ID A0A1A6HGN3_NEOLE Unreviewed; 513 AA.
AC A0A1A6HGN3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 ORFNames=A6R68_16423 {ECO:0000313|EMBL:OBS77120.1};
OS Neotoma lepida (Desert woodrat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Neotominae; Neotoma.
OX NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS77120.1, ECO:0000313|Proteomes:UP000092124};
RN [1] {ECO:0000313|EMBL:OBS77120.1, ECO:0000313|Proteomes:UP000092124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=417 {ECO:0000313|EMBL:OBS77120.1};
RC TISSUE=Liver {ECO:0000313|EMBL:OBS77120.1};
RA Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT lepida.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBS77120.1}.
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DR EMBL; LZPO01034768; OBS77120.1; -; Genomic_DNA.
DR STRING; 56216.A0A1A6HGN3; -.
DR Proteomes; UP000092124; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000092124};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..513
FT /note="N-acetylgalactosamine-6-sulfatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008346356"
FT DOMAIN 31..345
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT ACT_SITE 79
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-1"
FT ACT_SITE 142
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-1"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-2"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-2"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
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 BINDING 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-2"
FT MOD_RES 79
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-4"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-3"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-3"
SQ SEQUENCE 513 AA; 57212 MW; BFAE3A278AA223DC CRC64;
MASYATATRG GQLLLVLTAL GLLAAGAPQP PNIVLLLMDD MGWGDLGVYG EPSRETPNLD
QMAIEGMLFP NFYSANPLCS PSRAALLTGR LPIRNGFYTS NAHARNAYTP QEIMGGIPNS
EHLLPELLKK AGYTNKIVGK WHLGHRPQFH PLKHGFDEWF GSPNCHFGPY DNKVKPNIPV
YRDWEMVGRF YEEFPINLKT GEANLTQLYL QEALDFIRTQ HARQSPFFLY WAIDATHAPV
YASRPFLGTS HRGRYGDAVR EIDDSVGKIL SLLQNLGISK NTFVFFTSDN GGSNGPFLCG
KQTTFEGGMR EPAIAWWPGH IAAGQVSHQL GSIMDLFTTS LSLAGLKPPS DRVIDGLDLL
PNMLQGYTMD RPIFYYRGNT LMAVTLGQYK AHFWTWTNSW EEFRQGIDFC PGQNVSGVTT
XTQEEHTELP LIFHLGRDPG ERFPLSFAST EYEDVLSRIT QVVQQHQKSL VPGQPQLNVC
NQAVMNWAPP GCEKLGKCLT PPESVPEKCS WLH
//
