ID G1SL41_RABIT Unreviewed; 645 AA.
AC G1SL41;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 2.
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:ENSOCUP00000003565.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000003565.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000003565.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000003565.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000003565.3};
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 AlphaFoldDB; G1SL41; -.
DR SMR; G1SL41; -.
DR STRING; 9986.ENSOCUP00000003565; -.
DR PaxDb; 9986-ENSOCUP00000003565; -.
DR Ensembl; ENSOCUT00000004120.4; ENSOCUP00000003565.3; ENSOCUG00000004119.4.
DR eggNOG; KOG2024; Eukaryota.
DR GeneTree; ENSGT00390000001752; -.
DR HOGENOM; CLU_006501_6_1_1; -.
DR InParanoid; G1SL41; -.
DR OMA; IHDHVGW; -.
DR TreeFam; TF300685; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000004119; Expressed in liver and 16 other cell types or tissues.
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:UP000001811};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..645
FT /note="Beta-glucuronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003422718"
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 645 AA; 73907 MW; EC6D06AFBC9C052C CRC64;
MPGGPAAFRA LLGPLLWGCA LALQGGMLYP RESPSRERKE LDGLWSFRAD FSSGRHQGFE
QQWYRRPLRE SGPTLDMPVP SSFNDVSQDG QLRSFVGWVW YEREVALPQR WTQDLDRRVV
LRIGSAHYYA IVWVNGVHVT EHEGGHLPFE ADISKLVQSG PLASCRITIA VNNTLTPYTL
PPGAILYKTD TSKYPKGYFV QDTNFDFFNY AGLHRSVLLY TTPTAYIDDI TITTDVAQDT
GLVNYRIFVQ GTEHFQLEVS LLDEEGKVVA QGTGGWGQLL VPSANLWWPY LMHERPAYLY
SLEVRLIAQT AAGPVSDFYT LPVGIRTVAV TESRFLINGK PFYFHGVNKH EDSDIRGKGF
DWPLLVKDFH LLRWLGANSF RTSHYPYAEE VMQLCDRYGI VVIDECPGVG IVLPQNFGNV
SLQHHLQVME ELVRRDKNHP AVVMWSVANE PKSSLKPAGY YFKTVIAHTK ALDPSRPVTF
VTNSNYSTDL GVPYVDVICV NSYYSWYHDY GHLELIQLQL ETQFENWYRA HQKPIIQSEY
GAETIAGFHQ DPPLMFSEEY QKSMLEQYHL VLDQKRKEYV VGELIWNFAD FMTNQTPQRP
VGNKKGIFTR QRQPKSAAFL LRDRYWRLAN ETRTVSHNTF CNIRC
//
