| UniProt ID | SAP_RAT | |
|---|---|---|
| UniProt AC | P10960 | |
| Protein Name | Prosaposin | |
| Gene Name | Psap | |
| Organism | Rattus norvegicus (Rat). | |
| Sequence Length | 554 | |
| Subcellular Localization |
Lysosome . Prosaposin: Secreted . Secreted as a fully glycosylated 70 kDa protein composed of complex glycans. |
|
| Protein Description | 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.; 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.; 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.; Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12).; Saposins are specific low-molecular mass non-enzymic proteins, they participate in the lysosomal degradation of sphingolipids, which takes place by the sequential action of specific hydrolases.. | |
| Protein Sequence | MYALALLASLLVTALTSPVQDPKICSGGSAVVCRDVKTAVDCRAVKHCQQMVWSKPTAKSLPCDICKTVVTEAGNLLKDNATEEEILHYLEKTCAWIHDSSLSASCKEVVDSYLPVILDMIKGEMSNPGEVCSALNLCQSLQEYLAEQNQRQLESNKIPEVDLARVVAPFMSNIPLLLYPQDRPRSQPQPKANEDVCQDCMKLVTDIQTAVRTNSSFVQGLVDHVKEDCDRLGPGVSDICKNYVDQYSEVAVQMMMHMQPKEICVMVGFCDEVKRVPMRTLVPATEAIKNILPALELTDPYEQDVIQAQNVIFCQVCQLVMRKLSELIINNATEELLIKGLSKACSLLPAPASTKCQEVLVTFGPSLLDVLMHEVNPNFLCGVISLCSANPNLVGTLEQPAAAIVSALPKEPAPPKQPEEPKQSALRAHVPPQKNGGFCEVCKKLVIYLEHNLEKNSTKEEILAALEKGCSFLPDPYQKQCDEFVAEYEPLLLEILVEVMDPSFVCSKIGVCPSAYKLLLGTEKCVWGPGYWCQNSETAARCNAVDHCKRHVWN | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 80 | N-linked_Glycosylation | AGNLLKDNATEEEIL HHHHHHCCCCHHHHH | 47.37 | - | |
| 214 | N-linked_Glycosylation | IQTAVRTNSSFVQGL HHHHHHCCCHHHHHH | 25.70 | - | |
| 331 | N-linked_Glycosylation | LSELIINNATEELLI HHHHHHCCCCHHHHH | 37.52 | - | |
| 456 | N-linked_Glycosylation | LEHNLEKNSTKEEIL HHHHCCCCCCHHHHH | 45.60 | - | |
| 477 | Phosphorylation | CSFLPDPYQKQCDEF CCCCCCHHHHHHHHH | 35.40 | 21738781 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of SAP_RAT !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SAP_RAT !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of SAP_RAT !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of SAP_RAT !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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