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   27-MAR-2024, entry version 185.
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
CC         [NADPH--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
CC         [NADPH--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
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:48796, 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: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
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:48776, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57405,
CC         ChEBI:CHEBI:57618, 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
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:53932, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57403,
CC         ChEBI:CHEBI:57618, 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
CC         [NADPH--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
CC         [NADPH--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
CC         [NADPH--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
CC         [NADPH--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   PaxDb; 9606-ENSP00000477567; -.
DR   PeptideAtlas; P98187; -.
DR   ProteomicsDB; 57819; -.
DR   Antibodypedia; 43609; 72 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   AGR; HGNC:2648; -.
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; GHESTIP; -.
DR   OrthoDB; 1611592at2759; -.
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 266 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 99 other cell types or tissues.
DR   ExpressionAtlas; P98187; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
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   CDD; cd20679; CYP4F; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR24291:SF192; CYTOCHROME P450 4F8; 1.
DR   PANTHER; PTHR24291; CYTOCHROME P450 FAMILY 4; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
DR   Genevisible; P98187; HS.
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
FT                   9,11-diazo-prostadienoic acid (U-51605) hydroxylation; loss
FT                   of 20:4n-6 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
//