CLC (gene)

Galectin-10 is an enzyme that in humans is encoded by the CLC gene.^[3][4]

CLC
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 1G86, 1HDK, 1LCL, 1QKQ
Identifiers
Aliases	CLC, GAL10, Gal-10, LGALS10, LGALS10A, LPPL_HUMAN, Charcot-Leyden crystal galectin, galectin-10
External IDs	OMIM: 153310; HomoloGene: 130498; GeneCards: CLC; OMA:CLC - orthologs
Gene location (Human) Chr. Chromosome 19 (human)[1] Band 19q13.2 Start 39,731,255 bp[1] End 39,738,029 bp[1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in trabecular bone bone marrow bone marrow cells testicle monocyte blood gallbladder appendix granulocyte mucosa of transverse colon n/a More reference expression data BioGPS More reference expression data
Gene ontology Molecular function cysteine-type endopeptidase activity involved in apoptotic process lysophospholipase activity protein binding carbohydrate binding identical protein binding Cellular component cytoplasm cytosol collagen-containing extracellular matrix Biological process multicellular organism development T cell apoptotic process regulation of T cell cytokine production regulation of activated T cell proliferation regulation of T cell anergy Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1178 n/a Ensembl ENSG00000105205 n/a UniProt Q05315 n/a RefSeq (mRNA) NM_001828 n/a RefSeq (protein) NP_001819 n/a Location (UCSC) Chr 19: 39.73 – 39.74 Mb n/a PubMed search [2] n/a
Wikidata
View/Edit Human

Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. The protein encoded by this gene is a lysophospholipase expressed in eosinophils and basophils. It hydrolyzes lysophosphatidylcholine to glycerophosphocholine and a free fatty acid. This protein may possess carbohydrate or IgE-binding activities. It is both structurally and functionally related to the galectin family of beta-galactoside binding proteins. It may be associated with inflammation and some myeloid leukemias.^[4]

See also

• Charcot–Leyden crystals

References

1. GRCh38: Ensembl release 89: ENSG00000105205 – Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. Mastrianni DM, Eddy RL, Rosenberg HF, Corrette SE, Shows TB, Tenen DG, Ackerman SJ (Jun 1992). "Localization of the human eosinophil Charcot-Leyden crystal protein (lysophospholipase) gene (CLC) to chromosome 19 and the human ribonuclease 2 (eosinophil-derived neurotoxin) and ribonuclease 3 (eosinophil cationic protein) genes (RNS2 and RNS3) to chromosome 14". Genomics. 13 (1): 240–2. doi:10.1016/0888-7543(92)90237-M. PMID 1577491.
4. "CLC Charcot-Leyden crystal galectin [ Homo sapiens (human) ]".

