ID BGLR_HUMAN Reviewed; 651 AA. AC P08236; B4E1F6; E9PCV0; Q549U0; Q96CL9; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 2. DT 18-SEP-2019, entry version 207. DE RecName: Full=Beta-glucuronidase; DE EC=3.2.1.31; DE AltName: Full=Beta-G1; DE Flags: Precursor; GN Name=GUSB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PRO-649, AND RP ALTERNATIVE SPLICING. RC TISSUE=Placenta; RX PubMed=3468507; DOI=10.1073/pnas.84.3.685; RA Oshima A., Kyle J.W., Miller R.D., Hoffmann J.W., Powell P.P., RA Grubb J.H., Sly W.S., Tropak M., Guise K.S., Gravel R.A.; RT "Cloning, sequencing, and expression of cDNA for human beta- RT glucuronidase."; RL Proc. Natl. Acad. Sci. U.S.A. 84:685-689(1987). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT RP PRO-649. RC TISSUE=Lung; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., RA Mural R.J., Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-70. RX PubMed=1916806; DOI=10.1016/0888-7543(91)90192-h; RA Shipley J.M., Miller R.D., Wu B.M., Grubb J.H., Christensen S.G., RA Kyle J.W., Sly W.S.; RT "Analysis of the 5' flanking region of the human beta-glucuronidase RT gene."; RL Genomics 10:1009-1018(1991). RN [9] RP PROTEIN SEQUENCE OF 23-32 AND 160-175. RC TISSUE=Placenta; RX PubMed=1311180; DOI=10.1515/bchm3.1992.373.1.57; RA Tanaka J., Gasa S., Sakurada K., Miyazaki T., Kasai M., Makita A.; RT "Characterization of the subunits and sugar moiety of human placental RT and leukemic beta-glucuronidase."; RL Biol. Chem. Hoppe-Seyler 373:57-62(1992). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 520-585. RC TISSUE=Fibroblast; RX PubMed=3924735; DOI=10.1016/0378-1119(85)90300-2; RA Guise K.S., Korneluk R.G., Waye J., Lamhonwah A.-M., Quan F., RA Palmer R., Ganschow R.E., Sly W.S., Gravel R.A.; RT "Isolation and expression in Escherichia coli of a cDNA clone encoding RT human beta-glucuronidase."; RL Gene 34:105-110(1985). RN [11] RP INHIBITION BY L-ASPARTIC ACID. RX PubMed=11568288; DOI=10.1203/00006450-200110000-00007; RA Kreamer B.L., Siegel F.L., Gourley G.R.; RT "A novel inhibitor of beta-glucuronidase: L-aspartic acid."; RL Pediatr. Res. 50:460-466(2001). RN [12] RP GLYCOSYLATION AT ASN-272. RX PubMed=12754519; DOI=10.1038/nbt827; RA Zhang H., Li X.-J., Martin D.B., Aebersold R.; RT "Identification and quantification of N-linked glycoproteins using RT hydrazide chemistry, stable isotope labeling and mass spectrometry."; RL Nat. Biotechnol. 21:660-666(2003). RN [13] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-272. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [14] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-173; ASN-272 AND ASN-631. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX PubMed=8599764; DOI=10.1038/nsb0496-375; RA Jain S., Drendel W.B., Chen Z.W., Mathews F.S., Sly W.S., Grubb J.H.; RT "Structure of human beta-glucuronidase reveals candidate lysosomal RT targeting and active-site motifs."; RL Nat. Struct. Biol. 3:375-381(1996). RN [18] RP REVIEW ON VARIANTS. RX PubMed=19224584; DOI=10.1002/humu.20828; RA Tomatsu S., Montano A.M., Dung V.C., Grubb J.H., Sly W.S.; RT "Mutations and polymorphisms in GUSB gene in mucopolysaccharidosis VII RT (Sly Syndrome)."; RL Hum. Mutat. 30:511-519(2009). RN [19] RP VARIANT MPS7 TRP-216. RX PubMed=8111412; DOI=10.1002/humu.1380020604; RA Vervoort R., Lissens W., Liebaers I.; RT "Molecular analysis of a patient with hydrops fetalis caused by beta- RT glucuronidase deficiency, and evidence for additional pseudogenes."; RL Hum. Mutat. 2:443-445(1993). RN [20] RP VARIANTS MPS7 VAL-354 AND TRP-611. RX PubMed=8111413; DOI=10.1002/humu.1380020605; RA Wu B.M., Sly W.S.; RT "Mutational studies in a patient with the hydrops fetalis form of RT mucopolysaccharidosis type VII."; RL Hum. Mutat. 2:446-457(1993). RN [21] RP VARIANTS MPS7 CYS-382 AND VAL-619. RX PubMed=1702266; RA Tomatsu S., Fukuda S., Sukegawa K., Ikedo Y., Yamada S., Yamada Y., RA Sasaki T., Okamoto H., Kuwahara T., Yamaguchi S., Kiman T., RA Shintaku H., Isshiki G., Orii T.; RT "Mucopolysaccharidosis type VII: characterization of mutations and RT molecular heterogeneity."; RL Am. J. Hum. Genet. 48:89-96(1991). RN [22] RP VARIANT MPS7 CYS-627. RX PubMed=7680524; RA Shipley J.M., Klinkenberg M., Wu B.M., Bachinsky D.R., Grubb J.H., RA Sly W.S.; RT "Mutational analysis of a patient with mucopolysaccharidosis type VII, RT and identification of pseudogenes."; RL Am. J. Hum. Genet. 52:517-526(1993). RN [23] RP VARIANT MPS7 PHE-176, AND VARIANT PRO-649. RX PubMed=8089138; RA Wu B.M., Tomatsu S., Fukuda S., Sukegawa K., Orii T., Sly W.S.; RT "Overexpression rescues the mutant phenotype of L176F mutation causing RT beta-glucuronidase deficiency mucopolysaccharidosis in two Mennonite RT siblings."; RL J. Biol. Chem. 269:23681-23688(1994). RN [24] RP VARIANT MPS7 PHE-176, VARIANT ASN-152, AND CHARACTERIZATION OF VARIANT RP ASN-152. RX PubMed=7573038; RA Vervoort R., Islam M.R., Sly W., Chabas A., Wevers R., de Jong J., RA Liebaers I., Lissens W.; RT "A pseudodeficiency allele (D152N) of the human beta-glucuronidase RT gene."; RL Am. J. Hum. Genet. 57:798-804(1995). RN [25] RP VARIANTS MPS7 SER-148 AND CYS-495. RX PubMed=7633414; DOI=10.1093/hmg/4.4.651; RA Yamada S., Tomatsu S., Sly W.S., Islam R., Wenger D.A., Fukuda S., RA Sukegawa K., Orii T.; RT "Four novel mutations in mucopolysaccharidosis type VII including a RT unique base substitution in exon 10 of the beta-glucuronidase gene RT that creates a novel 5'-splice site."; RL Hum. Mol. Genet. 