Arylsulfatase A

Mammalian protein found in Homo sapiens
ARSA
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2HI8, 1AUK, 1E1Z, 1E2S, 1E33, 1E3C, 1N2K, 1N2L, 2AIJ, 2AIK

Identifiers
AliasesARSA, MLD, arylsulfatase A, ASA
External IDsOMIM: 607574 MGI: 88077 HomoloGene: 20138 GeneCards: ARSA
Gene location (Human)
Chromosome 22 (human)
Chr.Chromosome 22 (human)[1]
Chromosome 22 (human)
Genomic location for ARSA
Genomic location for ARSA
Band22q13.33Start50,622,754 bp[1]
End50,628,173 bp[1]
Gene location (Mouse)
Chromosome 15 (mouse)
Chr.Chromosome 15 (mouse)[2]
Chromosome 15 (mouse)
Genomic location for ARSA
Genomic location for ARSA
Band15|15 E3Start89,356,679 bp[2]
End89,361,628 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right uterine tube

  • anterior pituitary

  • minor salivary glands

  • right lobe of thyroid gland

  • left lobe of thyroid gland

  • right lobe of liver

  • body of pancreas

  • body of stomach

  • left coronary artery

  • ascending aorta
Top expressed in
  • spermatocyte

  • spermatid

  • seminiferous tubule

  • medial dorsal nucleus

  • left lobe of liver

  • calvaria

  • motor neuron

  • brown adipose tissue

  • lateral geniculate nucleus

  • medial geniculate nucleus
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • calcium ion binding
  • cerebroside-sulfatase activity
  • sulfuric ester hydrolase activity
  • protein binding
  • hydrolase activity
  • catalytic activity
  • metal ion binding
  • arylsulfatase activity
Cellular component
  • lysosome
  • lysosomal lumen
  • extracellular exosome
  • endoplasmic reticulum lumen
  • extracellular region
  • azurophil granule lumen
  • endoplasmic reticulum
Biological process
  • post-translational protein modification
  • metabolism
  • glycosphingolipid metabolic process
  • neutrophil degranulation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

410

11883

Ensembl

ENSG00000100299

ENSMUSG00000022620

UniProt

P15289

P50428

RefSeq (mRNA)
NM_000487
NM_001085425
NM_001085426
NM_001085427
NM_001085428

NM_001362782

NM_009713

RefSeq (protein)
NP_000478
NP_001078894
NP_001078895
NP_001078896
NP_001078897

NP_001349711

NP_033843

Location (UCSC)Chr 22: 50.62 – 50.63 MbChr 15: 89.36 – 89.36 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Arylsulfatase A (or cerebroside-sulfatase) is an enzyme that breaks down sulfatides, namely cerebroside 3-sulfate into cerebroside and sulfate. In humans, arylsulfatase A is encoded by the ARSA gene.[5][6]

Clinical significance

A deficiency in Arylsulfatase A is associated with metachromatic leukodystrophy, an autosomal recessive disease.[7] Multiple sulfatase deficiency (MSD) is also associated with the ARSA gene.[8]

Biochemistry

Enzyme regulation

Arylsulfatase A is inhibited by phosphate, which forms a covalent bond with the active site 3-oxoalanine.[9]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000100299 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000022620 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Stein C, Gieselmann V, Kreysing J, Schmidt B, Pohlmann R, Waheed A, Meyer HE, O'Brien JS, von Figura K (January 1989). "Cloning and expression of human arylsulfatase A". J. Biol. Chem. 264 (2): 1252–9. doi:10.1016/S0021-9258(19)85079-2. PMID 2562955.
  6. ^ Matzner U, Herbst E, Hedayati KK, Lüllmann-Rauch R, Wessig C, Schröder S, Eistrup C, Möller C, Fogh J, Gieselmann V (May 2005). "Enzyme replacement improves nervous system pathology and function in a mouse model for metachromatic leukodystrophy". Hum. Mol. Genet. 14 (9): 1139–52. doi:10.1093/hmg/ddi126. PMID 15772092.
  7. ^ Sevin C, Aubourg P, Cartier N (April 2007). "Enzyme, cell and gene-based therapies for metachromatic leukodystrophy". J. Inherit. Metab. Dis. 30 (2): 175–83. doi:10.1007/s10545-007-0540-z. PMID 17347913. S2CID 25848916.
  8. ^ "UniProt". www.uniprot.org. Retrieved 2023-10-31.
  9. ^ "Arylsulfatase A / ARSA". Sino Biological. Retrieved 12 September 2014.

