PLS1 | ||||||
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Identifiers | ||||||
Aliases | PLS1, Fimbrin | |||||
External IDs | MGI: 104809 HomoloGene: 68270 GeneCards: PLS1 | |||||
Genetically Related Diseases | ||||||
type 2 diabetes mellitus | ||||||
Orthologs | ||||||
Species | Human | Mouse | ||||
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Location (UCSC) | Chr 3: 142.6 – 142.71 Mb | Chr 9: 95.75 – 95.85 Mb | ||||
PubMed search | ||||||
NM_001145319
NM_001172312
NM_002670
NP_001138791
NP_001165783
NP_002661
Fimbrin also known as is plastin 1 is a protein that in humans is encoded by the PLS1 gene. Fimbrin is an actin cross-linking protein important in the formation of filopodia.
Fimbrin belongs to the calponin homology (CH) domain superfamily of actin cross-linking proteins. Like other members of this superfamily, which include α-actinin, β-spectrin, dystrophin, ABP-120 and filamin, it has a conserved 27 kDa actin-binding domain that contains a tandem duplication of a sequence that is homologous to calponin. In addition to cross-linking actin filaments into bundles and networks, CH domains also bind intermediate filaments and some signal transduction proteins to the actin cytoskeleton. Structural comparison of actin filaments and fimbrin CH domain-decorated actin filaments has revealed changes in the actin structure due to fimbrin-mediated cross-linking that may affect the actin filaments' affinity for other actin-binding proteins and may be part of the regulation of the cytoskeleton itself.