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COTL1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1T2L, 1T3X, 1T3Y, 1TMW, 1VFQ, 1WNJ
Identifiers
Aliases	COTL1, CLP, coactosin like F-actin binding protein 1
External IDs	OMIM: 606748; MGI: 1919292; HomoloGene: 10898; GeneCards: COTL1; OMA:COTL1 - orthologs
Gene location (Human) Chr. Chromosome 16 (human) Band 16q24.1 Start 84,565,596 bp End 84,618,078 bp
Gene location (Mouse) Chr. Chromosome 8 (mouse) Band 8|8 E1 Start 120,535,961 bp End 120,567,283 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte granulocyte blood spleen appendix lymph node retinal pigment epithelium ganglionic eminence bone marrow gallbladder Top expressed in granulocyte mesenteric lymph nodes epithelium of stomach migratory enteric neural crest cell epithelium of lens motor neuron yolk sac mucous cell of stomach fossa conjunctival fornix More reference expression data BioGPS More reference expression data
Gene ontology Molecular function enzyme binding protein binding actin binding Cellular component cytoplasm extracellular exosome cytoskeleton intracellular anatomical structure nucleus extracellular region secretory granule lumen ficolin-1-rich granule lumen Biological process defense response to fungus neutrophil degranulation biological process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 23406 72042 Ensembl ENSG00000103187 ENSMUSG00000031827 UniProt Q14019 Q9CQI6 RefSeq (mRNA) NM_021149 NM_028071 RefSeq (protein) NP_066972 NP_082347 Location (UCSC) Chr 16: 84.57 – 84.62 Mb Chr 8: 120.54 – 120.57 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Coactosin-like protein (COTL1 or CLP) is a protein that in humans is encoded by the COTL1 gene.

Function

This gene encodes one of the numerous actin-binding proteins which regulate the actin cytoskeleton. This protein binds F-actin, and also interacts with and thereby stabilizes 5-lipoxygenase (ALOX5). Although this gene has been reported to map to chromosome 17 in the Smith-Magenis syndrome region, the best alignments for this gene are to chromosome 16. The Smith-Magenis syndrome region is the site of two related pseudogenes.

Interactions

COTL1 has been shown to interact with ALOX5. ALOX5 is the first committed enzyme in the metabolism of arachidonic acid to an array of biologically important cell signaling agents: a) the pro-inflammatory mediator, leukotriene B4 (LTB4); b) the airways constrictors, LTC4, LTD4, and LTE4; c) the 5-hydroxyeicosatetraenoic acid family of pro-inflammatory and pro-allergic reactions mediators, 5-HETE and 5-oxo-eicosatetraenoic acid. ALOX5 also contributes to the metabolism of arachidonic acid and other polyunsaturated fatty acids to agents which act block inflammation and allergic reactions, the specialized pro-resolving mediators of the lipoxin and resolvin subclasses. Based on in vitro studies, COTL1 serves to stabilize ALOX5, acting as a chaperone or scaffold, to avert the enzyme's inactivation and thereby to promote its metabolic activity.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000103187 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000031827 – 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.
5. Provost P, Samuelsson B, Rådmark O (Apr 1999). "Interaction of 5-lipoxygenase with cellular proteins". Proc. Natl. Acad. Sci. U.S.A. 96 (5): 1881–5. Bibcode:1999PNAS...96.1881P. doi:10.1073/pnas.96.5.1881. PMC 26705. PMID 10051563.
6. Chen KS, Manian P, Koeuth T, Potocki L, Zhao Q, Chinault AC, Lee CC, Lupski JR (Nov 1997). "Homologous recombination of a flanking repeat gene cluster is a mechanism for a common contiguous gene deletion syndrome". Nat. Genet. 17 (2): 154–63. doi:10.1038/ng1097-154. PMID 9326934. S2CID 27742511.
7. Rakonjac M, Fischer L, Provost P, Werz O, Steinhilber D, Samuelsson B, Rådmark O (Sep 2006). "Coactosin-like protein supports 5-lipoxygenase enzyme activity and up-regulates leukotriene A4 production". Proc. Natl. Acad. Sci. U.S.A. 103 (35): 13150–5. Bibcode:2006PNAS..10313150R. doi:10.1073/pnas.0605150103. PMC 1559768. PMID 16924104.
8. ^ "Entrez Gene: COTL1 coactosin-like 1 (Dictyostelium)".
9. Provost P, Doucet J, Hammarberg T, Gerisch G, Samuelsson B, Radmark O (May 2001). "5-Lipoxygenase interacts with coactosin-like protein". J. Biol. Chem. 276 (19): 16520–7. doi:10.1074/jbc.M011205200. PMID 11297527.
10. Anwar Y, Sabir JS, Qureshi MI, Saini KS (2014). "5-lipoxygenase: a promising drug target against inflammatory diseases-biochemical and pharmacological regulation". Current Drug Targets. 15 (4): 410–22. doi:10.2174/1389450114666131209110745. PMID 24313690.

