CP26B_HUMAN
ID CP26B_HUMAN Reviewed; 512 AA.
AC Q9NR63; B2R8M7; B7Z2K6; B7Z2P4; B7Z3B8; E4W5W7; Q32MC0; Q53TW1; Q9NP41;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Cytochrome P450 26B1;
DE EC=1.14.13.- {ECO:0000269|PubMed:10823918, ECO:0000269|PubMed:22020119, ECO:0000269|PubMed:26937021};
DE AltName: Full=Cytochrome P450 26A2;
DE AltName: Full=Cytochrome P450 retinoic acid-inactivating 2;
DE Short=Cytochrome P450RAI-2;
DE AltName: Full=Retinoic acid-metabolizing cytochrome;
GN Name=CYP26B1; Synonyms=CYP26A2, P450RAI2;
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, CATALYTIC ACTIVITY,
RP TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Retina;
RX PubMed=10823918; DOI=10.1073/pnas.120161397;
RA White J.A., Ramshaw H., Taimi M., Stangle W., Zhang A., Everingham S.,
RA Creighton S., Tam S.-P., Jones G., Petkovich M.;
RT "Identification of the human cytochrome P450, P450RAI-2, which is
RT predominantly expressed in the adult cerebellum and is responsible for all-
RT trans-retinoic acid metabolism.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:6403-6408(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT SER-264.
RC TISSUE=Vascular smooth muscle;
RA Savenstrand H., Kumawat A., Karlsson M., Eriksson L.A., Sirsjo A.,
RA Strid A.;
RT "A spliced version of the human cytochrome P450 26B1 has an alternative
RT function in retinoic acid metabolism.";
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP SER-264.
RC TISSUE=Brain, Cerebellum, and Hippocampus;
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 [GENOMIC DNA], AND VARIANTS MET-181; VAL-185; HIS-191;
RP ASN-227; SER-264; LYS-380; GLY-420; CYS-473 AND ILE-479.
RG SeattleSNPs variation discovery resource;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP FUNCTION, AND VARIANTS RHFCA PRO-146 AND LEU-363.
RX PubMed=22019272; DOI=10.1016/j.ajhg.2011.09.015;
RA Laue K., Pogoda H.M., Daniel P.B., van Haeringen A., Alanay Y.,
RA von Ameln S., Rachwalski M., Morgan T., Gray M.J., Breuning M.H.,
RA Sawyer G.M., Sutherland-Smith A.J., Nikkels P.G., Kubisch C., Bloch W.,
RA Wollnik B., Hammerschmidt M., Robertson S.P.;
RT "Craniosynostosis and multiple skeletal anomalies in humans and zebrafish
RT result from a defect in the localized degradation of retinoic acid.";
RL Am. J. Hum. Genet. 89:595-606(2011).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND VARIANT
RP ARG-64.
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: Involved in the metabolism of retinoic acid (RA), rendering
CC this classical morphogen inactive through oxidation (PubMed:10823918,
CC PubMed:22020119). Involved in the specific inactivation of all-trans-
CC retinoic acid (all-trans-RA), with a preference for the following
CC substrates: all-trans-RA > 9-cis-RA > 13-cis-RA (PubMed:10823918,
CC PubMed:22020119). Generates several hydroxylated forms of RA, including
CC 4-OH-RA, 4-oxo-RA, and 18-OH-RA (PubMed:10823918). Catalyzes the
CC hydroxylation of carbon hydrogen bonds of atRA primarily at C-4
CC (PubMed:10823918, PubMed:22020119). Essential for postnatal survival
CC (By similarity). Plays a central role in germ cell development: acts by
CC degrading RA in the developing testis, preventing STRA8 expression,
CC thereby leading to delay of meiosis (By similarity). Required for the
CC maintenance of the undifferentiated state of male germ cells during
CC embryonic development in Sertoli cells, inducing arrest in G0 phase of
CC the cell cycle and preventing meiotic entry (By similarity). Plays a
CC role in skeletal development, both at the level of patterning and in
CC the ossification of bone and the establishment of some synovial joints
CC (PubMed:22019272). {ECO:0000250|UniProtKB:Q811W2,
CC ECO:0000269|PubMed:10823918, ECO:0000269|PubMed:22019272,
CC ECO:0000269|PubMed:22020119}.
