ID BGAL_HUMAN Reviewed; 677 AA. AC P16278; B2R7H8; B7Z6B0; P16279; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 2. DT 27-MAR-2024, entry version 241. DE RecName: Full=Beta-galactosidase; DE EC=3.2.1.23 {ECO:0000269|PubMed:15714521, ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:24737316, ECO:0000269|PubMed:2511208, ECO:0000269|PubMed:25936995, ECO:0000269|PubMed:3143362, ECO:0000269|PubMed:8200356}; DE AltName: Full=Acid beta-galactosidase; DE Short=Lactase; DE AltName: Full=Elastin receptor 1; DE Flags: Precursor; GN Name=GLB1; Synonyms=ELNR1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CATALYTIC ACTIVITY. RC TISSUE=Placenta; RX PubMed=3143362; DOI=10.1016/s0006-291x(88)80038-x; RA Oshima A., Tsuji A., Nagao Y., Sakuraba H., Suzuki Y.; RT "Cloning, sequencing, and expression of cDNA for human beta- RT galactosidase."; RL Biochem. Biophys. Res. Commun. 157:238-244(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 29-46; RP 287-299; 372-376 AND 443-457, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, AND VARIANT LEU-10. RC TISSUE=Testis; RX PubMed=2511208; DOI=10.1016/s0021-9258(19)47114-7; RA Morreau H., Galjart N.J., Gillemans N., Willemsen R., van der Horst G.T.J., RA D'Azzo A.; RT "Alternative splicing of beta-galactosidase mRNA generates the classic RT lysosomal enzyme and a beta-galactosidase-related protein."; RL J. Biol. Chem. 264:20655-20663(1989). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND RP VARIANT LEU-10. RX PubMed=2111707; DOI=10.1089/dna.1990.9.119; RA Yamamoto Y., Hake C.A., Martin B.M., Kretz K.A., Ahern-Rindell A.J., RA Naylor S.L., Mudd M., O'Brien J.S.; RT "Isolation, characterization, and mapping of a human acid beta- RT galactosidase cDNA."; RL DNA Cell Biol. 9:119-127(1990). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT RP LEU-10. 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-10. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT CYS-521. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-10. 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=3084261; RA Willemsen R., Hoogeveen A.T., Sips H.J., van Dongen J.M., Galjaard H.; RT "Immunoelectron microscopical localization of lysosomal beta-galactosidase RT and its precursor forms in normal and mutant human fibroblasts."; RL Eur. J. Cell Biol. 40:9-15(1986). RN [9] RP DOMAIN ELASTIN/LAMININ BINDING, AND TISSUE SPECIFICITY. RX PubMed=8383699; DOI=10.1172/jci116280; RA Hinek A., Rabinovitch M., Keeley F., Okamura-Oho Y., Callahan J.; RT "The 67-kD elastin/laminin-binding protein is related to an enzymatically RT inactive, alternatively spliced form of beta-galactosidase."; RL J. Clin. Invest. 91:1198-1205(1993). RN [10] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=8200356; DOI=10.1111/j.1432-1033.1994.tb18844.x; RA Zschoche A., Fuerst W., Schwarzmann G., Sanhoff K.; RT "Hydrolysis of lactosylceramide by human galactosylceramidase and GM1-beta- RT galactosidase in a detergent-free system and its stimulation by RT sphingolipid activator proteins, sap-B and sap-C. Activator proteins RT stimulate lactosylceramide hydrolysis."; RL Eur. J. Biochem. 