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MT000044

UniProt Annotations

Entry Information

Gene Name	arylsulfatase B
Protein Entry	ARSB_HUMAN
UniProt ID	P15848
Species	Human

Comments

Comment type	Description
Alternative Products	Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P15848-1; Sequence=Displayed; Name=2; IsoId=P15848-2; Sequence=VSP_042721; Note=No experimental confirmation available.;
Catalytic Activity	Hydrolysis of the 4-sulfate groups of the N- acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate.
Cofactor	Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 1 Ca(2+) ion per subunit.;
Disease	Mucopolysaccharidosis 6 (MPS6) [MIM:253200]: 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. {ECO:0000269\|PubMed:10036316, ECO:0000269\|PubMed:10738004, ECO:0000269\|PubMed:11802522, ECO:0000269\|PubMed:14974081, ECO:0000269\|PubMed:1550123, ECO:0000269\|PubMed:1718978, ECO:0000269\|PubMed:8116615, ECO:0000269\|PubMed:8125475, ECO:0000269\|PubMed:8541342, ECO:0000269\|PubMed:8651289}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Disease	Multiple sulfatase deficiency (MSD) [MIM:272200]: 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. {ECO:0000269\|PubMed:15146462}. Note=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.
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). {ECO:0000269\|PubMed:7628016}.
Similarity	Belongs to the sulfatase family. {ECO:0000305}.
Subcellular Location	Lysosome.
Subunit	Monomer.