Arsg
entrez
74008
canonical
uniprot
Q3TYD4
canonical
ensembl
ENSMUSG00000020604
resolver
ensp
ENSMUSP00000020928
resolver
ensp
ENSMUSP00000102307
resolver
ensp
ENSMUSP00000102308
resolver
ensp
ENSMUSP00000237258
resolver
ensp
ENSMUSP00000237259
resolver
ensp
ENSMUSP00000237261
resolver
ensp
ENSMUSP00000237267
resolver
ensp
ENSMUSP00000237272
resolver
genesymbol
Arsg
resolver
genesymbol_syn
Kiaa1001
resolver
uniprot
B1AT67
resolver
uniprot
B1AT68
resolver
uniprot
Q5XFU5
resolver
uniprot
Q69ZT6
resolver
uniprot
Q8CHS3
resolver
uniprot
Q8VBZ5
resolver
uniprot
Q9D3B4
resolver
uniprot_entry
ARSG_MOUSE
resolver
uniprot_sec
B1AT67
resolver
uniprot_sec
B1AT68
resolver
uniprot_sec
Q5XFU5
resolver
uniprot_sec
Q69ZT6
resolver
uniprot_sec
Q8CHS3
resolver
uniprot_sec
Q8VBZ5
resolver
uniprot_sec
Q9D3B4
resolver
amino_acid_sequence
MGWLFLKVLLVGMAFSGFFYPLVDFSISGKTRAPQPNIVIILADDMGWGDLGANWAETKDTTNLDKMASEGMRFVDFHAAASTCSPSRASLLTGRLGLRNGVTHNFAVTSVGGLPVNETTLAEVLRQEGYVTAMIGKWHLGHHGSYHPNFRGFDYYFGIPYSNDMGCTDAPGYNYPPCPACPQRDGLWRNPGRDCYTDVALPLYENLNIVEQPVNLSGLAQKYAERAVEFIEQASTSGRPFLLYVGLAHMHVPLSVTPPLAHPQRQSLYRASLREMDSLVGQIKDKVDHVARENTLLWFTGDNGPWAQKCELAGSVGPFFGLWQTHQGGSPTKQTTWEGGHRVPALAYWPGRVPANVTSTALLSLLDIFPTVIALAGASLPPNRKFDGRDVSEVLFGKSQMGHRVLFHPNSGAAGEYGALQTVRLNHYKAFYITGGAKACDGSVGPEQHHVAPLIFNLEDAADEGMPLQKGSPEYQEVLQQVTRALADVLQDIADDNSSRADYTQDPSVIPCCNPYQTTCRCQPV
uniprot
proteins
ec_number
3.1.6.1
uniprot
proteins
ec_number
3.1.6.15
uniprot
proteins
function
FUNCTION: Displays arylsulfatase activity at acidic pH towards the artificial substrate p-nitrocatechol sulfate (PubMed:25135642). Catalyzes the hydrolysis of the 3-sulfate groups of the N-sulfo-D-glucosamine 3-O-sulfate units of heparin (PubMed:22689975). {ECO:0000269|PubMed:22689975, ECO:0000269|PubMed:25135642}.
uniprot
proteins
mass_dalton
57434
uniprot
proteins
mutagenesis
MUTAGEN 117; /note="N->Q: Faster electrophoretic migration typical of a size reduction probably due to glycosylation loss."; /evidence="ECO:0000269|PubMed:25135642"; MUTAGEN 215; /note="N->Q: Faster electrophoretic migration typical of a size reduction probably due to glycosylation loss."; /evidence="ECO:0000269|PubMed:25135642"; MUTAGEN 356; /note="N->Q: Faster electrophoretic migration typical of a size reduction probably due to glycosylation loss."; /evidence="ECO:0000269|PubMed:25135642"; MUTAGEN 497; /note="N->Q: Faster electrophoretic migration typical of a size reduction probably due to glycosylation loss. Abolishes proteolytic cleavage."; /evidence="ECO:0000269|PubMed:25135642
uniprot
proteins
post_translational_modification
PTM: N-glycosylated with both high mannose and complex type sugars. {ECO:0000269|PubMed:25135642}.; 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. {ECO:0000250|UniProtKB:P15289}.; PTM: The 63-kDa precursor undergoes proteolytic processing in two steps, yielding two fragments in the first step (apparent molecular masses of 44 and 18 kDa). In the second step, the 44-kDa fragment is processed further to the 34- and 10-kDa chains. The 10-kDa chain is a cleavage product of the 44-kDa fragment but linked to the 18-kDa chain through a disulfide bridge. {ECO:0000269|PubMed:25135642}.
uniprot
proteins
protein_family
Sulfatase family
uniprot
proteins
pubmed
15368895
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16174644
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
22689975
uniprot
proteins
pubmed
25135642
uniprot
proteins
sequence_length
525
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:25135642}. Note=The 63-kDa precursor protein localizes to pre-lysosomal compartments and tightly associates with organelle membranes, most likely the endoplasmic reticulum. In contrast, proteolytically processed fragments of 34-, 18- and 10-kDa are found in lysosomal fractions and lose their membrane association. {ECO:0000269|PubMed:25135642}.
uniprot
proteins