222:83-90(1994). RN [11] RP FUNCTION (ISOFORM 2). RX PubMed=8922281; RA Hinek A.; RT "Biological roles of the non-integrin elastin/laminin receptor."; RL Biol. Chem. 377:471-480(1996). RN [12] RP IDENTITY OF BETA-GALACTOSIDASE-RELATED PROTEIN WITH EBP. RX PubMed=9497360; DOI=10.1074/jbc.273.11.6319; RA Privitera S., Prody C.A., Callahan J.W., Hinek A.; RT "The 67-kDa enzymatically inactive alternatively spliced variant of beta- RT galactosidase is identical to the elastin/laminin-binding protein."; RL J. Biol. Chem. 273:6319-6326(1998). RN [13] RP REVIEW. RX PubMed=10571006; DOI=10.1016/s0925-4439(99)00075-7; RA Callahan J.W.; RT "Molecular basis of GM1 gangliosidosis and Morquio disease, type B. RT Structure-function studies of lysosomal beta-galactosidase and the non- RT lysosomal beta-galactosidase-like protein."; RL Biochim. Biophys. Acta 1455:85-103(1999). RN [14] RP ELASTIC-FIBER ASSEMBLY STUDIES, AND FUNCTION (ISOFORM 2). RX PubMed=10841810; DOI=10.1086/302968; RA Hinek A., Zhang S., Smith A.C., Callahan J.W.; RT "Impaired elastic-fiber assembly by fibroblasts from patients with either RT Morquio B disease or infantile GM1-gangliosidosis is linked to deficiency RT in the 67-kD spliced variant of beta-galactosidase."; RL Am. J. Hum. Genet. 67:23-36(2000). RN [15] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-464. RC TISSUE=Platelet; RX PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200; RA Lewandrowski U., Moebius J., Walter U., Sickmann A.; RT "Elucidation of N-glycosylation sites on human platelet proteins: a RT glycoproteomic approach."; RL Mol. Cell. Proteomics 5:226-233(2006). RN [16] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-464 AND ASN-555. 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 multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] 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., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] 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., Ayoub D., RA 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 [20] {ECO:0007744|PDB:3THC, ECO:0007744|PDB:3THD} RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 24-677 IN COMPLEX WITH GALACTOSE, RP SUBUNIT, ACTIVE SITE, GLYCOSYLATION AT ASN-247; ASN-464; ASN-498 AND RP ASN-555, AND DISULFIDE BONDS. RX PubMed=22128166; DOI=10.1074/jbc.m111.293795; RA Ohto U., Usui K., Ochi T., Yuki K., Satow Y., Shimizu T.; RT "Crystal structure of human beta-galactosidase: structural basis of Gm1 RT gangliosidosis and morquio B diseases."; RL J. Biol. Chem. 287:1801-1812(2012). RN [21] {ECO:0007744|PDB:3WEZ, ECO:0007744|PDB:3WF0, ECO:0007744|PDB:3WF1, ECO:0007744|PDB:3WF2, ECO:0007744|PDB:3WF3, ECO:0007744|PDB:3WF4} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 24-677 IN COMPLEX WITH GALACTOSE, RP CATALYTIC ACTIVITY, GLYCOSYLATION AT ASN-247; ASN-464; ASN-498 AND ASN-555, RP DISULFIDE BONDS, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANT RP