CP26B_XENTR
ID CP26B_XENTR Reviewed; 511 AA.
AC Q08D50; F6S5X5;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Cytochrome P450 26B1;
DE EC=1.14.13.- {ECO:0000250|UniProtKB:Q9NR63};
GN Name=cyp26b1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a key role in retinoic acid metabolism. Appears to be
CC involved in the inactivation of all-trans-retinoic acid (RA).
CC {ECO:0000250|UniProtKB:Q9NR63}.
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:0000250|UniProtKB:Q9NR63};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51985;
CC Evidence={ECO:0000250|UniProtKB:Q9NR63};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6A2};
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 -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AAMC01080557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01080558; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01080559; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01080560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC123940; AAI23941.1; -; mRNA.
DR EMBL; BC135551; AAI35552.1; -; mRNA.
DR RefSeq; NP_001072655.1; NM_001079187.2.
DR AlphaFoldDB; Q08D50; -.
DR SMR; Q08D50; -.
DR STRING; 8364.ENSXETP00000046568; -.
DR PaxDb; Q08D50; -.
DR DNASU; 780112; -.
DR GeneID; 780112; -.
DR KEGG; xtr:780112; -.
DR CTD; 56603; -.
DR Xenbase; XB-GENE-991500; cyp26b1.
DR eggNOG; KOG0157; Eukaryota.
DR InParanoid; Q08D50; -.
DR OrthoDB; 871849at2759; -.
DR Reactome; R-XTR-211916; Vitamins.
DR Reactome; R-XTR-5365859; RA biosynthesis pathway.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008401; F:retinoic acid 4-hydroxylase activity; ISS:UniProtKB.
DR GO; GO:0034653; P:retinoic acid catabolic process; ISS:UniProtKB.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Heme; Iron; Lipid metabolism; Membrane;
KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..511
FT /note="Cytochrome P450 26B1"
FT /id="PRO_0000416907"
FT BINDING 440
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"
SQ SEQUENCE 511 AA; 57760 MW; CBE2F03F65DD28E7 CRC64;
MIFQSFDLVS ALATLAACLV SVALLLAVSQ QLWQLRWAAT RDKSCKLPIP KGSMGFPLVG
ETFHWILQGS DFQSSRREKY GNVFKTHLLG RPLIRVTGAE NVRKILMGEH HLVSTEWPRS
TRMLLGPNSL ANSIGDIHRH KRKVFSKIFS HEALESYLPK IQLVIQDTLR VWSSNPESIN
VYCEAQKLTF RMAIRVLLGF RLSDEELSQL FQVFQQFVEN VFSLPVDVPF SGYRRGIRAR
EMLLKSLEKA IQEKLQNTQG KDYADALDIL IESGKEHGKE LTMQELKDGT LELIFAAYAT
TASASTSLIM QLLKHPSVLE KLREELRGNS ILHNGCVCEG ALRVETISSL HYLDCVIKEI
LRLFSPVSGG YRTVLQTFEL DGFQIPKGWS VLYSIRDTHD TAPVFKDVDV FDPDRFGQDR
TEDKDGRFHY LPFGGGVRNC LGKHLAKLFL KVLAIELASM SRFELATRTF PKIMPVPVVH
PADELKVRFF GLDSNQNEIM TETEAMLGAT V