CC -!- FUNCTION: Has also a significant activity in oxidation of tazarotenic
CC acid and may therefore metabolize that xenobiotic in vivo.
CC {ECO:0000269|PubMed:26937021}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = all-trans-4-hydroxyretinoate + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51984, 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:134178;
CC Evidence={ECO:0000269|PubMed:10823918, ECO:0000269|PubMed:22020119};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51985;
CC Evidence={ECO:0000305|PubMed:22020119};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6A2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.01 uM for tazarotenic acid (measured in vitro by the production
CC of tazarotenic acid-sulfoxide) {ECO:0000269|PubMed:26937021};
CC KM=0.56 uM for tazarotenic acid (measured in vitro by the production
CC of hydroxytazarotenic acid production) {ECO:0000269|PubMed:26937021};
CC -!- INTERACTION:
CC Q9NR63; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-25928065, EBI-1055254;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O43174}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O43174}. Microsome membrane
CC {ECO:0000250|UniProtKB:O43174}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O43174}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NR63-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NR63-2; Sequence=VSP_042968;
CC Name=3;
CC IsoId=Q9NR63-3; Sequence=VSP_042967;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, particularly in the
CC cerebellum and pons. {ECO:0000269|PubMed:10823918}.
CC -!- INDUCTION: By retinoic acid. {ECO:0000269|PubMed:10823918}.
CC -!- DISEASE: Radiohumeral fusions with other skeletal and craniofacial
CC anomalies (RHFCA) [MIM:614416]: A disease characterized by craniofacial
CC malformations, occipital encephalocele, radiohumeral fusions,
CC oligodactyly, advanced osseous maturation, and calvarial mineralization
CC defects. {ECO:0000269|PubMed:22019272}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAH12154.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/cyp26b1/";
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DR EMBL; AF252297; AAF76003.1; -; mRNA.
DR EMBL; FJ467289; ACR19332.1; -; mRNA.
DR EMBL; AK294814; BAH11892.1; -; mRNA.
DR EMBL; AK294933; BAH11930.1; -; mRNA.
DR EMBL; AK295683; BAH12154.1; ALT_INIT; mRNA.
DR EMBL; AK313433; BAG36224.1; -; mRNA.
DR EMBL; AC007002; AAY14690.1; -; Genomic_DNA.
DR EMBL; BC069443; AAH69443.1; -; mRNA.
DR EMBL; BC109205; AAI09206.1; -; mRNA.
DR CCDS; CCDS1919.1; -. [Q9NR63-1]
DR CCDS; CCDS62934.1; -. [Q9NR63-2]
DR RefSeq; NP_001264671.1; NM_001277742.1. [Q9NR63-2]
DR RefSeq; NP_063938.1; NM_019885.3. [Q9NR63-1]
DR AlphaFoldDB; Q9NR63; -.
DR SMR; Q9NR63; -.
DR BioGRID; 121153; 35.
DR IntAct; Q9NR63; 1.
DR STRING; 9606.ENSP00000001146; -.
DR BindingDB; Q9NR63; -.
DR ChEMBL; CHEMBL3713687; -.
DR DrugBank; DB00755; Tretinoin.
DR SwissLipids; SLP:000001876; -.
DR iPTMnet; Q9NR63; -.
DR PhosphoSitePlus; Q9NR63; -.
DR BioMuta; CYP26B1; -.
DR DMDM; 20137526; -.
DR MassIVE; Q9NR63; -.
DR MaxQB; Q9NR63; -.
