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Entry version 216 (18 Sep 2019)
Sequence version 3 (01 Feb 1991)
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Protein

Arylsulfatase A

Gene

ARSA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Hydrolyzes cerebroside sulfate.2 Publications

Miscellaneous

The metal cofactor was first identified as magnesium ion, based on the structure of the recombinant protein, but when purified from human placenta, the protein contains 1 calcium ion per subunit.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+1 PublicationNote: Binds 1 Ca2+ ion per subunit.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by phosphate. The phosphate forms a covalent bond with the active site 3-oxoalanine.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 0,087 sec(-1) with galactosyl-3-sulfate ceramide as substrate.1 Publication
  1. KM=0.099 mM for galactosyl-3-sulfate ceramide1 Publication

    pH dependencei

    Optimum pH is 4.5.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi29CalciumCombined sources1 Publication1
    Metal bindingi30CalciumCombined sources1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei69Nucleophile1 Publication1
    Metal bindingi69Calcium; via 3-oxoalanineCombined sources1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei123Substrate1 Publication1
    Active sitei1251 Publication1
    Binding sitei150Substrate1 Publication1
    Binding sitei229Substrate1 Publication1
    Metal bindingi281CalciumCombined sources1 Publication1
    Metal bindingi282CalciumCombined sources1 Publication1
    Binding sitei302Substrate1 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionHydrolase
    LigandCalcium, Metal-binding

    Enzyme and pathway databases

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-1660662 Glycosphingolipid metabolism
    R-HSA-1663150 The activation of arylsulfatases
    R-HSA-6798695 Neutrophil degranulation

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P15289

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    P15289

    Chemistry databases

    SwissLipids knowledge resource for lipid biology

    More...
    SwissLipidsi
    SLP:000000913

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Arylsulfatase A (EC:3.1.6.82 Publications)
    Short name:
    ASA
    Alternative name(s):
    Cerebroside-sulfatase
    Cleaved into the following 2 chains:
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:ARSA
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 22

    Organism-specific databases

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:713 ARSA

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    607574 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P15289

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Endoplasmic reticulum, Lysosome

