ARSB

Arylsulfatase B encoded by this gene belongs to the sulfatase family. The arylsulfatase B homodimer hydrolyzes sulfate groups of N-Acetyl-D-galactosamine, chondriotin sulfate, and dermatan sulfate. The protein is targetted to the lysozyme. Mucopolysaccharidosis type VI is an autosomal recessive lysosomal storage disorder resulting from a deficiency of arylsulfatase B. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. [provided by RefSeq]

Full Name

arylsulfatase B

Function

Removes sulfate groups from chondroitin-4-sulfate (C4S) and regulates its degradation (PubMed:19306108).
Involved in the regulation of cell adhesion, cell migration and invasion in colonic epithelium (PubMed:19306108).
In the central nervous system, is a regulator of neurite outgrowth and neuronal plasticity, acting through the control of sulfate glycosaminoglycans and neurocan levels (By similarity).

Biological Process

Autophagy Source: Ensembl
Central nervous system development Source: Ensembl
Chondroitin sulfate catabolic process Source: Reactome
Colon epithelial cell migration Source: UniProtKB
Lysosomal transport Source: ProtInc
Lysosome organization Source: ProtInc
Neutrophil degranulation Source: Reactome
Positive regulation of neuron projection development Source: UniProtKB
Regulation of epithelial cell migration Source: UniProtKB
Response to estrogen Source: Ensembl
Response to methylmercury Source: Ensembl
Response to nutrient Source: Ensembl
Response to pH Source: Ensembl

Cellular Location

Lysosome; Cell surface

Involvement in disease

Mucopolysaccharidosis 6 (MPS6): An autosomal recessive lysosomal storage disease characterized by intracellular accumulation of dermatan sulfate. Clinical features can include abnormal growth, short stature, stiff joints, skeletal malformations, corneal clouding, hepatosplenomegaly, and cardiac abnormalities. A wide variation in clinical severity is observed.
Multiple sulfatase deficiency (MSD): The protein represented in this entry is involved in disease pathogenesis. Arylsulfatase B activity is impaired in multiple sulfatase deficiency due to mutations in SUMF1. SUMF1 mutations result in defective post-translational modification of ARSB at residue Cys-91 that is not converted to 3-oxoalanine. A clinically and biochemically heterogeneous disorder caused by the simultaneous impairment of all sulfatases, due to defective post-translational modification and activation. It combines features of individual sulfatase deficiencies such as metachromatic leukodystrophy, mucopolysaccharidosis, chondrodysplasia punctata, hydrocephalus, ichthyosis, neurologic deterioration and developmental delay.

PTM

The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. This post-translational modification is severely defective in multiple sulfatase deficiency (MSD).