GNS_BOVIN
ID GNS_BOVIN Reviewed; 560 AA.
AC Q1LZH9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=N-acetylglucosamine-6-sulfatase;
DE EC=3.1.6.14;
DE AltName: Full=Glucosamine-6-sulfatase;
DE Short=G6S;
DE Flags: Precursor;
GN Name=GNS;
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=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of the 6-sulfate groups of the N-acetyl-D-
CC glucosamine 6-sulfate units of heparan sulfate and keratan sulfate.;
CC EC=3.1.6.14;
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 -!- 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; BC115990; AAI15991.1; -; mRNA.
DR RefSeq; NP_001069030.1; NM_001075562.2.
DR AlphaFoldDB; Q1LZH9; -.
DR SMR; Q1LZH9; -.
DR STRING; 9913.ENSBTAP00000023218; -.
DR PaxDb; Q1LZH9; -.
DR PRIDE; Q1LZH9; -.
DR GeneID; 512444; -.
DR KEGG; bta:512444; -.
DR CTD; 2799; -.
DR eggNOG; KOG3731; Eukaryota.
DR InParanoid; Q1LZH9; -.
DR OrthoDB; 1273622at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005539; F:glycosaminoglycan binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008449; F:N-acetylglucosamine-6-sulfatase activity; IBA:GO_Central.
DR GO; GO:0030203; P:glycosaminoglycan metabolic process; IEA:InterPro.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR012251; GlcNAc_6-SO4ase.
DR InterPro; IPR015981; GlcNAc_6-SO4ase_met.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR PANTHER; PTHR43108:SF5; PTHR43108:SF5; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR PIRSF; PIRSF036666; G6S; 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; Glycoprotein; Hydrolase; Lysosome; Metal-binding; Phosphoprotein;
KW Reference proteome; Signal.
FT SIGNAL 1..48
FT /evidence="ECO:0000255"
FT CHAIN 49..560
FT /note="N-acetylglucosamine-6-sulfatase"
FT /id="PRO_0000273188"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 99
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 99
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15586"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 560 AA; 62776 MW; FF7507C6FD22D3C8 CRC64;
MRLLSLAPDR PRRGGPRHLT SGSPALPPPP PLLLLLLLLG GCLGVSGAAK SSRRPNVVLL
LADDQDEVLG GMTPLKKTKA LIGEMGMTFS SAYVPSALCC PSRASILTGK YPHNLHVVNN
TLEGNCSSKS WQKIQEPNTF PAILRSMCGY QTFFAGKYLN EYGAPDAGGL GHVPLGWSYW
YALEKNSKYY NYTLSINGKA RKHGENYSVD YLTDVLANVS LDFLDYKSNS EPFFMMISTP
APHSPWTAAP QYQNAFQNVF APRNKNFNIH GTNKHWLIRQ AKTPMTNSSI QFLDNAFRKR
WQTLLSVDDL VEKLVKRLEF NGELNNTYIF YTSDNGYHTG QFSLPIDKRQ LYEFDIKVPL
LVRGPGIKPN QTSKMLVANI DLGPTILDIA GYSLNKTQMD GMSFLPILKG ASNLTWRSDV
LVEYQGEGRN VTDPTCPSLS PGVSQCFPDC VCEDAYNNTY ACVRTMSERW NLQYCEFDDQ
EVFVEVYNLT ADPHQLNNIA KSIDPELLGK MNYRLMMLQS CSGPTCRTPG VFDPGYRFDP
RLMFSNHGSV RTRRFSKHLL
