PSAP
Sign in to saveAlso known as GLBA, SAP1, prosaposin, SAP2, PSAPD, PARK24
Prosaposin, also known as PSAP, is a protein which in humans is encoded by the PSAP gene.
Gene data
PSAP- Name
- prosaposin
- Type
- protein-coding
- Position
- 71,816,289–71,851,330 (−)
- Aliases
- GLBA, PARK24, PSAPD, SAP1, SAP2
- Ensembl
- ENSG00000197746
- RefSeq RNA
- NM_001042465.3, NM_001042466.3, NM_002778.4
- RefSeq protein
- NP_001035930.1, NP_001035931.1, NP_002769.1
This gene encodes a highly conserved preproprotein that is proteolytically processed to generate four main cleavage products including saposins A, B, C, and D. Each domain of the precursor protein is approximately 80 amino acid residues long with nearly identical placement of cysteine residues and glycosylation sites. Saposins A-D localize primarily to the lysosomal compartment where they facilitate the catabolism of glycosphingolipids with short oligosaccharide groups. The precursor protein exists both as a secretory protein and as an integral membrane protein and has neurotrophic activities. Mutations in this gene have been associated with Gaucher disease and metachromatic leukodystrophy. Alternative splicing results in multiple transcript variants, at least one of which encodes an isoform that is proteolytically processed. [provided by RefSeq, Feb 2016].
Gene Ontology
Biological process
Molecular function
Pathways
via MyGene.info
Wikidata facts
- Image
- Protein PSAP PDB 1m12.png
Show 5 more facts
- HomoloGene ID
- 37680
- exact match
- identifiers.org/ncbigene/5660
- genomic end
- 71851251
- genomic start
- 73576055
- cytogenetic location
- 10q22.1
via Wikidata · CC0
~4 min read
Article
8 sectionsContents
- Family members
- Structure
- Function
- Clinical significance
- See also
- References
- Further reading
- External links
Prosaposin, also known as PSAP, is a protein which in humans is encoded by the PSAP gene.
This highly conserved glycoprotein is a precursor for 4 cleavage products: saposins A, B, C, and D. Saposin is an acronym for Sphingolipid Activator PrO[S]teINs. Each domain of the precursor protein is approximately 80 amino acid residues long with nearly identical placement of cysteine residues and glycosylation sites. Saposins A-D localize primarily to the lysosomal compartment where they facilitate the catabolism of glycosphingolipids with short oligosaccharide groups. The precursor protein exists both as a secretory protein and as an integral membrane protein and has neurotrophic activities.