ID   BGLR_FELCA              Reviewed;         651 AA.
AC   O97524;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Beta-glucuronidase;
DE            EC=3.2.1.31;
DE   Flags: Precursor;
GN   Name=GUSB;
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], VARIANT MPS VII LYS-351, AND DISEASE.
RC   TISSUE=Liver;
RX   PubMed=10366443; DOI=10.1006/geno.1999.5825;
RA   Fyfe J.C., Kurzhals R.L., Lassaline M.E., Henthorn P.S., Alur P.R.,
RA   Wang P., Wolfe J.H., Giger U., Haskins M.E., Patterson D.F., Sun H.,
RA   Jain S., Yuhki N.;
RT   "Molecular basis of feline beta-glucuronidase deficiency: an animal model
RT   of mucopolysaccharidosis VII.";
RL   Genomics 58:121-128(1999).
CC   -!- FUNCTION: Plays an important role in the degradation of dermatan and
CC       keratan sulfates.
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:10366443}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR   EMBL; AF012423; AAD01498.1; -; mRNA.
DR   EMBL; AF012424; AAD01499.1; -; mRNA.
DR   RefSeq; NP_001009310.1; NM_001009310.1.
DR   AlphaFoldDB; O97524; -.
DR   SMR; O97524; -.
DR   STRING; 9685.ENSFCAP00000006431; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   PRIDE; O97524; -.
DR   GeneID; 493879; -.
DR   KEGG; fca:493879; -.
DR   CTD; 2990; -.
DR   eggNOG; KOG2024; Eukaryota.
DR   InParanoid; O97524; -.
DR   OrthoDB; 653343at2759; -.
DR   Proteomes; UP000011712; 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:0019391; P:glucuronoside catabolic process; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; -; 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   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; SSF49303; SSF49303; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 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_0000012160"
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         351
FT                   /note="E -> K (in MPS VII)"
FT                   /evidence="ECO:0000269|PubMed:10366443"
SQ   SEQUENCE   651 AA;  74610 MW;  2AE30884B70D4232 CRC64;
     MLRGPAAVWA ALGPLLWACG LALRGGMLYP RESPSRERKE LNGLWSFRAD FSENRRQGFE
     QQWYRTPLRE SGPTLDMPVP SSFNDVGQDR QLRSFVGWVW YEREATLPQR WTQDLGTRVV
     LRIGSAHYYA IVWVNGVHVA EHEGGHLPFE ADISKLVQSG PLASCRITIA INNTLTPHTL
     PPGTILYQTD TSKYPKGYFV QNINFDFFNY AGLHRPVLLY TTPTTYIDDI TISTSVNQDT
     GLVDYQIFVE GGEHFQLEVR LLDEEGKVVA QGTGGRGQLQ VPNAHLWWPY LMHEHPAYLY
     SLEVRLTAQT AAGSVSDFYT LPVGIRTVAV TEHQFLINGK PFYFHGVNKH EDADIRGKGF
     DWPLLVKDFN LLRWLGANAF RTSHYPYAEE VMQLCDRYGI VVIDESPGVG IVLVESYSNV
     SLQHHLEVME ELVRRDKNHP AVVMWSVANE PASFLKPAGY YFKTLIAHTK ALDPSRPVTF
     VTNSNYEADL GAPYVDVICV NSYYSWYHDY GHMEVIQLQL ATQFENWYRT YQKPIIQSEY
     GADTIAGFHQ DPPLMFSEEY QKGLLEQYHL VLDQKRKEYV VGELIWNFAD FMTNQSPQRV
     MGNKKGIFTR QRQPKGAAFL LRERYWKLAN ETRYPWSAVK SQCLENSPFT L