ID   CP4V2_HUMAN             Reviewed;         525 AA.
AC   Q6ZWL3; B7U6W2; Q6ZTM4;
DT   02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=Cytochrome P450 4V2;
DE   AltName: Full=Docosahexaenoic acid omega-hydroxylase CYP4V2 {ECO:0000305|PubMed:22772592};
DE            EC=1.14.14.79 {ECO:0000269|PubMed:22772592};
DE   AltName: Full=Long-chain fatty acid omega-monooxygenase {ECO:0000305|PubMed:19661213};
DE            EC=1.14.14.80 {ECO:0000269|PubMed:19661213};
GN   Name=CYP4V2;
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 1), TISSUE SPECIFICITY, AND VARIANTS
RP   BCD ARG-44; SER-61; ASP-79; THR-111; VAL-123; LYS-259; PRO-331; PRO-341 AND
RP   HIS-508.
RC   TISSUE=Retina;
RX   PubMed=15042513; DOI=10.1086/383228;
RA   Li A., Jiao X., Munier F.L., Schorderet D.F., Yao W., Iwata F.,
RA   Hayakawa M., Kanai A., Shy Chen M., Alan Lewis R., Heckenlively J.,
RA   Weleber R.G., Traboulsi E.I., Zhang Q., Xiao X., Kaiser-Kupfer M.,
RA   Sergeev Y.V., Hejtmancik J.F.;
RT   "Bietti crystalline corneoretinal dystrophy is caused by mutations in the
RT   novel gene CYP4V2.";
RL   Am. J. Hum. Genet. 74:817-826(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   LYS-259.
RC   TISSUE=Kidney, and Uterus;
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-22; ASN-213; LYS-275;
RP   ILE-372 AND GLN-443.
RG   NIEHS SNPs program;
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-259.
RC   TISSUE=Placenta;
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   [6]
RP   CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP   SPECIFICITY, ACTIVITY REGULATION, AND PATHWAY.
RX   PubMed=19661213; DOI=10.1124/dmd.109.028530;
RA   Nakano M., Kelly E.J., Rettie A.E.;
RT   "Expression and characterization of CYP4V2 as a fatty acid omega-
RT   hydroxylase.";
RL   Drug Metab. Dispos. 37:2119-2122(2009).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   CHARACTERIZATION OF VARIANT BCD PRO-331, AND PATHWAY.
RX   PubMed=22772592; DOI=10.1124/mol.112.080085;
RA   Nakano M., Kelly E.J., Wiek C., Hanenberg H., Rettie A.E.;
RT   "CYP4V2 in Bietti's crystalline dystrophy: ocular localization, metabolism
RT   of omega-3-polyunsaturated fatty acids, and functional deficit of the
RT   p.H331P variant.";
RL   Mol. Pharmacol. 82:679-686(2012).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: A cytochrome P450 monooxygenase involved in fatty acid
CC       metabolism in the eye. Catalyzes the omega-hydroxylation of
CC       polyunsaturated fatty acids (PUFAs) docosahexaenoate (DHA) and its
CC       precursor eicosapentaenoate (EPA), and may contribute to the
CC       homeostasis of these retinal PUFAs (PubMed:22772592). Omega
CC       hydroxylates saturated fatty acids such as laurate, myristate and
CC       palmitate, the catalytic efficiency decreasing in the following order:
CC       myristate > laurate > palmitate (C14>C12>C16) (PubMed:19661213).