GM1G3 THR-51, AND CHARACTERIZATION OF VARIANT GM1G1 AND GM1G2 CYS-201. RX PubMed=24737316; DOI=10.1074/jbc.m113.529529; RA Suzuki H., Ohto U., Higaki K., Mena-Barragan T., Aguilar-Moncayo M., RA Ortiz Mellet C., Nanba E., Garcia Fernandez J.M., Suzuki Y., Shimizu T.; RT "Structural basis of pharmacological chaperoning for human beta- RT galactosidase."; RL J. Biol. Chem. 289:14560-14568(2014). RN [22] RP VARIANTS MPS4B LEU-273; HIS-482 AND CYS-509, AND VARIANT GM1G1 CYS-494. RX PubMed=1928092; RA Oshima A., Yoshida K., Shimmoto M., Fukuhara Y., Sakuraba H., Suzuki Y.; RT "Human beta-galactosidase gene mutations in morquio B disease."; RL Am. J. Hum. Genet. 49:1091-1093(1991). RN [23] RP VARIANT GM1G1 CYS-49, VARIANT GM1G3 THR-51, AND VARIANT GM1G2 CYS-201. RX PubMed=1909089; RA Nishimoto J., Nanba E., Inui K., Okada S., Suzuki K.; RT "GM1-gangliosidosis (genetic beta-galactosidase deficiency): identification RT of four mutations in different clinical phenotypes among Japanese RT patients."; RL Am. J. Hum. Genet. 49:566-574(1991). RN [24] RP VARIANTS GM1G3 THR-51 AND GLN-457, VARIANTS GM1G1 ARG-123 AND CYS-316, AND RP VARIANT GM1G2 CYS-201. RX PubMed=1907800; RA Yoshida K., Oshima A., Shimmoto M., Fukuhara Y., Sakuraba H., RA Yanagisawa N., Suzuki Y.; RT "Human beta-galactosidase gene mutations in GM1-gangliosidosis: a common RT mutation among Japanese adult/chronic cases."; RL Am. J. Hum. Genet. 49:435-442(1991). RN [25] RP VARIANT GM1G1 HIS-482. RX PubMed=1487238; DOI=10.1007/bf00220071; RA Mosna G., Fattore S., Tubiello G., Brocca S., Trubia M., Gianazza E., RA Gatti R., Danesino C., Minelli A., Piantanida M.; RT "A homozygous missense arginine to histidine substitution at position 482 RT of the beta-galactosidase in an Italian infantile GM1-gangliosidosis RT patient."; RL Hum. Genet. 90:247-250(1992). RN [26] RP VARIANTS GM1G1 CYS-208 AND ARG-578, AND VARIANTS GM1G2 HIS-590 AND GLY-632. RX PubMed=8213816; RA Boustany R.-M.N., Qian W.-H., Suzuki K.; RT "Mutations in acid beta-galactosidase cause GM1-gangliosidosis in American RT patients."; RL Am. J. Hum. Genet. 53:881-888(1993). RN [27] RP VARIANT GM1G3 MET-82. RX PubMed=8198123; RA Chakraborty S., Rafi M.A., Wenger D.A.; RT "Mutations in the lysosomal beta-galactosidase gene that cause the adult RT form of GM1 gangliosidosis."; RL Am. J. Hum. Genet. 54:1004-1013(1994). RN [28] RP VARIANTS GM1G1 SER-148 AND ALA-216, VARIANT GM1G3 TYR-214, AND VARIANT RP GLY-532. RA Hilson W.L., Okamura-Oho Y., Zhang S., Clarke J.T.R., Mahuran D., RA Callahan J.W.; RT "Novel missense mutations in beta-galactosidase that result in GM1- RT gangliosidosis."; RL Am. J. Hum. Genet. 55:A223-A223(1994). RN [29] RP VARIANTS MPS4B HIS-83 AND CYS-482. RX PubMed=7586649; DOI=10.1111/j.1399-0004.1995.tb04065.x; RA Ishii N., Oohira T., Oshima A., Sakuraba H., Endo F., Matsuda I., RA Sukegawa K., Orii T., Suzuki Y.; RT "Clinical and molecular analysis of a Japanese boy with Morquio B RT disease."; RL Clin. Genet. 