ID   GALNS_PIG               Reviewed;         522 AA.
AC   Q8WNQ7;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=N-acetylgalactosamine-6-sulfatase;
DE            EC=3.1.6.4;
DE   AltName: Full=Chondroitinsulfatase;
DE            Short=Chondroitinase;
DE   AltName: Full=Galactose-6-sulfate sulfatase;
DE   AltName: Full=N-acetylgalactosamine-6-sulfate sulfatase;
DE            Short=GalNAc6S sulfatase;
DE   Flags: Precursor;
GN   Name=GALNS;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12489154; DOI=10.1080/03008200290001131;
RA   Yamakoshi Y., Hu J.C., Liu S., Sun X., Zhang C., Oida S., Fukae M.,
RA   Simmer J.P.;
RT   "Porcine N-acetylgalactosamine 6-sulfatase (GALNS) cDNA sequence and
RT   expression in developing teeth.";
RL   Connect. Tissue Res. 43:167-175(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of the 6-sulfate groups of the N-acetyl-D-
CC         galactosamine 6-sulfate units of chondroitin sulfate and of the D-
CC         galactose 6-sulfate units of keratan sulfate.; EC=3.1.6.4;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
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}.
CC   -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR   EMBL; AF322917; AAL55968.1; -; mRNA.
DR   RefSeq; NP_999120.1; NM_213955.1.
DR   RefSeq; XP_005653291.2; XM_005653234.2.
DR   AlphaFoldDB; Q8WNQ7; -.
DR   SMR; Q8WNQ7; -.
DR   STRING; 9823.ENSSSCP00000002856; -.
DR   PaxDb; Q8WNQ7; -.
DR   PeptideAtlas; Q8WNQ7; -.
DR   PRIDE; Q8WNQ7; -.
DR   GeneID; 397000; -.
DR   KEGG; ssc:397000; -.
DR   CTD; 2588; -.
DR   eggNOG; KOG3867; Eukaryota.
DR   InParanoid; Q8WNQ7; -.
DR   OrthoDB; 515367at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043890; F:N-acetylgalactosamine-6-sulfatase activity; IEA:UniProtKB-EC.
DR   CDD; cd16157; GALNS; 1.
DR   Gene3D; 3.40.720.10; -; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR035626; GALNS.
DR   InterPro; IPR024607; Sulfatase_CS.
DR   InterPro; IPR000917; Sulfatase_N.
DR   Pfam; PF00884; Sulfatase; 1.
DR   SUPFAM; SSF53649; SSF53649; 1.
DR   PROSITE; PS00523; SULFATASE_1; 1.
DR   PROSITE; PS00149; SULFATASE_2; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Metal-binding;
KW   Reference proteome; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000250"
FT   CHAIN           26..522
FT                   /note="N-acetylgalactosamine-6-sulfatase"
FT                   /id="PRO_0000273149"
FT   REGION          27..379
FT                   /note="Catalytic domain"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        78
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   BINDING         38
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         39
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /note="via 3-oxoalanine"
FT                   /evidence="ECO:0000250"
FT   BINDING         288
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         289
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         78
FT                   /note="3-oxoalanine (Cys)"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   CARBOHYD        203
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        423
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        308..419
FT                   /evidence="ECO:0000250"
FT   DISULFID        489..518
FT                   /evidence="ECO:0000250"
FT   DISULFID        501..507
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   522 AA;  57711 MW;  C6F14DE8C51BEBDE CRC64;
     MAAVAAATRW HLLLVLSAAG LGVTGAPQPP NILLLLMDDM GWGDLGVYGE PSRETPNLDR
     MAAEGMLFPS FYAANPLCSP SRAALLTGRL PIRTGFYTTN GHARNAYTPQ EIVGGIPDPE
     HLLPELLKGA GYASKIVGKW HLGHRPQFHP LKHGFDEWFG SPNCHFGPYD NRARPNIPVY
     RDWEMVGRFY EEFPINLKTG ESNLTQIYLQ EALDFIKRQQ ATHHPFFLYW AIDATHAPVY
     ASRAFLGTSQ RGRYGDAVRE IDDSVGRIVG LLRDLKIAGN TFVFFTSDNG AALVSAPKQG
     GSNGPFLCGK QTTFEGGMRE PAIAWWPGHI PAGQVSHQLG SVMDLFTTSL SLAGLEPPSD
     RAIDGLDLLP AMLQGRLTER PIFYYRGNTL MAATLGQYKA HFWTWTNSWE EFRQGVDFCP
     GQNVSGVTTH SQEEHTKLPL IFHLGRDPGE RFPLSFASTE YLDALRKITL VVQQHQESLV
     PGQPQLNVCN PAVMNWAPPG CEKLGKCLTP PESVPEKCSW PH