Alpha crystallin/Hsp20 domain
IPR002068
Definition
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) PMID:2853609. Amongst them is a family of proteins with an average molecular weight of 20 Kd, known as the hsp20 proteins PMID:7925426. 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 PMID:6285380. 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 and transparency of the lens. It is also found in other tissues where it seems to act as a chaperone [[cite:PMID:7925426], [cite:PMID:22120592]]. Other related proteins include certain surface antigens PMID:1370952. This entry represents a conserved C-terminal domain of about 100 residues characteristic of this group of proteins PMID:7723051.
10 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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