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Database: UniProt
Entry: A0A2D0Q8T1_ICTPU
LinkDB: A0A2D0Q8T1_ICTPU
Original site: A0A2D0Q8T1_ICTPU 
ID   A0A2D0Q8T1_ICTPU        Unreviewed;       522 AA.
AC   A0A2D0Q8T1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=N-acetylgalactosamine-6-sulfatase {ECO:0000256|ARBA:ARBA00019527};
DE            EC=3.1.6.4 {ECO:0000256|ARBA:ARBA00012117};
DE   AltName: Full=Chondroitinsulfatase {ECO:0000256|ARBA:ARBA00033059};
DE   AltName: Full=Galactose-6-sulfate sulfatase {ECO:0000256|ARBA:ARBA00030478};
DE   AltName: Full=N-acetylgalactosamine-6-sulfate sulfatase {ECO:0000256|ARBA:ARBA00032952};
GN   Name=galns {ECO:0000313|RefSeq:XP_017314699.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017314699.1};
RN   [1] {ECO:0000313|RefSeq:XP_017314699.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017314699.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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         Evidence={ECO:0000256|ARBA:ARBA00000027};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR635626-2};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR635626-2};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
CC   -!- SIMILARITY: Belongs to the sulfatase family.
CC       {ECO:0000256|ARBA:ARBA00008779}.
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DR   RefSeq; XP_017314699.1; XM_017459210.3.
DR   AlphaFoldDB; A0A2D0Q8T1; -.
DR   STRING; 7998.ENSIPUP00000035146; -.
DR   Ensembl; ENSIPUT00000036528; ENSIPUP00000035146; ENSIPUG00000023592.
DR   GeneID; 108259597; -.
DR   KEGG; ipu:108259597; -.
DR   CTD; 2588; -.
DR   OMA; YWEFHEG; -.
DR   OrthoDB; 2913702at2759; -.
DR   Proteomes; UP000221080; Chromosome 27.
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; 3.30.1120.10; -; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR035626; GALNS.
DR   InterPro; IPR024607; Sulfatase_CS.
DR   InterPro; IPR000917; Sulfatase_N.
DR   PANTHER; PTHR42693; ARYLSULFATASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR42693:SF50; N-ACETYLGALACTOSAMINE-6-SULFATASE; 1.
DR   Pfam; PF00884; Sulfatase; 1.
DR   Pfam; PF14707; Sulfatase_C; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   PROSITE; PS00523; SULFATASE_1; 1.
DR   PROSITE; PS00149; SULFATASE_2; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRSR:PIRSR635626-2};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR635626-2};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..522
FT                   /note="N-acetylgalactosamine-6-sulfatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012519535"
FT   DOMAIN          30..354
FT                   /note="Sulfatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00884"
FT   ACT_SITE        78
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR635626-1"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000256|PIRSR:PIRSR635626-1"
FT   BINDING         38
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR635626-2"
FT   BINDING         39
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR635626-2"
FT   BINDING         78
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /note="via 3-oxoalanine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR635626-2"
FT   BINDING         288
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR635626-2"
FT   BINDING         289
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR635626-2"
FT   MOD_RES         78
FT                   /note="3-oxoalanine (Cys)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR635626-4"
SQ   SEQUENCE   522 AA;  58751 MW;  459174EF3674BD04 CRC64;
     MEIRSVNYAF LLFWTISFIG TAETHNVSTP NIIIMLMDDM GWGDLGVFGE PSKETPHLDT
     MASQGMLFPN FYSANPLCSP SRAALLTGRL PIRNGFYTTN AHARNAYTPQ EVVGGITKDE
     ILLPQILKKQ GYVSKIVGKW HLGHREQHLP LEHGFDQFFG SPHCHFGPYK ESDRPNIPVY
     NNSQMIGRYY EEFKINRKTG ESELTQYFLQ EALDFVSHQN TAHQPFFLYW APDATHDPVY
     ASKQFLGQSQ RGLYGDAVME LDHSVGKILA HLVDLSIENN TFVFFTSDNG AAVMSGPGQS
     GSNGPFLCGK ETTFEGGMRE PAIAWWPGRI PAGTVSYQLG TVMDLFTTSL ALAGLNAPED
     RVIDGLDLSS TLFNKSLTER PVFYYRGNEM MAVRVGLYKA HYWTWTNSWE EFKQGVNFCP
     GQEVLGVTNH TQQEHTMQPL IFHLGRDPGE KQPINVLSEE YLQVQRWINT VVEQHKVTLV
     PGEPQLDMCD LAVMNWAPPG CEKLGKCLKP PPSHPQKCDW PH
//
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