Parvin (IPR028433)

Short name: Parvin

Overlapping homologous superfamilies

Family relationships



This entry include parvins from mammals and paralysed arrest at two-fold protein 6 (pat-6) from C. elegans. Parvins and pat-6 contain an actin-binding domain (ABD) that consists of two in tandem arranged calponin homology (CH) domains. The ABD domain enables parvins to recruit F-actin to focal adhesions and associate with stress fibres [PMID: 19798050]. Parvins bind to actin binding/regulatory proteins and co-localise with integrins [PMID: 19798050]. Therefore, they may be involved in integrin-mediated adhesion and actin-dependent processes such as cell shape regulation and cell migration [PMID: 19798050].

In humans, there are three parvins. Alpha-parvin (also known as actopaxin/CH-ILKBP) is ubiquitously expressed and is required for normal development of the embryonic cardiovascular system [PMID: 19798050, PMID: 11134073]. Beta-parvin (also known as affixin) is enriched in heart and skeletal muscle [PMID: 11402068]. The expression of gamma-parvin (gamma-pv) is restricted to haematopoietic cells and plays a subtle role for blood cell homeostasis [PMID: 16479001].

In C. elegans, pat-6 plays essential roles during the maturation of integrin-mediated muscle attachments [PMID: 11134073].

GO terms

Biological Process

GO:0031532 actin cytoskeleton reorganization
GO:0007155 cell adhesion

Molecular Function

GO:0003779 actin binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.