COTL1

Protein-coding gene in humans From Wikipedia, the free encyclopedia

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

AliasesCOTL1, CLP, coactosin like F-actin binding protein 1
PDBOrtholog search: PDBe RCSB
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COTL1
Identifiers
AliasesCOTL1, CLP, coactosin like F-actin binding protein 1
External IDsOMIM: 606748; MGI: 1919292; HomoloGene: 10898; GeneCards: COTL1; OMA:COTL1 - orthologs
Available structures
PDBOrtholog search: PDBe RCSB
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_021149

NM_028071

RefSeq (protein)

NP_066972

NP_082347

Location (UCSC)Chr 16: 84.57 – 84.62 MbChr 8: 120.54 – 120.57 Mb
PubMed search[3][4]
Wikidata
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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.[8]

Interactions

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

Further reading

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