ID   A0A3P9DC15_9CICH        Unreviewed;       640 AA.
AC   A0A3P9DC15;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   02-OCT-2024, entry version 24.
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:ENSMZEP00005031904.1};
OS   Maylandia zebra (zebra mbuna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX   NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005031904.1, ECO:0000313|Proteomes:UP000265160};
RN   [1] {ECO:0000313|Ensembl:ENSMZEP00005031904.1, ECO:0000313|Proteomes:UP000265160}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25186727; DOI=10.1038/nature13726;
RA   Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA   Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA   Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA   Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA   Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA   Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA   Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA   Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA   Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA   Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA   Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA   Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA   Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA   Di Palma F.;
RT   "The genomic substrate for adaptive radiation in African cichlid fish.";
RL   Nature 513:375-381(2014).
RN   [2] {ECO:0000313|Ensembl:ENSMZEP00005031904.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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_004557499.1; XM_004557442.3.
DR   AlphaFoldDB; A0A3P9DC15; -.
DR   STRING; 106582.ENSMZEP00005031904; -.
DR   Ensembl; ENSMZET00005032938.1; ENSMZEP00005031904.1; ENSMZEG00005023801.1.
DR   GeneID; 101477863; -.
DR   KEGG; mze:101477863; -.
DR   CTD; 2990; -.
DR   GeneTree; ENSGT00390000001752; -.
DR   OrthoDB; 1847696at2759; -.
DR   Proteomes; UP000265160; LG10.
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:UP000265160};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..640
FT                   /note="Beta-glucuronidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017943126"
FT   DOMAIN          41..225
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          227..328
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          330..631
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
SQ   SEQUENCE   640 AA;  73657 MW;  E23B0C5BF0D1CAD2 CRC64;
     MSVPGSFSVL RVLWLLSVFG TVLPLDGGML FPQESSFREV KELNGLWDFR ADGSPNRNEG
     FEKAWYKRRL TETGPVIEMP VPASYNDITQ DPTLRDFIGW VWYEREVFVP ARWISDEGTR
     VVLRVGSAHY YSIVWVNGEK VTEHEGGHLP FEAEISSLIR KEPTKPCRIT IAVNNTLTLE
     TLPPGTIQYM NDSSRYPDGF FVQNIDFDFF NYAGIHRSVL LYTTPKVHVD DISVETNFMD
     NTGLVRYKVS VQGGFNNTLN ITLMDKDGHF VASSNGSSGG LKVVDVKLWW PYLMHENPGY
     LYSMKVHLIA VSETSTYEDE YTLPVGIRTI NVTNTQFLIN NKPFYFHGVN KHEDSDIRGR
     GFDWPLIVKD FNLMKWLGVN SFRTSHYPYA EEILQMCDRH GIVVIDECPG VGIKDIRSFR
     NASLSHHLVV MDELVRRDKN HPSVVMWSVA NEPASEMPPA EFYFKTLIEH TKALDQTRPV
     TYVTIAAADM DKGGPYVDVV CANSYFAWYF DQGRLDIIPL QLSTHFENWY RKYQRPIIQS
     EYGADAVPGL HMDPPMMFTE EYQNALLQSY HDVFDQKRNQ YFVGELIWNF ADFMTSQGIY
     RVVGNKKGIF TRQRQPKAAA FLLRKRYWRL ANETGRLLPD
//