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Arylsulfatase

Is commonly produced by soil microorganisms and plays an important role in the mineralization of sulfates.

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Arylsulfatase A

Also known as Arylsulfatase A (ASA) (Cerebroside-sulfatase).
ARSA: Hydrolyzes cerebroside sulfate. Defects in ARSA are a cause of leukodystrophy metachromatic (MLD). MLD is a disease due to a lysosomal storage defect. It is characterized by intralysosomal storage of cerebroside-3-sulfate in neural and non-neural tissues, with a diffuse loss of myelin in the central nervous system. Progressive demyelination causes a variety of neurological symptoms, including gait disturbances, ataxias, optical atrophy, dementia, seizures, and spastic tetraparesis. Three forms of the disease can be distinguished according to the age at onset: late- infantile, juvenile and adult. Arylsulfatase A activity is defective in multiple sulfatase deficiency (MSD). 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. Arylsulfatase A activity is impaired in multiple sulfatase deficiency due to mutations in SUMF1. SUMF1 mutations result in defective post-translational modification of ARSA at residue Cys- 69 that is not converted to 3-oxoalanine. Belongs to the sulfatase family.

Protein type: EC 3.1.6.8; Hydrolase; Lipid Metabolism - sphingolipid

Chromosomal Location of Human Ortholog: 22q13.33

Cellular Component: endoplasmic reticulum lumen; lysosomal lumen; lysosome

Molecular Function: arylsulfatase activity; calcium ion binding; cerebroside-sulfatase activity; protein binding; sulfuric ester hydrolase activity

Biological Process: glycosphingolipid metabolic process; post-translational protein modification

Disease: Metachromatic Leukodystrophy

Arylsulfatase B

Also known as Arylsulfatase B (ASB) (N-acetylgalactosamine-4-sulfatase) (G4S).
ARSB: Defects in ARSB are the cause of mucopolysaccharidosis type 6 (MPS6); also known as Maroteaux-Lamy syndrome. MPS6 is 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. Arylsulfatase B activity is defective in multiple sulfatase deficiency (MSD). 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. 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. Belongs to the sulfatase family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 3.1.6.12; Glycan Metabolism - glycosaminoglycan degradation; Hydrolase

Cellular Component: cell surface; Golgi apparatus; lysosome; mitochondrion; rough endoplasmic reticulum

Molecular Function: arylsulfatase activity; N-acetylgalactosamine-4-sulfatase activity; sulfuric ester hydrolase activity

Biological Process: autophagy; central nervous system development; response to estrogen stimulus; response to methylmercury; response to nutrient; response to pH

Arylsulfatase D

Also known as Arylsulfatase D (ASD).
ARSD: is a member of the sulfatase family. Sulfatases are essential for the correct composition of bone and cartilage matrix. The encoded protein is postranslationally glycosylated and localized to the lysosome. This gene is located within a cluster of similar arylsulfatase genes on chromosome X. A related pseudogene has been identified in the pseudoautosomal region of chromosome Y. [provided by RefSeq, Jul 2011]

Protein type: EC 3.1.6.-; Hydrolase

Chromosomal Location of Human Ortholog: Xp22.3

Cellular Component: endoplasmic reticulum lumen

Molecular Function: arylsulfatase activity

Biological Process: glycosphingolipid metabolic process; post-translational protein modification

Arylsulfatase E

Also known as Arylsulfatase E (ASE).
ARSE: May be essential for the correct composition of cartilage and bone matrix during development. Has no activity toward steroid sulfates. Defects in ARSE are the cause of chondrodysplasia punctata X-linked recessive type 1 (CDPX1). CDP is a clinically and genetically heterogeneous disorder characterized by punctiform calcification of the bones. CDPX1 is a congenital defect of bone and cartilage development characterized by aberrant bone mineralization, severe underdevelopment of nasal cartilage, and distal phalangeal hypoplasia. This disease can also be induced by inhibition with the drug warfarin. Belongs to the sulfatase family.

Protein type: EC 3.1.6.-; Hydrolase

Chromosomal Location of Human Ortholog: Xp22.3

Cellular Component: endoplasmic reticulum lumen

Molecular Function: arylsulfatase activity

Biological Process: glycosphingolipid metabolic process; post-translational protein modification; skeletal development

Disease: Chondrodysplasia Punctata 1, X-linked Recessive

Arylsulfatase F

Also known as Arylsulfatase F (ASF).
ARSF: a member of the sulfatase family, and more specifically, the arylsulfatase subfamily. Members of the subfamily share similarity in sequence and splice sites, and are clustered together on chromosome X, suggesting that they are derived from recent gene duplication events. Sulfatases are essential for the correct composition of bone and cartilage matrix. The activity of this protein, unlike that of arylsulfatase E, is not inhibited by warfarin. Multiple alternatively spliced variants, encoding the same protein, have been identified.[provided by RefSeq, Jan 2011]

Protein type: EC 3.1.6.-; Hydrolase; Secreted; Secreted, signal peptide

Chromosomal Location of Human Ortholog: Xp22.3

Cellular Component: endoplasmic reticulum lumen

Molecular Function: arylsulfatase activity

Biological Process: glycosphingolipid metabolic process; post-translational protein modification

Arylsulfatase G

Also known as Arylsulfatase G (ASG).
ARSG: Displays arylsulfatase activity at acidic pH with pseudosubstrates, such as p-nitrocatechol sulfate and also, but with lower activity, p-nitrophenyl sulfate and 4- methylumbelliferyl sulfate. Belongs to the sulfatase family.

Protein type: EC 3.1.6.-; Endoplasmic reticulum; Hydrolase; Kinase, other; Secreted; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 17q24.2

Cellular Component: endoplasmic reticulum; endoplasmic reticulum lumen; extracellular space; lysosome

Molecular Function: arylsulfatase activity

Biological Process: glycosphingolipid metabolic process; post-translational protein modification; sulfur metabolic process

Arylsulfatase I

Also known as Arylsulfatase I (ASI).
ARSI: Displays arylsulfatase activity at neutral pH, when co- expressed with SUMF1; arylsulfatase activity is measured in the secretion medium of retinal cell line, but no activity is recorded when measured in cell extracts. Belongs to the sulfatase family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Calcium-binding; EC 3.1.6.-; Hydrolase; Secreted; Secreted, signal peptide

Arylsulfatase J

Also known as Arylsulfatase J (ASJ).
ARSJ: Belongs to the sulfatase family

Protein type: EC 3.1.6.-; Hydrolase; Secreted; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 4q26

Cellular Component: endoplasmic reticulum lumen

Molecular Function: arylsulfatase activity

Biological Process: glycosphingolipid metabolic process; post-translational protein modification
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