CP4V2_HUMAN
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 03-AUG-2022, entry version 168.
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 [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: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; Q6ZWL3; -.
DR PeptideAtlas; Q6ZWL3; -.
DR PRIDE; Q6ZWL3; -.
DR ProteomicsDB; 68494; -. [Q6ZWL3-1]
DR ProteomicsDB; 68495; -. [Q6ZWL3-2]
DR Antibodypedia; 29101; 212 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 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; IFRRMKM; -.
DR OrthoDB; 1247045at2759; -.
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 1079 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 176 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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 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
