InterPro : IPR002068

Name  Alpha crystallin/Hsp20 domain Short Name  a-crystallin/Hsp20_dom
Type  Domain Description  Prokaryotic and eukaryotic organisms respond to heat shock or other environmental stress by inducing the synthesis of proteins collectively known as heat-shock proteins (hsp) []. Amongst them is a family of proteins with an average molecular weight of 20 Kd, known as the hsp20 proteins []. These seem to act as chaperones that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates.These low-molecular-weight proteins are evolutionarily related to alpha-crystallin []. Alpha-crystallin is an abundant constituent of the eye lens of most vertebrate species. Its main function appears to be to maintain the correct refractive index of the lens. It is also found in other tissues where it seems to act as a chaperone []. Other related proteins include certain surface antigens [].This entry represents a conserved C-terminal domain of about 100 residues characteristic of this group of proteins [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

0 Contains

4 Found In

Id Name Short Name Type
IPR016952 Small heat shock protein, predicted, plant Small_heat_shock_prot_prd_pln Family
IPR001436 Alpha crystallin/Heat shock protein Alpha-crystallin/HSP Family
IPR012273 Alpha-crystallin, subunit B Alpha-crystallin_B Family
IPR012274 Alpha-crystallin, subunit A Alpha-crystallin_A Family

1 Parent Features

Id Name Short Name Type
IPR008978 HSP20-like chaperone HSP20-like_chaperone Domain

5 Publications

First Author Title Year Journal Volume Pages
Lindquist S The heat-shock proteins. 1988 Annu Rev Genet 22 631-77
Groenen PJ Structure and modifications of the junior chaperone alpha-crystallin. From lens transparency to molecular pathology. 1994 Eur J Biochem 225 1-19
Caspers GJ The expanding small heat-shock protein family, and structure predictions of the conserved "alpha-crystallin domain". 1995 J Mol Evol 40 238-48
Ingolia TD Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin. 1982 Proc Natl Acad Sci U S A 79 2360-4
Verbon A The 14,000-molecular-weight antigen of Mycobacterium tuberculosis is related to the alpha-crystallin family of low-molecular-weight heat shock proteins. 1992 J Bacteriol 174 1352-9



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)