CC       Mechanistically, uses molecular oxygen inserting one oxygen atom into a
CC       substrate, and reducing the second into a water molecule, with two
CC       electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-
CC       ferrihemoprotein reductase). {ECO:0000269|PubMed:19661213,
CC       ECO:0000269|PubMed:22772592}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] =
CC         12-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:38947, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:18262, ChEBI:CHEBI:36204, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:19661213};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38948;
CC         Evidence={ECO:0000305|PubMed:19661213};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + reduced [NADPH--hemoprotein reductase] + tetradecanoate =
CC         14-hydroxytetradecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:40203, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:30807, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:77033; Evidence={ECO:0000269|PubMed:19661213};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40204;
CC         Evidence={ECO:0000305|PubMed:19661213};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexadecanoate + O2 + reduced [NADPH--hemoprotein reductase] =
CC         16-hydroxyhexadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:40199, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:55329, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; EC=1.14.14.80;
CC         Evidence={ECO:0000269|PubMed:19661213};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40200;
CC         Evidence={ECO:0000305|PubMed:19661213};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced
CC         [NADPH--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:22772592};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39792;
CC         Evidence={ECO:0000305|PubMed:22772592};
CC   -!- CATALYTIC ACTIVITY:
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:22772592};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40156;
CC         Evidence={ECO:0000305|PubMed:22772592};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P51869};
CC   -!- ACTIVITY REGULATION: Inhibited by N-hydroxy-N'-(4-n-butyl-2-
CC       methylphenyl formamidine)(HET0016) with an IC(50) of 38 nM.
CC       {ECO:0000269|PubMed:19661213}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=65 uM for myristic acid {ECO:0000269|PubMed:19661213};
CC         KM=140 uM for lauric acid {ECO:0000269|PubMed:19661213};
CC         KM=430 uM for palmitic acid {ECO:0000269|PubMed:19661213};
CC         Note=Vmax is nearly the same for myristic acid and for lauric acid
CC         and reduced about 30% for palmitic acid.
CC         {ECO:0000269|PubMed:19661213};
CC   -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC       {ECO:0000305|PubMed:19661213, ECO:0000305|PubMed:22772592}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:22772592}; Single-pass membrane protein
CC       {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6ZWL3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZWL3-2; Sequence=VSP_014918;
CC   -!- TISSUE SPECIFICITY: Broadly expressed. Detected in heart, brain,
CC       placenta, lung, liver, skeletal muscle, kidney, pancreas, retina,
CC       retinal pigment epithelium (RPE) and lymphocytes.
CC       {ECO:0000269|PubMed:15042513, ECO:0000269|PubMed:22772592}.
CC   -!- DISEASE: Bietti crystalline corneoretinal dystrophy (BCD) [MIM:210370]:
CC       An autosomal recessive ocular disease characterized by retinal
CC       degeneration and marginal corneal dystrophy. Typical features include
CC       multiple glistening intraretinal crystals scattered over the fundus, a
CC       characteristic degeneration of the retina, and sclerosis of the
CC       choroidal vessels, ultimately resulting in progressive night blindness
CC       and constriction of the visual field. Most patients have similar
CC       crystals at the corneoscleral limbus. Patients develop decreased
CC       vision, nyctalopia, and paracentral scotomata between the 2nd and 4th
CC       decade of life. Later, they develop peripheral visual field loss and
CC       marked visual impairment, usually progressing to legal blindness by the
CC       5th or 6th decade of life. {ECO:0000269|PubMed:15042513,
CC       ECO:0000269|PubMed:22772592}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/cyp4v2/";
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DR   EMBL; AY422002; AAR31180.1; -; mRNA.
DR   EMBL; AK122600; BAC85487.1; -; mRNA.
DR   EMBL; AK126473; BAC86562.1; -; mRNA.
DR   EMBL; FJ440682; ACK44069.1; -; Genomic_DNA.
DR   EMBL; AC110771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC060857; AAH60857.1; -; mRNA.
DR   CCDS; CCDS34119.1; -. [Q6ZWL3-1]
DR   RefSeq; NP_997235.3; NM_207352.3. [Q6ZWL3-1]
DR   AlphaFoldDB; Q6ZWL3; -.
DR   SMR; Q6ZWL3; -.
DR   BioGRID; 130113; 12.
DR   IntAct; Q6ZWL3; 4.
DR   STRING; 9606.ENSP00000368079; -.
DR   SwissLipids; SLP:000000542; -.
DR   iPTMnet; Q6ZWL3; -.
DR   PhosphoSitePlus; Q6ZWL3; -.
