A0A8A0R1W6 · A0A8A0R1W6_TUPCH
- ProteinPolyunsaturated fatty acid lipoxygenase ALOX15
- GeneALOX15a
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids663 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
Catalytic activity
- (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = (8S)-hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoateThis reaction proceeds in the forward direction.
- (14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + O2 = (12S)-hydroperoxy-(14R,15S)-epoxy-(5Z,8Z,10E)-eicosatrienoateThis reaction proceeds in the forward direction.
- (14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + O2 = (5S)-hydroperoxy-(14R,15S)-epoxy-(6E,8Z,11Z)-eicosatrienoateThis reaction proceeds in the forward direction.
- (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + O2 = (12S)-hydroperoxy-(14S,15R)-epoxy-(5Z,8Z,10E)-eicosatrienoateThis reaction proceeds in the forward direction.
- (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + O2 = (8S)-hydroperoxy-(14S,15R)-epoxy-(5Z,9E,11Z)-eicosatrienoateThis reaction proceeds in the forward direction.
- (15R)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H2OThis reaction proceeds in the forward direction.
- (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = (14S,15S)-epoxy-(5Z,8Z,10E,12E)-eicosatetraenoate + H2OThis reaction proceeds in the forward direction.
- (4Z,7Z,10Z,13Z,16Z)-docosapentaenoate + O2 = 14-hydroperoxy-(4Z,7Z,10Z,12E,16Z)-docosapentaenoateThis reaction proceeds in the forward direction.
- (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (11S)-hydroperoxy-(4Z,7Z,9E,13Z,16Z,19Z)-docosahexaenoateThis reaction proceeds in the forward direction.
- (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (14S)-hydroperoxy-(4Z,7Z,10Z,12E,16Z,19Z)-docosahexaenoateThis reaction proceeds in the forward direction.
- (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (17S)-hydroperoxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoateThis reaction proceeds in the forward direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoate + 2 O2 = (14R,15S)-dihydroperoxy-(5Z,8Z,10E,12E)-eicosatetraenoateThis reaction proceeds in the forward direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoate + 2 O2 = (8S,15S)-dihydroperoxy-(5Z,9E,11Z,13E)-eicosatetraenoateThis reaction proceeds in the forward direction.
- (7S)-hydroperoxy-(4Z,8E,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (7S,14S)-dihydroperoxy-(4Z,8E,10Z,12E,16Z,19Z)-docosahexaenoateThis reaction proceeds in the forward direction.
- (7S)-hydroperoxy-(4Z,8E,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (7S,17S)-dihydroperoxy-(4Z,8E,10Z,13Z,15E,19Z)-docosahexaenoateThis reaction proceeds in the forward direction.
- (7Z,10Z,13Z,16Z,19Z)-docosapentaenoate + O2 = 14-hydroperoxy-(7Z,10Z,12E,16Z,19Z)-docosapentaenoateThis reaction proceeds in the forward direction.
- N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-alanine + O2 = N-(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-alanineThis reaction proceeds in the forward direction.
- N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-alanine + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-alanineThis reaction proceeds in the forward direction.
- N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-gamma-aminobutanoate + O2 = N-(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-gamma-aminobutanoateThis reaction proceeds in the forward direction.
- N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-gamma-aminobutanoate + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-gamma-aminobutanoateThis reaction proceeds in the forward direction.
- N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine + O2 = N-(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-glycineThis reaction proceeds in the forward direction.
- N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-glycineThis reaction proceeds in the forward direction.
- N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-taurine + O2 = N-(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-taurineThis reaction proceeds in the forward direction.
- N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-taurine + O2 = N-(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-taurineThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 Fe cation per subunit.
Pathway
Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 17 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 74 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 75 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Site | 100 | Essential for stabilizing binding to COTL1 | |||
Binding site | 361 | Fe cation (UniProtKB | ChEBI); catalytic | |||
Binding site | 366 | Fe cation (UniProtKB | ChEBI); catalytic | |||
Binding site | 541 | Fe cation (UniProtKB | ChEBI); catalytic | |||
Binding site | 663 | Fe cation (UniProtKB | ChEBI); catalytic | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | lipid droplet | |
Cellular Component | plasma membrane | |
Molecular Function | arachidonate 12(S)-lipoxygenase activity | |
Molecular Function | arachidonate 15-lipoxygenase activity | |
Molecular Function | iron ion binding | |
Molecular Function | lipid binding | |
Biological Process | arachidonic acid metabolic process | |
Biological Process | hepoxilin biosynthetic process | |
Biological Process | linoleic acid metabolic process | |
Biological Process | lipid oxidation | |
Biological Process | lipoxygenase pathway |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePolyunsaturated fatty acid lipoxygenase ALOX15
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Scandentia > Tupaiidae > Tupaia
Accessions
- Primary accessionA0A8A0R1W6
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
Interaction
Subunit
Interacts with PEBP1; in response to IL13/interleukin-13, prevents the interaction of PEBP1 with RAF1 to activate the ERK signaling cascade.
Structure
Sequence
- Sequence statusFragment
- Length663
- Mass (Da)75,206
- Last updated2021-09-29 v1
- ChecksumC700622C0C3A424C
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Non-terminal residue | 663 | ||||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MW690658 EMBL· GenBank· DDBJ | QSQ01680.1 EMBL· GenBank· DDBJ | mRNA |