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

    Metachromatic leukodystrophy (MLD)42 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionAn autosomal recessive disease caused by abnormal intralysosomal accumulation of cerebroside-3-sulfate in central and peripheral nervous systems, as well as other organs. MLD is clinically characterized by leukodystrophy, progressive demyelination and a variety of neurological symptoms, including gait disturbances, ataxias, optical atrophy, dementia, seizures, and spastic tetraparesis. Decreased arylsulfatase A activity is detected in urine, leukocytes, and fibroblasts of affected individuals. Several forms of the disease can be distinguished according to the age at onset and disease severity: late infantile, juvenile and adult forms, partial cerebroside sulfate deficiency, and pseudoarylsulfatase A deficiency. Individuals with pseudoarylsulfatase A deficiency have low arylsulfatase A activity but lack neurological manifestations and are apparently healthy.
    Related information in OMIM
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_05416418A → D in MLD; enzyme activity reduced to 5% of wild-type enzyme. 1 PublicationCorresponds to variant dbSNP:rs199476339Ensembl.1
    Natural variantiVAR_05416529D → N in MLD; infantile-onset; causes a severe reduction of enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs199476346Ensembl.1
    Natural variantiVAR_05416630D → H in MLD; enzyme activity reduced to 2.4% of wild-type enzyme. 1 PublicationCorresponds to variant dbSNP:rs199476340Ensembl.1
    Natural variantiVAR_05416732G → S in MLD; late-infantile form. 1 PublicationCorresponds to variant dbSNP:rs199476350Ensembl.1
    Natural variantiVAR_06741452L → P in MLD; loss of enzymatic activity. 1 PublicationCorresponds to variant dbSNP:rs199476357Ensembl.1
    Natural variantiVAR_05416868L → P in MLD; late-infantile form. 1 PublicationCorresponds to variant dbSNP:rs199476351Ensembl.1
    Natural variantiVAR_00724482P → L in MLD; late-infantile-onset. 2 PublicationsCorresponds to variant dbSNP:rs6151411Ensembl.1
    Natural variantiVAR_00724584R → Q in MLD; mild. 2 PublicationsCorresponds to variant dbSNP:rs74315458Ensembl.1
    Natural variantiVAR_05416984R → W in MLD; juvenile form. 1 PublicationCorresponds to variant dbSNP:rs199476352Ensembl.1
    Natural variantiVAR_00724686G → D in MLD; severe; no enzyme residual activity; leads to a decreased stability of the mutant enzyme; causes an arrest of the mutant enzyme polypeptide in a prelysosomal compartment. 2 PublicationsCorresponds to variant dbSNP:rs74315460Ensembl.1
    Natural variantiVAR_05417094P → A in MLD; adult form. 1 PublicationCorresponds to variant dbSNP:rs199476353Ensembl.1
    Natural variantiVAR_00724795S → N in MLD. 1 PublicationCorresponds to variant dbSNP:rs199476363Ensembl.1
    Natural variantiVAR_00724896S → F in MLD; severe. 1 PublicationCorresponds to variant dbSNP:rs74315456Ensembl.1
    Natural variantiVAR_00724996S → L in MLD; severe; no enzyme residual activity. 1 PublicationCorresponds to variant dbSNP:rs199476371Ensembl.1
    Natural variantiVAR_00725099G → D in MLD; adult type. 2 PublicationsCorresponds to variant dbSNP:rs74315455Ensembl.1
    Natural variantiVAR_05417199G → V in MLD; late-infantile form. 1 PublicationCorresponds to variant dbSNP:rs74315455Ensembl.1
    Natural variantiVAR_007251119G → R in MLD; juvenile-onset. 1 PublicationCorresponds to variant dbSNP:rs199476364Ensembl.1
    Natural variantiVAR_007252122G → S in MLD; adult type. 1 PublicationCorresponds to variant dbSNP:rs74315461Ensembl.1
    Natural variantiVAR_007253135L → P in MLD. 1 PublicationCorresponds to variant dbSNP:rs121434215Ensembl.1
    Natural variantiVAR_007254136P → L in MLD; severe late-infantile type; loss of enzymatic activity. 1 PublicationCorresponds to variant dbSNP:rs74315462Ensembl.1
    Natural variantiVAR_054172136P → S in MLD; late-infantile form. 2 PublicationsCorresponds to variant dbSNP:rs60504011Ensembl.1
    Natural variantiVAR_054173137Missing in MLD. 1 Publication1
    Natural variantiVAR_067415138H → D in MLD; significantly lower activity than wild-type protein. 1 PublicationCorresponds to variant dbSNP:rs199476358Ensembl.1
    Natural variantiVAR_054174143R → G in MLD; juvenile/adult-onset; generates 5% as much activity as the parallel normal control. 1 PublicationCorresponds to variant dbSNP:rs199476373Ensembl.1
    Natural variantiVAR_054175148P → L in MLD; juvenile-onset. 1 PublicationCorresponds to variant dbSNP:rs199476375Ensembl.1
    Natural variantiVAR_007255152D → Y in MLD. 1 PublicationCorresponds to variant dbSNP:rs199476365Ensembl.1
    Natural variantiVAR_054176153Q → H in MLD; late-infantile form; no enzyme residual activity. 1 PublicationCorresponds to variant dbSNP:rs199476377Ensembl.1
    Natural variantiVAR_007256154G → D in MLD. 1 PublicationCorresponds to variant dbSNP:rs74315463Ensembl.1
    Natural variantiVAR_054177155P → L in MLD; juvenile-onset. 1 PublicationCorresponds to variant dbSNP:rs74315464Ensembl.1
    Natural variantiVAR_007257155P → R in MLD. Corresponds to variant dbSNP:rs74315464Ensembl.1