48:103-108(1995). RN [30] RP VARIANT GM1G3 SER-263. RA Suzuki Y., Sakuraba H., Oshima A.; RT "Beta-galactosidase deficiency (beta-galactosidosis): GM1 gangliosidosis RT and Morquio B disease."; RL (In) Scriver C.R., Beaudet A.L., Sly W.S., Valle D. (eds.); RL The metabolic and molecular bases of inherited disease, pp.2787-2823, RL McGraw-Hill Publishing Co., New York (1995). RN [31] RP VARIANTS GM1G1 HIS-59; ASN-591 AND CYS-591. RA Morrone A., Bardelli T., Donati M.A., Giorgi M., Di Rocco R., Gatti R., RA Taddeucci G., Ricci R., D'Azzo A., Zammarchi E.; RT "Identification of new mutations in six Italian patients affected by a RT variant form of infantile GM1-gangliosidosis with severe cardiomyopathy."; RL Am. J. Hum. Genet. 61:A258-A258(1997). RN [32] RP VARIANTS SLOWLY PROGRESSIVE GM1-GANGLIOSIDOSIS HIS-201; SER-266 AND RP CYS-509. RX PubMed=9203065; DOI=10.1177/088307389701200404; RA Kaye E.M., Shalish C., Livermore J., Taylor H.A., Stevenson R.E., RA Breakefield X.O.; RT "Beta-Galactosidase gene mutations in patients with slowly progressive GM1 RT gangliosidosis."; RL J. Child Neurol. 12:242-247(1997). RN [33] RP VARIANTS MPS4B GLU-438; LYS-484 AND ALA-500. RX PubMed=12393180; DOI=10.1016/s0925-4439(02)00172-2; RA Bagshaw R.D., Zhang S., Hinek A., Skomorowski M.-A., Whelan D., RA Clarke J.T.R., Callahan J.W.; RT "Novel mutations (Asn 484 Lys, Thr 500 Ala, Gly 438 Glu) in Morquio B RT disease."; RL Biochim. Biophys. Acta 1588:247-253(2002). RN [34] RP VARIANTS GM1G1 HIS-59; SER-121; CYS-208; MET-240 AND ASN-491, AND VARIANTS RP LEU-10; CYS-521 AND GLY-532. RX PubMed=10338095; RX DOI=10.1002/(sici)1098-1004(1999)13:5<401::aid-humu9>3.0.co;2-n; RA Silva C.M.D., Severini M.H., Sopelsa A., Coelho J.C., Zaha A., d'Azzo A., RA Giugliani R.; RT "Six novel beta-galactosidase gene mutations in Brazilian patients with RT GM1-gangliosidosis."; RL Hum. Mutat. 13:401-409(1999). RN [35] RP VARIANTS GM1G1 SER-148 AND ASN-332, VARIANT GLY-532, AND CHARACTERIZATION RP OF VARIANT GLY-532. RX PubMed=10839995; DOI=10.1042/bj3480621; RA Zhang S., Bagshaw R., Hilson W., Oho Y., Hinek A., Clarke J.T.R., Hinek A., RA Callahan J.W.; RT "Characterization of beta-galactosidase mutations Asp332-->Asn and RT Arg148-->Ser, and a polymorphism, Ser532-->Gly, in a case of GM1 RT gangliosidosis."; RL Biochem. J. 348:621-632(2000). RN [36] RP VARIANTS GM1G1 HIS-59; HIS-482; ASN-591 AND CYS-591, AND VARIANTS GM1G2 RP HIS-201 AND ASP-579. RX PubMed=10737981; RX DOI=10.1002/(sici)1098-1004(200004)15:4<354::aid-humu8>3.0.co;2-l; RA Morrone A., Bardelli T., Donati M.A., Giorgi M., Di Rocco M., Gatti R., RA Parini R., Ricci R., Taddeucci G., D'Azzo A., Zammarchi E.; RT "Beta-galactosidase gene mutations affecting the lysosomal enzyme and the RT elastin-binding protein in GM1-gangliosidosis patients with cardiac RT involvement."; RL Hum. Mutat. 