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InterPro: IPR008999 Actin cross-linking

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UniProtKB

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436 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
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Accession

IPR008999 Actin_cross-linking

Type

Family

Signatures Help

Database	ID	Name	Proteins
SuperFamily	SSF50405	Actin_crosslink	436
Signatures in BioMart

InterPro Relationships Help

Children

IPR007679 Protein of unknown function DUF569
IPR010414 FRG1-like
IPR010431 Fascin

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents an actin-crosslinking domain with a beta-trefoil structure, consisting of a triplet of beta-hairpins packed against a six-stranded antiparallel beta-barrel. Proteins containing this domain include fascin, which carries a tandem repeat of four copies of this domain, and the histidine-rich actin-binding protein hisactophilin. Actin-crosslinking proteins organise actin filaments into dynamic and complex subcellular scaffolds that orchestrate important mechanical functions, including cell motility and adhesion [1].

The fascins are a structurally unique and evolutionarily conserved group of actin cross-linking proteins. Fascins function in the organisation of two major forms of actin-based structures: dynamic, cortical cell protrusions and cytoplasmic microfilament bundles [2].

A related protein, hisactophilin, is an essential protein for the osmoprotection of dictyostelium cells [3, 4].

Structural links Help

PDB - click here

SCOP: b.42.5.1 , b.42.5.2

CATH: 2.80.10.50

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR008999

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O18282 Protein FRG1 homolog

O18728 Fascin-2

P97376 Protein FRG1

Q16658 Fascin

Q24524 Protein singed

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR008999	Actin cross-linking
IPR010431	Fascin
IPR010414	FRG1-like
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Tseng Y, Kole TP, Lee JS, Fedorov E, Almo SC, Schafer BW, Wirtz D. How actin crosslinking and bundling proteins cooperate to generate an enhanced cell mechanical response. Biochem. Biophys. Res. Commun. 334 183-92 2005 [PubMed: 15992772] http://dx.doi.org/10.1016/j.bbrc.2005.05.205
2.	Jawhari AU, Buda A, Jenkins M, Shehzad K, Sarraf C, Noda M, Farthing MJ, Pignatelli M, Adams JC. Fascin, an actin-bundling protein, modulates colonic epithelial cell invasiveness and differentiation in vitro. Am. J. Pathol. 162 69-80 2003 [PubMed: 12507891] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=12507891
3.	Liu C, Gaspar JA, Wong HJ, Meiering EM. Conserved and nonconserved features of the folding pathway of hisactophilin, a beta-trefoil protein. Protein Sci. 11 669-79 2002 [PubMed: 11847289] http://dx.doi.org/10.1110/ps.31702
4.	Pintsch T, Zischka H, Schuster SC. Hisactophilin is involved in osmoprotection in Dictyostelium. BMC Biochem. 3 10 2002 [PubMed: 11996675] http://dx.doi.org/10.1186/1472-2091-3-10

Additional Reading Open in usermanual
	Habazettl J, Gondol D, Wiltscheck R, Otlewski J, Schleicher M, Holak TA. Structure of hisactophilin is similar to interleukin-1 beta and fibroblast growth factor. Nature 359 1992 855-8 [PubMed: 1436061] http://dx.doi.org/10.1038/359855a0

InterPro 23.1