Primary Information |
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| BoMiProt ID | Bomi303 |
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| Protein Name | Arachidonate 12-lipoxygenase, 12S-type |
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| Organism | Bos taurus |
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| Uniprot ID | P27479 |
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| Milk Fraction | MFGM, Exosome |
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| Ref Sequence ID | NP_776926.1 |
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| Aminoacid Length | 663 |
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| Molecular Weight | 75124 |
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| FASTA Sequence |
Download |
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| Gene Name | ALOX15 |
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| Gene ID | 282139 |
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| Protein Existence Status | Reviewed: Experimental evidence at protein level |
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Secondary Information |
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| Protein Function | heterogeneous family of lipid peroxidizing enzymes capable
of oxygenating polyunsaturated fatty acids to their corresponding hydroperoxy derivatives; involved in cell differentiation, inflammation, carcinogenesis and atherogenesis; Products of the 15-LOX pathway may also play a role in earlier erythropoiesis; may also be related to the differentiation of other cell types; xhibit a pro-atherogenic activity; have also been implicated in the synthesis of more complex bioactive lipid
mediators, such as lipoxins and hepoxilins |
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| Biochemical Properties | LOXs are classified with respect to their positional specificity of arachidonic acid oxygenation
into 5-, 8-, 12-, and 15-LOXs; leukocyte-type 12-LOXs are very similar
to the reticulocyte-type 15-LOXs, these enzymes are designated 12/15-LOXs; contains one non-heme iron per mole enzyme
and four histidines (H361, H366, H541, H545) and the C-terminal isoleucine constitute the
protein iron ligands; Ferrous LOXs are catalytically inactive and require activation by hydroperoxy fatty acids,
which involves oxidation of the non-heme iron to a ferric form |
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| PTMs | No major PTMs; elements of post-translational regulation are nitric oxide and calcium |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | Nitric oxide (NO) appears to be of regulatory importance for the 15-LOX pathway; during NO/15-LOX
interaction an oxidation of the ferrous non-heme iron may take place; membrane association with calcium increases of the fatty acid oxygenase activity |
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| Bibliography | 1. Antón, R. and Vila, L. (2000) ‘Stereoselective Biosynthesis of Hepoxilin B3 in Human Epidermis’, Journal of Investigative Dermatology, 114(3), pp. 554–559. doi: 10.1046/j.1523-1747.2000.00903.x.
2. Brinckmann, R. et al. (1998) ‘Membrane translocation of 15-lipoxygenase in hematopoietic cells is calcium-dependent and activates the oxygenase activity of the enzyme.’, Blood, 91(1), pp. 64–74. Available at: http://www.ncbi.nlm.nih.gov/pubmed/9414270 (Accessed: 4 October 2019). |
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