COTL1

Coactosin-like F-actin binding protein 1
PDB rendering based on 1t2l.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1T2L​, 1T3X​, 1T3Y​, 1TMW​, 1VFQ​, 1WNJ​
Identifiers
Symbols	COTL1 ; CLP
External IDs	OMIM: 606748 MGI: 1919292 HomoloGene: 10898 GeneCards: COTL1 Gene
Gene ontology Molecular function • actin binding • protein binding • enzyme binding Cellular component • cytoplasm • cytoskeleton • nuclear membrane • extracellular exosome Biological process • biological_process • leukotriene biosynthetic process • defense response to fungus Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
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: 119.81 – 119.84 Mb
PubMed search

Coactosin-like protein is a protein that in humans is encoded by the COTL1 gene.^[1][2][3][4]

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 5-lipoxygenase, which is the first committed enzyme in leukotriene biosynthesis. 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.^[4]

Interactions

COTL1 has been shown to interact with Arachidonate 5-lipoxygenase.^[5]

References

1. 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. doi:10.1073/pnas.96.5.1881. PMC 26705. PMID 10051563.
2. 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.
3. 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. doi:10.1073/pnas.0605150103. PMC 1559768. PMID 16924104.
4. "Entrez Gene: COTL1 coactosin-like 1 (Dictyostelium)".
5. 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.

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.
• 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.
• 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.
• 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 Biol. Crystallogr. 60 (Pt 9): 1651–3. 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 Biol. Crystallogr. 60 (Pt 12 Pt 2): 2387–8. 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.
• 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.