O55127 · CP26A_MOUSE
- ProteinCytochrome P450 26A1
- GeneCyp26a1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids497 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
A cytochrome P450 monooxygenase involved in the metabolism of retinoates (RAs), the active metabolites of vitamin A, and critical signaling molecules in animals (PubMed:15911617, PubMed:9250660, PubMed:9442090).
RAs exist as at least four different isomers: all-trans-RA (atRA), 9-cis-RA, 13-cis-RA, and 9,13-dicis-RA, where atRA is considered to be the biologically active isomer, although 9-cis-RA and 13-cis-RA also have activity (By similarity).
Catalyzes the hydroxylation of atRA primarily at C-4 and C-18, thereby contributing to the regulation of atRA homeostasis and signaling (PubMed:15911617, PubMed:9250660, PubMed:9442090).
Hydroxylation of atRA limits its biological activity and initiates a degradative process leading to its eventual elimination (By similarity).
Involved in the convertion of atRA to all-trans-4-oxo-RA (PubMed:15911617).
Able to metabolize other RAs such as 9-cis, 13-cis and 9,13-di-cis RA (PubMed:9250660).
Can oxidize all-trans-13,14-dihydroretinoate (DRA) to metabolites which could include all-trans-4-oxo-DRA, all-trans-4-hydroxy-DRA, all-trans-5,8-epoxy-DRA, and all-trans-18-hydroxy-DRA (Probable). May play a role in the oxidative metabolism of xenobiotics such as tazarotenic acid (By similarity).
RAs exist as at least four different isomers: all-trans-RA (atRA), 9-cis-RA, 13-cis-RA, and 9,13-dicis-RA, where atRA is considered to be the biologically active isomer, although 9-cis-RA and 13-cis-RA also have activity (By similarity).
Catalyzes the hydroxylation of atRA primarily at C-4 and C-18, thereby contributing to the regulation of atRA homeostasis and signaling (PubMed:15911617, PubMed:9250660, PubMed:9442090).
Hydroxylation of atRA limits its biological activity and initiates a degradative process leading to its eventual elimination (By similarity).
Involved in the convertion of atRA to all-trans-4-oxo-RA (PubMed:15911617).
Able to metabolize other RAs such as 9-cis, 13-cis and 9,13-di-cis RA (PubMed:9250660).
Can oxidize all-trans-13,14-dihydroretinoate (DRA) to metabolites which could include all-trans-4-oxo-DRA, all-trans-4-hydroxy-DRA, all-trans-5,8-epoxy-DRA, and all-trans-18-hydroxy-DRA (Probable). May play a role in the oxidative metabolism of xenobiotics such as tazarotenic acid (By similarity).
Catalytic activity
- all-trans-retinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-(4S)-hydroxyretinoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- all-trans-(4S)-hydroxyretinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-(4S,16)-dihydroxyretinoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- all-trans-retinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-18-hydroxyretinoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
Cofactor
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | all-trans retinoic acid 18-hydroxylase activity | |
Molecular Function | all-trans retinoic acid 4-hydrolase activity | |
Molecular Function | heme binding | |
Molecular Function | iron ion binding | |
Molecular Function | monooxygenase activity | |
Molecular Function | 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 | |
Molecular Function | retinoic acid 4-hydroxylase activity | |
Biological Process | anterior/posterior pattern specification | |
Biological Process | cellular response to retinoic acid | |
Biological Process | central nervous system development | |
Biological Process | neural crest cell development | |
Biological Process | retinoic acid catabolic process | |
Biological Process | retinoic acid metabolic process | |
Biological Process | retinoic acid receptor signaling pathway | |
Biological Process | sterol metabolic process | |
Biological Process | xenobiotic metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytochrome P450 26A1
- EC number
- Short namesCYP26A1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionO55127
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Peripheral membrane protein
Microsome membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000051981 | 1-497 | Cytochrome P450 26A1 | |||
Sequence: MGLPALLASALCTFVLPLLLFLAALKLWDLYCVSSRDRSCALPLPPGTMGFPFFGETLQMVLQRRKFLQMKRRKYGFIYKTHLFGRPTVRVMGADNVRRILLGEHRLVSVHWPASVRTILGAGCLSNLHDSSHKQRKKVIMQAFSREALQCYVLVIAEEVSSCLEQWLSCGERGLLVYPEVKRLMFRIAMRILLGCEPGPAGGGEDEQQLVEAFEEMTRNLFSLPIDVPFSGLYRGVKARNLIHARIEENIRAKIRRLQATEPDGGCKDALQLLIEHSWERGERLDMQALKQSSTELLFGGHETTASAATSLITYLGLYPHVLQKVREEIKSKGLLCKSNQDNKLDMETLEQLKYIGCVIKETLRLNPPVPGGFRVALKTFELNGYQIPKGWNVIYSICDTHDVADIFTNKEEFNPDRFIVPHPEDASRFSFIPFGGGLRSCVGKEFAKILLKIFTVELARHCDWQLLNGPPTMKTSPTVYPVDNLPARFTYFQGDI |
Proteomic databases
PTM databases
Expression
Induction
By retinoic acid.
Structure
Sequence
- Sequence statusComplete
- Length497
- Mass (Da)56,178
- Last updated1998-06-01 v1
- Checksum33B07D7C29134471
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0R4J061 | A0A0R4J061_MOUSE | Cyp26a1 | 497 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 9 | in Ref. 3; AAD17217 | ||||
Sequence: S → T | ||||||
Sequence conflict | 154 | in Ref. 4; AAH12673 | ||||
Sequence: L → P | ||||||
Sequence conflict | 356 | in Ref. 4; AAH12673 | ||||
Sequence: I → T | ||||||
Sequence conflict | 492 | in Ref. 4; AAH12673 | ||||
Sequence: Y → H |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y12657 EMBL· GenBank· DDBJ | CAA73206.1 EMBL· GenBank· DDBJ | mRNA | ||
AF115769 EMBL· GenBank· DDBJ | AAD17217.1 EMBL· GenBank· DDBJ | mRNA | ||
BC012673 EMBL· GenBank· DDBJ | AAH12673.1 EMBL· GenBank· DDBJ | mRNA |