Further reading

  • Narahara K, Takahashi Y, Murakami M, et al. (1992). "Terminal 22q deletion associated with a partial deficiency of arylsulphatase A". J. Med. Genet. 29 (6): 432–3. doi:10.1136/jmg.29.6.432. PMC 1016000. PMID 1352356.
  • Gieselmann V, Zlotogora J, Harris A, et al. (1995). "Molecular genetics of metachromatic leukodystrophy". Hum. Mutat. 4 (4): 233–42. doi:10.1002/humu.1380040402. PMID 7866401. S2CID 23519007.
  • DeLuca C, Brown JA, Shows TB (1979). "Lysosomal arylsulfatase deficiencies in humans: Chromosome assignments for arylsulfatase A and B". Proc. Natl. Acad. Sci. U.S.A. 76 (4): 1957–61. Bibcode:1979PNAS...76.1957D. doi:10.1073/pnas.76.4.1957. PMC 383512. PMID 36611.
  • Fujii T, Kobayashi T, Honke K, et al. (1992). "Proteolytic processing of human lysosomal arylsulfatase A". Biochim. Biophys. Acta. 1122 (1): 93–8. doi:10.1016/0167-4838(92)90132-W. PMID 1352993.
  • Kappler J, von Figura K, Gieselmann V (1992). "Late-onset metachromatic leukodystrophy: molecular pathology in two siblings". Ann. Neurol. 31 (3): 256–61. doi:10.1002/ana.410310305. PMID 1353340. S2CID 5481565.
  • Li ZG, Waye JS, Chang PL (1992). "Diagnosis of arylsulfatase A deficiency". Am. J. Med. Genet. 43 (6): 976–82. doi:10.1002/ajmg.1320430614. PMID 1357970.
  • Polten A, Fluharty AL, Fluharty CB, et al. (1991). "Molecular basis of different forms of metachromatic leukodystrophy". N. Engl. J. Med. 324 (1): 18–22. doi:10.1056/NEJM199101033240104. PMID 1670590.
  • Kondo R, Wakamatsu N, Yoshino H, et al. (1991). "Identification of a mutation in the arylsulfatase A gene of a patient with adult-type metachromatic leukodystrophy". Am. J. Hum. Genet. 48 (5): 971–8. PMC 1683039. PMID 1673291.
  • Nelson PV, Carey WF, Morris CP (1991). "Population frequency of the arylsulphatase A pseudo-deficiency allele". Hum. Genet. 87 (1): 87–8. doi:10.1007/BF01213099. PMID 1674719. S2CID 12287382.
  • Bohne W, von Figura K, Gieselmann V (1991). "An 11-bp deletion in the arylsulfatase A gene of a patient with late infantile metachromatic leukodystrophy". Hum. Genet. 87 (2): 155–8. doi:10.1007/BF00204172. PMID 1676699. S2CID 21529779.
  • Gieselmann V, Fluharty AL, Tønnesen T, Von Figura K (1991). "Mutations in the arylsulfatase A pseudodeficiency allele causing metachromatic leukodystrophy". Am. J. Hum. Genet. 49 (2): 407–13. PMC 1683316. PMID 1678251.
  • Fluharty AL, Fluharty CB, Bohne W, et al. (1992). "Two new arylsulfatase A (ARSA) mutations in a juvenile metachromatic leukodystrophy (MLD) patient". Am. J. Hum. Genet. 49 (6): 1340–50. PMC 1686463. PMID 1684088.
  • Kreysing J, von Figura K, Gieselmann V (1990). "Structure of the arylsulfatase A gene". Eur. J. Biochem. 191 (3): 627–31. doi:10.1111/j.1432-1033.1990.tb19167.x. PMID 1975241.
  • Gieselmann V, Polten A, Kreysing J, von Figura K (1990). "Arylsulfatase A pseudodeficiency: loss of a polyadenylylation signal and N-glycosylation site". Proc. Natl. Acad. Sci. U.S.A. 86 (23): 9436–40. doi:10.1073/pnas.86.23.9436. PMC 298511. PMID 2574462.
  • Geurts van Kessel AH (1981). "Regional localization of the genes coding for human ACO2, ARSA, and NAGA on chromosome 22". Cytogenet. Cell Genet. 28 (3): 169–72. doi:10.1159/000131527. PMID 7192199.
  • Barth ML, Fensom A, Harris A (1995). "Identification of seven novel mutations associated with metachromatic leukodystrophy". Hum. Mutat. 6 (2): 170–6. doi:10.1002/humu.1380060210. PMID 7581401. S2CID 27966734.
  • Schmidt B, Selmer T, Ingendoh A, von Figura K (1995). "A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency". Cell. 82 (2): 271–8. doi:10.1016/0092-8674(95)90314-3. PMID 7628016.
  • Barth ML, Ward C, Harris A, et al. (1995). "Frequency of arylsulphatase A pseudodeficiency associated mutations in a healthy population". J. Med. Genet. 31 (9): 667–71. doi:10.1136/jmg.31.9.667. PMC 1050073. PMID 7815433.

