ALOX12

Arachidonate 12-lipoxygenase

Rendering based on PDB 2ABU.

Available structures
PDB	2ABU, 3D3L

Identifiers

Symbols

ALOX12; 12-LOX; 12S-LOX; LOG12

External IDs

OMIM: 152391 MGI: 87998 HomoloGene: 560 GeneCards: ALOX12 Gene

EC number

1.13.11.31

Gene Ontology
Molecular function	• arachidonate 12-lipoxygenase activity • iron ion binding • protein binding • lipoxygenase activity • oxidoreductase activity • metal ion binding • hepoxilin-epoxide hydrolase activity
Cellular component	• cytoplasm • cytosol • sarcolemma
Biological process	• anti-apoptosis • anti-apoptosis • cellular component movement • positive regulation of cell proliferation • positive regulation of cell proliferation • positive regulation of endothelial cell migration • positive regulation of gene expression • leukotriene biosynthetic process • fatty acid oxidation • positive regulation of cell growth • negative regulation of cell killing • positive regulation of cell killing • superoxide anion generation • positive regulation of apoptosis • positive regulation of caspase activity • positive regulation of endothelial cell differentiation • positive regulation of cell adhesion • response to protein stimulus • positive regulation of mitochondrial depolarization • reactive oxygen species metabolic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 17:
6.9 – 6.91 Mb

Chr 11:
70.05 – 70.07 Mb

PubMed search

[1]

[2]

Arachidonate 12-lipoxygenase, 12S-type is an enzyme that in humans is encoded by the ALOX12 gene.^[1]^[2]

Interactions

ALOX12 has been shown to interact with Keratin 5^[3] and LMNA.^[3]

References

^ Funk CD, Funk LB, FitzGerald GA, Samuelsson B (May 1992). "Characterization of human 12-lipoxygenase genes". Proc Natl Acad Sci U S A 89 (9): 3962–6. doi:10.1073/pnas.89.9.3962. PMC 525611. PMID 1570320. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=525611.
^ "Entrez Gene: ALOX12 arachidonate 12-lipoxygenase". http://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=retrieve&dopt=default&list_uids=239&rn=1.
^ ^a ^b Tang, K; Finley; Finley R L, Nie D, Honn K V (Mar. 2000). "Identification of 12-lipoxygenase interaction with cellular proteins by yeast two-hybrid screening". Biochemistry (UNITED STATES) 39 (12): 3185–91. doi:10.1021/bi992664v. ISSN 0006-2960. PMID 10727209.

