PLA2G1B

PLA2G1B
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3ELO
Identifiers
Aliases	PLA2G1B, PLA2, PLA2A, PPLA2, phospholipase A2 group IB
External IDs	OMIM: 172410 MGI: 101842 HomoloGene: 715 GeneCards: PLA2G1B
Gene location (Human)
Chr.	Chromosome 12 (human)
End	120,327,779 bp
Gene location (Mouse)
Chr.	Chromosome 5 (mouse)
End	115,612,781 bp
RNA expression pattern
	Top expressed in
	body of pancreas; ; islet of Langerhans; ; lower lobe of lung; ; sperm; ; upper lobe of lung; ; right lung; ; upper lobe of left lung; ; right adrenal gland; ; left adrenal gland; ; right lobe of liver;
	Top expressed in
	epithelium of stomach; ; pyloric antrum; ; mucous cell of stomach; ; islet of Langerhans; ; duodenum; ; esophagus; ; right lung; ; left lung; ; left lung lobe; ; right lung lobe;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	calcium ion binding; calcium-dependent phospholipase A2 activity; metal ion binding; bile acid binding; signaling receptor binding; hydrolase activity; phospholipase A2 activity; phospholipid binding;
Cellular component	secretory granule; extracellular region; cell surface; extracellular space; cytosol;
Biological process	phosphatidic acid biosynthetic process; phosphatidylserine acyl-chain remodeling; intracellular signal transduction; phosphatidylethanolamine acyl-chain remodeling; positive regulation of calcium ion transport into cytosol; lipid metabolism; actin filament organization; interleukin-8 production; phosphatidylinositol acyl-chain remodeling; activation of phospholipase A2 activity; neutrophil chemotaxis; fatty acid biosynthetic process; positive regulation of immune response; innate immune response in mucosa; positive regulation of NF-kappaB transcription factor activity; phosphatidylglycerol acyl-chain remodeling; positive regulation of protein secretion; cellular response to insulin stimulus; neutrophil mediated immunity; leukotriene biosynthetic process; phosphatidylcholine metabolic process; phosphatidylcholine acyl-chain remodeling; positive regulation of transcription by RNA polymerase II; signal transduction; phospholipid metabolic process; arachidonic acid secretion; antimicrobial humoral immune response mediated by antimicrobial peptide; regulation of glucose import; positive regulation of cell population proliferation; lipid catabolic process; positive regulation of fibroblast proliferation; antibacterial humoral response; defense response to Gram-positive bacterium;
	Sources:Amigo / QuickGO
Orthologs
	5319
	18778
	ENSG00000170890
	ENSMUSG00000029522
	P04054
	Q9Z0Y2
	NM_000928
	NM_011107; NM_001356586; NM_001356587
	NP_000919
	NP_035237; NP_001343515; NP_001343516
	Wikidata
View/Edit Human	View/Edit Mouse

Phospholipase A2, group 1B is an enzyme that in humans is encoded by the PLA2G1B gene.^[5]^[6]

Function

Phospholipase A2 (EC 3.1.1.4) catalyzes the release of fatty acids from glycero-3-phosphocholines. The best known varieties are the digestive enzymes secreted as zymogens by the pancreas of mammals as well as fish.^[7] Sequences of pancreatic PLA2 enzymes from a variety of mammals have been reported. One striking feature of these enzymes is their close homology to venom phospholipases of snakes. Other forms of PLA2 have been isolated from brain, liver, lung, spleen, intestine, macrophages, leukocytes, erythrocytes, inflammatory exudates, chondrocytes, and platelets (Seilhamer et al., 1986) .^[6]^[8]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000170890 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000029522 - 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.
↑ Dennis EA (Jun 1994). "Diversity of group types, regulation, and function of phospholipase A2". J Biol Chem. 269 (18): 13057–60. doi:10.1016/S0021-9258(17)36794-7. PMID 8175726.
1 2 "Entrez Gene: PLA2G1B phospholipase A2, group IB (pancreas)".
↑ Sæle O, Nordgreen A, Olsvik PA, Hamre K (2010). "Characterisation and expression of secretory phospholipase A2 group IB during ontogeny of Atlantic cod ( Gadus morhua)". Br J Nutr. 105 (2): 1–10. doi:10.1017/S0007114510003466. PMID 20836903.
↑ Seilhamer JJ, Randall TL, Yamanaka M, Johnson LK (1987). "Pancreatic phospholipase A2: isolation of the human gene and cDNAs from porcine pancreas and human lung". DNA. 5 (6): 519–27. doi:10.1089/dna.1.1986.5.519. PMID 3028739.