    Natural variantiVAR_054178156C → R in MLD; adult type; enzyme activity reduced to 50% of wild-type enzyme. 1 PublicationCorresponds to variant dbSNP:rs199476348Ensembl.1
    Natural variantiVAR_007258167P → R in MLD. Corresponds to variant dbSNP:rs74315465Ensembl.1
    Natural variantiVAR_007259169D → N in MLD. Corresponds to variant dbSNP:rs74315466Ensembl.1
    Natural variantiVAR_007260172C → Y in MLD; juvenile-onset. 1 PublicationCorresponds to variant dbSNP:rs199476381Ensembl.1
    Natural variantiVAR_007261179I → S in MLD; mild. 5 PublicationsCorresponds to variant dbSNP:rs74315457Ensembl.1
    Natural variantiVAR_054179181L → Q in MLD; infantile form. 1 PublicationCorresponds to variant dbSNP:rs199476378Ensembl.1
    Natural variantiVAR_054180190Q → H in MLD; no enzyme residual activity. 1 PublicationCorresponds to variant dbSNP:rs199476372Ensembl.1
    Natural variantiVAR_054181191P → T in MLD; juvenile-onset. 1 PublicationCorresponds to variant dbSNP:rs199476374Ensembl.1
    Natural variantiVAR_007263201Y → C in MLD; juvenile-onset; results in highly reduced enzyme activity and stability; the mutant enzyme is kept in a prelysosomal compartment. 3 PublicationsCorresponds to variant dbSNP:rs199476345Ensembl.1
    Natural variantiVAR_054182212A → P in MLD; loss of enzymatic activity. 2 PublicationsCorresponds to variant dbSNP:rs199476341Ensembl.1
    Natural variantiVAR_007264212A → V in MLD. 3 PublicationsCorresponds to variant dbSNP:rs74315467Ensembl.1
    Natural variantiVAR_054183217R → H in MLD; enzyme activity reduced to 15.6% of wild-type enzyme. 1 PublicationCorresponds to variant dbSNP:rs148403406Ensembl.1
    Natural variantiVAR_054184219F → V in MLD; enzyme activity reduced to less than 1% of normal activity. 1 PublicationCorresponds to variant dbSNP:rs199476383Ensembl.1
    Natural variantiVAR_007265224A → V in MLD. 1 PublicationCorresponds to variant dbSNP:rs74315468Ensembl.1
    Natural variantiVAR_054185227H → Y in MLD; late-infantile form. 1 PublicationCorresponds to variant dbSNP:rs199476354Ensembl.1
    Natural variantiVAR_007266231P → T in MLD. Corresponds to variant dbSNP:rs74315469Ensembl.1
    Natural variantiVAR_007267244R → C in MLD; juvenile-onset. Corresponds to variant dbSNP:rs74315470Ensembl.1
    Natural variantiVAR_007268244R → H in MLD; infantile-onset. 1 PublicationCorresponds to variant dbSNP:rs199476366Ensembl.1
    Natural variantiVAR_007269245G → R in MLD; severe. 1 PublicationCorresponds to variant dbSNP:rs74315471Ensembl.1
    Natural variantiVAR_054186247F → S in MLD. 2 PublicationsCorresponds to variant dbSNP:rs199476384Ensembl.1
    Natural variantiVAR_007270250S → Y in MLD; infantile-onset. 1 PublicationCorresponds to variant dbSNP:rs199476367Ensembl.1
    Natural variantiVAR_054187253E → K in MLD; late-infantile; decreased enzymatic activity. 2 PublicationsCorresponds to variant dbSNP:rs74315483Ensembl.1
    Natural variantiVAR_054188255D → H in MLD; late-infantile form; no enzyme residual activity; leads to a decreased stability of the mutant enzyme; causes an arrest of the mutant enzyme polypeptide in a prelysosomal compartment. 2 PublicationsCorresponds to variant dbSNP:rs80338819Ensembl.1
    Natural variantiVAR_007271274T → M in MLD; severe; 35% of normal activity. 3 PublicationsCorresponds to variant dbSNP:rs74315472Ensembl.1
    Natural variantiVAR_054189281D → Y in MLD. 1 PublicationCorresponds to variant dbSNP:rs199476386Ensembl.1
    Natural variantiVAR_054190282N → S in MLD; enzyme activity reduced to 0.6% of wild-type enzyme. 1 PublicationCorresponds to variant dbSNP:rs199476342Ensembl.1
    Natural variantiVAR_054191286T → P in MLD; adult type. 1 PublicationCorresponds to variant dbSNP:rs28940894Ensembl.1
    Natural variantiVAR_007272288R → C in MLD. 1 PublicationCorresponds to variant dbSNP:rs74315473Ensembl.1
    Natural variantiVAR_054192288R → H in MLD; adult form. 1 PublicationCorresponds to variant dbSNP:rs199476355Ensembl.1
    Natural variantiVAR_054193293G → D in MLD; late-onset. 1 PublicationCorresponds to variant dbSNP:rs199476387Ensembl.1
    Natural variantiVAR_054194293G → S in MLD; adult type; causes a severe reduction of enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs199476349Ensembl.1
    Natural variantiVAR_054195294C → Y in MLD; juvenile-onset; causes a severe reduction of enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs199476347Ensembl.1
    Natural variantiVAR_007273295S → Y in MLD; severe. 1 PublicationCorresponds to variant dbSNP:rs74315474Ensembl.1
    Natural variantiVAR_054196298L → S in MLD; late-infantile form; complete loss of enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs199476389Ensembl.1
    Natural variantiVAR_008132300C → F in MLD; late-infantile-onset; enzyme activity reduced to less than 1%; the mutant protein is more rapidly degraded in lysosomes; strongly interferes with the octamerization process of the enzyme at low pH. 3 PublicationsCorresponds to variant dbSNP:rs74315484Ensembl.1
    Natural variantiVAR_054197302K → N in MLD; enzyme activity reduced to 2.8% of wild-type enzyme. 1 PublicationCorresponds to variant dbSNP:rs199476343Ensembl.1