15:354-366(2000). RN [37] RP VARIANTS MPS4B LEU-273; PRO-408 AND ALA-500, VARIANTS GM1G3 MET-82; ASP-270 RP AND TYR-281, AND VARIANT LEU-10. RX PubMed=11511921; DOI=10.1007/s004390100570; RA Paschke E., Milos I., Kreimer-Erlacher H., Hoefler G., Beck M., RA Hoeltzenbein M., Kleijer W., Levade T., Michelakakis H., Radeva B.; RT "Mutation analyses in 17 patients with deficiency in acid beta- RT galactosidase: three novel point mutations and high correlation of mutation RT W273L with Morquio disease type B."; RL Hum. Genet. 109:159-166(2001). RN [38] RP VARIANTS GM1G2 TRP-68 AND CYS-201, CHARACTERIZATION OF VARIANTS GM1G2 RP TRP-68 AND CYS-201, VARIANT PHE-436, AND MODULATING ACTION OF VARIANT RP PHE-436. RX PubMed=12644936; DOI=10.1007/s00439-003-0930-8; RA Caciotti A., Bardelli T., Cunningham J., D'Azzo A., Zammarchi E., RA Morrone A.; RT "Modulating action of the new polymorphism L436F detected in the GLB1 gene RT of a type-II GM1 gangliosidosis patient."; RL Hum. Genet. 113:44-50(2003). RN [39] RP VARIANT GM1G1 TYR-151, AND CHARACTERIZATION OF VARIANT GM1G1 TYR-151. RX PubMed=15365997; DOI=10.1002/humu.9279; RA Georgiou T., Drousiotou A., Campos Y., Caciotti A., Sztriha L., Gururaj A., RA Ozand P., Zammarchi E., Morrone A., D'Azzo A.; RT "Four novel mutations in patients from the Middle East with the infantile RT form of GM1-gangliosidosis."; RL Hum. Mutat. 24:352-352(2004). RN [40] RP ERRATUM OF PUBMED:15365997. RA Georgiou T., Drousiotou A., Campos Y., Caciotti A., Sztriha L., Gururaj A., RA Ozand P., Zammarchi E., Morrone A., D'Azzo A.; RL Hum. Mutat. 24:536-537(2004). RN [41] RP VARIANTS GM1G1 HIS-59; CYS-59; CYS-208; MET-239; TYR-281; HIS-482; ASP-579; RP ASN-591 AND CYS-591, VARIANT GM1G2 HIS-201, VARIANT GM1G3 CYS-521, RP CHARACTERIZATION OF VARIANTS GM1G1 HIS-59; CYS-59; CYS-208; MET-239; RP TYR-281; HIS-482; ASP-579; ASN-591 AND CYS-591, CHARACTERIZATION OF VARIANT RP GM1G2 HIS-201, CHARACTERIZATION OF VARIANT GM1G3 CYS-521, FUNCTION, AND RP CATALYTIC ACTIVITY. RX PubMed=15714521; DOI=10.1002/humu.20147; RA Caciotti A., Donati M.A., Boneh A., d'Azzo A., Federico A., Parini R., RA Antuzzi D., Bardelli T., Nosi D., Kimonis V., Zammarchi E., Morrone A.; RT "Role of beta-galactosidase and elastin binding protein in lysosomal and RT nonlysosomal complexes of patients with GM1-gangliosidosis."; RL Hum. Mutat. 25:285-292(2005). RN [42] RP VARIANT GM1G1 TYR-151, AND VARIANT LEU-10. RX PubMed=15791924; DOI=10.1177/08830738050200010901; RA Gururaj A., Sztriha L., Hertecant J., Johansen J.G., Georgiou T., RA Campos Y., Drousiotou A., d'Azzo A.; RT "Magnetic resonance imaging findings and novel mutations in GM1 RT gangliosidosis."; RL J. Child Neurol. 20:57-60(2005). RN [43] RP VARIANTS GM1G3 HIS-49; GLU-73; CYS-148 AND GLU-438. RX PubMed=15986423; DOI=10.1002/mds.20593; RA Roze E., Paschke E., Lopez N., Eck T., Yoshida K., Maurel-Ollivier A., RA Doummar D., Caillaud C., Galanaud D., Billette de Villemeur T., RA Vidailhet M., Roubergue A.; RT "Dystonia and parkinsonism in GM1 type 3 gangliosidosis."; RL Mov. Disord. 