ID   BGLR_PIG                Reviewed;         652 AA.
AC   Q4FAT7;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   24-JAN-2024, entry version 105.
DE   RecName: Full=Beta-glucuronidase;
DE            EC=3.2.1.31;
DE   Flags: Precursor;
GN   Name=GUSB;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Beck J., Knorr C., Brenig B.;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ095863; AAZ03639.1; -; Genomic_DNA.
DR   RefSeq; NP_001116593.1; NM_001123121.1.
DR   AlphaFoldDB; Q4FAT7; -.
DR   SMR; Q4FAT7; -.
DR   STRING; 9823.ENSSSCP00000043718; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   GlyCosmos; Q4FAT7; 3 sites, No reported glycans.
DR   PaxDb; 9823-ENSSSCP00000008265; -.
DR   PeptideAtlas; Q4FAT7; -.
DR   Ensembl; ENSSSCT00000040486.3; ENSSSCP00000043718.2; ENSSSCG00000007739.5.
DR   Ensembl; ENSSSCT00025089382.1; ENSSSCP00025039105.1; ENSSSCG00025065003.1.
DR   Ensembl; ENSSSCT00030087031.1; ENSSSCP00030040167.1; ENSSSCG00030062228.1.
DR   Ensembl; ENSSSCT00035058882.1; ENSSSCP00035023669.1; ENSSSCG00035044326.1.
DR   Ensembl; ENSSSCT00045055720.1; ENSSSCP00045038860.1; ENSSSCG00045032453.1.
DR   Ensembl; ENSSSCT00055056257.1; ENSSSCP00055044949.1; ENSSSCG00055028361.1.
DR   GeneID; 100144519; -.
DR   KEGG; ssc:100144519; -.
DR   CTD; 2990; -.
DR   VGNC; VGNC:103960; GUSB.
DR   eggNOG; KOG2024; Eukaryota.
DR   GeneTree; ENSGT00390000001752; -.
DR   HOGENOM; CLU_006501_6_1_1; -.
DR   InParanoid; Q4FAT7; -.
DR   OrthoDB; 1847696at2759; -.
DR   TreeFam; TF300685; -.
DR   Reactome; R-SSC-2024096; HS-GAG degradation.
DR   Reactome; R-SSC-2160916; Hyaluronan uptake and degradation.
DR   Reactome; R-SSC-6798695; Neutrophil degranulation.
DR   Proteomes; UP000008227; Chromosome 3.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   Bgee; ENSSSCG00000007739; Expressed in ovary and 43 other cell types or tissues.
DR   ExpressionAtlas; Q4FAT7; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0043202; C:lysosomal lumen; IEA:Ensembl.
DR   GO; GO:0004566; F:beta-glucuronidase activity; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:Ensembl.
DR   GO; GO:0030207; P:chondroitin sulfate catabolic process; IEA:Ensembl.
DR   GO; GO:0019391; P:glucuronoside catabolic process; IBA:GO_Central.
DR   GO; GO:0030200; P:heparan sulfate proteoglycan catabolic process; IEA:Ensembl.
DR   GO; GO:0030214; P:hyaluronan catabolic process; IEA:Ensembl.
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.
DR   Genevisible; Q4FAT7; SS.
PE   3: Inferred from homology;
KW   Glycoprotein; Glycosidase; Hydrolase; Lysosome; Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..652
FT                   /note="Beta-glucuronidase"
FT                   /id="PRO_0000231599"
FT   ACT_SITE        451
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        420
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        631
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   652 AA;  74710 MW;  7B9386564DFF2CA7 CRC64;
     MVRGPAGAWA VLGPLLWGCG LALLQGGMLY PQESRSRERK ELNGLWSFRA DFSDNRRQGF
     EQQWYRKPLR ESGPTLDMPV PSSFNDISQD GRLRSFIGWV WYEREAILPQ RWTQDLGTRV
     VLRISSAHYY AIVWVNGVHV TEHEGGHLPF EADISKLVQT GPLSSCRITI AINNTLSPHT
     LPPGTILYKT DTSKYPKGYF VQNTNFDFFN YAGLHRPVLL YTTPTAYIDD ITVTTDVDQD
     TGLVNYQIFV QGSDHFQLEV HLLDEEGRVV AKGTGGQGQL QVPSAHLWWP YLMHERPAYL
     YSLEVKLTAQ TSAGPLSDFY TLPVGIRTVA VTERQFLING KPFYFHGVNK HEDADIRGKG
     FDWSLLVKDF NLLRWLGANA FRTSHYPYAE EVMQLCDRYG IVVIDESPGV GIVLAQSFSN
     ASLQHHLEVM EEMVRRDKNH PAVVMWSVAN EPSSFLEQAA YYFKMLIGHT KALDPSRPVT
     FVTSSSYEKD LGVPYVDVIC VNSYYSWYHD YGHMEVIQLQ LATQFERWHE AYQKPIIQSE
     YGAETIIGFH EDPPLMFSEE YQKGLLQQYH VILDQKRKEY VVGELIWNFA DFMTDQSPQR
     AIGNRKGIFT RQRQPKSAAF LLRERYWKLA NETRYLQSAV MSQCVGNSPF TV
//