    Natural variantiVAR_067416304T → M in MLD; loss of enzymatic activity. 1 PublicationCorresponds to variant dbSNP:rs199476359Ensembl.1
    Natural variantiVAR_054198306Y → H in MLD; juvenile-onset. 1 PublicationCorresponds to variant dbSNP:rs199476379Ensembl.1
    Natural variantiVAR_067417307E → K in MLD; loss of enzymatic activity. 1 PublicationCorresponds to variant dbSNP:rs199476360Ensembl.1
    Natural variantiVAR_054199308G → D in MLD; late-infantile form. 1 PublicationCorresponds to variant dbSNP:rs199476356Ensembl.1
    Natural variantiVAR_054200308G → V in MLD; late-infantile form; no enzyme residual activity. 1 PublicationCorresponds to variant dbSNP:rs199476356Ensembl.1
    Natural variantiVAR_007274309G → S in MLD; severe; 13% of normal activity. 2 PublicationsCorresponds to variant dbSNP:rs74315459Ensembl.1
    Natural variantiVAR_007275311R → Q in MLD; juvenile-onset. 1 PublicationCorresponds to variant dbSNP:rs199476382Ensembl.1
    Natural variantiVAR_054201312E → D in MLD; low amounts of residual enzyme activity; leads to a decreased stability of the mutant enzyme. 1 PublicationCorresponds to variant dbSNP:rs199476390Ensembl.1
    Natural variantiVAR_007276314A → T in MLD; infantile-onset. 1 PublicationCorresponds to variant dbSNP:rs199476368Ensembl.1
    Natural variantiVAR_054202325G → S in MLD; juvenile-onset. 1 PublicationCorresponds to variant dbSNP:rs148092995Ensembl.1
    Natural variantiVAR_054203327T → I in MLD; late-infantile form. 1 Publication1
    Natural variantiVAR_007277335D → V in MLD; late-infantile-onset; loss of enzymatic activity. 5 PublicationsCorresponds to variant dbSNP:rs74315475Ensembl.1
    Natural variantiVAR_007279367K → N in MLD. 1 PublicationCorresponds to variant dbSNP:rs199476369Ensembl.1
    Natural variantiVAR_007280370R → Q in MLD; mild. Corresponds to variant dbSNP:rs74315477Ensembl.1
    Natural variantiVAR_007281370R → W in MLD; severe; no enzyme residual activity. 2 PublicationsCorresponds to variant dbSNP:rs74315476Ensembl.1
    Natural variantiVAR_054204376Y → N in MLD; enzyme activity reduced to 4.7% of wild-type enzyme. 1 PublicationCorresponds to variant dbSNP:rs199476344Ensembl.1
    Natural variantiVAR_007282377P → L in MLD; severe. 1 PublicationCorresponds to variant dbSNP:rs74315478Ensembl.1
    Natural variantiVAR_054205381D → E in MLD; early-infantile form. Corresponds to variant dbSNP:rs6151425Ensembl.1
    Natural variantiVAR_007283382E → K in MLD; intermediate. 1 PublicationCorresponds to variant dbSNP:rs74315479Ensembl.1
    Natural variantiVAR_007284384R → C in MLD. 1 PublicationCorresponds to variant dbSNP:rs199476370Ensembl.1
    Natural variantiVAR_007285390R → Q in MLD; juvenile-onset. 2 PublicationsCorresponds to variant dbSNP:rs199476391Ensembl.1
    Natural variantiVAR_007286390R → W in MLD; late-infantile and juvenile-onset. 3 PublicationsCorresponds to variant dbSNP:rs74315480Ensembl.1
    Natural variantiVAR_007288397H → Y in MLD; adult-onset. 3 PublicationsCorresponds to variant dbSNP:rs199476376Ensembl.1
    Natural variantiVAR_007289398Missing in MLD. 1
    Natural variantiVAR_007290406 – 408Missing in MLD; late-infantile-onset. 1 Publication3
    Natural variantiVAR_067418406S → G in MLD; loss of enzymatic activity. 1 PublicationCorresponds to variant dbSNP:rs199476361Ensembl.1
    Natural variantiVAR_054206408T → I in MLD; adult type. 1 PublicationCorresponds to variant dbSNP:rs28940895Ensembl.1
    Natural variantiVAR_054207409T → I in MLD; mild. 2 PublicationsCorresponds to variant dbSNP:rs74315481Ensembl.1
    Natural variantiVAR_008133425P → T in MLD; juvenile-onset; retains about 12% of specific enzyme activity; the mutant protein is unstable; results in more rapid enzyme degradation in lysosomes; addition of the cysteine protease inhibitor leupeptin increases the amount of the enzyme activity; displays a modest reduction in the octamerization process of the enzyme at low pH. 3 PublicationsCorresponds to variant dbSNP:rs74315485Ensembl.1
    Natural variantiVAR_007291426P → L in MLD; juvenile/adult-onset; mild; common mutation; decreased enzyme activity. 8 PublicationsCorresponds to variant dbSNP:rs28940893Ensembl.1
    Natural variantiVAR_054208428L → P in MLD; late-infantile form. 2 PublicationsCorresponds to variant dbSNP:rs199476392Ensembl.1
    Natural variantiVAR_054209429Y → S in MLD; adult-onset. 1 PublicationCorresponds to variant dbSNP:rs199476380Ensembl.1
    Natural variantiVAR_054210469A → G in MLD; early-infantile form. 1 PublicationCorresponds to variant dbSNP:rs199476385Ensembl.1
    Natural variantiVAR_054211489C → G in MLD; late-onset. 1 PublicationCorresponds to variant dbSNP:rs199476388Ensembl.1
    Multiple sulfatase deficiency (MSD)1 Publication
    The protein represented in this entry is involved in disease pathogenesis. Arylsulfatase A activity is impaired in multiple sulfatase deficiency due to mutations in SUMF1 (PubMed:15146462). SUMF1 mutations result in defective post-translational modification of ARSA at residue Cys-69 that is not converted to 3-oxoalanine (PubMed:7628016).2 Publications
    Disease descriptionA 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.
    Related information in OMIM

