Cloned (Comment) | Organism |
---|---|
expression in HT-1080 cells | Mus musculus |
Protein Variants | Comment | Organism |
---|---|---|
N215Q | residue Asn215 functions as glycosylation site | Mus musculus |
N356Q | residue Asn356 functions as glycosylation site | Mus musculus |
N497Q | mutation of glycosylation site N497 abrogates transport to lysosomes, due to impaired mannose 6-phosphate modification | Mus musculus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
lysosome | 63-kDa single-chain precursor protein localizes to pre-lysosomal compartments and tightly associates with organelle membranes. Proteolytically processed arylsulfatase G fragments of 34-, 18-, and 10-kDa are found in lysosomal fractions and lost their membrane association. Lysosomal transport of arylsulfatase G in the liver is independent of mannose 6-phosphate, sortilin, and Limp2. Mutation of glycosylation site N497 abrogates transport to lysosomes, due to impaired mannose 6-phosphate modification | Mus musculus | 5764 | - |
membrane | 63-kDa single-chain precursor protein localizes to pre-lysosomal compartments and tightly associates with organelle membranes. Proteolytically processed arylsulfatase G fragments of 34-, 18-, and 10-kDa are found in lysosomal fractions and lost their membrane association | Mus musculus | 16020 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | Q3TYD4 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
additional information | presence of a disulfide bridge between the processed 18-kDa fragment and another smaller polypeptide, probably involving residue Cys195 of the 10-kDa chain | Mus musculus |
proteolytic modification | 63-kDa single-chain precursor protein localizes to pre-lysosomal compartments and tightly associates with organelle membranes. Proteolytically processed arylsulfatase G fragments of 34-, 18-, and 10-kDa are found in lysosomal fractions and lost their membrane association. Proteases participating in the processing are cathepsins B and L. Proteolytic processing is dispensable for hydrolytic sulfatase activity in vitro | Mus musculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
brain | - |
Mus musculus | - |
heart | poor expression | Mus musculus | - |
kidney | - |
Mus musculus | - |
liver | - |
Mus musculus | - |
lung | poor expression | Mus musculus | - |
spleen | - |
Mus musculus | - |
testis | - |
Mus musculus | - |
Synonyms | Comment | Organism |
---|---|---|
arylsulfatase G | - |
Mus musculus |