oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
lipid binding
arachidonate 15-lipoxygenase activity
arachidonate 12(S)-lipoxygenase activity
Cellular component
cytoplasm
cytosol
membrane
extrinsic component of cytoplasmic side of plasma membrane
lipid droplet
plasma membrane
Biological process
cellular response to calcium ion
bone mineralization
leukotriene metabolic process
positive regulation of heterotypic cell-cell adhesion
positive regulation of actin filament polymerization
negative regulation of adaptive immune response
ossification
lipoxin A4 biosynthetic process
lipid metabolism
wound healing
phosphatidylethanolamine biosynthetic process
regulation of peroxisome proliferator activated receptor signaling pathway
response to endoplasmic reticulum stress
fatty acid metabolic process
apoptotic cell clearance
lipoxygenase pathway
hepoxilin biosynthetic process
regulation of engulfment of apoptotic cell
positive regulation of ERK1 and ERK2 cascade
inflammatory response
cellular response to interleukin-13
positive regulation of cell-substrate adhesion
arachidonic acid metabolic process
cytokine-mediated signaling pathway
long-chain fatty acid biosynthetic process
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
246
11687
Ensembl
ENSG00000161905
ENSMUSG00000018924
UniProt
P16050
P39654
RefSeq (mRNA)
NM_001140
NM_009660
RefSeq (protein)
NP_001131
NP_033790
Location (UCSC)
Chr 17: 4.63 – 4.64 Mb
Chr 11: 70.23 – 70.24 Mb
PubMed search
[3]
[4]
Wikidata
View/Edit Human
View/Edit Mouse
ALOX15 (also termed arachidonate 15-lipoxygenase, 15-lipoxygenase-1, 15-LO-1, 15-LOX-1) is, like other lipoxygenases, a seminal enzyme in the metabolism of polyunsaturated fatty acids to a wide range of physiologically and pathologically important products.
▼ Gene Function
Kelavkar and Badr (1999) stated that the ALOX15 gene product is implicated in antiinflammation, membrane remodeling, and cancer development/metastasis. Kelavkar and Badr (1999) described experiments yielding data that supported the hypothesis that loss of the TP53 gene, or gain-of-function activities resulting from the expression of its mutant forms, regulates ALOX15 promoter activity in human and in mouse, albeit in directionally opposite manners. These studies defined a direct link between ALOX15 gene activity and an established tumor-suppressor gene located in close chromosomal proximity. Kelavkar and Badr (1999) referred to this as evidence that 15-lipoxygenase is a mutator gene.
▼ Mapping
By PCR analysis of a human-hamster somatic hybrid DNA panel, Funk et al. (1992) demonstrated that genes for 12-lipoxygenase and 15-lipoxygenase are located on human chromosome 17, whereas the most unrelated lipoxygenase (5-lipoxygenase) was mapped to chromosome 10.
Kelavkar and Badr (1999) stated that the ALOX15 gene maps to 17p13.3 in close proximity to the tumor-suppressor gene TP53 (191170). In humans, it is encoded by the ALOX15 gene located on chromosome 17p13.3.[5] This 11 kilobase pair gene consists of 14 exons and 13 introns coding for a 75 kilodalton protein composed of 662 amino acids. 15-LO is to be distinguished from another human 15-lipoxygenase enzyme, ALOX15B (also termed 15-lipoxygenase-2).[6] Orthologs of ALOX15, termed Alox15, are widely distributed in animal and plant species but commonly have different enzyme activities and make somewhat different products than ALOX15.
^ abcGRCh38: Ensembl release 89: ENSG00000161905 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000018924 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Funk CD, Funk LB, FitzGerald GA, Samuelsson B (May 1992). "Characterization of human 12-lipoxygenase genes". Proceedings of the National Academy of Sciences of the United States of America. 89 (9): 3962–6. Bibcode:1992PNAS...89.3962F. doi:10.1073/pnas.89.9.3962. PMC 525611. PMID 1570320.
^Ivanov I, Kuhn H, Heydeck D (November 2015). "Structural and functional biology of arachidonic acid 15-lipoxygenase-1 (ALOX15)". Gene. 573 (1): 1–32. doi:10.1016/j.gene.2015.07.073. PMC 6728142. PMID 26216303.
ALOX15 (also termed arachidonate 15-lipoxygenase, 15-lipoxygenase-1, 15-LO-1, 15-LOX-1) is, like other lipoxygenases, a seminal enzyme in the metabolism...
similar fashions, 15-lipoxygenase (15-lipoxygenase 1, 15-LOX, 15-LOX1, or ALOX15) initiates the metabolism of arachidonic acid to 15-HpETE, 15-HETE, eoxins...
(also see 5-Hydroxyeicosatetraenoic acid). The enzymes 15-lipoxygenase-1 (ALOX15) and 15-lipoxygenase-2 (ALOX15B). ALOX15B catalyzes the oxidation of arachidonic...
deemed an ortholog of ALOX15 and is designated as Alox15. Human ALOX12 and ALOX15 along with rodent leukocyte-type Alox12 and Alox15 are commonly termed...
15-lipoxygenase-2 (15-LO-2 or 15-LOX-2), is distinguished from its related oxygenase, ALOX15 or 15-lipoxygenase-1. This gene encodes a member of the lipoxygenase family...
15-oxo-eicosatetraenoic acid is an eicosanoid metabolite of arachidonic acid made my ALOX15; it has weak chemotactic activity for human monocytes (sees 15-Hydroxyeicosatetraenoic...
the maresins, this class of mediators includes: the 15-lipoxygenase (i.e. ALOX15 and/or possibly ALOX15B)-derived lipoxin A4 and B4 metabolites of the omega...
leukotriene and 5-hydroxyicosatetraenoic acid metabolites and 15-lipoxygenase (ALOX15) to overproduce pro-inflammatory 15-hydroxyicosatetraenoic acid metabolites...
catalyzed by enzymes with 15-lipoxygenase activity which in humans includes ALOX15, ALOX12, aspirin-treated cyclooxygenase 2, and cytochrome P450s of the microsomal...
distinction to the other three human lipoxygenases (ALOX5, ALOX12, and ALOX15), because they were initially defined as being highly or even exclusively...
activity may be responsible for blocking the formation of the hepoxilins. ALOX15 is responsible for metabolizing arachidonic acid to 14,15-HxA3 and 14,15-HxB3...
regulation of the animals’ ability to survive in low-oxygen environments (ALOX15). In the Yosemite transect, no significant change in avian species abundance...