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi69 – 70CT → TC: Strongly reduces formation of 3-oxoalanine (also known as C-formylglycine, FGly). 1 Publication2
    Mutagenesisi69C → A: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi69C → S: Abolishes formation of 3-oxoalanine (also known as C-formylglycine, FGly). Strongly decreases enzyme activity. 2 Publications1

    Keywords - Diseasei

    Disease mutation, Ichthyosis, Leukodystrophy, Metachromatic leukodystrophy

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    410

    GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

    More...
    GeneReviewsi
    ARSA

    MalaCards human disease database

    More...
    MalaCardsi
    ARSA
    MIMi250100 phenotype
    272200 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000100299

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...
    Orphaneti
    309271 Metachromatic leukodystrophy, adult form
    309263 Metachromatic leukodystrophy, juvenile form
    309256 Metachromatic leukodystrophy, late infantile form
    751 NON RARE IN EUROPE: Pseudoarylsulfatase A deficiency

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA25005

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL2193

    Drug and drug target database

    More...
    DrugBanki
    DB03821 2-Amino-3-Hydroxy-3-Phosphonooxy-Propionic Acid
    DB01141 Micafungin
    DB01800 N,4-Dihydroxy-N-Oxo-3-(Sulfooxy)Benzenaminium
    DB04786 Suramin

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    ARSA

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 181 PublicationAdd BLAST18
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003341719 – 507Arylsulfatase AAdd BLAST489
    ChainiPRO_000003341819 – 444Arylsulfatase A component BAdd BLAST426
    ChainiPRO_0000033419448 – 507Arylsulfatase A component CAdd BLAST60

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei693-oxoalanine (Cys)2 Publications1
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi156 ↔ 172Combined sources1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi158N-linked (GlcNAc...) asparagineCombined sources2 Publications1
    Disulfide bondi161 ↔ 168Combined sources1 Publication
    Glycosylationi184N-linked (GlcNAc...) asparagineCombined sources1 Publication1
    Disulfide bondi300 ↔ 414Combined sources1 Publication
    Glycosylationi350N-linked (GlcNAc...) asparagine1 Publication1
    Disulfide bondi488 ↔ 500Combined sources1 Publication
    Disulfide bondi489 ↔ 502Combined sources1 Publication
    Disulfide bondi493 ↔ 499Combined sources1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    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).2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P15289

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P15289

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    P15289

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P15289

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P15289

    PeptideAtlas

    More...
    PeptideAtlasi
    P15289

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P15289

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    31108
    53123 [P15289-1]

    PTM databases

    GlyConnect protein glycosylation platform

    More...
    GlyConnecti
    61

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P15289

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    P15289

    UniCarbKB; an annotated and curated database of glycan structures

    More...
    UniCarbKBi
    P15289

    Miscellaneous databases

    CutDB - Proteolytic event database

    More...
    PMAP-CutDBi
    P15289

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000100299 Expressed in 130 organ(s), highest expression level in right testis

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P15289 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P15289 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB025183
    HPA005554

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer at neutral pH and homooctamer at acidic pH. Exists both as a single chain of 58 kDa (component A) or as a chain of 50 kDa (component B) linked by disulfide bond(s) to a 7 kDa chain (component C).

    Interacts with SUMF1.

    3 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    106903, 21 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    P15289, 30 interactors

    Molecular INTeraction database

    More...
    MINTi
    P15289

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000216124

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1507
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P15289

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P15289

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the sulfatase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG3867 Eukaryota
    COG3119 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000157610

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000135352

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P15289

    KEGG Orthology (KO)

    More...
    KOi
    K01134

    Database of Orthologous Groups

    More...
    OrthoDBi
    515367at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P15289

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.720.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR017850 Alkaline_phosphatase_core_sf
    IPR024607 Sulfatase_CS
    IPR000917 Sulfatase_N

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00884 Sulfatase, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53649 SSF53649, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00523 SULFATASE_1, 1 hit
    PS00149 SULFATASE_2, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

