ALOX15B

Arachidonate 15-lipoxygenase, type B
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 4NRE​
Identifiers
Symbols	ALOX15B ; 15-LOX-2
External IDs	OMIM: 603697 MGI: 1098228 HomoloGene: 886 IUPHAR: 1389 ChEMBL: 2457 GeneCards: ALOX15B Gene
EC number	1.13.11.33
Gene ontology Molecular function • iron ion binding • calcium ion binding • lipid binding • linoleate 13S-lipoxygenase activity • arachidonate 8(S)-lipoxygenase activity • arachidonate 15-lipoxygenase activity Cellular component • intracellular • nucleus • cytoplasm • cytosol • cytoskeleton • plasma membrane • membrane • extrinsic component of membrane • extracellular exosome Biological process • lipid metabolic process • apoptotic process • negative regulation of cell proliferation • positive regulation of macrophage derived foam cell differentiation • arachidonic acid metabolic process • lipoxygenase pathway • negative regulation of cell migration • prostate gland development • regulation of epithelial cell differentiation • positive regulation of peroxisome proliferator activated receptor signaling pathway • linoleic acid metabolic process • small molecule metabolic process • positive regulation of keratinocyte differentiation • negative regulation of cell cycle • negative regulation of growth • hepoxilin biosynthetic process • oxidation-reduction process • positive regulation of chemokine secretion Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	247	11688
Ensembl	ENSG00000179593	ENSMUSG00000020891
UniProt	O15296	O35936
RefSeq (mRNA)	NM_001039130	NM_009661
RefSeq (protein)	NP_001034219	NP_033791
Location (UCSC)	Chr 17: 8.04 – 8.05 Mb	Chr 11: 69.18 – 69.2 Mb
PubMed search

Arachidonate 15-lipoxygenase type II is an enzyme that in humans is encoded by the ALOX15B gene.^[1][2] ALOX15B, also known as 15-lipoxygenase-2 (15-LO-2 or 15-LOX-2), is distinguished from its related oxygenase, ALOX15 or 15-lipoxygenase-1.

Function

This gene encodes a member of the lipoxygenase family of structurally related nonheme iron dioxygenases involved in the production of fatty acid hydroperoxides. 15-LOX-2 has 38-39% amino acid sequence identity to human 15-LOX-1 and 12-lipoxygenase and 44% amino acid sequence identity to human 5-lipoxygenase.^[1] 15-LOX-2 converts arachidonic acid almost exclusively to the S stereoisomer of 15-Hydroperoxyicosatetraenoic acid which is commonly reduced to the S stereoisomer 15-Hydroxyeicosatetraenoic acid by ubiquitous cellular peroxidases; it metabolizes linoleic acid less effectively, converting this fatty acid to the S stereoisomer of 13-hydroperoxyoctadecadienoic acid which is likewise rapidly reduced to the S stereoisomer of 13-Hydroxyoctadecadienoic acid.^[1] The ALOX15B gene is located in a cluster of related genes and a pseudogene that spans approximately 100 kilobases on the short arm of chromosome 17. Alternatively spliced transcript variants encoding different isoforms have been described.^[2]

See also

• Arachidonate 15-lipoxygenase
• 15-hydroxyicosatetraenoic acid
• ALOX15

References

1. Brash AR, Boeglin WE, Chang MS (Jun 1997). "Discovery of a second 15S-lipoxygenase in humans". Proceedings of the National Academy of Sciences of the United States of America 94 (12): 6148–52. doi:10.1073/pnas.94.12.6148. PMC 21017. PMID 9177185.
2. "Entrez Gene: ALOX15B arachidonate 15-lipoxygenase, type B".

