ARSK_BOVIN
ID ARSK_BOVIN Reviewed; 540 AA.
AC Q148F3;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-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 -!- PTM: The 75-kDa precursor undergoes proteolytic processing to yield a
CC 23 kDa form. {ECO:0000250|UniProtKB:Q6UWY0}.
CC -!- PTM: N-glycosylated with both high mannose and complex type sugars.
CC {ECO:0000250|UniProtKB:Q6UWY0}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR EMBL; BC118383; AAI18384.1; -; mRNA.
DR AlphaFoldDB; Q148F3; -.
DR SMR; Q148F3; -.
DR STRING; 9913.ENSBTAP00000026877; -.
DR PaxDb; Q148F3; -.
DR Ensembl; ENSBTAT00000026877; ENSBTAP00000026877; ENSBTAG00000020178.
DR VEuPathDB; HostDB:ENSBTAG00000020178; -.
DR VGNC; VGNC:26179; ARSK.
DR eggNOG; KOG3731; Eukaryota.
DR eggNOG; KOG3867; Eukaryota.
DR GeneTree; ENSGT00940000158982; -.
DR HOGENOM; CLU_006332_6_0_1; -.
DR InParanoid; Q148F3; -.
DR OMA; YGWAVNW; -.
DR TreeFam; TF313545; -.
DR Reactome; R-BTA-1660662; Glycosphingolipid metabolism.
DR Reactome; R-BTA-1663150; The activation of arylsulfatases.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000020178; Expressed in caput epididymis and 101 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..540
FT /note="Arylsulfatase K"
FT /id="PRO_0000250471"
FT ACT_SITE 84
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 318
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT MOD_RES 84
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:Q6UWY0"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 540 AA; 61361 MW; B9B113F30DD575FC CRC64;
MLLLWVSVVA ASALAAPAPG ADGQRRGAIQ AWPDAPNVLL VVSDSFDGRL TFYPGSQVVK
LPFINFMKAH GTSFLNAYTN SPICCPSRAA MWSGLFTHLT ESWNNFKGLD PNYTTWMDVM
EKHGYRTQKF GKLDYTSGHH SISNRVEAWT RDVAFLLRQE GRPMVNLAPK KTKVRVMQVD
WKNTDRAVNW LRKEASNSTQ PFVLYLGLNL PHPYPSPSSG ENFGSSTFHT SRYWLKKVSY
DAIKIPKWSP LSEMHPVDYY SSYTKNCTGK FTEKEIKNIR AFYYAMCAET DAMLGEIILA
LRQLGLLQKT IVIYTSDHGE LAMEHRQFYK MSMYEASSHV PLLIMGPGIQ ANLQVSSVVS
LVDIYPTMLD IAGIPLPQNL SGYSLLPSSS EMFKNEQKFK NLHPPWILSE FHGCNVNAST
YMLRTNQWKY IAYSDGASVL PQLFDLSSDP DELTNIAAKF PEVTSSLDQK LRSIINYPKV
SASVHQYNKE QFIKWKQSIG QNYSNVIANL RWHQDWLKKP KKYENAIDQW LKSHSDAKTI