    This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: P15289-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide
            10         20         30         40         50
    MGAPRSLLLA LAAGLAVARP PNIVLIFADD LGYGDLGCYG HPSSTTPNLD
    60 70 80 90 100
    QLAAGGLRFT DFYVPVSLCT PSRAALLTGR LPVRMGMYPG VLVPSSRGGL
    110 120 130 140 150
    PLEEVTVAEV LAARGYLTGM AGKWHLGVGP EGAFLPPHQG FHRFLGIPYS
    160 170 180 190 200
    HDQGPCQNLT CFPPATPCDG GCDQGLVPIP LLANLSVEAQ PPWLPGLEAR
    210 220 230 240 250
    YMAFAHDLMA DAQRQDRPFF LYYASHHTHY PQFSGQSFAE RSGRGPFGDS
    260 270 280 290 300
    LMELDAAVGT LMTAIGDLGL LEETLVIFTA DNGPETMRMS RGGCSGLLRC
    310 320 330 340 350
    GKGTTYEGGV REPALAFWPG HIAPGVTHEL ASSLDLLPTL AALAGAPLPN
    360 370 380 390 400
    VTLDGFDLSP LLLGTGKSPR QSLFFYPSYP DEVRGVFAVR TGKYKAHFFT
    410 420 430 440 450
    QGSAHSDTTA DPACHASSSL TAHEPPLLYD LSKDPGENYN LLGGVAGATP
    460 470 480 490 500
    EVLQALKQLQ LLKAQLDAAV TFGPSQVARG EDPALQICCH PGCTPRPACC

    HCPDPHA
    Length:507
    Mass (Da):53,588
    Last modified:February 1, 1991 - v3
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i3DDBE1378B4176A6
    GO
    Isoform 2 (identifier: P15289-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-84: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:423
    Mass (Da):44,881
    Checksum:iD67E0EE072BEC7BB
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    A0A0C4DFZ2A0A0C4DFZ2_HUMAN
    Arylsulfatase A
    ARSA
    509Annotation score:

