ID A0A0D9S0B5_CHLSB Unreviewed; 651 AA.
AC A0A0D9S0B5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Beta-glucuronidase {ECO:0000256|ARBA:ARBA00016205, ECO:0000256|RuleBase:RU361154};
DE EC=3.2.1.31 {ECO:0000256|ARBA:ARBA00012761, ECO:0000256|RuleBase:RU361154};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000014304.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000014304.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000014304.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Plays an important role in the degradation of dermatan and
CC keratan sulfates. {ECO:0000256|ARBA:ARBA00003025,
CC ECO:0000256|RuleBase:RU361154}.
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:0000256|RuleBase:RU361154};
CC -!- ACTIVITY REGULATION: Inhibited by L-aspartic acid.
CC {ECO:0000256|RuleBase:RU361154}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361154}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR EMBL; AQIB01140047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01140048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01140049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008016438.1; XM_008018247.1.
DR AlphaFoldDB; A0A0D9S0B5; -.
DR STRING; 60711.ENSCSAP00000014304; -.
DR Ensembl; ENSCSAT00000016389.1; ENSCSAP00000014304.1; ENSCSAG00000018292.1.
DR KEGG; csab:103246571; -.
DR eggNOG; KOG2024; Eukaryota.
DR GeneTree; ENSGT00390000001752; -.
DR OMA; IHDHVGW; -.
DR OrthoDB; 1847696at2759; -.
DR BioGRID-ORCS; 103246571; 0 hits in 7 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 28.
DR Bgee; ENSCSAG00000018292; Expressed in liver and 7 other cell types or tissues.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004566; F:beta-glucuronidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228, ECO:0000256|RuleBase:RU361154};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..651
FT /note="Beta-glucuronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002346188"
FT DOMAIN 39..224
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 226..327
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 329..630
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 651 AA; 75005 MW; 97C374C47C58536F CRC64;
MARGLAMAWA VLGPLLWGCA LALQGGMLYP RESQSRERKE LDGLWSFRAD FSDNRRRGFE
EQWYRRPLRE SGPTLDMPVP SSFNDISQDW RLRHFVGWVW YEREVILPER WTQDLSTRVV
LRIGSAHAYA IVWVNGVHTL EHEGGYLPFE ADISNLVQVG PLSSQLRITI AINNTLTSTT
LPPGTIQYLT DISKYPKGYF VQNTYFDFFN YAGLQRSVLL YTTPTAYIDD ITVTTGVQHD
TGLVNYQISV KGSNLFELEV RLLDAEHKLV ANGTGTQGQL KVPGARLWWP YLMHERPAYL
YSLEVRLTAQ MSPGPVSDFY TLPVGIRTVA VTESQFLING KPFYFHGVNK HEDADIRGKG
FDWPLLVKDF NLLRWLGANA FRTSHYPYAE EVLQMCDRYG IVVIDECPGV GLALPQFFNN
VSLQNHMRVM EEVVRRDKNH PAVVMWSVAN EPASHLESAG YYLKMVITHT KALDPSRPVT
FVTNSNYAAD KGAPYVDVIC LNSYYSWYHD YGHLELIQRQ LTTQFENWYK TYQKPIIQSE
YGAETIVGFH QDPPLMFTEE YQKSLLEQYH VVLDQKRRKY VVGELIWNFA DFMTEQSPTR
VLGNKKGVFT RQRQPKSAAF LLRERYWKIA NETRYPHSIA KSQCLENSPF T
//
