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PLA2G1B
Identifiers
Aliases	PLA2G1B, PLA2, PLA2A, PPLA2, phospholipase A2 group IB
External IDs	OMIM: 172410; MGI: 101842; GeneCards: PLA2G1B
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3ELO
Enzyme activity EC # BRENDA ExPASy KEGG MetaCyc 3.1.1.4 ↗ ↗ ↗ ↗
Gene location (Human) Chr. Chromosome 12 (human) Band 12q24.31 Start 120,322,115 bp End 120,327,779 bp
Gene location (Mouse) Chr. Chromosome 5 (mouse) Band 5|5 F Start 115,604,321 bp End 115,612,781 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of pancreas islet of Langerhans beta cell lower lobe of lung sperm testicle upper lobe of lung right lung upper lobe of left lung left ovary Top expressed in epithelium of stomach pyloric antrum mucous cell of stomach islet of Langerhans embryo duodenum embryo esophagus right lung left lung More reference expression data BioGPS 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 Databases NCBI: entry; OMA: entry Species Human Mouse Entrez 5319 18778 Ensembl ENSG00000170890 ENSMUSG00000029522 UniProt P04054 Q9Z0Y2 RefSeq (mRNA) NM_000928 NM_011107 NM_001356586 NM_001356587 RefSeq (protein) NP_000919 NP_035237 NP_001343515 NP_001343516 Location (UCSC) Chr 12: 120.32 – 120.33 Mb Chr 5: 115.6 – 115.61 Mb PubMed search
Wikidata
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Phospholipase A₂, group 1B is an enzyme that in humans is encoded by the PLA2G1B gene. This protein functions as a digestive enzyme which is secreted by the acinar cells of the pancreas into the small intestines. In the intestines, it helps break down dietary phospholipids.

Function

Main article: Phospholipase A2

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. 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.

Further reading

• Schröder HC, Perovic S, Kavsan V, Ushijima H, Müller WE (1998). "Mechanisms of prionSc- and HIV-1 gp120 induced neuronal cell death". Neurotoxicology. 19 (4–5): 683–688. PMID 9745929.
• Sapirstein A, Bonventre JV (2000). "Phospholipases A2 in ischemic and toxic brain injury". Neurochemical Research. 25 (5): 745–753. doi:10.1023/A:1007583708713. PMID 10905638. S2CID 30097342.
• Svensson CI, Yaksh TL (2002). "The spinal phospholipase-cyclooxygenase-prostanoid cascade in nociceptive processing". Annual Review of Pharmacology and Toxicology. 42: 553–583. doi:10.1146/annurev.pharmtox.42.092401.143905. PMID 11807183.
• Clark MA, Ozgür LE, Conway TM, Dispoto J, Crooke ST, Bomalaski JS (June 1991). "Cloning of a phospholipase A2-activating protein". Proceedings of the National Academy of Sciences of the United States of America. 88 (12): 5418–5422. 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". Biochimica et Biophysica Acta. 747 (1–2): 93–99. 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". Biochimica et Biophysica Acta. 789 (2): 164–169. doi:10.1016/0167-4838(84)90201-2. PMID 6477929.
• Grataroli R, Dijkman R, Dutilh CE, van der Ouderaa F, De Haas GH, Figarella C (February 1982). "Studies on prophospholipase A2 and its enzyme from human pancreatic juice. Catalytic properties and sequence of the N-terminal region". European Journal of Biochemistry. 122 (1): 111–117. doi:10.1111/j.1432-1033.1982.tb05855.x. PMID 7060561.
• Rönkkö S (March 1995). "Immunohistochemical localization of phospholipase A2 in human and bovine male reproductive organs". Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology. 110 (3): 503–509. doi:10.1016/0305-0491(94)00190-6. PMID 7584826.
• Lilja I, Smedh K, Olaison G, Sjödahl R, Tagesson C, Gustafson-Svärd C (September 1995). "Phospholipase A2 gene expression and activity in histologically normal ileal mucosa and in Crohn's ileitis". Gut. 37 (3): 380–385. 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". The Journal of Biological Chemistry. 270 (15): 8963–8970. 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". The Journal of Biological Chemistry. 269 (4): 2365–2368. doi:10.1016/S0021-9258(17)41952-1. PMID 8300559.
• Gispert S, Twells R, Orozco G, Brice A, Weber J, Heredero L, et al. (July 1993). "Chromosomal assignment of the second locus for autosomal dominant cerebellar ataxia (SCA2) to chromosome 12q23-24.1". Nature Genetics. 4 (3): 295–299. doi:10.1038/ng0793-295. PMID 8358438. S2CID 7387082.
• Cupillard L, Koumanov K, Mattéi MG, Lazdunski M, Lambeau G (June 1997). "Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2". The Journal of Biological Chemistry. 272 (25): 15745–15752. doi:10.1074/jbc.272.25.15745. PMID 9188469.
• Mavoungou E, Georges-Courbot MC, Poaty-Mavoungou V, Nguyen HT, Yaba P, Delicat A, et al. (September 1997). "HIV and SIV envelope glycoproteins induce phospholipase A2 activation in human and macaque lymphocytes". Journal of Acquired Immune Deficiency Syndromes and Human Retrovirology. 16 (1): 1–9. doi:10.1097/00042560-199709010-00001. PMID 9377118.
• Sanger Centre T, Washington University Genome Sequencing Cente T (November 1998). "Toward a complete human genome sequence". Genome Research. 8 (11): 1097–1108. 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". Arteriosclerosis, Thrombosis, and Vascular Biology. 18 (12): 1934–1941. doi:10.1161/01.ATV.18.12.1934. PMID 9848887.