Further reading

• Gleich GJ, Loegering DA, Mann KG, Maldonado JE (1976). "Comparative properties of the Charcot-Leyden crystal protein and the major basic protein from human eosinophils". J. Clin. Invest. 57 (3): 633–40. doi:10.1172/JCI108319. PMC 436696. PMID 942977.
• Golightly LM, Thomas LL, Dvorak AM, Ackerman SJ (1992). "Charcot-Leyden crystal protein in the degranulation and recovery of activated basophils". J. Leukoc. Biol. 51 (4): 386–92. doi:10.1002/jlb.51.4.386. PMID 1373430. S2CID 24236041.
• Dvorak AM, Weller PF, Monahan-Earley RA, et al. (1990). "Ultrastructural localization of Charcot-Leyden crystal protein (lysophospholipase) and peroxidase in macrophages, eosinophils, and extracellular matrix of the skin in the hypereosinophilic syndrome". Lab. Invest. 62 (5): 590–607. PMID 2160562.
• Dvorak AM, Letourneau L, Weller PF, Ackerman SJ (1990). "Ultrastructural localization of Charcot-Leyden crystal protein (lysophospholipase) to intracytoplasmic crystals in tumor cells of primary solid and papillary epithelial neoplasm of the pancreas". Lab. Invest. 62 (5): 608–15. PMID 2160563.
• Dvorak AM, Ackerman SJ (1989). "Ultrastructural localization of the Charcot-Leyden crystal protein (lysophospholipase) to granules and intragranular crystals in mature human basophils". Lab. Invest. 60 (4): 557–67. doi:10.1111/1523-1747.ep12703656. PMID 2709814.
• Sieker LC, Turley S, Le Trong I, et al. (1989). "Crystallographic characterization of human eosinophil Charcot-Leyden crystals". J. Mol. Biol. 204 (2): 489–91. doi:10.1016/0022-2836(88)90590-6. PMID 3221396.
• Weller PF, Bach D, Austen KF (1982). "Human eosinophil lysophospholipase: the sole protein component of Charcot-Leyden crystals". J. Immunol. 128 (3): 1346–9. doi:10.4049/jimmunol.128.3.1346. PMID 6173432.
• Weller PF, Bach DS, Austen KF (1985). "Biochemical characterization of human eosinophil Charcot-Leyden crystal protein (lysophospholipase)". J. Biol. Chem. 259 (24): 15100–5. doi:10.1016/S0021-9258(17)42520-8. PMID 6511787.
• Gomolin HI, Yamaguchi Y, Paulpillai AV, et al. (1993). "Human eosinophil Charcot-Leyden crystal protein: cloning and characterization of a lysophospholipase gene promoter". Blood. 82 (6): 1868–74. doi:10.1182/blood.V82.6.1868.1868. PMID 8400237.
• Ackerman SJ, Corrette SE, Rosenberg HF, et al. (1993). "Molecular cloning and characterization of human eosinophil Charcot-Leyden crystal protein (lysophospholipase). Similarities to IgE binding proteins and the S-type animal lectin superfamily". J. Immunol. 150 (2): 456–68. doi:10.4049/jimmunol.150.2.456. PMID 8419478.
• Leonidas DD, Elbert BL, Zhou Z, et al. (1996). "Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins". Structure. 3 (12): 1379–93. doi:10.1016/S0969-2126(01)00275-1. PMID 8747464.
• Dyer KD, Handen JS, Rosenberg HF (1997). "The genomic structure of the human Charcot-Leyden crystal protein gene is analogous to those of the galectin genes". Genomics. 40 (2): 217–21. doi:10.1006/geno.1996.4590. PMID 9119387.
• Swaminathan GJ, Leonidas DD, Savage MP, et al. (1999). "Selective recognition of mannose by the human eosinophil Charcot-Leyden crystal protein (galectin-10): a crystallographic study at 1.8 A resolution". Biochemistry. 38 (42): 13837–43. doi:10.1021/bi990756e. PMID 10529229.
• Larramendy ML, Niini T, Elonen E, et al. (2003). "Overexpression of translocation-associated fusion genes of FGFRI, MYC, NPMI, and DEK, but absence of the translocations in acute myeloid leukemia. A microarray analysis". Haematologica. 87 (6): 569–77. PMID 12031912.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Abedin MJ, Kashio Y, Seki M, et al. (2003). "Potential roles of galectins in myeloid differentiation into three different lineages". J. Leukoc. Biol. 73 (5): 650–6. doi:10.1189/jlb.0402163. PMID 12714580. S2CID 21337581.
• Grimwood J, Gordon LA, Olsen A, et al. (2004). "The DNA sequence and biology of human chromosome 19". Nature. 428 (6982): 529–35. Bibcode:2004Natur.428..529G. doi:10.1038/nature02399. PMID 15057824.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Nielsen K, Heegaard S, Vorum H, et al. (2005). "Altered expression of CLC, DSG3, EMP3, S100A2, and SLPI in corneal epithelium from keratoconus patients". Cornea. 24 (6): 661–8. doi:10.1097/01.ico.0000153556.59407.69. PMID 16015083. S2CID 21026845.

External links

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