External links

  • GeneReviews/NCBI/NIH/UW entry on Arylsulfatase A Deficiency - Metachromatic Leukodystrophy
  • OMIM entries on ARSA Deficiency
  • Arylsulfatase+A at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
  • Human ARSA genome location and ARSA gene details page in the UCSC Genome Browser.
  • Overview of all the structural information available in the PDB for UniProt: P15289 (Human Arylsulfatase A) at the PDBe-KB.
  • v
  • t
  • e
  • 1auk: HUMAN ARYLSULFATASE A
    1auk: HUMAN ARYLSULFATASE A
  • 1e1z: CRYSTAL STRUCTURE OF AN ARYLSULFATASE A MUTANT C69S
    1e1z: CRYSTAL STRUCTURE OF AN ARYLSULFATASE A MUTANT C69S
  • 1e2s: CRYSTAL STRUCTURE OF AN ARYLSULFATASE A MUTANT C69A
    1e2s: CRYSTAL STRUCTURE OF AN ARYLSULFATASE A MUTANT C69A
  • 1e33: CRYSTAL STRUCTURE OF AN ARYLSULFATASE A MUTANT P426L
    1e33: CRYSTAL STRUCTURE OF AN ARYLSULFATASE A MUTANT P426L
  • 1e3c: CRYSTAL STRUCTURE OF AN ARYLSULFATASE A MUTANT C69S SOAKED IN SYNTHETIC SUBSTRATE
    1e3c: CRYSTAL STRUCTURE OF AN ARYLSULFATASE A MUTANT C69S SOAKED IN SYNTHETIC SUBSTRATE
  • 1n2k: Crystal structure of a covalent intermediate of endogenous human arylsulfatase A
    1n2k: Crystal structure of a covalent intermediate of endogenous human arylsulfatase A
  • 1n2l: Crystal structure of a covalent intermediate of endogenous human arylsulfatase A
    1n2l: Crystal structure of a covalent intermediate of endogenous human arylsulfatase A
  • v
  • t
  • e
3.1.1: Carboxylic
ester hydrolases
3.1.2: Thioesterase
3.1.3: Phosphatase
3.1.4:
Phosphodiesterase
3.1.6: Sulfatase
Nuclease (includes
deoxyribonuclease
and ribonuclease)
3.1.11-16:
Exonuclease
Exodeoxyribonuclease
Exoribonuclease
3.1.21-31:
Endonuclease
Endodeoxyribonuclease
Endoribonuclease
either deoxy- or ribo-    


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