BGLR_RAT
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 03-AUG-2022, entry version 151.
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 GlyGen; P06760; 3 sites.
DR iPTMnet; P06760; -.
DR PhosphoSitePlus; P06760; -.
DR jPOST; P06760; -.
DR PaxDb; P06760; -.
DR PeptideAtlas; P06760; -.
DR PRIDE; P06760; -.
DR GeneID; 24434; -.
DR KEGG; rno:24434; -.
DR CTD; 2990; -.
DR RGD; 2772; Gusb.
DR eggNOG; KOG2024; Eukaryota.
DR InParanoid; P06760; -.
DR OrthoDB; 653343at2759; -.
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:0005764; C:lysosome; IDA: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:0019391; P:glucuronoside catabolic process; ISO:RGD.
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 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
