ID BGLR_HUMAN Reviewed; 651 AA. AC P08236; Q549U0; Q96CL9; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 2. DT 14-APR-2009, entry version 107. 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], VARIANT PRO-649, AND ALTERNATIVE SPLICING. RC TISSUE=Placenta; RX MEDLINE=87118233; PubMed=3468507; 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]. RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22737999; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22616434; 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 [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-70. RX MEDLINE=92009900; 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 [8] RP PROTEIN SEQUENCE OF 23-32 AND 160-175. RC TISSUE=Placenta; RX MEDLINE=92162201; PubMed=1311180; 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 [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 520-585. RC TISSUE=Fibroblast; RX MEDLINE=85232043; 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 [10] 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 [11] RP GLYCOSYLATION AT ASN-272. RX MEDLINE=22660472; 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 [12] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-272, AND MASS RP SPECTROMETRY. 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 [13] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX MEDLINE=96185449; 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 [14] RP VARIANT MPS7 TRP-216. RX MEDLINE=94154730; 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 [15] RP VARIANTS MPS7 VAL-354 AND TRP-611. RX MEDLINE=94154731; 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 [16] RP VARIANTS MPS7 CYS-382 AND VAL-619. RX MEDLINE=91090114; 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 [17] RP VARIANT MPS7 CYS-627. RX MEDLINE=93190983; 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 [18] 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 [19] 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 [20] 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 [21] 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 [22] 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 [23] 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 [24] 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 [25] 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 [26] 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: A beta-D-glucuronoside + H(2)O = D-glucuronate CC + an alcohol. CC -!- ENZYME REGULATION: Inhibited by L-aspartic acid. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Lysosome. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P08236-1; Sequence=Displayed; CC Name=Short; CC IsoId=P08236-2; Sequence=VSP_001799; CC -!- PTM: N-linked glycosylated with 3 to 4 oligosaccharide chains. CC -!- DISEASE: Defects in GUSB are the cause of mucopolysaccharidosis CC type 7 (MPS7) [MIM:253220]; also known as Sly syndrome. MPS7 is an CC autosomal recessive lysosomal storage disease characterized by CC inability to degrade glucuronic acid-containing CC glycosaminoglycans. The phenotype is highly variable, ranging from CC severe lethal hydrops fetalis to mild forms with survival into CC adulthood. Most patients with the intermediate phenotype show CC hepatomegaly, skeletal anomalies, coarse facies, and variable CC degrees of mental impairment. CC -!- DISEASE: Mucopolysaccharidosis type 7 is associated with non- CC immune hydrops fetalis [MIM:236750]. Hydrops fetalis is a CC generalized edema of the fetus with fluid accumulation in the body CC cavities. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. CC -!- WEB RESOURCE: Name=GeneReviews; CC URL="http://www.genetests.org/query?gene=GUSB"; 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; 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 IPI; IPI00027745; -. DR IPI; IPI00219516; -. DR PIR; A26581; A26581. DR RefSeq; NP_000172.1; -. DR UniGene; Hs.255230; -. DR PDB; 1BHG; X-ray; 2.53 A; A/B=21-633. DR PDBsum; 1BHG; -. DR CAZy; GH2; Glycoside Hydrolase Family 2. DR PRIDE; P08236; -. DR Ensembl; ENSG00000169919; Homo sapiens. DR GeneID; 2990; -. DR KEGG; hsa:2990; -. DR GeneCards; GC07M065064; -. DR H-InvDB; HIX0006717; -. DR H-InvDB; HIX0032616; -. DR H-InvDB; HIX0057487; -. DR H-InvDB; HIX0057503; -. DR H-InvDB; HIX0057683; -. DR H-InvDB; HIX0058602; -. DR HGNC; HGNC:4696; GUSB. DR MIM; 236750; phenotype. DR MIM; 253220; phenotype. DR MIM; 611499; gene. DR Orphanet; 584; Mucopolysaccharidosis type 7. DR PharmGKB; PA29075; -. DR HOGENOM; P08236; -. DR HOVERGEN; P08236; -. DR BRENDA; 3.2.1.31; 247. DR LinkHub; P08236; -. DR NextBio; 11852; -. DR ArrayExpress; P08236; -. DR Bgee; P08236; -. DR CleanEx; HS_GUSB; -. DR GermOnline; ENSG00000169919; Homo sapiens. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-KW. DR GO; GO:0004566; F:beta-glucuronidase activity; TAS:ProtInc. DR GO; GO:0043169; F:cation binding; IEA:InterPro. DR GO; GO:0006027; P:glycosaminoglycan catabolic process; TAS:ProtInc. DR InterPro; IPR006101; Glyco_hydro_2. DR InterPro; IPR013812; Glyco_hydro_2/20_Ig-like. DR InterPro; IPR006104; Glyco_hydro_2_carb-bd. DR InterPro; IPR006102; Glyco_hydro_2_Ig-like. DR InterPro; IPR006103; Glyco_hydro_2_TIM. DR InterPro; IPR013781; Glyco_hydro_sub_cat. DR Gene3D; G3DSA:2.60.40.320; Glyco_hydro_2/20_Ig-like; 1. DR Gene3D; G3DSA:3.20.20.80; Glyco_hydro_cat; 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 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; Direct protein sequencing; KW Disease mutation; Glycoprotein; Glycosidase; Hydrolase; Lysosome; KW Mucopolysaccharidosis; Polymorphism; Signal. FT SIGNAL 1 22 FT CHAIN 23 651 Beta-glucuronidase. FT /FTId=PRO_0000012161. FT ACT_SITE 451 451 Proton donor. FT CARBOHYD 173 173 N-linked (GlcNAc...). FT CARBOHYD 272 272 N-linked (GlcNAc...). FT CARBOHYD 420 420 N-linked (GlcNAc...). FT CARBOHYD 631 631 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 305 355 Missing (in isoform Short). FT /FTId=VSP_001799. FT VARIANT 38 38 C -> G (in MPS7; very mild phenotype). FT /FTId=VAR_037914. FT VARIANT 52 52 S -> F (in MPS7; loss of activity). FT /FTId=VAR_037915. FT VARIANT 136 136 G -> R (in MPS7). FT /FTId=VAR_037916. FT VARIANT 148 148 P -> S (in MPS7). FT /FTId=VAR_037917. FT VARIANT 150 150 E -> K (in MPS7). FT /FTId=VAR_037918. FT VARIANT 152 152 D -> N (reduced activity levels without FT apparent pathogenic consequences). FT /FTId=VAR_037919. FT VARIANT 176 176 L -> F (in MPS7). FT /FTId=VAR_037920. FT VARIANT 216 216 R -> W (in MPS7). FT /FTId=VAR_003196. FT VARIANT 320 320 Y -> C (in MPS7). FT /FTId=VAR_037921. FT VARIANT 320 320 Y -> S (in MPS7). FT /FTId=VAR_037922. FT VARIANT 350 350 K -> N (in MPS7). FT /FTId=VAR_037923. FT VARIANT 351 351 H -> Y (in MPS7). FT /FTId=VAR_037924. FT VARIANT 354 354 A -> V (in MPS7). FT /FTId=VAR_003197. FT VARIANT 374 374 R -> C (in MPS7). FT /FTId=VAR_037925. FT VARIANT 382 382 R -> C (in MPS7). FT /FTId=VAR_003198. FT VARIANT 382 382 R -> H (in MPS7). FT /FTId=VAR_037926. FT VARIANT 408 408 P -> S (in MPS7). FT /FTId=VAR_037927. FT VARIANT 415 415 P -> L (in MPS7). FT /FTId=VAR_037928. FT VARIANT 435 435 R -> P (in MPS7). FT /FTId=VAR_037929. FT VARIANT 477 477 R -> W (in MPS7). FT /FTId=VAR_037930. FT VARIANT 495 495 Y -> C (in MPS7). FT /FTId=VAR_037931. FT VARIANT 508 508 Y -> C (in MPS7). FT /FTId=VAR_037932. FT VARIANT 572 572 G -> D (in MPS7). FT /FTId=VAR_037933. FT VARIANT 577 577 R -> L (in MPS7; loss of activity). FT /FTId=VAR_037934. FT VARIANT 606 606 K -> N (in MPS7). FT /FTId=VAR_037935. FT VARIANT 611 611 R -> W (in MPS7). FT /FTId=VAR_003199. FT VARIANT 619 619 A -> V (in MPS7). FT /FTId=VAR_003200. FT VARIANT 626 626 Y -> H (in MPS7; very mild phenotype). FT /FTId=VAR_037936. FT VARIANT 627 627 W -> C (in MPS7). FT /FTId=VAR_003201. FT VARIANT 649 649 L -> P (in dbSNP:rs9530). FT /FTId=VAR_016179. FT STRAND 33 35 FT STRAND 41 43 FT STRAND 46 50 FT STRAND 52 55 FT HELIX 57 60 FT HELIX 63 65 FT HELIX 68 71 FT STRAND 83 88 FT HELIX 90 93 FT STRAND 97 106 FT TURN 109 112 FT STRAND 115 124 FT STRAND 128 133 FT STRAND 135 146 FT STRAND 149 151 FT STRAND 165 172 FT STRAND 177 185 FT STRAND 192 195 FT STRAND 206 208 FT STRAND 218 226 FT STRAND 232 234 FT STRAND 239 242 FT STRAND 245 247 FT STRAND 256 263 FT STRAND 265 267 FT STRAND 269 273 FT STRAND 275 278 FT TURN 291 293 FT STRAND 301 310 FT STRAND 312 319 FT STRAND 322 324 FT STRAND 329 331 FT STRAND 336 338 FT STRAND 345 349 FT TURN 355 357 FT HELIX 363 376 FT STRAND 380 382 FT HELIX 392 396 FT STRAND 402 405 FT HELIX 416 418 FT HELIX 420 437 FT STRAND 441 451 FT HELIX 457 471 FT STRAND 479 483 FT TURN 487 489 FT HELIX 493 495 FT STRAND 497 502 FT STRAND 507 510 FT HELIX 514 531 FT STRAND 536 540 FT HELIX 559 576 FT TURN 577 580 FT STRAND 581 590 FT STRAND 600 604 FT HELIX 617 631 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 //