DR   BioMuta; CYP4V2; -.
DR   DMDM; 296434466; -.
DR   EPD; Q6ZWL3; -.
DR   jPOST; Q6ZWL3; -.
DR   MassIVE; Q6ZWL3; -.
DR   MaxQB; Q6ZWL3; -.
DR   PaxDb; 9606-ENSP00000368079; -.
DR   PeptideAtlas; Q6ZWL3; -.
DR   ProteomicsDB; 68494; -. [Q6ZWL3-1]
DR   ProteomicsDB; 68495; -. [Q6ZWL3-2]
DR   Antibodypedia; 29101; 234 antibodies from 24 providers.
DR   DNASU; 285440; -.
DR   Ensembl; ENST00000378802.5; ENSP00000368079.4; ENSG00000145476.16. [Q6ZWL3-1]
DR   GeneID; 285440; -.
DR   KEGG; hsa:285440; -.
DR   MANE-Select; ENST00000378802.5; ENSP00000368079.4; NM_207352.4; NP_997235.3.
DR   UCSC; uc003iyw.5; human. [Q6ZWL3-1]
DR   AGR; HGNC:23198; -.
DR   CTD; 285440; -.
DR   DisGeNET; 285440; -.
DR   GeneCards; CYP4V2; -.
DR   GeneReviews; CYP4V2; -.
DR   HGNC; HGNC:23198; CYP4V2.
DR   HPA; ENSG00000145476; Tissue enhanced (liver).
DR   MalaCards; CYP4V2; -.
DR   MIM; 210370; phenotype.
DR   MIM; 608614; gene.
DR   neXtProt; NX_Q6ZWL3; -.
DR   OpenTargets; ENSG00000145476; -.
DR   Orphanet; 41751; Bietti crystalline dystrophy.
DR   PharmGKB; PA134912942; -.
DR   VEuPathDB; HostDB:ENSG00000145476; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   GeneTree; ENSGT00940000157278; -.
DR   HOGENOM; CLU_001570_5_1_1; -.
DR   InParanoid; Q6ZWL3; -.
DR   OMA; DIDHMPY; -.
DR   OrthoDB; 1611592at2759; -.
DR   PhylomeDB; Q6ZWL3; -.
DR   TreeFam; TF105088; -.
DR   BRENDA; 1.14.14.79; 2681.
DR   PathwayCommons; Q6ZWL3; -.
DR   Reactome; R-HSA-211976; Endogenous sterols.
DR   Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision).
DR   SignaLink; Q6ZWL3; -.
DR   UniPathway; UPA00199; -.
DR   BioGRID-ORCS; 285440; 9 hits in 1159 CRISPR screens.
DR   ChiTaRS; CYP4V2; human.
DR   GeneWiki; CYP4V2; -.
DR   GenomeRNAi; 285440; -.
DR   Pharos; Q6ZWL3; Tbio.
DR   PRO; PR:Q6ZWL3; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q6ZWL3; Protein.
DR   Bgee; ENSG00000145476; Expressed in kidney epithelium and 178 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0102033; F:long-chain fatty acid omega-hydroxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004497; F:monooxygenase activity; TAS:Reactome.
DR   GO; GO:0010430; P:fatty acid omega-oxidation; IDA:UniProtKB.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
DR   GO; GO:0016125; P:sterol metabolic process; TAS:Reactome.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   CDD; cd20680; CYP4V; 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:SF189; CYTOCHROME P450 4V2; 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.
PE   1: Evidence at protein level;
KW   Alternative splicing; Corneal dystrophy; Disease variant;
KW   Endoplasmic reticulum; Heme; Iron; Lipid metabolism; Membrane;
KW   Metal-binding; Monooxygenase; NADP; Oxidoreductase; Reference proteome;
KW   Sensory transduction; Transmembrane; Transmembrane helix; Vision.