DR PaxDb; Q9NR63; -.
DR PeptideAtlas; Q9NR63; -.
DR PRIDE; Q9NR63; -.
DR ProteomicsDB; 82286; -. [Q9NR63-1]
DR ProteomicsDB; 82287; -. [Q9NR63-2]
DR ProteomicsDB; 82288; -. [Q9NR63-3]
DR Antibodypedia; 2113; 283 antibodies from 34 providers.
DR DNASU; 56603; -.
DR Ensembl; ENST00000001146.7; ENSP00000001146.2; ENSG00000003137.9. [Q9NR63-1]
DR Ensembl; ENST00000546307.5; ENSP00000443304.1; ENSG00000003137.9. [Q9NR63-2]
DR GeneID; 56603; -.
DR KEGG; hsa:56603; -.
DR MANE-Select; ENST00000001146.7; ENSP00000001146.2; NM_019885.4; NP_063938.1.
DR UCSC; uc002sih.3; human. [Q9NR63-1]
DR CTD; 56603; -.
DR DisGeNET; 56603; -.
DR GeneCards; CYP26B1; -.
DR HGNC; HGNC:20581; CYP26B1.
DR HPA; ENSG00000003137; Tissue enhanced (brain).
DR MalaCards; CYP26B1; -.
DR MIM; 605207; gene.
DR MIM; 614416; phenotype.
DR neXtProt; NX_Q9NR63; -.
DR OpenTargets; ENSG00000003137; -.
DR Orphanet; 293925; Lethal occipital encephalocele-skeletal dysplasia syndrome.
DR PharmGKB; PA134879191; -.
DR VEuPathDB; HostDB:ENSG00000003137; -.
DR eggNOG; KOG0157; Eukaryota.
DR GeneTree; ENSGT00800000124060; -.
DR InParanoid; Q9NR63; -.
DR OMA; WTATRDR; -.
DR OrthoDB; 871849at2759; -.
DR PhylomeDB; Q9NR63; -.
DR TreeFam; TF105093; -.
DR PathwayCommons; Q9NR63; -.
DR Reactome; R-HSA-211916; Vitamins.
DR Reactome; R-HSA-5365859; RA biosynthesis pathway.
DR Reactome; R-HSA-5579015; Defective CYP26B1 causes RHFCA.
DR SABIO-RK; Q9NR63; -.
DR SignaLink; Q9NR63; -.
DR BioGRID-ORCS; 56603; 17 hits in 1084 CRISPR screens.
DR ChiTaRS; CYP26B1; human.
DR GeneWiki; CYP26B1; -.
DR GenomeRNAi; 56603; -.
DR Pharos; Q9NR63; Tchem.
DR PRO; PR:Q9NR63; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9NR63; protein.
DR Bgee; ENSG00000003137; Expressed in pons and 164 other tissues.
DR ExpressionAtlas; Q9NR63; baseline and differential.
DR Genevisible; Q9NR63; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
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:0016491; F:oxidoreductase 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:0008401; F:retinoic acid 4-hydroxylase activity; IDA:BHF-UCL.
DR GO; GO:0001972; F:retinoic acid binding; IDA:BHF-UCL.
DR GO; GO:0060349; P:bone morphogenesis; IMP:UniProtKB.
DR GO; GO:0001709; P:cell fate determination; ISS:BHF-UCL.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
DR GO; GO:0070268; P:cornification; IEA:Ensembl.
DR GO; GO:0030326; P:embryonic limb morphogenesis; ISS:BHF-UCL.
DR GO; GO:0061436; P:establishment of skin barrier; IEA:Ensembl.
DR GO; GO:0001768; P:establishment of T cell polarity; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0007140; P:male meiotic nuclear division; ISS:BHF-UCL.
DR GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; TAS:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:2001037; P:positive regulation of tongue muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0009954; P:proximal/distal pattern formation; ISS:BHF-UCL.