4:651-655(1995). RN [26] RP VARIANTS MPS7 ARG-136; LYS-150; PHE-176; TRP-216; CYS-320; SER-320; RP TYR-351; CYS-374; CYS-382; HIS-382; PRO-435; TRP-477; CYS-508; RP ASP-572; ASN-606 AND CYS-627. RX PubMed=8644704; RA Vervoort R., Islam M.R., Sly W.S., Zabot M.T., Kleijer W.J., RA Chabas A., Fensom A., Young E.P., Liebaers I., Lissens W.; RT "Molecular analysis of patients with beta-glucuronidase deficiency RT presenting as hydrops fetalis or as early mucopolysaccharidosis VII."; RL Am. J. Hum. Genet. 58:457-471(1996). RN [27] RP VARIANTS MPS7 SER-408 AND LEU-415. RX PubMed=8707294; DOI=10.1007/s004390050207; RA Islam M.R., Vervoort R., Lissens W., Hoo J.J., Valentino L.A., RA Sly W.S.; RT "beta-Glucuronidase P408S, P415L mutations: evidence that both RT mutations combine to produce an MPS VII allele in certain Mexican RT patients."; RL Hum. Genet. 98:281-284(1996). RN [28] RP VARIANT MPS7 PHE-52, AND CHARACTERIZATION OF VARIANT MPS7 PHE-52. RX PubMed=9099834; DOI=10.1007/s004390050389; RA Vervoort R., Buist N.R., Kleijer W.J., Wevers R., Fryns J.P., RA Liebaers I., Lissens W.; RT "Molecular analysis of the beta-glucuronidase gene: novel mutations in RT mucopolysaccharidosis type VII and heterogeneity of the RT polyadenylation region."; RL Hum. Genet. 99:462-468(1997). RN [29] RP VARIANT ASN-152, AND VARIANTS MPS7 GLY-38 AND HIS-626. RX PubMed=9490302; DOI=10.1007/s004390050656; RA Vervoort R., Gitzelmann R., Bosshard N., Maire I., Liebaers I., RA Lissens W.; RT "Low beta-glucuronidase enzyme activity and mutations in the human RT beta-glucuronidase gene in mild mucopolysaccharidosis type VII, RT pseudodeficiency and a heterozygote."; RL Hum. Genet. 102:69-78(1998). RN [30] RP VARIANT MPS7 PHE-176. RX PubMed=12859417; DOI=10.1034/j.1399-0004.2003.00119.x; RA Schwartz I., Silva L.R., Leistner S., Todeschini L.A., Burin M.G., RA Pina-Neto J.M., Islam R.M., Shah G.N., Sly W.S., Giugliani R.; RT "Mucopolysaccharidosis VII: clinical, biochemical and molecular RT investigation of a Brazilian family."; RL Clin. Genet. 64:172-175(2003). RN [31] RP VARIANTS MPS7 ASN-350 AND LEU-577, AND CHARACTERIZATION OF VARIANT RP MPS7 ASN-350 LEU-577. RX PubMed=12522561; DOI=10.1007/s00439-002-0849-5; RA Storch S., Wittenstein B., Islam R., Ullrich K., Sly W.S., Braulke T.; RT "Mutational analysis in longest known survivor of RT mucopolysaccharidosis type VII."; RL Hum. Genet. 112:190-194(2003). CC -!- FUNCTION: Plays an important role in the degradation of dermatan CC and keratan sulfates. 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; CC -!- ACTIVITY REGULATION: Inhibited by L-aspartic acid. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Lysosome. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=Long; CC IsoId=P08236-1; Sequence=Displayed; CC Name=2; Synonyms=Short; CC IsoId=P08236-2; Sequence=VSP_001799; CC Name=3; CC IsoId=P08236-3; Sequence=VSP_054830; CC Note=No experimental confirmation available.; CC -!- PTM: N-linked glycosylated with 3 to 4 oligosaccharide chains. CC {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, CC ECO:0000269|PubMed:19159218}. CC -!- DISEASE: Mucopolysaccharidosis 7 (MPS7) [MIM:253220]: An autosomal CC recessive lysosomal storage disease characterized by inability to CC degrade glucuronic acid-containing glycosaminoglycans. The CC phenotype is highly variable, ranging from severe lethal hydrops CC fetalis to mild forms with survival into adulthood. Most patients CC with the intermediate phenotype show hepatomegaly, skeletal CC anomalies, coarse facies, and variable degrees of mental CC impairment. {ECO:0000269|PubMed:12522561, CC ECO:0000269|PubMed:12859417, ECO:0000269|PubMed:1702266, CC ECO:0000269|PubMed:7573038, ECO:0000269|PubMed:7633414, CC ECO:0000269|PubMed:7680524, ECO:0000269|PubMed:8089138, CC ECO:0000269|PubMed:8111412, ECO:0000269|PubMed:8111413, CC ECO:0000269|PubMed:8644704, ECO:0000269|PubMed:8707294, CC ECO:0000269|PubMed:9099834, ECO:0000269|PubMed:9490302}. Note=The CC disease is caused by mutations affecting the gene represented in CC this entry. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. CC {ECO:0000305}. 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 EMBL; M15182; AAA52561.1; -; mRNA. DR EMBL; AK303819; BAG64768.1; -; mRNA. DR EMBL; AK223406; BAD97126.1; -; mRNA. DR EMBL; AC073261; AAQ96851.1; -; Genomic_DNA. DR EMBL; CH236961; EAL23740.1; -; Genomic_DNA. DR EMBL; CH471140; EAX07951.1; -; Genomic_DNA. DR EMBL; BC014142; AAH14142.1; -; mRNA. DR EMBL; M65002; AAA52622.1; -; Genomic_DNA. DR EMBL; M10618; AAA52621.1; -; mRNA. DR EMBL; S72462; AAD14101.1; -; Genomic_DNA. DR CCDS; CCDS5530.1; -. [P08236-1] DR CCDS; CCDS64665.1; -. [P08236-3] DR PIR; A26581; A26581. DR RefSeq; NP_000172.2; NM_000181.3. [P08236-1] DR RefSeq; NP_001271219.1; NM_001284290.1. [P08236-3] DR RefSeq; NP_001280033.1; NM_001293104.1. DR RefSeq; NP_001280034.1; NM_001293105.1. DR RefSeq; XP_005250354.1; XM_005250297.3. [P08236-2] DR PDB; 1BHG; X-ray; 2.53 A; A/B=21-633. DR PDB; 3HN3; X-ray; 1.70 A; A/B/D/E=21-633. DR PDBsum; 1BHG; -. DR PDBsum; 3HN3; -. DR SMR; P08236; -. DR BioGrid; 109245; 13. DR DIP; DIP-29724N; -. DR IntAct; P08236; 10. DR MINT; P08236; -. DR STRING; 9606.ENSP00000302728; -. DR BindingDB; P08236; -. DR ChEMBL; CHEMBL2728; -. DR DrugBank; DB09301; Chondroitin sulfate. DR DrugBank; DB11793; Niraparib. DR DrugBank; DB09340; Tyropanoic acid. DR CAZy; GH2; Glycoside