ID CP26A_HUMAN Reviewed; 497 AA.
AC O43174; B3KNI4; Q5VXH9; Q5VXI0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 184.
DE RecName: Full=Cytochrome P450 26A1;
DE Short=CYP26A1;
DE EC=1.14.13.- {ECO:0000269|PubMed:22020119, ECO:0000269|PubMed:26937021, ECO:0000269|PubMed:9228017, ECO:0000269|PubMed:9716180};
DE AltName: Full=Cytochrome P450 retinoic acid-inactivating 1;
DE Short=Cytochrome P450RAI {ECO:0000303|PubMed:9228017};
DE Short=hP450RAI {ECO:0000303|PubMed:9228017};
DE AltName: Full=Retinoic acid 4-hydroxylase {ECO:0000303|PubMed:9716180};
DE AltName: Full=Retinoic acid-metabolizing cytochrome;
GN Name=CYP26A1 {ECO:0000303|PubMed:26937021, ECO:0000312|HGNC:HGNC:2603};
GN Synonyms=CYP26, P450RAI1;
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), FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9228017; DOI=10.1074/jbc.272.30.18538;
RA White J.A., Beckett-Jones B., Guo Y.-D., Dilworth F.J., Bonasoro J.,
RA Jones G., Petkovich M.;
RT "cDNA cloning of human retinoic acid-metabolizing enzyme (hP450RAI)
RT identifies a novel family of cytochromes P450.";
RL J. Biol. Chem. 272:18538-18541(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBSTRATE SPECIFICITY,
RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=9716180;
RA Sonneveld E., van den Brink C.E., van der Leede B.M., Schulkes R.K.,
RA Petkovich M., van der Burg B., van der Saag P.T.;
RT "Human retinoic acid (RA) 4-hydroxylase (CYP26) is highly specific for all-
RT trans-RA and can be induced through RA receptors in human breast and colon
RT carcinoma cells.";
RL Cell Growth Differ. 9:629-637(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=9826557; DOI=10.1006/bbrc.1998.9659;
RA Trofimova-Griffin M.E., Juchau M.R.;
RT "Expression of cytochrome P450RAI (CYP26) in human fetal hepatic and
RT cephalic tissues.";
RL Biochem. Biophys. Res. Commun. 252:487-491(1998).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=22020119; DOI=10.1016/j.bcp.2011.10.007;
RA Topletz A.R., Thatcher J.E., Zelter A., Lutz J.D., Tay S., Nelson W.L.,
RA Isoherranen N.;
RT "Comparison of the function and expression of CYP26A1 and CYP26B1, the two
RT retinoic acid hydroxylases.";
RL Biochem. Pharmacol. 83:149-163(2012).
RN [8]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=26937021; DOI=10.1124/jpet.116.232637;
RA Foti R.S., Isoherranen N., Zelter A., Dickmann L.J., Buttrick B.R.,
RA Diaz P., Douguet D.;
RT "Identification of tazarotenic acid as the first xenobiotic substrate of
RT human retinoic acid hydroxylase CYP26A1 and CYP26B1.";
RL J. Pharmacol. Exp. Ther. 357:281-292(2016).
CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of
CC retinoates (RAs), the active metabolites of vitamin A, and critical
CC signaling molecules in animals (PubMed:22020119, PubMed:9228017,
CC PubMed:9716180). RAs exist as at least four different isomers: all-
CC trans-RA (atRA), 9-cis-RA, 13-cis-RA, and 9,13-dicis-RA, where atRA is
CC considered to be the biologically active isomer, although 9-cis-RA and
CC 13-cis-RA also have activity (Probable). Catalyzes the hydroxylation of
CC atRA primarily at C-4 and C-18, thereby contributing to the regulation
CC of atRA homeostasis and signaling (PubMed:22020119, PubMed:9228017,
CC PubMed:9716180). Hydroxylation of atRA limits its biological activity
CC and initiates a degradative process leading to its eventual elimination
CC (Probable). Involved in the convertion of atRA to all-trans-4-oxo-RA.
CC Able to metabolize other RAs such as 9-cis, 13-cis and 9,13-di-cis RA
CC (By similarity) (PubMed:9228017). Can oxidize all-trans-13,14-
CC dihydroretinoate (DRA) to metabolites which could include all-trans-4-
CC oxo-DRA, all-trans-4-hydroxy-DRA, all-trans-5,8-epoxy-DRA, and all-
CC trans-18-hydroxy-DRA (By similarity). May play a role in the oxidative
CC metabolism of xenobiotics such as tazarotenic acid (PubMed:26937021).
