ID A0A3P9DC15_9CICH Unreviewed; 640 AA. AC A0A3P9DC15; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 31-JUL-2019, entry version 5. DE RecName: Full=Beta-glucuronidase {ECO:0000256|RuleBase:RU361154}; DE EC=3.2.1.31 {ECO:0000256|RuleBase:RU361154}; 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; OC Maylandia zebra complex. OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005031904, ECO:0000313|Proteomes:UP000265160}; RN [1] {ECO:0000313|Ensembl:ENSMZEP00005031904, 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., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C.P., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA 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 RT fish."; RL Nature 513:375-381(2014). RN [2] {ECO:0000313|Ensembl:ENSMZEP00005031904} RP IDENTIFICATION. RG Ensembl; RL Submitted (DEC-2018) to UniProtKB. CC -!- FUNCTION: Plays an important role in the degradation of dermatan CC and keratan sulfates. {ECO:0000256|RuleBase:RU361154}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a beta-D-glucuronoside + H2O = an alcohol + D- CC glucuronate; Xref=Rhea:RHEA:17633, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:30879, ChEBI:CHEBI:58720, ChEBI:CHEBI:83411; CC EC=3.2.1.31; 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. CC {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_004557499.1; XM_004557442.3. DR Ensembl; ENSMZET00005032938; ENSMZEP00005031904; ENSMZEG00005023801. DR GeneID; 101477863; -. DR KEGG; mze:101477863; -. DR GeneTree; ENSGT00390000001752; -. DR KO; K01195; -. DR Proteomes; UP000265160; LG10. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-KW. 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; -; 1. DR Gene3D; 2.60.40.10; -; 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 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; SSF49303; SSF49303; 1. DR SUPFAM; SSF49785; SSF49785; 1. DR SUPFAM; SSF51445; SSF51445; 1. DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1. DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000265160}; KW Glycosidase {ECO:0000256|RuleBase:RU361154}; KW Hydrolase {ECO:0000256|RuleBase:RU361154}; KW Lysosome {ECO:0000256|RuleBase:RU361154}; KW Reference proteome {ECO:0000313|Proteomes:UP000265160}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 640 Beta-glucuronidase. {ECO:0000256|SAM: FT SignalP}. FT /FTId=PRO_5017943126. FT DOMAIN 41 225 Glyco_hydro_2_N. {ECO:0000259|Pfam: FT PF02837}. FT DOMAIN 227 328 Glyco_hydro_2. {ECO:0000259|Pfam: FT PF00703}. FT DOMAIN 330 631 Glyco_hydro_2_C. {ECO:0000259|Pfam: FT 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 //