Further reading

• Sigal E, Grunberger D, Highland E, Gross C, Dixon RA, Craik CS (Mar 1990). "Expression of cloned human reticulocyte 15-lipoxygenase and immunological evidence that 15-lipoxygenases of different cell types are related". The Journal of Biological Chemistry 265 (9): 5113–20. PMID 2318885.
• Kilty I, Logan A, Vickers PJ (Nov 1999). "Differential characteristics of human 15-lipoxygenase isozymes and a novel splice variant of 15S-lipoxygenase". European Journal of Biochemistry / FEBS 266 (1): 83–93. doi:10.1046/j.1432-1327.1999.00818.x. PMID 10542053.
• Krieg P, Marks F, Fürstenberger G (May 2001). "A gene cluster encoding human epidermis-type lipoxygenases at chromosome 17p13.1: cloning, physical mapping, and expression". Genomics 73 (3): 323–30. doi:10.1006/geno.2001.6519. PMID 11350124.
• Tang S, Bhatia B, Maldonado CJ, Yang P, Newman RA, Liu J, Chandra D, Traag J, Klein RD, Fischer SM, Chopra D, Shen J, Zhau HE, Chung LW, Tang DG (May 2002). "Evidence that arachidonate 15-lipoxygenase 2 is a negative cell cycle regulator in normal prostate epithelial cells". The Journal of Biological Chemistry 277 (18): 16189–201. doi:10.1074/jbc.M111936200. PMID 11839751.
• Xu XC, Shappell SB, Liang Z, Song S, Menter D, Subbarayan V, Iyengar S, Tang DG, Lippman SM (2003). "Reduced 15S-lipoxygenase-2 expression in esophageal cancer specimens and cells and upregulation in vitro by the cyclooxygenase-2 inhibitor, NS398". Neoplasia 5 (2): 121–7. doi:10.1016/s1476-5586(03)80003-9. PMC 1502398. PMID 12659684.
• Bhatia B, Maldonado CJ, Tang S, Chandra D, Klein RD, Chopra D, Shappell SB, Yang P, Newman RA, Tang DG (Jul 2003). "Subcellular localization and tumor-suppressive functions of 15-lipoxygenase 2 (15-LOX2) and its splice variants". The Journal of Biological Chemistry 278 (27): 25091–100. doi:10.1074/jbc.M301920200. PMID 12704195.
• Tang S, Bhatia B, Zhou J, Maldonado CJ, Chandra D, Kim E, Fischer SM, Butler AP, Friedman SL, Tang DG (Sep 2004). "Evidence that Sp1 positively and Sp3 negatively regulate and androgen does not directly regulate functional tumor suppressor 15-lipoxygenase 2 (15-LOX2) gene expression in normal human prostate epithelial cells". Oncogene 23 (41): 6942–53. doi:10.1038/sj.onc.1207913. PMID 15247906.
• Suzuki Y, Yamashita R, Shirota M, Sakakibara Y, Chiba J, Mizushima-Sugano J, Nakai K, Sugano S (Sep 2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Research 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
• Limor R, Kaplan M, Sawamura T, Sharon O, Keidar S, Weisinger G, Knoll E, Naidich M, Stern N (Mar 2005). "Angiotensin II increases the expression of lectin-like oxidized low-density lipoprotein receptor-1 in human vascular smooth muscle cells via a lipoxygenase-dependent pathway". American Journal of Hypertension 18 (3): 299–307. doi:10.1016/j.amjhyper.2004.09.008. PMID 15797645.
• Subbarayan V, Xu XC, Kim J, Yang P, Hoque A, Sabichi AL, Llansa N, Mendoza G, Logothetis CJ, Newman RA, Lippman SM, Menter DG (Mar 2005). "Inverse relationship between 15-lipoxygenase-2 and PPAR-gamma gene expression in normal epithelia compared with tumor epithelia". Neoplasia 7 (3): 280–93. doi:10.1593/neo.04457. PMC 1501140. PMID 15799828.
• Jiang WG, Watkins G, Douglas-Jones A, Mansel RE (Apr 2006). "Reduction of isoforms of 15-lipoxygenase (15-LOX)-1 and 15-LOX-2 in human breast cancer". Prostaglandins, Leukotrienes, and Essential Fatty Acids 74 (4): 235–45. doi:10.1016/j.plefa.2006.01.009. PMID 16556493.
• Subbarayan V, Krieg P, Hsi LC, Kim J, Yang P, Sabichi AL, Llansa N, Mendoza G, Logothetis CJ, Newman RA, Lippman SM, Menter DG (Sep 2006). "15-Lipoxygenase-2 gene regulation by its product 15-(S)-hydroxyeicosatetraenoic acid through a negative feedback mechanism that involves peroxisome proliferator-activated receptor gamma". Oncogene 25 (44): 6015–25. doi:10.1038/sj.onc.1209617. PMID 16682954.
• Lesueur F, Bouadjar B, Lefèvre C, Jobard F, Audebert S, Lakhdar H, Martin L, Tadini G, Karaduman A, Emre S, Saker S, Lathrop M, Fischer J (Apr 2007). "Novel mutations in ALOX12B in patients with autosomal recessive congenital ichthyosis and evidence for genetic heterogeneity on chromosome 17p13". The Journal of Investigative Dermatology 127 (4): 829–34. doi:10.1038/sj.jid.5700640. PMID 17139268.