{"metadata":{"accession":"PF02199","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR003119","hierarchy":null,"name":{"name":"Saposin A-type domain","short":"SapA"},"description":null,"wikipedia":[{"title":"Saposin_protein_domain","extract":"<p>The <b>saposin domains</b> refers to two evolutionally-conserved protein domains found in saposin and related proteins (SAPLIP). Saposins are small lysosomal proteins that serve as activators of various lysosomal lipid-degrading enzymes. They probably act by isolating the lipid substrate from the membrane surroundings, thus making it more accessible to the soluble degradative enzymes. All mammalian saposins are synthesized as a single precursor molecule (prosaposin) which contains four <i>Saposin-B domains</i>, yielding the active saposins after proteolytic cleavage, and two <i>Saposin-A domains</i> that are removed in the activation reaction.</p>","thumbnail":null}],"literature":null,"set_info":{"accession":"CL0707","name":"Saposin_like"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":398,"interactions":0,"matches":6428,"pathways":0,"proteins":4380,"proteomes":1157,"sets":1,"structural_models":{"alphafold":3950,"bfvd":0},"structures":0,"taxa":4079},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":76,"alignment:full":4293},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}