ID GNS_CAPHI Reviewed; 559 AA.
AC P50426;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 27-MAR-2024, entry version 103.
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 Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7605804; DOI=10.1016/0925-4439(95)00054-8;
RA Friderici K., Cavanagh K.T., Leipprandt J.R., Traviss C.E., Anson D.S.,
RA Hopwood J.J., Jones M.Z.;
RT "Cloning and sequence analysis of caprine N-acetylglucosamine 6-sulfatase
RT cDNA.";
RL Biochim. Biophys. Acta 1271:369-373(1995).
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.
CC -!- PTM: Processed by internal peptidase. {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; U17694; AAB01663.1; -; mRNA.
DR RefSeq; NP_001272619.1; NM_001285690.1.
DR AlphaFoldDB; P50426; -.
DR SMR; P50426; -.
DR STRING; 9925.ENSCHIP00000010847; -.
DR GlyCosmos; P50426; 13 sites, No reported glycans.
DR GeneID; 100750233; -.
DR KEGG; chx:100750233; -.
DR CTD; 2799; -.
DR OrthoDB; 1365192at2759; -.
DR Proteomes; UP000291000; Unassembled WGS sequence.
DR Proteomes; UP000694566; Unplaced.
DR Proteomes; UP000694900; Genome assembly.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008449; F:N-acetylglucosamine-6-sulfatase activity; IEA:UniProtKB-EC.
DR GO; GO:0030203; P:glycosaminoglycan metabolic process; IEA:InterPro.
DR CDD; cd16147; G6S; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR012251; GlcNAc_6-SO4ase.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR PANTHER; PTHR43108:SF5; N-ACETYLGLUCOSAMINE-6-SULFATASE; 1.
DR PANTHER; PTHR43108; N-ACETYLGLUCOSAMINE-6-SULFATASE FAMILY MEMBER; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR PIRSF; PIRSF036666; G6S; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 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;
KW Mucopolysaccharidosis; Phosphoprotein; Reference proteome; Signal.
FT SIGNAL 1..47
FT /evidence="ECO:0000255"
FT CHAIN 48..559
FT /note="N-acetylglucosamine-6-sulfatase"
FT /id="PRO_0000033412"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 98
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 98
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15586"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 559 AA; 62712 MW; 786CCDC48334A458 CRC64;
MRFLSLAPDR PRRGGPRHLP SGSPAPPPPP PLLLLLLLGG CLGVSGAAKG SRRPNVVLVL
ADDQDEVLGG MTPLKKTKAL IGEMGMTFSS AYVPSALCCP SRASILTGKY PHNHHVVNNT
LEGNCSSKSW QKIQEPNTFP AILRSMCGYQ TFFAGKYLNE YGAPDAGGLG HVPLGWSYWY
ALEKNSKYYN YTLSINGKAR KHGENYSVDY LTDVLANVSL DFLDYKSNSE PFFMMISTPA
PHSPWTAAPQ YQNAFQNVFA PRNKNFNIHG TNKHWLIRQA KTPMTNSSIQ FLDNAFRERW
QTLLSVDDLV EKLVKRLEFN GELNNTYIFY TSDNGYHTGQ FSLPIDKRQL YEFDIKVPLL
VRGPGIKPNQ TSKMLVANID LGPTILDIAG YGLNKTQMDG MSFLPILRGA SNLTWRSDVL
VEYQGEGRNV TDPTCPSLSP GVSQCFPDCV CEDAYNNTYA CVRTMSELWN LQYCEFDDQE
VFVEVYNLTA DPHQLNNIAK SIDPELLGKM NYRLMMLQSC SGPTCRTPRV FDPGYRFDPR
LMFSNHGSVR TRRFSKHLL
//