Yoshimoto T, Arakawa T, Hada T, et al. (1992). "Structure and chromosomal localization of human arachidonate 12-lipoxygenase gene". J. Biol. Chem. 267 (34): 24805–9. PMID 1447217.
Izumi T, Hoshiko S, Rådmark O, Samuelsson B (1990). "Cloning of the cDNA for human 12-lipoxygenase". Proc. Natl. Acad. Sci. U.S.A. 87 (19): 7477–81. doi:10.1073/pnas.87.19.7477. PMC 54770. PMID 2217179. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=54770.
Yoshimoto T, Yamamoto Y, Arakawa T, et al. (1990). "Molecular cloning and expression of human arachidonate 12-lipoxygenase". Biochem. Biophys. Res. Commun. 172 (3): 1230–5. doi:10.1016/0006-291X(90)91580-L. PMID 2244907.
Funk CD, Furci L, FitzGerald GA (1990). "Molecular cloning, primary structure, and expression of the human platelet/erythroleukemia cell 12-lipoxygenase". Proc. Natl. Acad. Sci. U.S.A. 87 (15): 5638–42. doi:10.1073/pnas.87.15.5638. PMC 54382. PMID 2377602. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=54382.
Flatman S, Morgan A, McDonald-Gibson RG, et al. (1988). "12-Lipoxygenase activity in human uterine cervix". Prostaglandins Leukot. Essent. Fatty Acids 32 (2): 87–94. doi:10.1016/0952-3278(88)90101-9. PMID 3406043.
Wong PY, Westlund P, Hamberg M, et al. (1985). "15-Lipoxygenase in human platelets". J. Biol. Chem. 260 (16): 9162–5. PMID 3926763.
Nakamura M, Ueda N, Kishimoto K, et al. (1995). "Immunocytochemical localization of platelet-type arachidonate 12-lipoxygenase in mouse blood cells". J. Histochem. Cytochem. 43 (3): 237–44. doi:10.1177/43.3.7868854. PMID 7868854.
Hussain H, Shornick LP, Shannon VR, et al. (1994). "Epidermis contains platelet-type 12-lipoxygenase that is overexpressed in germinal layer keratinocytes in psoriasis". Am. J. Physiol. 266 (1 Pt 1): C243–53. PMID 8304420.
Arora JK, Lysz TW, Zelenka PS (1996). "A role for 12(S)-HETE in the response of human lens epithelial cells to epidermal growth factor and insulin". Invest. Ophthalmol. Vis. Sci. 37 (7): 1411–8. PMID 8641843.
Hagmann W, Gao X, Timar J, et al. (1996). "12-Lipoxygenase in A431 cells: genetic identity, modulation of expression, and intracellular localization". Exp. Cell Res. 228 (2): 197–205. doi:10.1006/excr.1996.0317. PMID 8912711.
Nakamura M, Yamamoto S, Ishimura K (1997). "Subcellular localization of arachidonate 12-lipoxygenase and morphological effect of its overexpression on murine keratinocytes". Cell Tissue Res. 288 (2): 327–34. doi:10.1007/s004410050818. PMID 9082968.
Nigam S, Kumar GS, Sutherland M, et al. (1999). "Metabolic suppression of platelet-type 12-lipoxygenase in human uterine cervix with invasive carcinoma". Int. J. Cancer 82 (6): 827–31. doi:10.1002/(SICI)1097-0215(19990909)82:6<827::AID-IJC10>3.0.CO;2-Q. PMID 10446449.
Tang K, Finley RL, Nie D, Honn KV; Finley (2000). "Identification of 12-lipoxygenase interaction with cellular proteins by yeast two-hybrid screening". Biochemistry 39 (12): 3185–91. doi:10.1021/bi992664v. PMID 10727209.
Tornhamre S, Elmqvist A, Lindgren JA (2000). "15-Lipoxygenation of leukotriene A(4). Studies Of 12- and 15-lipoxygenase efficiency to catalyze lipoxin formation". Biochim. Biophys. Acta 1484 (2–3): 298–306. doi:10.1016/S1388-1981(00)00017-2. PMID 10760478.
Chen BK, Tsai TY, Huang HS, et al. (2003). "Functional role of extracellular signal-regulated kinase activation and c-Jun induction in phorbol ester-induced promoter activation of human 12(S)-lipoxygenase gene". J. Biomed. Sci. 9 (2): 156–65. PMID 11914583.
Winer I, Normolle DP, Shureiqi I, et al. (2003). "Expression of 12-lipoxygenase as a biomarker for melanoma carcinogenesis". Melanoma Res. 12 (5): 429–34. doi:10.1097/00008390-200209000-00003. PMID 12394183.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Gu J, Wen Y, Mison A, Nadler JL (2003). "12-lipoxygenase pathway increases aldosterone production, 3',5'-cyclic adenosine monophosphate response element-binding protein phosphorylation, and p38 mitogen-activated protein kinase activation in H295R human adrenocortical cells". Endocrinology 144 (2): 534–43. doi:10.1210/en.2002-220580. PMID 12538614.
Fridman C, Ojopi EP, Gregório SP, et al. (2003). "Association of a new polymorphism in ALOX12 gene with bipolar disorder". European archives of psychiatry and clinical neuroscience 253 (1): 40–3. doi:10.1007/s00406-003-0404-y. PMID 12664313.

Oxidoreductases: monooxygenases (EC 1.13)

1.13.11: two atoms of oxygen	lipoxygenase: Arachidonate 5-lipoxygenase · Arachidonate 12-lipoxygenase/ALOX12 · Arachidonate 8-lipoxygenase · Arachidonate 15-lipoxygenase/ALOX15 · Linoleate 11-lipoxygenase other dioxygenase: Catechol dioxygenase · Homogentisate 1,2-dioxygenase · Cysteine dioxygenase · 4-Hydroxyphenylpyruvate dioxygenase · Indoleamine 2,3-dioxygenase

1.13.12: one atom of oxygen	Firefly luciferase

1.13.99: other	Inositol oxygenase

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

ALOX12

Interactions

References

Further reading