    Annotation score:2 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    V9GYR0V9GYR0_HUMAN
    Arylsulfatase A
    ARSA
    69Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence AAB03341 differs from that shown. Reason: Erroneous initiation.Curated
    The sequence BAH11167 differs from that shown. Reason: Erroneous initiation.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti290S → P in AK098659 (PubMed:14702039).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_05416418A → D in MLD; enzyme activity reduced to 5% of wild-type enzyme. 1 PublicationCorresponds to variant dbSNP:rs199476339Ensembl.1
    Natural variantiVAR_05416529D → N in MLD; infantile-onset; causes a severe reduction of enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs199476346Ensembl.1
    Natural variantiVAR_05416630D → H in MLD; enzyme activity reduced to 2.4% of wild-type enzyme. 1 PublicationCorresponds to variant dbSNP:rs199476340Ensembl.1
    Natural variantiVAR_05416732G → S in MLD; late-infantile form. 1 PublicationCorresponds to variant dbSNP:rs199476350Ensembl.1
    Natural variantiVAR_06741452L → P in MLD; loss of enzymatic activity. 1 PublicationCorresponds to variant dbSNP:rs199476357Ensembl.1
    Natural variantiVAR_05416868L → P in MLD; late-infantile form. 1 PublicationCorresponds to variant dbSNP:rs199476351Ensembl.1
    Natural variantiVAR_00724376L → P1 PublicationCorresponds to variant dbSNP:rs199476362Ensembl.1
    Natural variantiVAR_00724482P → L in MLD; late-infantile-onset. 2 PublicationsCorresponds to variant dbSNP:rs6151411Ensembl.1
    Natural variantiVAR_00724584R → Q in MLD; mild. 2 PublicationsCorresponds to variant dbSNP:rs74315458Ensembl.1
    Natural variantiVAR_05416984R → W in MLD; juvenile form. 1 PublicationCorresponds to variant dbSNP:rs199476352Ensembl.1
    Natural variantiVAR_00724686G → D in MLD; severe; no enzyme residual activity; leads to a decreased stability of the mutant enzyme; causes an arrest of the mutant enzyme polypeptide in a prelysosomal compartment. 2 PublicationsCorresponds to variant dbSNP:rs74315460Ensembl.1
    Natural variantiVAR_05417094P → A in MLD; adult form. 1 PublicationCorresponds to variant dbSNP:rs199476353Ensembl.1
    Natural variantiVAR_00724795S → N in MLD. 1 PublicationCorresponds to variant dbSNP:rs199476363Ensembl.1
    Natural variantiVAR_00724896S → F in MLD; severe. 1 PublicationCorresponds to variant dbSNP:rs74315456Ensembl.1
    Natural variantiVAR_00724996S → L in MLD; severe; no enzyme residual activity. 1 PublicationCorresponds to variant dbSNP:rs199476371Ensembl.1
    Natural variantiVAR_00725099G → D in MLD; adult type. 2 PublicationsCorresponds to variant dbSNP:rs74315455Ensembl.1
    Natural variantiVAR_05417199G → V in MLD; late-infantile form. 1 PublicationCorresponds to variant dbSNP:rs74315455Ensembl.1
    Natural variantiVAR_007251119G → R in MLD; juvenile-onset. 1 PublicationCorresponds to variant dbSNP:rs199476364Ensembl.1
    Natural variantiVAR_007252122G → S in MLD; adult type. 1 PublicationCorresponds to variant dbSNP:rs74315461Ensembl.1
    Natural variantiVAR_007253135L → P in MLD. 1 PublicationCorresponds to variant dbSNP:rs121434215Ensembl.1
    Natural variantiVAR_007254136P → L in MLD; severe late-infantile type; loss of enzymatic activity. 1 PublicationCorresponds to variant dbSNP:rs74315462Ensembl.1
    Natural variantiVAR_054172136P → S in MLD; late-infantile form. 2 PublicationsCorresponds to variant dbSNP:rs60504011Ensembl.1
    Natural variantiVAR_054173137Missing in MLD. 1 Publication1
    Natural variantiVAR_067415138H → D in MLD; significantly lower activity than wild-type protein. 1 PublicationCorresponds to variant dbSNP:rs199476358Ensembl.1
    Natural variantiVAR_054174143R → G in MLD; juvenile/adult-onset; generates 5% as much activity as the parallel normal control. 1 PublicationCorresponds to variant dbSNP:rs199476373Ensembl.1
    Natural variantiVAR_054175148P → L in MLD; juvenile-onset. 1 PublicationCorresponds to variant dbSNP:rs199476375Ensembl.1
    Natural variantiVAR_007255152D → Y in MLD. 1 PublicationCorresponds to variant dbSNP:rs199476365Ensembl.1
    Natural variantiVAR_054176153Q → H in MLD; late-infantile form; no enzyme residual activity. 1 PublicationCorresponds to variant dbSNP:rs199476377Ensembl.1
    Natural variantiVAR_007256154G → D in MLD. 1 PublicationCorresponds to variant dbSNP:rs74315463Ensembl.1
    Natural variantiVAR_054177155P → L in MLD; juvenile-onset. 1 PublicationCorresponds to variant dbSNP:rs74315464Ensembl.1
    Natural variantiVAR_007257155P → R in MLD. Corresponds to variant dbSNP:rs74315464Ensembl.1
    Natural variantiVAR_054178156C → R in MLD; adult type; enzyme activity reduced to 50% of wild-type enzyme. 1 PublicationCorresponds to variant dbSNP:rs199476348Ensembl.1
    Natural variantiVAR_007258167P → R in MLD. Corresponds to variant dbSNP:rs74315465Ensembl.1
    Natural variantiVAR_007259169D → N in MLD. Corresponds to variant dbSNP:rs74315466Ensembl.1
    Natural variantiVAR_007260172C → Y in MLD; juvenile-onset. 1 PublicationCorresponds to variant dbSNP:rs199476381Ensembl.1
    Natural variantiVAR_007261179I → S in MLD; mild. 5 PublicationsCorresponds to variant dbSNP:rs74315457Ensembl.1
    Natural variantiVAR_054179181L → Q in MLD; infantile form. 1 PublicationCorresponds to variant dbSNP:rs199476378Ensembl.1
    Natural variantiVAR_054180190Q → H in MLD; no enzyme residual activity. 1 PublicationCorresponds to variant dbSNP:rs199476372Ensembl.1
    Natural variantiVAR_054181191P → T in MLD; juvenile-onset. 1 PublicationCorresponds to variant dbSNP:rs199476374Ensembl.1
