InterPro : IPR004000

Name  Actin family Short Name  Actin
Type  Family Description  Actin [, ]is a ubiquitous protein involved in the formation of filaments that are major components of the cytoskeleton. These filaments interact with myosin to produce a sliding effect, which is the basis of muscular contraction and many aspects of cell motility, including cytokinesis. Each actin protomer binds one molecule of ATP and has one high affinity site for either calcium or magnesium ions, as well as several low affinity sites. Actin exists as a monomer in low salt concentrations, but filaments form rapidly as salt concentration rises, with the consequent hydrolysis of ATP. Actin from many sources forms a tight complex with deoxyribonuclease (DNase I) although the significance of this is still unknown. The formation of this complex results in the inhibition of DNase I activity, and actin loses its ability to polymerise. It has been shown that an ATPase domain of actin shares similarity with ATPase domains of hexokinase and hsp70proteins [, ].In vertebrates there are three groups of actin isoforms: alpha, beta and gamma. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins co-exists in most cell types as components of the cytoskeleton and as mediators of internal cell motility. In plants there are many isoforms which are probably involved in a variety of functions such as cytoplasmic streaming, cell shape determination, tip growth, graviperception, cell wall deposition, etc.Recently some divergent actin-like proteins have been identified in several species. These proteins include centractin (actin-RPV) from mammals, fungi yeast ACT5, Neurospora crassaro-4) and Pneumocystis carinii, which seems to be a component of a multi-subunit centrosomal complex involved in microtubule based vesicle motility (this subfamily is known as ARP1); ARP2 subfamily, which includes chicken ACTL, Saccharomyces cerevisiaeACT2, Drosophila melanogaster14D and Caenorhabditis elegansactC; ARP3 subfamily, which includes actin 2 from mammals, Drosophila 66B, yeast ACT4 and Schizosaccharomyces pombeact2; and ARP4 subfamily, which includes yeast ACT3 and Drosophila 13E.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

19 Child Features

Id Name Short Name Type
IPR027127 Actin-related protein 10 Arp10 Family
IPR027306 Actin-related protein 2 Arp2 Family
IPR027667 Actin-related protein 4 Arp4 Family
IPR029909 Actin-related protein 1 family Arp1 Family
IPR027668 Actin-related protein 8/Plant actin-related protein 9 Arp8/plant_Arp9 Family
IPR030054 Actin-related protein 6 Arp6 Family
IPR027664 Actin-related protein 5 Arp5 Family
IPR015623 Actin-related protein 3 Arp3 Family
IPR029912 Actin-like protein 6A ACL6A Family
IPR030068 Actin-related protein T3 ARP-T3 Family
IPR027665 Actin-related protein 9, fungi Arp9_fungi Family
IPR027666 Actin-related protein T2 ACTRT2 Family
IPR027678 Actin-related protein 7, plant Arp7_plant Family
IPR027679 Actin-like protein 7A ACTL7A Family
IPR027680 Actin-like protein 7B ACTL7B Family
IPR029911 Actin-related protein 7, fungi Arp7_fungi Family
IPR030071 Plant actin-related protein 8 Plant_Arp8 Family
IPR030074 Actin-like protein 9 ACTL9 Family
IPR030139 Actin-related protein T1 Arp-T1 Family

2 Contains

Id Name Short Name Type
IPR020902 Actin/actin-like conserved site Actin/actin-like_CS Conserved_site
IPR004001 Actin, conserved site Actin_CS Conserved_site

0 Found In

0 Parent Features

4 Publications

First Author Title Year Journal Volume Pages
Kabsch W Structure and function of actin. 1992 Annu Rev Biophys Biomol Struct 21 49-76
Herman IM Actin isoforms. 1993 Curr Opin Cell Biol 5 48-55
Flaherty KM Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein. 1991 Proc Natl Acad Sci U S A 88 5041-5
Bork P An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. 1992 Proc Natl Acad Sci U S A 89 7290-4



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)