Saposin-like
IPR011001
Definition
The lysosomal degradation of several sphingolipids requires the presence of four small glycoproteins called saposins, generated by proteolytic processing of a common precursor, prosaposin PMID:9972880. Saposins have three conserved disulphide bridges, and display a 5-helical, closed, folded leaf topology. Other proteins have been shown to have structures that closely resemble saposin, such as the antimicrobial peptides NK-lysin and granulysin [[cite:PMID:8988855], [cite:PMID:14499265]]. Some proteins contain saposin-like domains, such as prophytepsin, an acid protease from plants, and J3-crystallin, an eye-lens protein from jellyfish, both of which contain circularly permuted saposin motifs called swaposin [[cite:PMID:10406799], [cite:PMID:11675486]]. In some saposins and saposin-like domains, lipid-binding can promote conformational changes and oligomerization.
6 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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