| IED ID | IndEnz0002010133 |
| Enzyme Type ID | protease010133 |
| Protein Name |
Prosaposin Sulfated glycoprotein 1 SGP-1 Cleaved into: Saposin-A; Saposin-B-Val; Saposin-B; Saposin-C; Saposin-D |
| Gene Name | Psap Sgp1 |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MYALALFASLLATALTSPVQDPKTCSGGSAVLCRDVKTAVDCGAVKHCQQMVWSKPTAKSLPCDICKTVVTEAGNLLKDNATQEEILHYLEKTCEWIHDSSLSASCKEVVDSYLPVILDMIKGEMSNPGEVCSALNLCQSLQEYLAEQNQKQLESNKIPEVDMARVVAPFMSNIPLLLYPQDHPRSQPQPKANEDVCQDCMKLVSDVQTAVKTNSSFIQGFVDHVKEDCDRLGPGVSDICKNYVDQYSEVCVQMLMHMQDQQPKEICVLAGFCNEVKRVPMKTLVPATETIKNILPALEMMDPYEQNLVQAHNVILCQTCQFVMNKFSELIVNNATEELLVKGLSNACALLPDPARTKCQEVVGTFGPSLLDIFIHEVNPSSLCGVIGLCAARPELVEALEQPAPAIVSALLKEPTPPKQPAQPKQSALPAHVPPQKNGGFCEVCKKLVLYLEHNLEKNSTKEEILAALEKGCSFLPDPYQKQCDDFVAEYEPLLLEILVEVMDPGFVCSKIGVCPSAYKLLLGTEKCVWGPSYWCQNMETAARCNAVDHCKRHVWN |
| Enzyme Length | 557 |
| Uniprot Accession Number | Q61207 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | 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 and saposin-C stimulate the hydrolysis of glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). Saposin-C apparently acts by combining with the enzyme and acidic lipid to form an activated complex, rather than by solubilizing the substrate. {ECO:0000250|UniProtKB:P07602}.; FUNCTION: Saposin-B stimulates the hydrolysis of galacto-cerebroside sulfate by arylsulfatase A (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-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12). {ECO:0000250|UniProtKB:P07602}.; FUNCTION: Saposins are specific low-molecular mass non-enzymatic proteins, they participate in the lysosomal degradation of sphingolipids, which takes place by the sequential action of specific hydrolases. {ECO:0000250|UniProtKB:P07602}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (6); Disulfide bond (12); Domain (6); Glycosylation (4); Helix (4); Propeptide (5); Sequence conflict (21); Signal peptide (1) |
| Keywords | 3D-structure;Direct protein sequencing;Disulfide bond;Glycoprotein;Lysosome;Reference proteome;Repeat;Secreted;Signal |
| Interact With | P28798 |
| Induction | |
| Subcellular Location | 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}.; SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P07602}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000250|UniProtKB:P07602 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 5NXB; 5U85; |
| Mapped Pubmed ID | 10196186; 10818106; 11105903; 11371512; 11726558; 11734895; 11741941; 11750125; 11856752; 12208132; 12466851; 12520002; 12652657; 12810822; 12813057; 12867159; 12904583; 14651853; 14681479; 14684827; 15102471; 15236333; 15290897; 15345707; 15469878; 15743835; 16061944; 16141072; 16413927; 16615898; 16861620; 17167097; 17353235; 17560524; 17883393; 18292516; 18480170; 19732768; 19907127; 19913121; 19934382; 20015957; 20042390; 20047948; 20175216; 20463296; 20498017; 20628086; 21257328; 21267068; 21700325; 22167193; 22326583; 22465952; 22832923; 23325523; 23446636; 23520473; 24006456; 24244600; 24371137; 24872419; 25609427; 25698761; 26045750; 26312487; 26420838; 27356620; 27655403; 28541286; 28640985; 28835281; 28972074; 29323104; 29514215; 30026085; 30026265; 30944381; 31143101; 31929594; 32595447; 34033896; 7835907; 7992842; 8573994; 8776585; 9021161; 9022042; 9266755; 9582364; 9678511; |
| Motif | |
| Gene Encoded By | |
| Mass | 61,422 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |