ARSA
entrez
410
canonical
uniprot
P15289
canonical
ensembl
ENSG00000100299
resolver
ensp
ENSP00000216124
resolver
ensp
ENSP00000348406
resolver
ensp
ENSP00000378981
resolver
ensp
ENSP00000378983
resolver
ensp
ENSP00000412542
resolver
ensp
ENSP00000665344
resolver
enst
ENST00000216124
resolver
enst
ENST00000356098
resolver
enst
ENST00000395619
resolver
enst
ENST00000395621
resolver
genesymbol
ARSA
resolver
hgnc
HGNC:713
resolver
uniprot
A0A0C4DFZ2
resolver
uniprot
B2RCA6
resolver
uniprot
B4DVI5
resolver
uniprot
B7XD04
resolver
uniprot
F8WCC8
resolver
uniprot
Q6ICI5
resolver
uniprot
Q96CJ0
resolver
uniprot_entry
A0A0C4DFZ2_HUMAN
resolver
uniprot_entry
ARSA_HUMAN
resolver
uniprot_entry
B4DVI5_HUMAN
resolver
uniprot_sec
B2RCA6
resolver
uniprot_sec
B7XD04
resolver
uniprot_sec
F8WCC8
resolver
uniprot_sec
Q6ICI5
resolver
uniprot_sec
Q96CJ0
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by phosphate. The phosphate forms a covalent bond with the active site 3-oxoalanine. {ECO:0000269|PubMed:12888274}.
uniprot
proteins
amino_acid_sequence
MGAPRSLLLALAAGLAVARPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCDGGCDQGLVPIPLLANLSVEAQPPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNVTLDGFDLSPLLLGTGKSPRQSLFFYPSYPDEVRGVFAVRTGKYKAHFFTQGSAHSDTTADPACHASSSLTAHEPPLLYDLSKDPGENYNLLGGVAGATPEVLQALKQLQLLKAQLDAAVTFGPSQVARGEDPALQICCHPGCTPRPACCHCPDPHA
uniprot
proteins
disease_involvement
DISEASE: Metachromatic leukodystrophy (MLD) [MIM:250100]: An 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. {ECO:0000269|PubMed:10220151, ECO:0000269|PubMed:10381328, ECO:0000269|PubMed:10477432, ECO:0000269|PubMed:10533072, ECO:0000269|PubMed:10751093, ECO:0000269|PubMed:11020646, ECO:0000269|PubMed:11061266, ECO:0000269|PubMed:11456299, ECO:0000269|PubMed:11941485, ECO:0000269|PubMed:12503099, ECO:0000269|PubMed:12788103, ECO:0000269|PubMed:1353340, ECO:0000269|PubMed:14517960, ECO:0000269|PubMed:14680985, ECO:0000269|PubMed:15026521, ECO:0000269|PubMed:15326627, ECO:0000269|PubMed:15710861, ECO:0000269|PubMed:1670590, ECO:0000269|PubMed:1673291, ECO:0000269|PubMed:1678251, ECO:0000269|PubMed:18693274, ECO:0000269|PubMed:19606494, ECO:0000269|PubMed:20339381, ECO:0000269|PubMed:21265945, ECO:0000269|PubMed:2574462, ECO:0000269|PubMed:7581401, ECO:0000269|PubMed:7825603, ECO:0000269|PubMed:7860068, ECO:0000269|PubMed:7902317, ECO:0000269|PubMed:7906588, ECO:0000269|PubMed:7909527, ECO:0000269|PubMed:8095918, ECO:0000269|PubMed:8101038, ECO:0000269|PubMed:8101083, ECO:0000269|PubMed:8104633, ECO:0000269|PubMed:8891236, ECO:0000269|PubMed:9090526, ECO:0000269|PubMed:9272717, ECO:0000269|PubMed:9452102, ECO:0000269|PubMed:9490297, ECO:0000269|PubMed:9600244, ECO:0000269|PubMed:9819708}. Note=The disease is caused by variants 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 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). {ECO:0000269|PubMed:15146462, ECO:0000269|PubMed:7628016}.
uniprot
proteins
ec_number
3.1.6.8
uniprot
proteins
function
FUNCTION: Lysosomal enzyme that catalyzes the hydrolysis of cerebroside-3-sulfate (N-acyl-1-beta-D-(3-O-sulfo)-galactosyl-sphing-4-enine) into cerebroside and sulfate, a reaction that requires the activator protein saposin B (PubMed:10751093, PubMed:19224915, PubMed:24294900). Also involved in the catabolism of other sulfoglycosphingolipids such as SB1a and SM3 (beta-D-3-sulfogalactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine) (By similarity). {ECO:0000250|UniProtKB:P50428, ECO:0000269|PubMed:10751093, ECO:0000269|PubMed:19224915, ECO:0000269|PubMed:24294900}.
uniprot
proteins
mass_dalton
53588
uniprot
proteins
mutagenesis
MUTAGEN 69..70; /note="CT->TC: Strongly reduces formation of 3-oxoalanine (also known as C-formylglycine, FGly)."; /evidence="ECO:0000269|PubMed:9342345"; MUTAGEN 69; /note="C->A: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:11124905"; MUTAGEN 69; /note="C->S: Abolishes formation of 3-oxoalanine (also known as C-formylglycine, FGly). Strongly decreases enzyme activity."; /evidence="ECO:0000269|PubMed:11124905, ECO:0000269|PubMed:9342345
uniprot
proteins
post_translational_modification
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, ECO:0000269|PubMed:9342345}.
uniprot
proteins
protein_family
Sulfatase family
uniprot
proteins
pubmed
10220151
uniprot
proteins
pubmed
10381328
uniprot
proteins
pubmed
10477432
uniprot
proteins
pubmed
10533072
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
10751093
uniprot
proteins
pubmed
11020646
uniprot
proteins
pubmed
11061266
uniprot
proteins
pubmed
11124905
uniprot
proteins
pubmed
11456299
uniprot
proteins
pubmed
11941485
uniprot
proteins
pubmed
12503099
uniprot
proteins
pubmed
12788103
uniprot
proteins
pubmed
12888274
uniprot
proteins
pubmed
1352993
uniprot
proteins
pubmed
1353340
uniprot
proteins
pubmed
14517960
uniprot
proteins
pubmed
14680985
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15026521
uniprot
proteins
pubmed
15146462
uniprot
proteins
pubmed
15326627
uniprot
proteins
pubmed
15461802
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15710861
uniprot
proteins
pubmed
16368756
uniprot
proteins
pubmed
1670590
uniprot
proteins
pubmed
1673291
uniprot
proteins
pubmed
1678251
uniprot
proteins
pubmed
18693274
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19224915
uniprot
proteins
pubmed
19262745
uniprot
proteins
pubmed
19606494
uniprot
proteins
pubmed
1975241
uniprot
proteins
pubmed
20339381
uniprot
proteins
pubmed
21265945
uniprot
proteins
pubmed
24294900
uniprot
proteins
pubmed
2562955
uniprot
proteins
pubmed
2574462
uniprot
proteins
pubmed
7581401
uniprot
proteins
pubmed
7628016
uniprot
proteins
pubmed
7825603
uniprot
proteins
pubmed
7860068
uniprot
proteins
pubmed
7866401
uniprot
proteins
pubmed
7902317
uniprot
proteins
pubmed
7906588
uniprot
proteins
pubmed
7909527
uniprot
proteins
pubmed
8095918
uniprot
proteins
pubmed
8101038
uniprot
proteins
pubmed
8101083
uniprot
proteins
pubmed
8104633
uniprot
proteins
pubmed
8723680
uniprot
proteins
pubmed
8891236
uniprot
proteins
pubmed
9090526
uniprot
proteins
pubmed
9272717
uniprot
proteins
pubmed
9342345
uniprot
proteins
pubmed
9452102
uniprot
proteins
pubmed
9490297
uniprot
proteins
pubmed
9521684
uniprot
proteins
pubmed
9600244
uniprot
proteins
pubmed
9744473
uniprot
proteins
pubmed
9819708
uniprot
proteins
pubmed
9888390
uniprot
proteins
sequence_length
507
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:9342345}. Lysosome {ECO:0000305|PubMed:2562955}.
uniprot
proteins