ID   BGLR_RAT                Reviewed;         648 AA.
AC   P06760;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   08-NOV-2023, entry version 156.
DE   RecName: Full=Beta-glucuronidase;
DE            EC=3.2.1.31 {ECO:0000305|PubMed:3355537};
DE   Flags: Precursor;
GN   Name=Gusb; Synonyms=Gus;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Preputial gland;
RX   PubMed=3463967; DOI=10.1073/pnas.83.19.7292;
RA   Nishimura Y., Rosenfeld M.G., Kreibich G., Gubler U., Sabatini D.D.,
RA   Adesnik M., Andy R.;
RT   "Nucleotide sequence of rat preputial gland beta-glucuronidase cDNA and in
RT   vitro insertion of its encoded polypeptide into microsomal membranes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:7292-7296(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 14-648, AND CATALYTIC ACTIVITY.
RC   TISSUE=Liver;
RX   PubMed=3355537; DOI=10.1042/bj2500547;
RA   Powell P.P., Kyle J.W., Miller R.D., Pantano J., Grubb J.H., Sly W.S.;
RT   "Rat liver beta-glucuronidase. cDNA cloning, sequence comparisons and
RT   expression of a chimeric protein in COS cells.";
RL   Biochem. J. 250:547-555(1988).
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         Evidence={ECO:0000305|PubMed:3355537};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17634;
CC         Evidence={ECO:0000305|PubMed:3355537};
CC   -!- ACTIVITY REGULATION: Inhibited by L-aspartic acid. {ECO:0000250}.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Lysosome.
CC   -!- PTM: Undergoes a post-transcriptional proteolytic cleavage near its C-
CC       terminal end, which reduces its size by approximately 3 kDa. The site
CC       of this cleavage has as yet not been determined.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR   EMBL; M13962; AAA41228.1; -; mRNA.
DR   EMBL; Y00717; CAA68705.1; -; mRNA.
DR   PIR; A25047; A25047.
DR   RefSeq; NP_058711.2; NM_017015.2.
DR   AlphaFoldDB; P06760; -.
DR   SMR; P06760; -.
DR   IntAct; P06760; 1.
DR   STRING; 10116.ENSRNOP00000045033; -.
DR   BindingDB; P06760; -.
DR   ChEMBL; CHEMBL4814; -.
DR   DrugCentral; P06760; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   GlyCosmos; P06760; 3 sites, No reported glycans.
DR   GlyGen; P06760; 3 sites.
DR   iPTMnet; P06760; -.
DR   PhosphoSitePlus; P06760; -.
DR   SwissPalm; P06760; -.
DR   jPOST; P06760; -.
DR   PaxDb; 10116-ENSRNOP00000045033; -.
DR   PeptideAtlas; P06760; -.
DR   GeneID; 24434; -.
DR   KEGG; rno:24434; -.
DR   AGR; RGD:2772; -.
DR   CTD; 2990; -.
DR   RGD; 2772; Gusb.
DR   eggNOG; KOG2024; Eukaryota.
DR   InParanoid; P06760; -.
DR   OrthoDB; 1847696at2759; -.
DR   Reactome; R-RNO-2024096; HS-GAG degradation.
DR   Reactome; R-RNO-2160916; Hyaluronan uptake and degradation.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   SABIO-RK; P06760; -.
DR   PRO; PR:P06760; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
DR   GO; GO:0043202; C:lysosomal lumen; ISO:RGD.
DR   GO; GO:0005764; C:lysosome; ISO:RGD.
DR   GO; GO:0004566; F:beta-glucuronidase activity; IDA:RGD.
DR   GO; GO:0030246; F:carbohydrate binding; IDA:RGD.
DR   GO; GO:0016787; F:hydrolase activity; ISO:RGD.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR   GO; GO:0005975; P:carbohydrate metabolic process; ISO:RGD.
DR   GO; GO:0030207; P:chondroitin sulfate catabolic process; ISO:RGD.
DR   GO; GO:0019391; P:glucuronoside catabolic process; ISO:RGD.
DR   GO; GO:0030200; P:heparan sulfate proteoglycan catabolic process; ISO:RGD.
DR   GO; GO:0030214; P:hyaluronan catabolic process; ISO:RGD.
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   Glycoprotein; Glycosidase; Hydrolase; Lysosome; Reference proteome; Signal.
FT   SIGNAL          1..22
FT   CHAIN           23..648
FT                   /note="Beta-glucuronidase"
FT                   /id="PRO_0000012163"
FT   ACT_SITE        447
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        172
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        416
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        627
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        14
FT                   /note="Q -> E (in Ref. 2; CAA68705)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        21
FT                   /note="V -> L (in Ref. 2; CAA68705)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        487
FT                   /note="M -> L (in Ref. 2; CAA68705)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   648 AA;  74793 MW;  5ADE8F5234F0907E CRC64;
     MSPRRSVCWF VLGQLLCSCA VALQGGMLFP KETPSRELKV LDGLWSFRAD YSNNRLQGFE
     KQWYRQPLRE SGPTLDMPVP SSFNDITQEA ELRNFIGWVW YEREAVLPQR WTQDTDRRVV
     LRINSAHYYA VVWVNGIHVV EHEGGHLPFE ADITKLVQSG PLTTFRVTIA INNTLTPYTL
     PPGTIVYKTD PSMYPKGYFV QDISFDFFNY AGLHRSVVLY TTPTTYIDDI TVTTDVDRDV
     GLVNYWISVQ GSDHFQLEVR LLDEDGKIVA RGTGNEGQLK VPRAHLWWPY LMHEHPAYLY
     SLEVTMTTPE SVSDFYTLPV GIRTVAVTKS KFLINGKPFY FQGVNKHEDS DIRGRGFDWP
     LLIKDFNLLR WLGANSFRTS HYPYSEEVLQ LCDRYGIVVI DECPGVGIVL PQSFGNVSLR
     HHLEVMDELV RRDKNHPAVV MWSVANEPVS SLKPAGYYFK TLIAHTKALD PTRPVTFVSN
     TRYDADMGAP YVDVICVNSY LSWYHDYGHL EVIQLQLTSQ FENWYKMYQK PIIQSEYGAD
     AVSGLHEDPP RMFSEEYQTA LLENYHLILD EKRKEYVIGE LIWNFADFMT NQSPLRVTGN
     KKGIFTRQRN PKMAAFILRE RYWRIANETR GYGSVPRTQC MGSRPFTF
//