Hydrolase Family 2. DR GlyConnect; 1037; -. DR iPTMnet; P08236; -. DR PhosphoSitePlus; P08236; -. DR BioMuta; GUSB; -. DR DMDM; 146345377; -. DR EPD; P08236; -. DR jPOST; P08236; -. DR MassIVE; P08236; -. DR MaxQB; P08236; -. DR PaxDb; P08236; -. DR PeptideAtlas; P08236; -. DR PRIDE; P08236; -. DR ProteomicsDB; 19519; -. DR ProteomicsDB; 52092; -. [P08236-1] DR ProteomicsDB; 52093; -. [P08236-2] DR DNASU; 2990; -. DR Ensembl; ENST00000304895; ENSP00000302728; ENSG00000169919. [P08236-1] DR Ensembl; ENST00000421103; ENSP00000391390; ENSG00000169919. [P08236-3] DR GeneID; 2990; -. DR KEGG; hsa:2990; -. DR UCSC; uc003tun.4; human. [P08236-1] DR CTD; 2990; -. DR DisGeNET; 2990; -. DR GeneCards; GUSB; -. DR HGNC; HGNC:4696; GUSB. DR HPA; HPA036322; -. DR HPA; HPA036323; -. DR MalaCards; GUSB; -. DR MIM; 253220; phenotype. DR MIM; 611499; gene. DR neXtProt; NX_P08236; -. DR OpenTargets; ENSG00000169919; -. DR Orphanet; 584; Mucopolysaccharidosis type 7. DR PharmGKB; PA29075; -. DR eggNOG; KOG2024; Eukaryota. DR eggNOG; COG3250; LUCA. DR GeneTree; ENSGT00390000001752; -. DR HOGENOM; HOG000120896; -. DR InParanoid; P08236; -. DR KO; K01195; -. DR OMA; QRWTQDL; -. DR OrthoDB; 653343at2759; -. DR PhylomeDB; P08236; -. DR TreeFam; TF300685; -. DR Reactome; R-HSA-2024096; HS-GAG degradation. DR Reactome; R-HSA-2160916; Hyaluronan uptake and degradation. DR Reactome; R-HSA-2206292; MPS VII - Sly syndrome. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR ChiTaRS; GUSB; human. DR EvolutionaryTrace; P08236; -. DR GeneWiki; GUSB; -. DR GenomeRNAi; 2990; -. DR Pharos; P08236; -. DR PRO; PR:P08236; -. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; ENSG00000169919; Expressed in 234 organ(s), highest expression level in endometrium epithelium. DR ExpressionAtlas; P08236; baseline and differential. DR Genevisible; P08236; HS. DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0004566; F:beta-glucuronidase activity; IBA:GO_Central. DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central. DR GO; GO:0019904; F:protein domain specific binding; IPI:AgBase. DR GO; GO:0005102; F:signaling receptor binding; IPI:AgBase. DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc. DR GO; GO:0019391; P:glucuronoside catabolic process; IBA:GO_Central. DR GO; GO:0006027; P:glycosaminoglycan catabolic process; TAS:Reactome. DR GO; GO:0030214; P:hyaluronan catabolic process; TAS:Reactome. DR GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome. 