Psap
entrez
19156
canonical
uniprot
Q61207
canonical
ensembl
ENSMUSG00000004207
resolver
ensp
ENSMUSP00000101105
resolver
ensp
ENSMUSP00000126407
resolver
ensp
ENSMUSP00000137476
resolver
ensp
ENSMUSP00000202836
resolver
ensp
ENSMUSP00000202843
resolver
enst
ENSMUST00000105465
resolver
enst
ENSMUST00000165878
resolver
enst
ENSMUST00000179238
resolver
genesymbol
Psap
resolver
genesymbol_syn
Sgp1
resolver
uniprot
B2RUD7
resolver
uniprot
E9PZ00
resolver
uniprot
F7D9Z9
resolver
uniprot
Q3TWM9
resolver
uniprot
Q3TXJ0
resolver
uniprot
Q3UAS4
resolver
uniprot
Q3UE29
resolver
uniprot
Q3UFE8
resolver
uniprot
Q60861
resolver
uniprot
Q64006
resolver
uniprot
Q64219
resolver
uniprot
Q8BFQ1
resolver
uniprot_entry
B2RUD7_MOUSE
resolver
uniprot_entry
E9PZ00_MOUSE
resolver
uniprot_entry
F7D9Z9_MOUSE
resolver
uniprot_entry
Q3TWM9_MOUSE
resolver
uniprot_entry
Q3TXJ0_MOUSE
resolver
uniprot_entry
Q3UAS4_MOUSE
resolver
uniprot_entry
Q3UE29_MOUSE
resolver
uniprot_entry
Q3UFE8_MOUSE
resolver
uniprot_entry
Q8BFQ1_MOUSE
resolver
uniprot_entry
SAP_MOUSE
resolver
uniprot_sec
Q60861
resolver
uniprot_sec
Q64006
resolver
uniprot_sec
Q64219
resolver
amino_acid_sequence
MYALALFASLLATALTSPVQDPKTCSGGSAVLCRDVKTAVDCGAVKHCQQMVWSKPTAKSLPCDICKTVVTEAGNLLKDNATQEEILHYLEKTCEWIHDSSLSASCKEVVDSYLPVILDMIKGEMSNPGEVCSALNLCQSLQEYLAEQNQKQLESNKIPEVDMARVVAPFMSNIPLLLYPQDHPRSQPQPKANEDVCQDCMKLVSDVQTAVKTNSSFIQGFVDHVKEDCDRLGPGVSDICKNYVDQYSEVCVQMLMHMQDQQPKEICVLAGFCNEVKRVPMKTLVPATETIKNILPALEMMDPYEQNLVQAHNVILCQTCQFVMNKFSELIVNNATEELLVKGLSNACALLPDPARTKCQEVVGTFGPSLLDIFIHEVNPSSLCGVIGLCAARPELVEALEQPAPAIVSALLKEPTPPKQPAQPKQSALPAHVPPQKNGGFCEVCKKLVLYLEHNLEKNSTKEEILAALEKGCSFLPDPYQKQCDDFVAEYEPLLLEILVEVMDPGFVCSKIGVCPSAYKLLLGTEKCVWGPSYWCQNMETAARCNAVDHCKRHVWN
uniprot
proteins
function
FUNCTION: Saposins are specific low-molecular mass non-enzymatic glycoproteins that act as activator proteins for lysosomal sphingolipid-degrading enzymes, facilitating the hydrolysis of sphingolipids by extracting lipid substrates from membranes and presenting them to their respective enzymes. They are derived from a common precursor protein, prosaposin, which is proteolytically cleaved to yield four homologous proteins (saposin A, B, C, and D), each with distinct but partially overlapping lipid and enzyme specificities. {ECO:0000250|UniProtKB:P07602}.; FUNCTION: [Prosaposin]: Behaves as a myelinotrophic and neurotrophic factor, these effects are mediated by its G protein-coupled receptors, GPR37 and GPR37L1, undergoing ligand-mediated internalization followed by ERK phosphorylation signaling. {ECO:0000269|PubMed:23690594}.; FUNCTION: [Saposin-A]: Acts as an essential lysosomal cofactor that activates galactocerebrosidase (GALC, EC 3.2.1.46) by facilitating enzyme access to its membrane-embedded galactosylceramide substrate, the principal lipid component of myelin. {ECO:0000250|UniProtKB:P07602}.; FUNCTION: [Saposin-B]: Stimulates the hydrolysis of galacto-cerebroside sulfate by arylsulfatase A ARSA (EC 3.1.6.8), GM1 gangliosides by beta-galactosidase (EC 3.2.1.23) and globotriaosylceramide by alpha-galactosidase A (EC 3.2.1.22). Saposin-B forms a solubilizing complex with the substrates of the sphingolipid hydrolases. {ECO:0000250|UniProtKB:P07602}.; FUNCTION: [Saposin-C]: Acts as an essential lysosomal cofactor that activates acid beta-glucosylceramidases (EC 3.2.1.45) by altering lipid bilayer properties to facilitate enzyme access to its membrane-embedded glucosylceramide substrate, while also protecting glucocerebrosidase from intralysosomal proteolytic degradation. {ECO:0000269|PubMed:12813057}.; FUNCTION: [Saposin-D]: Acts as a lysosomal activator protein that stimulates acid ceramidase (EC 3.5.1.23) by solubilizing and presenting ceramide substrates at the lipid-water interface, facilitating their hydrolysis into sphingosine and fatty acids. It also activates acid sphingomyelinase (EC 3.1.4.12), though ceramide catabolism represents its primary physiological role. {ECO:0000269|PubMed:37337846}.
uniprot
proteins
mass_dalton
61422
uniprot
proteins
mutagenesis
MUTAGEN 509; /note="C->S: Affects the intracellular trafficking, resulting in endoplasmic reticulum retention. Mice carrying homozygous and heterozygous C509S exhibit a progressive decline in locomotor function and a reduction in the number of tyrosine hydroxylase-positive neurons."; /evidence="ECO:0000269|PubMed:32201884
uniprot
proteins
pubmed
12813057
uniprot
proteins
pubmed
1590788
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23690594
uniprot
proteins
pubmed
26370502
uniprot
proteins
pubmed
32201884
uniprot
proteins
pubmed
37337846
uniprot
proteins
pubmed
8003952
uniprot
proteins
pubmed
8334382
uniprot
proteins
pubmed
8565332
uniprot
proteins
sequence_length
557
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P07602}.; SUBCELLULAR LOCATION: [Prosaposin]: Secreted {ECO:0000269|PubMed:23690594}. Note=Secreted as a fully glycosylated 70 kDa protein composed of complex glycans. {ECO:0000269|PubMed:23690594}.
uniprot
proteins