ID   D4AAL3_RAT              Unreviewed;       518 AA.
AC   D4AAL3;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   02-SEP-2026, entry version 102.
DE   SubName: Full=Cytochrome P450, family 26, subfamily C, polypeptide 1 {ECO:0000313|Ensembl:ENSRNOP00000033390.3};
GN   Name=Cyp26c1 {ECO:0000313|Ensembl:ENSRNOP00000033390.3,
GN   ECO:0000313|RGD:1308843};
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|Ensembl:ENSRNOP00000033390.3, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000033390.3}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000033390.3};
RA   Doris P.A., Kalbfleisch T., Li K., Howe K., Wood J.;
RT   "GRCr8: a new rat reference genome assembly contstructed from accurate long
RT   reads and long range scaffolding.";
RL   Submitted (JAN-2024) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000033390.3}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000033390.3};
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-retinoate + reduced [NADPH--hemoprotein reductase] +
CC         O2 = all-trans-4-hydroxyretinoate + oxidized [NADPH--hemoprotein
CC         reductase] + H2O + H(+); Xref=Rhea:RHEA:51984, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:35291, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:134178;
CC         Evidence={ECO:0000256|ARBA:ARBA00048965};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51985;
CC         Evidence={ECO:0000256|ARBA:ARBA00048965};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR602401-1};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   RefSeq; XP_217935.3; XM_217935.8.
DR   AlphaFoldDB; D4AAL3; -.
DR   SMR; D4AAL3; -.
DR   FunCoup; D4AAL3; 4.
DR   STRING; 10116.ENSRNOP00000033390; -.
DR   PhosphoSitePlus; D4AAL3; -.
DR   PaxDb; 10116-ENSRNOP00000033390; -.
DR   Ensembl; ENSRNOT00000030962.5; ENSRNOP00000033390.3; ENSRNOG00000030698.5.
DR   GeneID; 308190; -.
DR   KEGG; rno:308190; -.
DR   UCSC; RGD:1308843; rat.
DR   AGR; RGD:1308843; -.
DR   CTD; 340665; -.
DR   RGD; 1308843; Cyp26c1.
DR   eggNOG; KOG0157; Eukaryota.
DR   GeneTree; ENSGT00800000124060; -.
DR   HOGENOM; CLU_001570_15_6_1; -.
DR   InParanoid; D4AAL3; -.
DR   OMA; MIIHSTR; -.
DR   OrthoDB; 1372046at2759; -.
DR   PhylomeDB; D4AAL3; -.
DR   Reactome; R-RNO-211916; Vitamins.
DR   Reactome; R-RNO-5365859; RA biosynthesis pathway.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000030698; Expressed in frontal cortex.
DR   GO; GO:0016020; C: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: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:0007417; P:central nervous system development; ISO:RGD.
DR   GO; GO:0014032; P:neural crest cell development; ISO:RGD.
DR   GO; GO:0048284; P:organelle fusion; ISO:RGD.
DR   GO; GO:0034653; P:retinoic acid catabolic process; ISO:RGD.
DR   FunFam; 1.10.630.10:FF:000009; Cytochrome P450 26B1 isoform 1; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24286; CYTOCHROME P450 26; 1.
DR   PANTHER; PTHR24286:SF100; CYTOCHROME P450 26C1; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602401-1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602401-1};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602401-1};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW   ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT   BINDING         455
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:PIRSR602401-1"
SQ   SEQUENCE   518 AA;  57298 MW;  0B1410C3912DAE3F CRC64;
     MFSWGLSCLS MLGAAGTALL CAGLLLGLAQ QLWTLRWTLS RDWASTLPLP KGSMGWPFFG
     ETLHWLVQGS RFHSSRRERY GTVFKTHLLG RPVIRVSGAE NVRTILLGEH RLVRSQWPQS
     AHILLGSHTL LGAVGERHRQ RRKVLARVFS RPALEQFVPR LQEALRREVR SWCAAQRPVA
     VYQAAKALTF RMAARILLGL QLDEARCTEL AQTFERLVEN LFSLPLDVPF SGLRKGIRAR
     DQLYQHLDEV IAEKLREELT AEPGDALHLI INSARELGRE LSVQELKELA VELLFAAFFT
     TASASTSLIL LLLQHPAAIA KIQQELSAQG LGSPCSCAPR ASGSRPDCSC EPDLSLAVLG
     RLRYVDCVVK EVLRLLPPVS GGYRTALRTF ELDGYQIPKG WSVMYSIRDT HETAAVYRSP
     PEGFDPERFG VESEDARGSG GRFHYIPFGG GARSCLGQEL AQAVLQLLAV ELVRTARWEL
     ATPAFPVMQT VPIVHPVDGL LLLFHPLPTL GAGDGSPF
//