Saposin protein domain

Saposin A-type domain
Identifiers
SymbolSapA
PfamPF02199
InterProIPR003119
PROSITEPDOC51110
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Saposin-like type B, region 1 (SapB1)
Crystal structure of human saposin C dimer in an open conformation.
Identifiers
SymbolSapB_1
PfamPF05184
InterProIPR007856
PROSITEPDOC50015
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Saposin-like type B, region 2 (SapB2)
Identifiers
SymbolSapB_2
PfamPF03489
InterProIPR008138
PROSITEPDOC50015
CATH1qdmC03
SCOP21nkl / SCOPe / SUPFAM
OPM superfamily76
OPM protein1sn6
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

The saposin domains 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 Saposin-B domains, yielding the active saposins after proteolytic cleavage, and two Saposin-A domains that are removed in the activation reaction.

The Saposin-B domains also occur in other proteins, most of them playing a role in interacting with membranes.