DR GO; GO:0045580; P:regulation of T cell differentiation; 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:0048384; P:retinoic acid receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; ISS:BHF-UCL.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR GO; GO:0043587; P:tongue morphogenesis; IEA:Ensembl.
DR GO; GO:0006766; P:vitamin metabolic process; TAS:Reactome.
DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
DR Gene3D; 1.10.630.10; -; 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 Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Craniosynostosis; Disease variant;
KW Endoplasmic reticulum; Heme; Iron; Lipid metabolism; Membrane;
KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..512
FT /note="Cytochrome P450 26B1"
FT /id="PRO_0000051985"
FT BINDING 441
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..67
FT /note="MLFEGLDLVSALATLAACLVSVTLLLAVSQQLWQLRWAATRDKSCKLPIPKG
FT SMGFPLIGETGHWLL -> MKNKTCVLVCVSVFGGERGQVTVPRVGVRRPSLAGPLQKC
FT TLRETRVWLP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042967"
FT VAR_SEQ 69..143
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_042968"
FT VARIANT 64
FT /note="H -> R"
FT /evidence="ECO:0000269|PubMed:26937021"
FT /id="VAR_075982"
FT VARIANT 146
FT /note="S -> P (in RHFCA; dbSNP:rs281875232)"
FT /evidence="ECO:0000269|PubMed:22019272"
FT /id="VAR_067923"
FT VARIANT 181
FT /note="V -> M (in dbSNP:rs142999899)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_038722"
FT VARIANT 185
FT /note="A -> V (in dbSNP:rs765423228)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_038723"
FT VARIANT 191
FT /note="R -> H (in dbSNP:rs76025186)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_038724"
FT VARIANT 227
FT /note="D -> N (in dbSNP:rs143738797)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_038725"
FT VARIANT 264
FT /note="L -> S (in dbSNP:rs2241057)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.4"
FT /id="VAR_024383"
FT VARIANT 363
FT /note="R -> L (in RHFCA; dbSNP:rs281875231)"
FT /evidence="ECO:0000269|PubMed:22019272"
FT /id="VAR_067924"
FT VARIANT 380
FT /note="E -> K (in dbSNP:rs2286965)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_038726"
FT VARIANT 420
FT /note="A -> G (in dbSNP:rs7568553)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_038727"
FT VARIANT 473
FT /note="R -> C (in dbSNP:rs61751056)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_038728"
FT VARIANT 479
FT /note="V -> I (in dbSNP:rs148075682)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_038729"
FT CONFLICT 265
FT /note="D -> G (in Ref. 3; BAH11930)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 57513 MW; A06D1D9944E6726F CRC64;
MLFEGLDLVS ALATLAACLV SVTLLLAVSQ QLWQLRWAAT RDKSCKLPIP KGSMGFPLIG
ETGHWLLQGS GFQSSRREKY GNVFKTHLLG RPLIRVTGAE NVRKILMGEH HLVSTEWPRS
TRMLLGPNTV SNSIGDIHRN KRKVFSKIFS HEALESYLPK IQLVIQDTLR AWSSHPEAIN
VYQEAQKLTF RMAIRVLLGF SIPEEDLGHL FEVYQQFVDN VFSLPVDLPF SGYRRGIQAR
QILQKGLEKA IREKLQCTQG KDYLDALDLL IESSKEHGKE MTMQELKDGT LELIFAAYAT
TASASTSLIM QLLKHPTVLE KLRDELRAHG ILHSGGCPCE GTLRLDTLSG LRYLDCVIKE
VMRLFTPISG GYRTVLQTFE LDGFQIPKGW SVMYSIRDTH DTAPVFKDVN VFDPDRFSQA
RSEDKDGRFH YLPFGGGVRT CLGKHLAKLF LKVLAVELAS TSRFELATRT FPRITLVPVL
HPVDGLSVKF FGLDSNQNEI LPETEAMLSA TV
