ALOX15B

ALOX15B
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4NRE
Identifiers
Aliases	ALOX15B, 15-LOX-2, arachidonate 15-lipoxygenase, type B, arachidonate 15-lipoxygenase type B
External IDs	OMIM: 603697; MGI: 1098228; HomoloGene: 886; GeneCards: ALOX15B; OMA:ALOX15B - orthologs
Gene location (Human) Chr. Chromosome 17 (human) Band 17p13.1 Start 8,039,034 bp End 8,049,134 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11|11 B3 Start 69,074,758 bp End 69,088,669 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in skin of thigh skin of arm vulva prostate right lung nipple vagina skin of abdomen upper lobe of lung upper lobe of left lung Top expressed in lip dentate gyrus of hippocampal formation granule cell embryo hair follicle skin of external ear superior frontal gyrus primary visual cortex otic vesicle cerebellar cortex skin of abdomen More reference expression data BioGPS More reference expression data
Gene ontology Molecular function iron ion binding calcium ion binding dioxygenase activity metal ion binding arachidonate 8(S)-lipoxygenase activity linoleate 13S-lipoxygenase activity oxidoreductase activity oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen lipid binding arachidonate 15-lipoxygenase activity Cellular component intracellular anatomical structure extracellular exosome extrinsic component of membrane cytosol nucleus membrane cytoskeleton plasma membrane cytoplasm Biological process apoptotic process linoleic acid metabolic process negative regulation of growth lipid metabolism positive regulation of keratinocyte differentiation negative regulation of cell cycle prostate gland development lipoxygenase pathway hepoxilin biosynthetic process positive regulation of macrophage derived foam cell differentiation negative regulation of cell migration positive regulation of peroxisome proliferator activated receptor signaling pathway regulation of epithelial cell differentiation negative regulation of cell population proliferation arachidonic acid metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 247 11688 Ensembl ENSG00000179593 ENSMUSG00000020891 UniProt O15296 O35936 RefSeq (mRNA) NM_001141 NM_001039130 NM_001039131 NM_009661 RefSeq (protein) NP_001034219 NP_001034220 NP_001132 NP_033791 Location (UCSC) Chr 17: 8.04 – 8.05 Mb Chr 11: 69.07 – 69.09 Mb PubMed search
Wikidata
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Arachidonate 15-lipoxygenase type II is an enzyme that in humans is encoded by the ALOX15B gene. 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. 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. 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.

See also

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

External links

• Human ALOX15B genome location and ALOX15B gene details page in the UCSC Genome Browser.

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. doi:10.1016/S0021-9258(19)34092-X. 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. 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.