ID   BGLR_CANLF              Reviewed;         651 AA.
AC   O18835;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=Beta-glucuronidase;
DE            EC=3.2.1.31;
DE   Flags: Precursor;
GN   Name=GUSB;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], VARIANT MPS VII HIS-166, AND DISEASE.
RX   PubMed=9521879; DOI=10.1006/geno.1997.5189;
RA   Ray J., Bouvet A., Desanto C., Fyfe J.C., Xu D., Wolfe J.H., Aguirre G.D.,
RA   Patterson D.F., Haskins M.E., Henthorn P.S.;
RT   "Cloning of the canine beta-glucuronidase cDNA, mutation identification in
RT   canine MPS VII, and retroviral vector-mediated correction of MPS VII
RT   cells.";
RL   Genomics 48:248-253(1998).
CC   -!- FUNCTION: Plays an important role in the degradation of dermatan and
CC       keratan sulfates. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate;
CC         Xref=Rhea:RHEA:17633, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:58720, ChEBI:CHEBI:83411; EC=3.2.1.31;
CC   -!- ACTIVITY REGULATION: Inhibited by L-aspartic acid. {ECO:0000250}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Lysosome.
CC   -!- DISEASE: Note=Defects in GUSB are the cause of mucopolysaccharidosis
CC       type VII (MPS VII), an inherited disease reported in humans, mice,
CC       cats, and dogs. {ECO:0000269|PubMed:9521879}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR   EMBL; AF019759; AAC48809.1; -; mRNA.
DR   RefSeq; NP_001003191.1; NM_001003191.1.
DR   AlphaFoldDB; O18835; -.
DR   SMR; O18835; -.
DR   STRING; 9615.ENSCAFP00000014967; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   GlyCosmos; O18835; 3 sites, No reported glycans.
DR   PaxDb; 9612-ENSCAFP00000014967; -.
DR   GeneID; 403831; -.
DR   KEGG; cfa:403831; -.
DR   CTD; 2990; -.
DR   eggNOG; KOG2024; Eukaryota.
DR   InParanoid; O18835; -.
DR   OrthoDB; 1847696at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   Proteomes; UP000694429; Unplaced.
DR   Proteomes; UP000694542; Unplaced.
DR   Proteomes; UP000805418; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004566; F:beta-glucuronidase activity; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0019391; P:glucuronoside catabolic process; IBA:GO_Central.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR023232; Glyco_hydro_2_AS.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR023230; Glyco_hydro_2_CS.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR10066; BETA-GLUCURONIDASE; 1.
DR   PANTHER; PTHR10066:SF67; BETA-GLUCURONIDASE; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   1: Evidence at protein level;
KW   Disease variant; Glycoprotein; Glycosidase; Hydrolase; Lysosome;
KW   Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..651
FT                   /note="Beta-glucuronidase"
FT                   /id="PRO_0000012158"
FT   ACT_SITE        450
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        172
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        419
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        630
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         166
FT                   /note="R -> H (in MPSVII; loss of activity)"
FT                   /evidence="ECO:0000269|PubMed:9521879"
SQ   SEQUENCE   651 AA;  74433 MW;  E8991B1E65C60120 CRC64;
     MSRGPAGAWV ALGPLLWTCG LALEGGMLYP RESPSRERKD LDGLWSFRAD FSDGRRQGFE
     QQWYRAPLRE SGPTLDMPVP SSFNDVGQDR QLRSFVGWVW YEREATLPRR WSQDPGTRVV
     LRIGSAHYYA IVWVNGVHVA EHEGGHLPFE ADISKLVQSG PLSSCRITLA INNTLTPHTL
     PPGTIVYKTD ASKYPKGYFV QNTYFDFFNY AGLHRPVLLY TTPTTYIDDI TVTTGVDQDT
     GLVDYQIFVQ GSEHFQLEVY LLDEEGKVVA QGTGSQGRLQ VPNVHLWWPY LMHEHPAYLY
     SLEVRLTAQM AAGPVSDFYT LPVGIRTVAV TERQFLINGK PFYFHGVNKH EDADIRGKGF
     DWPLLVKDFN LLRWLGANAF RTSHYPYAEE VMQLCDRYGI VVIDESPGVG IMLVQSYSNV
     SLQHHLEVMG ELVRRDKNHP SVVMWSVANE PTSFLKPAAY YFKTLIAHTK ALDPSRPVTF
     VTNSNYEADL GAPYVDVICV NSYYSWYHDY GHMEVIQLQL ATEFENWYRT YQKPIIQSEY
     GAETIAGFHQ DPPLMFSEEY QKGLLEQYHL VLDQKRKEYV VGELIWNFAD FMTDQSPQRA
     VGNRKGIFTR QRQPKAAAFL LRERYWKLAN ETGHHRSAAK SQCLENSPFA L
//