Schröder HC, Perovic S, Kavsan V, et al. (1998). "Mechanisms of prionSc- and HIV-1 gp120 induced neuronal cell death". Neurotoxicology. 19 (4–5): 683–8. PMID 9745929.
Sapirstein A, Bonventre JV (2000). "Phospholipases A2 in ischemic and toxic brain injury". Neurochem. Res. 25 (5): 745–53. doi:10.1023/A:1007583708713. PMID 10905638. S2CID 30097342.
Svensson CI, Yaksh TL (2002). "The spinal phospholipase-cyclooxygenase-prostanoid cascade in nociceptive processing". Annu. Rev. Pharmacol. Toxicol. 42: 553–83. doi:10.1146/annurev.pharmtox.42.092401.143905. PMID 11807183.
Clark MA, Ozgür LE, Conway TM, et al. (1991). "Cloning of a phospholipase A2-activating protein". Proc. Natl. Acad. Sci. U.S.A. 88 (12): 5418–22. Bibcode:1991PNAS...88.5418C. doi:10.1073/pnas.88.12.5418. PMC 51884. PMID 2052621.
Verheij HM, Westerman J, Sternby B, De Haas GH (1983). "The complete primary structure of phospholipase A2 from human pancreas". Biochim. Biophys. Acta. 747 (1–2): 93–9. doi:10.1016/0167-4838(83)90126-7. PMID 6349696.
Sternby B, Akerström B (1984). "Immunoreactive pancreatic colipase, lipase and phospholipase A2 in human plasma and urine from healthy individuals". Biochim. Biophys. Acta. 789 (2): 164–9. doi:10.1016/0167-4838(84)90201-2. PMID 6477929.
Grataroli R, Dijkman R, Dutilh CE, et al. (1982). "Studies on prophospholipase A2 and its enzyme from human pancreatic juice. Catalytic properties and sequence of the N-terminal region". Eur. J. Biochem. 122 (1): 111–7. doi:10.1111/j.1432-1033.1982.tb05855.x. PMID 7060561.
Rönkkö S (1995). "Immunohistochemical localization of phospholipase A2 in human and bovine male reproductive organs". Comp. Biochem. Physiol. B. 110 (3): 503–9. doi:10.1016/0305-0491(94)00190-6. PMID 7584826.
Lilja I, Smedh K, Olaison G, et al. (1995). "Phospholipase A2 gene expression and activity in histologically normal ileal mucosa and in Crohn's ileitis". Gut. 37 (3): 380–5. doi:10.1136/gut.37.3.380. PMC 1382819. PMID 7590434.
Ancian P, Lambeau G, Mattéi MG, Lazdunski M (1995). "The human 180-kDa receptor for secretory phospholipases A2. Molecular cloning, identification of a secreted soluble form, expression, and chromosomal localization". J. Biol. Chem. 270 (15): 8963–70. doi:10.1074/jbc.270.15.8963. PMID 7721806.
Chen J, Engle SJ, Seilhamer JJ, Tischfield JA (1994). "Cloning and recombinant expression of a novel human low molecular weight Ca(2+)-dependent phospholipase A2". J. Biol. Chem. 269 (4): 2365–8. doi:10.1016/S0021-9258(17)41952-1. PMID 8300559.
Gispert S, Twells R, Orozco G, et al. (1993). "Chromosomal assignment of the second locus for autosomal dominant cerebellar ataxia (SCA2) to chromosome 12q23-24.1". Nat. Genet. 4 (3): 295–9. doi:10.1038/ng0793-295. PMID 8358438. S2CID 7387082.
Cupillard L, Koumanov K, Mattéi MG, et al. (1997). "Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2". J. Biol. Chem. 272 (25): 15745–52. doi:10.1074/jbc.272.25.15745. PMID 9188469.
Mavoungou E, Georges-Courbot MC, Poaty-Mavoungou V, et al. (1997). "HIV and SIV envelope glycoproteins induce phospholipase A2 activation in human and macaque lymphocytes". J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. 16 (1): 1–9. doi:10.1097/00042560-199709010-00001. PMID 9377118.
Sanger Centre, The; Washington University Genome Sequencing Cente, The (1999). "Toward a complete human genome sequence". Genome Res. 8 (11): 1097–108. doi:10.1101/gr.8.11.1097. PMID 9847074.
Sartipy P, Bondjers G, Hurt-Camejo E (1999). "Phospholipase A2 type II binds to extracellular matrix biglycan: modulation of its activity on LDL by colocalization in glycosaminoglycan matrixes". Arterioscler. Thromb. Vasc. Biol. 18 (12): 1934–41. doi:10.1161/01.ATV.18.12.1934. PMID 9848887.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000170890 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000029522 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8175726-5] Dennis EA (Jun 1994). "Diversity of group types, regulation, and function of phospholipase A2". J Biol Chem. 269 (18): 13057–60. doi:10.1016/S0021-9258(17)36794-7. PMID 8175726.

[entrez-6] 1 2 "Entrez Gene: PLA2G1B phospholipase A2, group IB (pancreas)".

[pmid20836903-7] Sæle O, Nordgreen A, Olsvik PA, Hamre K (2010). "Characterisation and expression of secretory phospholipase A2 group IB during ontogeny of Atlantic cod ( Gadus morhua)". Br J Nutr. 105 (2): 1–10. doi:10.1017/S0007114510003466. PMID 20836903.

[pmid3028739-8] Seilhamer JJ, Randall TL, Yamanaka M, Johnson LK (1987). "Pancreatic phospholipase A2: isolation of the human gene and cDNAs from porcine pancreas and human lung". DNA. 5 (6): 519–27. doi:10.1089/dna.1.1986.5.519. PMID 3028739.

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Function

References

Further reading