CP26B_BOVIN
ID CP26B_BOVIN Reviewed; 512 AA.
AC E1BHJ4;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Cytochrome P450 26B1;
DE EC=1.14.13.- {ECO:0000250|UniProtKB:Q9NR63};
GN Name=CYP26B1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
CC -!- FUNCTION: Involved in the metabolism of retinoic acid (RA), rendering
CC this classical morphogen inactive through oxidation. Involved in the
CC specific inactivation of all-trans-retinoic acid (all-trans-RA), with a
CC preference for the following substrates: all-trans-RA > 9-cis-RA > 13-
CC cis-RA. Generates several hydroxylated forms of RA, including 4-OH-RA,
CC 4-oxo-RA, and 18-OH-RA. Essential for postnatal survival. Plays a
CC central role in germ cell development: acts by degrading RA in the
CC developing testis, preventing STRA8 expression, thereby leading to
CC delay of meiosis. Required for the maintenance of the undifferentiated
CC state of male germ cells during embryonic development in Sertoli cells,
CC inducing arrest in G0 phase of the cell cycle and preventing meiotic
CC entry. Plays a role in skeletal development, both at the level of
CC patterning and in the ossification of bone and the establishment of
CC some synovial joints (By similarity). {ECO:0000250|UniProtKB:Q811W2,
CC ECO:0000250|UniProtKB:Q9NR63}.
CC -!- FUNCTION: Has also a significant activity in oxidation of tazarotenic
CC acid and may therefore metabolize that xenobiotic in vivo.
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; DAAA02030376; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001179722.1; NM_001192793.1.
DR AlphaFoldDB; E1BHJ4; -.
DR SMR; E1BHJ4; -.
DR STRING; 9913.ENSBTAP00000016198; -.
DR PaxDb; E1BHJ4; -.
DR PRIDE; E1BHJ4; -.
DR Ensembl; ENSBTAT00000016198; ENSBTAP00000016198; ENSBTAG00000012212.
DR GeneID; 540868; -.
DR KEGG; bta:540868; -.
DR CTD; 56603; -.
DR VEuPathDB; HostDB:ENSBTAG00000012212; -.
DR eggNOG; KOG0157; Eukaryota.
DR GeneTree; ENSGT00800000124060; -.
DR HOGENOM; CLU_001570_15_6_1; -.
DR InParanoid; E1BHJ4; -.
DR OMA; WTATRDR; -.
DR OrthoDB; 871849at2759; -.
DR TreeFam; TF105093; -.
DR Reactome; R-BTA-211916; Vitamins.
DR Reactome; R-BTA-5365859; RA biosynthesis pathway.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000012212; Expressed in thymus and 96 other tissues.
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: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; ISS:UniProtKB.
DR GO; GO:0008401; F:retinoic acid 4-hydroxylase activity; ISS:UniProtKB.
DR GO; GO:0001972; F:retinoic acid binding; IEA:Ensembl.
DR GO; GO:0060349; P:bone morphogenesis; ISS:UniProtKB.
DR GO; GO:0001709; P:cell fate determination; IEA:Ensembl.
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; IEA:Ensembl.
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:0007140; P:male meiotic nuclear division; IEA:Ensembl.
DR GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0045580; P:regulation of T cell differentiation; IEA:Ensembl.
DR GO; GO:0034653; P:retinoic acid catabolic process; ISS:UniProtKB.
DR GO; GO:0042573; P:retinoic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR GO; GO:0043587; P:tongue morphogenesis; IEA:Ensembl.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISS: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 3: Inferred from homology;
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_0000416904"
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"
SQ SEQUENCE 512 AA; 57414 MW; 5DD8BB8CF788B101 CRC64;
MLFEGLELVS ALATLAACLV SVTLLLAVSQ QLWQLRWAAT RDKSCKLPIP KGSMGFPLIG
ETGHWLLQGS GFQSSRREKY GNVFKTHLLG RPLIRVTGAE NVRKILMGEH HLVSTEWPRS
TRMLLGPNTV SNSIGDIHRN KRKVFSKIFS HEALESYLPK IQLVIQDTLR AWSSHPEAIN
VYQEAQKLTF RMAIRVLLGF SIPEEDLGHL FEVYQQFVEN VFSLPVDLPF SGYRRGIQAR
QTLQKGLEKA IREKLQCTQG KDYSDALDIL IESSKEHGKE MTMQELKDGT LELIFAAYAT
TASASTSLIM QLLKHPAVLE KLREELRAKG LLHSGGCPCE GTLRLDTLSG LHYLDCVIKE
VMRLFTPVSG GYRTVLQTFE LDGFQIPKGW SVMYSIRDTH DTAPVFKDVN VFDPDRFGQA
RSEDKDGRFH YLPFGGGVRT CLGKHLAKLF LKVLAVELAS TSRFELATRT FPRITLVPVL
HPVDGLSVKF FGLDSNQNKI LPETEAMLSA TV
