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(Top) 1 Function 2 Interactions 3 References 4 External links 5 Further reading

COTL1

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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)^[1]

Band	16q24.1	Start	84,565,596 bp^[1]
Band	16q24.1	End	84,618,078 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 8 (mouse)^[2]

Band	8\|8 E1	Start	120,535,961 bp^[2]
Band	8\|8 E1	End	120,567,283 bp^[2]

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

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Coactosin-like protein (COTL1orCLP) is a protein that in humans is encoded by the COTL1 gene.^[5]^[6]^[7]^[8]

Function[edit]

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.^[8]

Interactions[edit]

COTL1 has been shown to interact with ALOX5.^[9] 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.^[10]

References[edit]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000103187 – Ensembl, May 2017

^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000031827 – 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.

^ 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.

^ 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.

^ 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.

^ ^a ^b "Entrez Gene: COTL1 coactosin-like 1 (Dictyostelium)".

^ 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.

^ 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[edit]

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

Further reading[edit]

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.

PDB gallery

1t2l: Three Crystal Structures of Human Coactosin-like Protein

1t3x: Three Crystal Structures of Human Coactosin-like Protein

1t3y: Three Crystal Structures of Human Coactosin-like Protein

1tmw: Solution structure of Human Coactosin Like Protein D123N

1udm: Solution structure of Coactosin-like protein (Cofilin family) from Mus Musculus

1vfq: The Crystal Structure of Human Coactosin-like Protein at 1.9 A Resolution

1wm4: Solution structure of mouse coactosin, an actin filament binding protein

1wnj: NMR structure of human coactosin-like protein

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