ID A0A1S3KA21_LINUN Unreviewed; 639 AA.
AC A0A1S3KA21;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=LOC106180001 {ECO:0000313|RefSeq:XP_013419299.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013419299.1};
RN [1] {ECO:0000313|RefSeq:XP_013419299.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26383154;
RA Luo Y.J., Takeuchi T., Koyanagi R., Yamada L., Kanda M., Khalturina M.,
RA Fujie M., Yamasaki S.I., Endo K., Satoh N.;
RT "The Lingula genome provides insights into brachiopod evolution and the
RT origin of phosphate biomineralization.";
RL Nat. Commun. 6:8301-8301(2015).
RN [2] {ECO:0000313|RefSeq:XP_013419299.1}
RP IDENTIFICATION.
RG RefSeq;
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}.
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 RefSeq; XP_013419299.1; XM_013563845.1.
DR AlphaFoldDB; A0A1S3KA21; -.
DR STRING; 7574.A0A1S3KA21; -.
DR EnsemblMetazoa; XM_013563845.1; XP_013419299.1; LOC106180001.
DR GeneID; 106180001; -.
DR KEGG; lak:106180001; -.
DR InParanoid; A0A1S3KA21; -.
DR OrthoDB; 1847696at2759; -.
DR Proteomes; UP000085678; Unplaced.
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|RuleBase:RU361154};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..639
FT /note="Beta-glucuronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010342644"
FT DOMAIN 34..214
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 216..314
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 317..616
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 639 AA; 73572 MW; 44904C643D06E498 CRC64;
MLWGIFLVVF FLVQEVWAIH GGMLYPRESE SRQIQELNGM WKFRADYSPN RLRGFDQKWF
AKPLDQTGPV IPMPVPSSYN DITTNQSLRD FVGWTWYDRT FFVSPEWQNK RVVLRVDSAH
YNSIVWVNSI QVMNHSGGHL PFEAEVNKAL NFAGENRITI TINNTLSPTT LPPGSIEYKT
DKNRYPAGYF VQNLQMDFFN YAGIHRSVRL YSTPRTYIDD ITIVTRDTSG VVDYNVTLEG
NTAGATLTVD VIDKSGVTVA SSSQPRGKIM IPKPHLWWPY TSNGQDPAYF YTFKVAIKDS
KNIADFYRLP FGIRSVEWTN TQLLINGKPF YCQGVAKHED ADIRGKGLDY PLIARDFNLL
KWLGANCFRT SHYPYAEEIM DQADQQGIVV IDECPGVGIK EVSNMGKVSL NHHLEVMEEL
VRRDKNRPSV IMWSVANEPG SARPEAGPYF KAVIGHTKYL DPYRPVTFVV GGSDFYEDKA
AQYTDIICVN HYYAWYSDMG HLDVIQLQMN YDITNWHKTF NKPVIITEYG ADTVAGLHKL
PSDAFTEEYQ VQFMRKYHEI FDALRKQFLA GEMVWNFADF QTDQATTRVD GNKKGVFTRQ
RQPKMAAHFL RDRYQGLINR RSGRTCRKSF NLSTYFQEL
//