CC {ECO:0000250|UniProtKB:O55127, ECO:0000269|PubMed:22020119,
CC ECO:0000269|PubMed:26937021, ECO:0000269|PubMed:9228017,
CC ECO:0000269|PubMed:9716180, ECO:0000305|PubMed:22020119,
CC ECO:0000305|PubMed:9228017}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = all-trans-(4S)-hydroxyretinoate + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51492, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:35291,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:134185;
CC Evidence={ECO:0000269|PubMed:22020119};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51493;
CC Evidence={ECO:0000305|PubMed:22020119};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-(4S)-hydroxyretinoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = all-trans-(4S,16)-dihydroxyretinoate + H(+)
CC + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:51632, 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:134185,
CC ChEBI:CHEBI:134233; Evidence={ECO:0000269|PubMed:22020119};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51633;
CC Evidence={ECO:0000305|PubMed:22020119};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = all-trans-18-hydroxyretinoate + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:55856, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:35291,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:139258;
CC Evidence={ECO:0000269|PubMed:22020119};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55857;
CC Evidence={ECO:0000305|PubMed:22020119};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50.1 nM for all-trans-retinoate (4-hydroxylation)
CC {ECO:0000269|PubMed:22020119};
CC KM=48.9 nM for all-trans-retinoate (18-hydroxylation)
CC {ECO:0000269|PubMed:22020119};
CC KM=0.24 uM for tazarotenic acid (tazarotenic acid sulfoxide
CC formation) {ECO:0000269|PubMed:26937021};
CC KM=0.39 uM for tazarotenic acid (hydroxytazarotenic acid formation)
CC {ECO:0000269|PubMed:26937021};
CC Vmax=9.5 pmol/min/pmol enzyme toward all-trans-retinoate (4-
CC hydroxylation) {ECO:0000269|PubMed:22020119};
CC Vmax=5.0 pmol/min/pmol enzyme toward all-trans-retinoate (18-
CC hydroxylation) {ECO:0000269|PubMed:22020119};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:9716180}; Peripheral membrane protein. Microsome
CC membrane {ECO:0000269|PubMed:9716180}; Peripheral membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43174-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43174-2; Sequence=VSP_045087;
CC -!- TISSUE SPECIFICITY: Expressed in most fetal and adult tissues with
CC highest levels in adult liver, heart, pituitary gland, adrenal gland,
CC placenta and regions of the brain (PubMed:9826557). Expressed at high
CC levels in lung, pancreas, skin and uterus (at protein level)
CC (PubMed:22020119). Lower expression level is detected in spleen,
CC kidney, intestine and adipose tissue (at protein level)
CC (PubMed:22020119). {ECO:0000269|PubMed:22020119,
CC ECO:0000269|PubMed:9826557}.
CC -!- INDUCTION: By retinoic acid. {ECO:0000269|PubMed:9716180}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF005418; AAB88881.1; -; mRNA.
DR EMBL; AK027560; BAG51346.1; -; mRNA.
DR EMBL; AL358613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW50078.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW50079.1; -; Genomic_DNA.
DR CCDS; CCDS7426.1; -. [O43174-1]
DR CCDS; CCDS7427.1; -. [O43174-2]
DR RefSeq; NP_000774.2; NM_000783.3. [O43174-1]
DR RefSeq; NP_476498.1; NM_057157.2. [O43174-2]
DR AlphaFoldDB; O43174; -.
DR SMR; O43174; -.
DR BioGRID; 107964; 16.
DR STRING; 9606.ENSP00000224356; -.
DR BindingDB; O43174; -.
DR ChEMBL; CHEMBL5141; -.
DR DrugBank; DB13083; Talarozole.
DR DrugBank; DB00755; Tretinoin.
DR DrugBank; DB00162; Vitamin A.
DR GuidetoPHARMACOLOGY; 1366; -.
DR SwissLipids; SLP:000001674; -.
DR iPTMnet; O43174; -.
DR PhosphoSitePlus; O43174; -.
DR BioMuta; CYP26A1; -.
DR EPD; O43174; -.
DR jPOST; O43174; -.
DR MassIVE; O43174; -.
DR PaxDb; 9606-ENSP00000224356; -.
DR PeptideAtlas; O43174; -.
DR ProteomicsDB; 48791; -. [O43174-1]
DR ProteomicsDB; 65593; -.
DR Antibodypedia; 4222; 351 antibodies from 35 providers.
DR DNASU; 1592; -.
DR Ensembl; ENST00000224356.5; ENSP00000224356.4; ENSG00000095596.12. [O43174-1]
DR Ensembl; ENST00000371531.5; ENSP00000360586.1; ENSG00000095596.12. [O43174-2]
DR GeneID; 1592; -.
