLGLVTPT EEGLRVLTQL VATYPQGFVR WLGPITPIIN LCHPDIVRSV INTSDAITDK
DIVFYKTLKP WLGDGLLLSV GDKWRHHRRL LTPAFHFNIL KPYIKIFSKS ANIMHAKWQR
LAMEGSTCLD VFEHISLMTL DSLQKCIFSF DSNCQEKPSE YITAIMELSA LVVKRNNQFF
RYKDFLYFLT PCGRRFHRAC RLVHDFTDAV IQERRRTLTS QGVDDFLQAK AKSKTLDFID
VLLLSEDKNG KELSDEDIRA EADTFMFGGH DTTASGLSWV LYNLARHPEY QERCRQEVQE
LLKDREPKEI EWDDLAQLPF LTMCLKESLR LHPPIPTFAR GCTQDVVLPD SRVIPKGNVC
NINIFAIHHN PSVWPDPEVY DPFRFDPENA QKRSPMAFIP FSAGPRNCIG QKFAMAEMKV
VLALTLLRFR ILPDHREPRR TPEIVLRAED GLWLRVEPLG
