Saposin

Saposins are small lysosomal proteins that serve as activators of various lysosomal lipid-degrading enzymescite journal |author=Munford RS, Sheppard PO, O Hara PJ |title=Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure |journal=J. Lipid Res. |volume=36 |issue=8 |pages=1653–1663 |year=1995 |pmid=7595087] . 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, many of them active in the lysis of membranescite journal |author=Ponting CP |title=Acid sphingomyelinase possesses a domain homologous to its activator proteins: saposins B and D |journal=Protein Sci. |volume=3 |issue=2 |pages=359–361 |year=1994 |pmid=8003971] cite journal |author=Hofmann K, Tschopp J |title=Cytotoxic T cells: more weapons for new targets? |journal=Trends Microbiol. |volume=4 |issue=3 |pages=91–94 |year=1996 |pmid=8868085 |doi=10.1016/0966-842X(96)81522-8] .

Human proteins containing this domain

AOAH; GNLY; Prosaposin; PSAPL1; SFTPB;

References

Further reading

*Swaposins: circular permutations within genes encoding saposin homologues. Ponting CP, Russell RB; Trends Biochem Sci 1995;20: 179-180. PMID|7610480

External links

* [http://www.expasy.org/cgi-bin/nicedoc.pl?PDOC50015 Saposin B-type domain] in PROSITE

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Saposin

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