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 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; KW Direct protein sequencing; Disease mutation; Glycoprotein; KW Glycosidase; Hydrolase; Lysosome; Mucopolysaccharidosis; Polymorphism; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000269|PubMed:1311180}. FT CHAIN 23 651 Beta-glucuronidase. FT /FTId=PRO_0000012161. FT ACT_SITE 451 451 Proton donor. FT CARBOHYD 173 173 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19159218}. FT CARBOHYD 272 272 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:12754519, FT ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218}. FT CARBOHYD 420 420 N-linked (GlcNAc...) asparagine. FT CARBOHYD 631 631 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19159218}. FT VAR_SEQ 159 304 Missing (in isoform 3). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_054830. FT VAR_SEQ 305 355 Missing (in isoform 2). {ECO:0000305}. FT /FTId=VSP_001799. FT VARIANT 30 30 P -> S (in MPS7; dbSNP:rs747792546). FT /FTId=VAR_058511. FT VARIANT 38 38 C -> G (in MPS7; very mild phenotype; FT dbSNP:rs779499448). FT {ECO:0000269|PubMed:9490302}. FT /FTId=VAR_037914. FT VARIANT 52 52 S -> F (in MPS7; loss of activity; FT dbSNP:rs1424546265). FT {ECO:0000269|PubMed:9099834}. FT /FTId=VAR_037915. FT VARIANT 136 136 G -> R (in MPS7; dbSNP:rs1417426295). FT {ECO:0000269|PubMed:8644704}. FT /FTId=VAR_037916. FT VARIANT 148 148 P -> S (in MPS7; dbSNP:rs121918177). FT {ECO:0000269|PubMed:7633414}. FT /FTId=VAR_037917. FT VARIANT 150 150 E -> K (in MPS7). FT {ECO:0000269|PubMed:8644704}. FT /FTId=VAR_037918. FT VARIANT 152 152 D -> G (in MPS7). FT /FTId=VAR_058512. FT VARIANT 152 152 D -> N (functional polymorphism with no FT clinical consequences; reduced activity FT levels; dbSNP:rs149606212). FT {ECO:0000269|PubMed:7573038, FT ECO:0000269|PubMed:9490302}. FT /FTId=VAR_037919. FT VARIANT 176 176 L -> F (in MPS7; dbSNP:rs121918181). FT {ECO:0000269|PubMed:12859417, FT ECO:0000269|PubMed:7573038, FT ECO:0000269|PubMed:8089138, FT ECO:0000269|PubMed:8644704}. FT /FTId=VAR_037920. FT VARIANT 216 216 R -> W (in MPS7; dbSNP:rs121918174). FT {ECO:0000269|PubMed:8111412, FT ECO:0000269|PubMed:8644704}. FT /FTId=VAR_003196. FT VARIANT 243 243 L -> P (in MPS7). FT /FTId=VAR_058513. FT VARIANT 320 320 Y -> C (in MPS7). FT {ECO:0000269|PubMed:8644704}. FT /FTId=VAR_037921. FT VARIANT 320 320 Y -> S (in MPS7; dbSNP:rs886044680). FT {ECO:0000269|PubMed:8644704}. FT /FTId=VAR_037922. FT VARIANT 339 339 N -> S (in MPS7). FT /FTId=VAR_058514. FT VARIANT 350 350 K -> N (in MPS7; dbSNP:rs121918182). FT {ECO:0000269|PubMed:12522561}. FT /FTId=VAR_037923. FT VARIANT 351 351 H -> Y (in MPS7; dbSNP:rs191153460). FT {ECO:0000269|PubMed:8644704}. FT /FTId=VAR_037924. FT VARIANT 354 354 A -> V (in MPS7; dbSNP:rs121918175). FT {ECO:0000269|PubMed:8111413}. FT /FTId=VAR_003197. FT VARIANT 361 369 Missing (in MPS7). FT /FTId=VAR_058515. FT VARIANT 362 362 D -> N (in MPS7; dbSNP:rs398123234). FT /FTId=VAR_058516. FT VARIANT 364 364 P -> L (in MPS7; dbSNP:rs771629102). FT /FTId=VAR_058517. FT VARIANT 374 374 R -> C (in MPS7; dbSNP:rs747572640). FT {ECO:0000269|PubMed:8644704}. FT /FTId=VAR_037925. FT VARIANT 376 376 L -> F (in dbSNP:rs11559283). FT /FTId=VAR_055884. FT VARIANT 382 382 R -> C (in MPS7; dbSNP:rs121918173). FT {ECO:0000269|PubMed:1702266, FT ECO:0000269|PubMed:8644704}. FT /FTId=VAR_003198. FT VARIANT 382 382 R -> H (in MPS7; dbSNP:rs764018631). FT {ECO:0000269|PubMed:8644704}. FT /FTId=VAR_037926. FT VARIANT 408 408 P -> S (in MPS7; dbSNP:rs779091113). FT {ECO:0000269|PubMed:8707294}. FT /FTId=VAR_037927. FT VARIANT 415 415 P -> L (in MPS7; dbSNP:rs751025746). FT {ECO:0000269|PubMed:8707294}. FT /FTId=VAR_037928. FT VARIANT 435 435 R -> P (in MPS7). FT {ECO:0000269|PubMed:8644704}. FT /FTId=VAR_037929. FT VARIANT 477 477 R -> W (in MPS7; dbSNP:rs774393243). FT {ECO:0000269|PubMed:8644704}. FT /FTId=VAR_037930. FT VARIANT 495 495 Y -> C (in MPS7; dbSNP:rs121918178). FT {ECO:0000269|PubMed:7633414}. FT /FTId=VAR_037931. FT VARIANT 508 508 Y -> C (in MPS7). FT {ECO:0000269|PubMed:8644704}. FT /FTId=VAR_037932. FT VARIANT 540 540 E -> K (in MPS7). FT /FTId=VAR_058518. FT VARIANT 572 572 G -> D (in MPS7). FT {ECO:0000269|PubMed:8644704}. FT /FTId=VAR_037933. FT VARIANT 577 577 R -> L (in MPS7; loss of activity; FT dbSNP:rs121918183). FT {ECO:0000269|PubMed:12522561}. FT /FTId=VAR_037934. FT VARIANT 606 606 K -> N (in MPS7). FT {ECO:0000269|PubMed:8644704}. FT /FTId=VAR_037935. FT VARIANT 607 607 G -> A (in MPS7; dbSNP:rs1250112198). FT /FTId=VAR_058519. FT VARIANT 611 611 R -> W (in MPS7; dbSNP:rs121918176). FT {ECO:0000269|PubMed:8111413}. FT /FTId=VAR_003199. FT VARIANT 619 619 A -> V (in MPS7; dbSNP:rs121918172). FT {ECO:0000269|PubMed:1702266}. FT /FTId=VAR_003200. FT VARIANT 626 626 Y -> H (in MPS7; very mild phenotype; FT dbSNP:rs777613366). FT {ECO:0000269|PubMed:9490302}. FT /FTId=VAR_037936. FT VARIANT 627 627 W -> C (in MPS7; dbSNP:rs121918184). FT {ECO:0000269|PubMed:7680524, FT ECO:0000269|PubMed:8644704}. FT /FTId=VAR_003201. FT VARIANT 649 649 L -> P (in dbSNP:rs9530). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:3468507, FT ECO:0000269|PubMed:8089138}. FT /FTId=VAR_016179. FT STRAND 33 35 {ECO:0000244|PDB:1BHG}. FT STRAND 38 40 {ECO:0000244|PDB:3HN3}. FT STRAND 43 49 {ECO:0000244|PDB:3HN3}. FT STRAND 52 55 {ECO:0000244|PDB:1BHG}. FT HELIX 57 60 {ECO:0000244|PDB:3HN3}. FT HELIX 63 65 {ECO:0000244|PDB:3HN3}. FT HELIX 68 71 {ECO:0000244|PDB:3HN3}. FT STRAND 75 81 {ECO:0000244|PDB:3HN3}. FT TURN 84 86 {ECO:0000244|PDB:3HN3}. FT HELIX 90 93 {ECO:0000244|PDB:3HN3}. FT STRAND 97 105 {ECO:0000244|PDB:3HN3}. FT HELIX 109 113 {ECO:0000244|PDB:3HN3}. FT