ARSK_DANRE
ID ARSK_DANRE Reviewed; 523 AA.
AC Q08CJ7;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
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; ORFNames=zgc:153019;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Zebrafish Gene Collection (ZGC) 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; BC124212; AAI24213.1; -; mRNA.
DR RefSeq; NP_001070625.1; NM_001077157.1.
DR AlphaFoldDB; Q08CJ7; -.
DR SMR; Q08CJ7; -.
DR STRING; 7955.ENSDARP00000077752; -.
DR PaxDb; Q08CJ7; -.
DR GeneID; 562412; -.
DR KEGG; dre:562412; -.
DR CTD; 153642; -.
DR ZFIN; ZDB-GENE-060929-332; arsk.
DR eggNOG; KOG3731; Eukaryota.
DR InParanoid; Q08CJ7; -.
DR OrthoDB; 349944at2759; -.
DR PhylomeDB; Q08CJ7; -.
DR Reactome; R-DRE-1660662; Glycosphingolipid metabolism.
DR Reactome; R-DRE-1663150; The activation of arylsulfatases.
DR PRO; PR:Q08CJ7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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..16
FT /evidence="ECO:0000255"
FT CHAIN 17..523
FT /note="Arylsulfatase K"
FT /id="PRO_0000356289"
FT ACT_SITE 75
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 35
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 308
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT MOD_RES 75
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:Q6UWY0"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 523 AA; 59499 MW; 16C87DCE83BCB0FA CRC64;
MLRVFVLLIF NVNAYCMYLN WTSHDRPNIV MIMSDAFDGR LTFQPGNKVV QLPYINYMRE
LGSVFLNSYT NSPICCPSRA AMWSGQFVHL TQSWNNNKCL HPNATTWMDD LRKSGYHTHS
MGKLDYTSGH HSVSNRVEAW TRDVPFLLRQ EGRPVTDLVG DASTKRVMIK DWTITDAAVQ
WIRNTTASLT QPFALYLGLN LPHPYRTDSL GPTAGGSTFR TSPYWLNKVS YNQVSVPKWL
RFKDMHPVDY YSTVTKNCSG HFTEEEIRNI RAFYYAMCAE TDGMLGEVMA ALRDTGSLNK
TVVLFTSDHG DLAMEHRQFY KMSMFEGSSH VPLLIMGPGV KSGFEVSLPV SLVDIYPTVL
DLAGVPQTGG LSGHSLIPLI SRVSIHSAEP HPAWAFSEYH GCNANTSTYM LRIAEWKYIA
YADGLNVPPQ LFNLSKDESE LRNIASQFPD VCQDLDKLLR SIVDYPSVSK SVHRYNKQQF
LEWKQSLGDS YSQVIASLRW HVDWKKDAKS YERDIDEWLL GLD