DR KEGG; hsa:1592; -.
DR MANE-Select; ENST00000224356.5; ENSP00000224356.4; NM_000783.4; NP_000774.2.
DR UCSC; uc001kik.1; human. [O43174-1]
DR AGR; HGNC:2603; -.
DR CTD; 1592; -.
DR DisGeNET; 1592; -.
DR GeneCards; CYP26A1; -.
DR HGNC; HGNC:2603; CYP26A1.
DR HPA; ENSG00000095596; Tissue enriched (liver).
DR MIM; 602239; gene.
DR neXtProt; NX_O43174; -.
DR OpenTargets; ENSG00000095596; -.
DR PharmGKB; PA27098; -.
DR VEuPathDB; HostDB:ENSG00000095596; -.
DR eggNOG; KOG0157; Eukaryota.
DR GeneTree; ENSGT00800000124060; -.
DR HOGENOM; CLU_001570_15_6_1; -.
DR InParanoid; O43174; -.
DR OMA; KLWEVYM; -.
DR OrthoDB; 758626at2759; -.
DR PhylomeDB; O43174; -.
DR TreeFam; TF105093; -.
DR PathwayCommons; O43174; -.
DR Reactome; R-HSA-211916; Vitamins.
DR Reactome; R-HSA-5365859; RA biosynthesis pathway.
DR SABIO-RK; O43174; -.
DR SIGNOR; O43174; -.
DR BioGRID-ORCS; 1592; 12 hits in 1151 CRISPR screens.
DR ChiTaRS; CYP26A1; human.
DR GeneWiki; CYP26A1; -.
DR GenomeRNAi; 1592; -.
DR Pharos; O43174; Tchem.
DR PRO; PR:O43174; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O43174; Protein.
DR Bgee; ENSG00000095596; Expressed in cortical plate and 71 other cell types or tissues.
DR ExpressionAtlas; O43174; baseline and differential.
DR Genevisible; O43174; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0062183; F:all-trans retinoic acid 18-hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0062182; F:all-trans retinoic acid 4-hydrolase activity; IEA:RHEA.
DR GO; GO:0020037; F:heme binding; NAS:BHF-UCL.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
DR GO; GO:0019825; F:oxygen binding; TAS:ProtInc.
DR GO; GO:0008401; F:retinoic acid 4-hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0001972; F:retinoic acid binding; IDA:BHF-UCL.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; TAS:BHF-UCL.
DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
DR GO; GO:0034653; P:retinoic acid catabolic process; IDA:BHF-UCL.
DR GO; GO:0042573; P:retinoic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR GO; GO:0006766; P:vitamin metabolic process; TAS:Reactome.
DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
DR CDD; cd20638; CYP26A1; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24286; CYTOCHROME P450 26; 1.
DR PANTHER; PTHR24286:SF194; CYTOCHROME P450 26A1; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
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; Endoplasmic reticulum; Heme; Iron; Lipid metabolism;
KW Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..497
FT /note="Cytochrome P450 26A1"
FT /id="PRO_0000051980"
FT BINDING 442
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:0000255"
FT VAR_SEQ 1..69
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045087"
FT CONFLICT 104..105
FT /note="EH -> DD (in Ref. 1; AAB88881)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="R -> G (in Ref. 3; BAG51346)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 56199 MW; 834318FA493E76D4 CRC64;
MGLPALLASA LCTFVLPLLL FLAAIKLWDL YCVSGRDRSC ALPLPPGTMG FPFFGETLQM
VLQRRKFLQM KRRKYGFIYK THLFGRPTVR VMGADNVRRI LLGEHRLVSV HWPASVRTIL
GSGCLSNLHD SSHKQRKKVI MRAFSREALE CYVPVITEEV GSSLEQWLSC GERGLLVYPE
VKRLMFRIAM RILLGCEPQL AGDGDSEQQL VEAFEEMTRN LFSLPIDVPF SGLYRGMKAR
NLIHARIEQN IRAKICGLRA SEAGQGCKDA LQLLIEHSWE RGERLDMQAL KQSSTELLFG
GHETTASAAT SLITYLGLYP HVLQKVREEL KSKGLLCKSN QDNKLDMEIL EQLKYIGCVI
KETLRLNPPV PGGFRVALKT FELNGYQIPK GWNVIYSICD THDVAEIFTN KEEFNPDRFM
LPHPEDASRF SFIPFGGGLR SCVGKEFAKI LLKIFTVELA RHCDWQLLNG PPTMKTSPTV
YPVDNLPARF THFHGEI
//