STRAND 117 124 {ECO:0000244|PDB:3HN3}. FT STRAND 128 134 {ECO:0000244|PDB:3HN3}. FT STRAND 137 147 {ECO:0000244|PDB:3HN3}. FT STRAND 149 152 {ECO:0000244|PDB:3HN3}. FT HELIX 154 157 {ECO:0000244|PDB:3HN3}. FT STRAND 166 173 {ECO:0000244|PDB:3HN3}. FT STRAND 180 182 {ECO:0000244|PDB:3HN3}. FT STRAND 185 188 {ECO:0000244|PDB:3HN3}. FT TURN 192 194 {ECO:0000244|PDB:3HN3}. FT STRAND 200 203 {ECO:0000244|PDB:3HN3}. FT STRAND 206 208 {ECO:0000244|PDB:3HN3}. FT STRAND 218 238 {ECO:0000244|PDB:3HN3}. FT STRAND 241 252 {ECO:0000244|PDB:3HN3}. FT STRAND 256 263 {ECO:0000244|PDB:3HN3}. FT STRAND 265 267 {ECO:0000244|PDB:1BHG}. FT STRAND 269 282 {ECO:0000244|PDB:3HN3}. FT TURN 291 293 {ECO:0000244|PDB:1BHG}. FT STRAND 294 296 {ECO:0000244|PDB:3HN3}. FT STRAND 301 311 {ECO:0000244|PDB:3HN3}. FT STRAND 314 324 {ECO:0000244|PDB:3HN3}. FT STRAND 329 331 {ECO:0000244|PDB:3HN3}. FT STRAND 336 338 {ECO:0000244|PDB:3HN3}. FT STRAND 341 343 {ECO:0000244|PDB:3HN3}. FT STRAND 345 349 {ECO:0000244|PDB:3HN3}. FT TURN 355 357 {ECO:0000244|PDB:3HN3}. FT HELIX 363 376 {ECO:0000244|PDB:3HN3}. FT STRAND 380 382 {ECO:0000244|PDB:3HN3}. FT HELIX 390 399 {ECO:0000244|PDB:3HN3}. FT STRAND 402 406 {ECO:0000244|PDB:3HN3}. FT HELIX 415 417 {ECO:0000244|PDB:3HN3}. FT HELIX 420 437 {ECO:0000244|PDB:3HN3}. FT STRAND 443 451 {ECO:0000244|PDB:3HN3}. FT HELIX 457 473 {ECO:0000244|PDB:3HN3}. FT STRAND 479 483 {ECO:0000244|PDB:3HN3}. FT TURN 487 489 {ECO:0000244|PDB:3HN3}. FT HELIX 493 495 {ECO:0000244|PDB:3HN3}. FT STRAND 497 502 {ECO:0000244|PDB:3HN3}. FT TURN 505 507 {ECO:0000244|PDB:3HN3}. FT STRAND 508 510 {ECO:0000244|PDB:3HN3}. FT HELIX 514 516 {ECO:0000244|PDB:3HN3}. FT HELIX 517 532 {ECO:0000244|PDB:3HN3}. FT STRAND 536 540 {ECO:0000244|PDB:3HN3}. FT HELIX 559 574 {ECO:0000244|PDB:3HN3}. FT TURN 575 580 {ECO:0000244|PDB:3HN3}. FT STRAND 581 587 {ECO:0000244|PDB:3HN3}. FT STRAND 600 604 {ECO:0000244|PDB:3HN3}. FT HELIX 617 631 {ECO:0000244|PDB:3HN3}. SQ SEQUENCE 651 AA; 74732 MW; 6BA7B1D935C9ABBD CRC64; MARGSAVAWA ALGPLLWGCA LGLQGGMLYP QESPSRECKE LDGLWSFRAD FSDNRRRGFE EQWYRRPLWE SGPTVDMPVP SSFNDISQDW RLRHFVGWVW YEREVILPER WTQDLRTRVV LRIGSAHSYA IVWVNGVDTL EHEGGYLPFE ADISNLVQVG PLPSRLRITI AINNTLTPTT LPPGTIQYLT DTSKYPKGYF VQNTYFDFFN YAGLQRSVLL YTTPTTYIDD ITVTTSVEQD SGLVNYQISV KGSNLFKLEV RLLDAENKVV ANGTGTQGQL KVPGVSLWWP YLMHERPAYL YSLEVQLTAQ TSLGPVSDFY TLPVGIRTVA VTKSQFLING KPFYFHGVNK HEDADIRGKG FDWPLLVKDF NLLRWLGANA FRTSHYPYAE EVMQMCDRYG IVVIDECPGV GLALPQFFNN VSLHHHMQVM EEVVRRDKNH PAVVMWSVAN EPASHLESAG YYLKMVIAHT KSLDPSRPVT FVSNSNYAAD KGAPYVDVIC LNSYYSWYHD YGHLELIQLQ LATQFENWYK KYQKPIIQSE YGAETIAGFH QDPPLMFTEE YQKSLLEQYH LGLDQKRRKY VVGELIWNFA DFMTEQSPTR VLGNKKGIFT RQRQPKSAAF LLRERYWKIA NETRYPHSVA KSQCLENSLF T //