ID G3TL90_LOXAF Unreviewed; 523 AA.
AC G3TL90;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
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|Ensembl:ENSLAFP00000015642.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000015642.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000015642.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000015642.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000015642.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000015642.3};
RG Ensembl;
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 AlphaFoldDB; G3TL90; -.
DR STRING; 9785.ENSLAFP00000015642; -.
DR Ensembl; ENSLAFT00000018664.3; ENSLAFP00000015642.3; ENSLAFG00000018664.3.
DR eggNOG; KOG3867; Eukaryota.
DR GeneTree; ENSGT00940000157787; -.
DR HOGENOM; CLU_006332_13_5_1; -.
DR InParanoid; G3TL90; -.
DR OMA; YWEFHEG; -.
DR TreeFam; TF314186; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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.
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 Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..523
FT /note="N-acetylgalactosamine-6-sulfatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003455461"
FT DOMAIN 28..352
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT REGION 447..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 76
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-1"
FT ACT_SITE 139
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-1"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-2"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-2"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-2"
FT BINDING 286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-2"
FT BINDING 287
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-2"
FT MOD_RES 76
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-4"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-3"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-3"
SQ SEQUENCE 523 AA; 58010 MW; 9CF69AED43BE8668 CRC64;
VAAATKWWRL LLVLSAAGLG AVGAPQPPNI VLMLMDDMGW GDLGVNGEPS RETPNLDRMA
AEGMLFPSFY SANPLCSPSR AALLTGRLPI RNGFYTTNGH ARNAYTPQDI VGGIPDSEHL
LPELLKKANY ATKIVGKWHL GHRPQFHPLK HGFDEWFGSP NCHFGPYDNR AKPNIPVYRD
WEMVGRFYEE FPINLKTGEA NLTQIYLQEA LDFIKRQQSQ QRPFFLYWAI DATHAPVYAS
KPFLGTSQRG RYGDAVREVD DSVGQLLQLL RGLGIAEHTF IFFTSDNGAA LVSAPKEAGS
NGPFLCGKQT TFEGGVREPA IAWWPGHIPA GQVSHQLGSL MDLFTTSLSL AGLEPPSDRE
IDGLDLLPVL LRGHLIDRPI FYYRGNELMA ATVGQYKAHF WTWTNSWEEF RQGINYCPGQ
NISGVTTHTQ EEHTALPLLF HLGRDPGERY PLSEHTQQAA PAGSRDTGET LQHQHSLRPP
SPGQVSLEKC SHPEQNWAPP GCEKLGKCLT PPESAPEKCS WPH
//
