ARSK_XENLA
ID ARSK_XENLA Reviewed; 536 AA.
AC Q0IHJ2;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Arylsulfatase K;
DE Short=ASK;
DE EC=3.1.6.1 {ECO:0000250|UniProtKB:Q6UWY0};
DE AltName: Full=Glucuronate-2-sulfatase;
DE EC=3.1.6.18 {ECO:0000250|UniProtKB:Q6UWY0};
DE Flags: Precursor;
GN Name=arsk;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolysis of pseudosubstrates such as p-
CC nitrocatechol sulfate and p-nitrophenyl sulfate (By similarity).
CC Catalyzes the hydrolysis of the 2-sulfate groups of the 2-O-sulfo-D-
CC glucuronate residues of chondroitin sulfate, heparin and heparitin
CC sulfate (By similarity). Acts selectively on 2-sulfoglucuronate and
CC lacks activity against 2-sulfoiduronate (By similarity).
CC {ECO:0000250|UniProtKB:Q6UWY0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aryl sulfate + H2O = a phenol + H(+) + sulfate;
CC Xref=Rhea:RHEA:17261, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:33853, ChEBI:CHEBI:140317; EC=3.1.6.1;
CC Evidence={ECO:0000250|UniProtKB:Q6UWY0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of the 2-sulfate groups of the 2-O-sulfo-D-
CC glucuronate residues of chondroitin sulfate, heparin and heparitin
CC sulfate.; EC=3.1.6.18; Evidence={ECO:0000250|UniProtKB:Q6UWY0};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P15289};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P15289};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q6UWY0}. Lysosome
CC {ECO:0000250|UniProtKB:Q6UWY0}.
CC -!- PTM: The conversion to 3-oxoalanine (also known as C-formylglycine,
CC FGly), of a serine or cysteine residue in prokaryotes and of a cysteine
CC residue in eukaryotes, is critical for catalytic activity.
CC {ECO:0000250|UniProtKB:Q6UWY0}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR EMBL; BC123132; AAI23133.1; -; mRNA.
DR RefSeq; NP_001090303.1; NM_001096834.1.
DR AlphaFoldDB; Q0IHJ2; -.
DR SMR; Q0IHJ2; -.
DR DNASU; 779212; -.
DR GeneID; 779212; -.
DR KEGG; xla:779212; -.
DR CTD; 779212; -.
DR Xenbase; XB-GENE-1000372; arsk.L.
DR OrthoDB; 349944at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 779212; Expressed in liver and 15 other tissues.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0004065; F:arylsulfatase activity; ISS:UniProtKB.
DR GO; GO:0015024; F:glucuronate-2-sulfatase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR000917; Sulfatase_N.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 2: Evidence at transcript level;
KW Calcium; Glycoprotein; Hydrolase; Lysosome; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..536
FT /note="Arylsulfatase K"
FT /id="PRO_0000356290"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 315
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT MOD_RES 82
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:Q6UWY0"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 536 AA; 60658 MW; 87974CA3254A3292 CRC64;
MIQKCIALSL FLFSALPEDN IVRALSLSPN NPKSNVVMVM SDAFDGRLTL LPENGLVSLP
YINFMKKHGA LFLNAYTNSP ICCPSRAAMW SGLFPHLTES WNNYKCLDSD YPTWMDIVEK
NGYVTQRLGK QDYKSGSHSL SNRVEAWTRD VPFLLRQEGR PCANLTGNKT QTRVMALDWK
NVDTATAWIQ KAAQNHSQPF FLYLGLNLPH PYPSETMGEN FGSSTFLTSP YWLQKVPYKN
VTIPKWKPLQ SMHPVDYYSS YTKNCTAPFT EQEIRDIRAY YYAMCAEADG LLGEIISALN
DTGLLGRTYV VFTSDHGELA MEHRQFYKMS MYEGSSHIPL LIMGPRISPG QQISTVVSLV
DLYPTMLEIA GVQIPQNISG YSLMPLLSAS SNKNVSPSIS VHPNWAMSEF HGSDANASTY
MLWDNYWKYV AYADGDSVAP QLFDLSSDPD ELTNVAGQVP EKVQEMDKKL RSIVDYPKVS
ASVHVYNKQQ FALWKASVGA NYTNVIANLR WHADWNKRPR AYEMAIEKWI KSTRQH
