A4F3V8 · A4F3V8_HUMAN
- ProteinCytochrome P450 1A
- GeneCYP1A1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids175 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Catalytic activity
- (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-(5Z,8Z,10E,14Z)-eicosatetraenoate + H2OThis reaction proceeds in the forward direction.
- (13S)-hydroperoxy-(9Z,11E)-octadecadienoate = 13-oxo-(9Z,11E)-octadecadienoate + H2OThis reaction proceeds in the forward direction.
- (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H2OThis reaction proceeds in the forward direction.
- (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced [NADPH--hemoprotein reductase] = (19R,20S)-epoxy-(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate = 5-oxo-(6E,8Z,11Z,14Z)-eicosatetraenoate + H2OThis reaction proceeds in the forward direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = (17R,18S)-epoxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- 17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase] = 2-hydroxy-17beta-estradiol + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- 17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase] = 4-hydroxy-17beta-estradiol + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- all-trans-retinal + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-retinoate + 2 H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- all-trans-retinol + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-retinal + H+ + 2 H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- estrone + O2 + reduced [NADPH--hemoprotein reductase] = 2-hydroxyestrone + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- estrone + O2 + reduced [NADPH--hemoprotein reductase] = 4-hydroxyestrone + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
Cofactor
Pathway
Cofactor metabolism; retinol metabolism.
Lipid metabolism.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | aromatase activity | |
Molecular Function | heme binding | |
Molecular Function | hydroperoxy icosatetraenoate dehydratase activity | |
Molecular Function | iron ion binding | |
Molecular Function | steroid hydroxylase activity | |
Biological Process | retinol metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytochrome P450 1A
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA4F3V8
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Peripheral membrane protein
Microsome membrane ; Peripheral membrane protein
Membrane ; Peripheral membrane protein
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 202 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Proteomic databases
Expression
Gene expression databases
Structure
Sequence
- Sequence statusFragment
- Length175
- Mass (Da)20,612
- Last updated2007-04-17 v1
- Checksum58BBB13714D3DA49
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 175 | |||||
Sequence: D |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC091230 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AM233517 EMBL· GenBank· DDBJ | CAJ80720.1 EMBL· GenBank· DDBJ | mRNA |