FT   CHAIN           1..525
FT                   /note="Cytochrome P450 4V2"
FT                   /id="PRO_0000051859"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         329
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250|UniProtKB:P51869"
FT   BINDING         467
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         42..63
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_014918"
FT   VARIANT         22
FT                   /note="L -> V (in dbSNP:rs1055138)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_038606"
FT   VARIANT         44
FT                   /note="W -> R (in BCD; dbSNP:rs119103282)"
FT                   /evidence="ECO:0000269|PubMed:15042513"
FT                   /id="VAR_023084"
FT   VARIANT         61
FT                   /note="G -> S (in BCD; dbSNP:rs119103285)"
FT                   /evidence="ECO:0000269|PubMed:15042513"
FT                   /id="VAR_023085"
FT   VARIANT         79
FT                   /note="E -> D (in BCD; dbSNP:rs199476185)"
FT                   /evidence="ECO:0000269|PubMed:15042513"
FT                   /id="VAR_023086"
FT   VARIANT         111
FT                   /note="I -> T (in BCD; dbSNP:rs119103283)"
FT                   /evidence="ECO:0000269|PubMed:15042513"
FT                   /id="VAR_023087"
FT   VARIANT         123
FT                   /note="M -> V (in BCD; dbSNP:rs149684063)"
FT                   /evidence="ECO:0000269|PubMed:15042513"
FT                   /id="VAR_023088"
FT   VARIANT         213
FT                   /note="S -> N (in dbSNP:rs34331648)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_038607"
FT   VARIANT         259
FT                   /note="Q -> K (in dbSNP:rs13146272)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15042513, ECO:0000269|PubMed:15489334"
FT                   /id="VAR_033821"
FT   VARIANT         275
FT                   /note="E -> K (in dbSNP:rs34745240)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_055379"
FT   VARIANT         331
FT                   /note="H -> P (in BCD; impaired omega hydroxylase activity;
FT                   dbSNP:rs199476197)"
FT                   /evidence="ECO:0000269|PubMed:15042513,
FT                   ECO:0000269|PubMed:22772592"
FT                   /id="VAR_023089"
FT   VARIANT         341
FT                   /note="S -> P (in BCD; dbSNP:rs199476199)"
FT                   /evidence="ECO:0000269|PubMed:15042513"
FT                   /id="VAR_023090"
FT   VARIANT         372
FT                   /note="V -> I (in dbSNP:rs61755911)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_055380"
FT   VARIANT         443
FT                   /note="R -> Q (in dbSNP:rs72646291)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_055381"
FT   VARIANT         508
FT                   /note="R -> H (in BCD; dbSNP:rs119103284)"
FT                   /evidence="ECO:0000269|PubMed:15042513"
FT                   /id="VAR_023091"
SQ   SEQUENCE   525 AA;  60724 MW;  A26F0A517C9569AD CRC64;
     MAGLWLGLVW QKLLLWGAAS ALSLAGASLV LSLLQRVASY ARKWQQMRPI PTVARAYPLV
     GHALLMKPDG REFFQQIIEY TEEYRHMPLL KLWVGPVPMV ALYNAENVEV ILTSSKQIDK
     SSMYKFLEPW LGLGLLTSTG NKWRSRRKML TPTFHFTILE DFLDIMNEQA NILVKKLEKH
     INQEAFNCFF YITLCALDII CETAMGKNIG AQSNDDSEYV RAVYRMSEMI FRRIKMPWLW
     LDLWYLMFKE GWEHKKSLQI LHTFTNSVIA ERANEMNANE DCRGDGRGSA PSKNKRRAFL
     DLLLSVTDDE GNRLSHEDIR EEVDTFMFEG HDTTAAAINW SLYLLGSNPE VQKKVDHELD
     DVFGKSDRPA TVEDLKKLRY LECVIKETLR LFPSVPLFAR SVSEDCEVAG YRVLKGTEAV
     IIPYALHRDP RYFPNPEEFQ PERFFPENAQ GRHPYAYVPF SAGPRNCIGQ KFAVMEEKTI
     LSCILRHFWI ESNQKREELG LEGQLILRPS NGIWIKLKRR NADER
//