ID G3TP98_LOXAF Unreviewed; 651 AA.
AC G3TP98;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
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};
GN Name=GUSB {ECO:0000313|Ensembl:ENSLAFP00000017185.2};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000017185.2, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000017185.2, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000017185.2,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000017185.2}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000017185.2};
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 RefSeq; XP_003416590.1; XM_003416542.2.
DR AlphaFoldDB; G3TP98; -.
DR SMR; G3TP98; -.
DR STRING; 9785.ENSLAFP00000017185; -.
DR Ensembl; ENSLAFT00000022963.2; ENSLAFP00000017185.2; ENSLAFG00000022591.2.
DR GeneID; 100664107; -.
DR KEGG; lav:100664107; -.
DR CTD; 2990; -.
DR eggNOG; KOG2024; Eukaryota.
DR GeneTree; ENSGT00390000001752; -.
DR HOGENOM; CLU_006501_6_1_1; -.
DR InParanoid; G3TP98; -.
DR OMA; IHDHVGW; -.
DR OrthoDB; 1847696at2759; -.
DR TreeFam; TF300685; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0043202; C:lysosomal lumen; IEA:Ensembl.
DR GO; GO:0004566; F:beta-glucuronidase activity; IEA:UniProtKB-EC.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
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; IEA:Ensembl.
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.
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:UP000007646}.
FT DOMAIN 39..223
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 225..326
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 328..629
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 651 AA; 74035 MW; 1C9E07BE07871425 CRC64;
MARRPAVAVA VLGPLLWGCG LTLQGGMLYP RESPSRERKE LGGLWSFRAD SSESRRQGFE
QQWYRRPLRE LGPTLDMPVP SSFNDVTQDR WLRGFVGWVW YEREATLPQR WTQDLGTRVV
LRIGSAHYYA IVWVNGVHVA EHEGGHLPFE VDISKLVQAG PLDACRITIA INNTLTPNTL
PPGTILYKND TSKYPKGYFV QDTNFDFFNY AGLHRPVLLY TTPTTYIDDI TVITGVDQDT
GLVNYQISVQ GSKHFELEVR LLDAEGQIVA HSMGAQGQLQ VPSAHLWWPY LMHNYPAYLY
SLEVRLAAET AAGPVADFYT LPVGIRTVAV TASQFLINGK PFYFHGVNKH EDADIRGKGF
DWPLLVKDFN LLRWLGANAF RTSHYPYAEE VMELCDRYGI VVIDESPGVG IVLVESFGNV
SLHHHLEVME ELVRRDKNHP AVVMWSVANE PASFLKPAGY YFKTLIAHTK ALDPSRPVTY
VTSSSYAVDL GAPYVDVICV NSYYSWYHDY GHLEVIPLQL ATQFEKWYST YQKPIIQSEY
GAETIAGLHQ DPPLMFSEEY QRGLLEQYHL VLDQKRREYV VGELIWNFAD FMTDQTPQRV
LGNKKGIFTR QRQPKGAAFV LRERYWKIAN ETTHHPSAVK AQCLGNSLFT L
//