External links

• Human COTL1 genome location and COTL1 gene details page in the UCSC Genome Browser.

Further reading

• Wu C, Friedlander P, Lamoureux C, Zannis-Hadjopoulos M, Price GB (1993). "cDNA clones contain autonomous replication activity". Biochim. Biophys. Acta. 1174 (3): 241–57. doi:10.1016/0167-4781(93)90193-h. PMID 7690594.
• Provost P, Doucet J, Hammarberg T, Gerisch G, Samuelsson B, Radmark O (2001). "5-Lipoxygenase interacts with coactosin-like protein". J. Biol. Chem. 276 (19): 16520–7. doi:10.1074/jbc.M011205200. PMID 11297527.
• Provost P, Doucet J, Stock A, Gerisch G, Samuelsson B, Rådmark O (2001). "Coactosin-like protein, a human F-actin-binding protein: critical role of lysine-75". Biochem. J. 359 (Pt 2): 255–63. doi:10.1042/0264-6021:3590255. PMC 1222143. PMID 11583571.
• Nakatsura T, Senju S, Ito M, Nishimura Y, Itoh K (2002). "Cellular and humoral immune responses to a human pancreatic cancer antigen, coactosin-like protein, originally defined by the SEREX method". Eur. J. Immunol. 32 (3): 826–36. doi:10.1002/1521-4141(200203)32:3<826::AID-IMMU826>3.0.CO;2-Y. PMID 11870627. S2CID 21684580.
• Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. S2CID 23783563.
• Dai H, Wu J, Xu Y, Yajun T, Husheng D, Shi Y (2004). "1H, 13C and 15N resonance assignments and the secondary structures of human coactosin like protein (hCLP) D123N". J. Biomol. NMR. 29 (3): 455–6. doi:10.1023/B:JNMR.0000032550.18424.aa. PMID 15213466. S2CID 27858479.
• Liu L, Wang Y, Zhang P, Cheng Z, Wan M, Zhou Z, Gong W (2004). "Expression, purification and preliminary crystallographic studies of human coactosin-like protein". Acta Crystallogr. D. 60 (Pt 9): 1651–3. Bibcode:2004AcCrD..60.1651L. doi:10.1107/S0907444904016701. PMID 15333945.
• Li X, Liu X, Lou Z, Duan X, Wu H, Liu Y, Rao Z (2004). "Crystal structure of human coactosin-like protein at 1.9 A resolution". Protein Sci. 13 (11): 2845–51. doi:10.1110/ps.04937304. PMC 2286586. PMID 15459340.
• Li X, Liu X, Zhao Q, Liu Y, Duan X, Rao Z (2004). "Crystallization and preliminary crystallographic studies of human coactosin-like protein (CLP)". Acta Crystallogr. D. 60 (Pt 12 Pt 2): 2387–8. Bibcode:2004AcCrD..60.2387L. doi:10.1107/S0907444904028112. PMID 15583396.
• Gevaert K, Staes A, Van Damme J, De Groot S, Hugelier K, Demol H, Martens L, Goethals M, Vandekerckhove J (2005). "Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC". Proteomics. 5 (14): 3589–99. doi:10.1002/pmic.200401217. PMID 16097034. S2CID 895879.
• Dai H, Huang W, Xu J, Yao B, Xiong S, Ding H, Tang Y, Liu H, Wu J, Shi Y (2006). "Binding model of human coactosin-like protein with filament actin revealed by mutagenesis". Biochim. Biophys. Acta. 1764 (11): 1688–700. doi:10.1016/j.bbapap.2006.06.017. PMID 17070122.

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