    Natural variantiVAR_007262193W → C6 PublicationsCorresponds to variant dbSNP:rs6151415Ensembl.1
    Natural variantiVAR_007263201Y → C in MLD; juvenile-onset; results in highly reduced enzyme activity and stability; the mutant enzyme is kept in a prelysosomal compartment. 3 PublicationsCorresponds to variant dbSNP:rs199476345Ensembl.1
    Natural variantiVAR_054182212A → P in MLD; loss of enzymatic activity. 2 PublicationsCorresponds to variant dbSNP:rs199476341Ensembl.1
    Natural variantiVAR_007264212A → V in MLD. 3 PublicationsCorresponds to variant dbSNP:rs74315467Ensembl.1
    Natural variantiVAR_054183217R → H in MLD; enzyme activity reduced to 15.6% of wild-type enzyme. 1 PublicationCorresponds to variant dbSNP:rs148403406Ensembl.1
    Natural variantiVAR_054184219F → V in MLD; enzyme activity reduced to less than 1% of normal activity. 1 PublicationCorresponds to variant dbSNP:rs199476383Ensembl.1
    Natural variantiVAR_007265224A → V in MLD. 1 PublicationCorresponds to variant dbSNP:rs74315468Ensembl.1
    Natural variantiVAR_054185227H → Y in MLD; late-infantile form. 1 PublicationCorresponds to variant dbSNP:rs199476354Ensembl.1
    Natural variantiVAR_007266231P → T in MLD. Corresponds to variant dbSNP:rs74315469Ensembl.1
    Natural variantiVAR_007267244R → C in MLD; juvenile-onset. Corresponds to variant dbSNP:rs74315470Ensembl.1
    Natural variantiVAR_007268244R → H in MLD; infantile-onset. 1 PublicationCorresponds to variant dbSNP:rs199476366Ensembl.1
    Natural variantiVAR_007269245G → R in MLD; severe. 1 PublicationCorresponds to variant dbSNP:rs74315471Ensembl.1
    Natural variantiVAR_054186247F → S in MLD. 2 PublicationsCorresponds to variant dbSNP:rs199476384Ensembl.1
    Natural variantiVAR_007270250S → Y in MLD; infantile-onset. 1 PublicationCorresponds to variant dbSNP:rs199476367Ensembl.1
    Natural variantiVAR_054187253E → K in MLD; late-infantile; decreased enzymatic activity. 2 PublicationsCorresponds to variant dbSNP:rs74315483Ensembl.1
    Natural variantiVAR_054188255D → H in MLD; late-infantile form; no enzyme residual activity; leads to a decreased stability of the mutant enzyme; causes an arrest of the mutant enzyme polypeptide in a prelysosomal compartment. 2 PublicationsCorresponds to variant dbSNP:rs80338819Ensembl.1
    Natural variantiVAR_007271274T → M in MLD; severe; 35% of normal activity. 3 PublicationsCorresponds to variant dbSNP:rs74315472Ensembl.1
    Natural variantiVAR_054189281D → Y in MLD. 1 PublicationCorresponds to variant dbSNP:rs199476386Ensembl.1
    Natural variantiVAR_054190282N → S in MLD; enzyme activity reduced to 0.6% of wild-type enzyme. 1 PublicationCorresponds to variant dbSNP:rs199476342Ensembl.1
    Natural variantiVAR_054191286T → P in MLD; adult type. 1 PublicationCorresponds to variant dbSNP:rs28940894Ensembl.1
    Natural variantiVAR_007272288R → C in MLD. 1 PublicationCorresponds to variant dbSNP:rs74315473Ensembl.1
    Natural variantiVAR_054192288R → H in MLD; adult form. 1 PublicationCorresponds to variant dbSNP:rs199476355Ensembl.1
    Natural variantiVAR_054193293G → D in MLD; late-onset. 1 PublicationCorresponds to variant dbSNP:rs199476387Ensembl.1
    Natural variantiVAR_054194293G → S in MLD; adult type; causes a severe reduction of enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs199476349Ensembl.1
    Natural variantiVAR_054195294C → Y in MLD; juvenile-onset; causes a severe reduction of enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs199476347Ensembl.1
    Natural variantiVAR_007273295S → Y in MLD; severe. 1 PublicationCorresponds to variant dbSNP:rs74315474Ensembl.1
    Natural variantiVAR_054196298L → S in MLD; late-infantile form; complete loss of enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs199476389Ensembl.1
    Natural variantiVAR_008132300C → F in MLD; late-infantile-onset; enzyme activity reduced to less than 1%; the mutant protein is more rapidly degraded in lysosomes; strongly interferes with the octamerization process of the enzyme at low pH. 3 PublicationsCorresponds to variant dbSNP:rs74315484Ensembl.1
    Natural variantiVAR_054197302K → N in MLD; enzyme activity reduced to 2.8% of wild-type enzyme. 1 PublicationCorresponds to variant dbSNP:rs199476343Ensembl.1
    Natural variantiVAR_067416304T → M in MLD; loss of enzymatic activity. 1 PublicationCorresponds to variant dbSNP:rs199476359Ensembl.1
    Natural variantiVAR_054198306Y → H in MLD; juvenile-onset. 1 PublicationCorresponds to variant dbSNP:rs199476379Ensembl.1
    Natural variantiVAR_067417307E → K in MLD; loss of enzymatic activity. 1 PublicationCorresponds to variant dbSNP:rs199476360Ensembl.1
    Natural variantiVAR_054199308G → D in MLD; late-infantile form. 1 PublicationCorresponds to variant dbSNP:rs199476356Ensembl.1
    Natural variantiVAR_054200308G → V in MLD; late-infantile form; no enzyme residual activity. 1 PublicationCorresponds to variant dbSNP:rs199476356Ensembl.1
    Natural variantiVAR_007274309G → S in MLD; severe; 13% of normal activity. 2 PublicationsCorresponds to variant dbSNP:rs74315459Ensembl.1
    Natural variantiVAR_007275311R → Q in MLD; juvenile-onset. 1 PublicationCorresponds to variant dbSNP:rs199476382Ensembl.1
    Natural variantiVAR_054201312E → D in MLD; low amounts of residual enzyme activity; leads to a decreased stability of the mutant enzyme. 1 PublicationCorresponds to variant dbSNP:rs199476390Ensembl.1
    Natural variantiVAR_007276314A → T in MLD; infantile-onset. 1 PublicationCorresponds to variant dbSNP:rs199476368Ensembl.1
    Natural variantiVAR_054202325G → S in MLD; juvenil