ID   Q8VIL0_RAT              Unreviewed;       497 AA.
AC   Q8VIL0;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 2.
DT   27-MAR-2024, entry version 148.
DE   RecName: Full=Cytochrome P450 26A1 {ECO:0000256|ARBA:ARBA00040248};
GN   Name=Cyp26a1 {ECO:0000313|RGD:620161};
GN   Synonyms=CYP26A1 {ECO:0000313|EMBL:AAL32056.2};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|EMBL:AAL32056.2};
RN   [1] {ECO:0000313|EMBL:AAL32056.2}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Liver {ECO:0000313|EMBL:AAL32056.2};
RX   PubMed=12054474; DOI=10.1016/S0003-9861(02)00043-7;
RA   Wang Y., Zolfaghari R., Ross A.C.;
RT   "Cloning of rat cytochrome P450RAI (CYP26) cDNA and regulation of its gene
RT   expression by all-trans-retinoic acid in vivo.";
RL   Arch. Biochem. Biophys. 401:235-243(2002).
RN   [2] {ECO:0000313|EMBL:AAL32056.2}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Liver {ECO:0000313|EMBL:AAL32056.2};
RA   Zolfaghari R., Ross A.C.;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00036912};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51493;
CC         Evidence={ECO:0000256|ARBA:ARBA00036912};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602403-1};
CC   -!- SUBCELLULAR LOCATION: Microsome membrane
CC       {ECO:0000256|ARBA:ARBA00004174}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004174}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   EMBL; AF439720; AAL32056.2; -; mRNA.
DR   RefSeq; NP_569092.2; NM_130408.2.
DR   AlphaFoldDB; Q8VIL0; -.
DR   GeneID; 154985; -.
DR   KEGG; rno:154985; -.
DR   UCSC; RGD:620161; rat.
DR   AGR; RGD:620161; -.
DR   CTD; 1592; -.
DR   RGD; 620161; Cyp26a1.
DR   OrthoDB; 758626at2759; -.
DR   PhylomeDB; Q8VIL0; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0062183; F:all-trans retinoic acid 18-hydroxylase activity; ISO:RGD.
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: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; ISO:RGD.
DR   GO; GO:0008401; F:retinoic acid 4-hydroxylase activity; ISO:RGD.
DR   GO; GO:0001972; F:retinoic acid binding; ISO:RGD.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; ISO:RGD.
DR   GO; GO:0071300; P:cellular response to retinoic acid; ISO:RGD.
DR   GO; GO:0007417; P:central nervous system development; ISO:RGD.
DR   GO; GO:0001822; P:kidney development; IEP:RGD.
DR   GO; GO:0014032; P:neural crest cell development; ISO:RGD.
DR   GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR   GO; GO:0033189; P:response to vitamin A; IEP:RGD.
DR   GO; GO:0034653; P:retinoic acid catabolic process; ISO:RGD.
DR   GO; GO:0042573; P:retinoic acid metabolic process; ISO:RGD.
DR   GO; GO:0048384; P:retinoic acid receptor signaling pathway; ISO:RGD.
DR   GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR   GO; GO:0006805; P:xenobiotic metabolic process; ISO:RGD.
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.
DR   Genevisible; Q8VIL0; RN.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602403-1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602403-1};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW   ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000461}.
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:0000256|PIRSR:PIRSR602403-1"
SQ   SEQUENCE   497 AA;  56174 MW;  242A6441F0E399EC CRC64;
     MGLPALLASA LCTFVLPLLL FLAALKLWDL YCVSSRDRSC ALPLPPGTMG FPFFGETLQM
     VLQRRKFLQM KRRKYGFIYK THLFGRPTVR VMGADNVRRI LLGEHRLVSV HWPASVRTIL
     GAGCLSNLHD SSHKQRKKVI MQAFNREALQ CYVPVIAEEV SGCLEQWLSC GERGLLVYPE
     VKRLMFRIAM RILLGCEPGP AGGGEDEQQL VEAFEEMTRN LFSLPIDVPF SGLYRGVKAR
     NLIHARIEEN IRAKIRRLQA AEPDAGCKDA LQLLIEHSWE RGERLDMQAL KQSSTELLFG
     GHETTASAAT SLITYLGLYP HVLQKVREEI KSKGLLCKSH HEDKLDMETL EQLKYIGCVI
     KETLRLNPPV PGGFRVALKT FELNGYQIPK GWNVIYSICD THDVADSFTN KEEFNPDRFT
     SLHPEDTSRF SFIPFGGGLR SCVGKEFAKI LLKIFTVELA RRCDWQLLNG PPTMKTSPPV
     YPVDNLPARF THFQGDI
//