BGLR_PIG
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 03-AUG-2022, entry version 97.
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}.
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DR EMBL; DQ095863; AAZ03639.1; -; Genomic_DNA.
DR RefSeq; NP_001116593.1; NM_001123121.1.
DR AlphaFoldDB; Q4FAT7; -.
DR SMR; Q4FAT7; -.
DR STRING; 9823.ENSSSCP00000008265; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR PaxDb; Q4FAT7; -.
DR PeptideAtlas; Q4FAT7; -.
DR PRIDE; Q4FAT7; -.
DR Ensembl; ENSSSCT00000040486; ENSSSCP00000043718; ENSSSCG00000007739.
DR Ensembl; ENSSSCT00025089382; ENSSSCP00025039105; ENSSSCG00025065003.
DR Ensembl; ENSSSCT00030087031; ENSSSCP00030040167; ENSSSCG00030062228.
DR Ensembl; ENSSSCT00035058882; ENSSSCP00035023669; ENSSSCG00035044326.
DR Ensembl; ENSSSCT00045055720; ENSSSCP00045038860; ENSSSCG00045032453.
DR Ensembl; ENSSSCT00055056257; ENSSSCP00055044949; ENSSSCG00055028361.
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; 653343at2759; -.
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 Bgee; ENSSSCG00000007739; Expressed in ovary and 43 other tissues.
DR ExpressionAtlas; Q4FAT7; baseline and differential.
DR Genevisible; Q4FAT7; SS.
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:0019904; F:protein domain specific binding; IEA:Ensembl.
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 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
