"accession"	"counters"	"cross_references"	"description"	"entry_id"	"go_terms"	"hierarchy"	"integrated"	"is_llm"	"is_reviewed_llm"	"is_updated_llm"	"literature"	"member_databases"	"name"	"overlaps_with"	"representative_structure"	"set_info"	"source_database"	"type"	"wikipedia"
"PF02199"	"{'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}"	"{}"	""	""	""	""	"IPR003119"	False	False	False	""	""	"{'name': 'Saposin A-type domain', 'short': 'SapA'}"	""	""	"{'accession': 'CL0707', 'name': 'Saposin_like'}"	"pfam"	"family"	"[{'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': None}]"