20:1366-1369(2005). RN [44] RP VARIANTS GM1G1 CYS-59; HIS-59; SER-136; VAL-151; PRO-173; CYS-199; ASP-272; RP ASN-346; CYS-347; PRO-420; ARG-422; ASN-441 AND CYS-590, VARIANT GM1G2 RP SER-264, VARIANTS GM1G3 HIS-201 AND LYS-420, VARIANTS MPS4B CYS-83; RP CYS-444; SER-494 AND ALA-500, AND VARIANTS PHE-436; CYS-521 AND GLY-532. RX PubMed=16941474; DOI=10.1002/humu.9451; RA Santamaria R., Chabas A., Coll M.J., Miranda C.S., Vilageliu L., RA Grinberg D.; RT "Twenty-one novel mutations in the GLB1 gene identified in a large group of RT GM1-gangliosidosis and Morquio B patients: possible common origin for the RT prevalent p.R59H mutation among Gypsies."; RL Hum. Mutat. 27:1060-1060(2006). RN [45] RP VARIANTS MPS4B LEU-273; HIS-482 AND CYS-509, AND VARIANTS GM1G1 CYS-201; RP HIS-201 AND HIS-318. RX PubMed=16538002; DOI=10.2152/jmi.53.103; RA Tatano Y., Takeuchi N., Kuwahara J., Sakuraba H., Takahashi T., Takada G., RA Itoh K.; RT "Elastogenesis in cultured dermal fibroblasts from patients with lysosomal RT beta-galactosidase, protective protein/cathepsin A and neuraminidase-1 RT deficiencies."; RL J. Med. Invest. 53:103-112(2006). RN [46] RP VARIANTS GM1G1 CYS-59; HIS-59; VAL-134; LEU-147 DEL; SER-162; CYS-208; RP ASP-272; 377-VAL--LYS-381 DEL; TYR-491; LEU-549 AND CYS-590, VARIANT GM1G2 RP HIS-201, VARIANT GM1G3 ARG-155, AND VARIANTS GM1-GANGLIOSIDOSIS LEU-434 AND RP GLU-554. RX PubMed=17309651; DOI=10.1111/j.1399-0004.2007.00767.x; RA Santamaria R., Blanco M., Chabas A., Grinberg D., Vilageliu L.; RT "Identification of 14 novel GLB1 mutations, including five deletions, in 19 RT patients with GM1 gangliosidosis from South America."; RL Clin. Genet. 71:273-279(2007). RN [47] RP VARIANT TRP-595, AND CHARACTERIZATION OF VARIANT TRP-595. RX PubMed=17661814; DOI=10.1111/j.1399-0004.2007.00843.x; RA Gort L., Santamaria R., Grinberg D., Vilageliu L., Chabas A.; RT "Identification of a novel pseudodeficiency allele in the GLB1 gene in a RT carrier of GM1 gangliosidosis."; RL Clin. Genet. 72:109-111(2007). RN [48] RP CHARACTERIZATION OF VARIANTS GM1G1 HIS-59; SER-162; PRO-173; HIS-201; RP PRO-420; ASN-441 AND CYS-590, CHARACTERIZATION OF VARIANTS MPS4B CYS-83; RP CYS-444 AND SER-494, CHARACTERIZATION OF VARIANT GM1G3 LYS-420 AND CYS-521, RP AND CHARACTERIZATION OF VARIANT GLY-532. RX PubMed=17664528; DOI=10.1194/jlr.m700308-jlr200; RA Santamaria R., Chabas A., Callahan J.W., Grinberg D., Vilageliu L.; RT "Expression and characterization of 14 GLB1 mutant alleles found in GM1- RT gangliosidosis and Morquio B patients."; RL J. Lipid Res. 48:2275-2282(2007). RN [49] RP VARIANTS GM1G1 HIS-59; THR-132; ARG-184; ASP-190; CYS-201; HIS-201; RP MET-239; HIS-255; ILE-329; GLU-332; ASN-346; GLN-442 AND SER-597, VARIANTS RP GM1G2 GLN-68; ARG-155 AND HIS-333, VARIANTS GM1G3 MET-82; ASP-270 AND RP GLU-438, VARIANTS MPS4B PHE-149; TYR-198; LEU-273; ALA-397; PRO-408 AND RP ALA-500, CHARACTERIZATION OF VARIANTS GM1G1 THR-132; ARG-184; ASP-190; RP CYS-201; HIS-201; HIS-255; ILE-329; GLU-332 AND SER-597, CHARACTERIZATION RP OF VARIANTS GM1G2 GLN-68; ARG-155 AND HIS-333, CHARACTERIZATION OF VARIANTS RP GM1G3 ASP-270 AND GLU-438, CHARACTERIZATION OF VARIANTS MPS4B PHE-149; RP TYR-198; LEU-273; ALA-397; PRO-408 AND ALA-500, CATALYTIC ACTIVITY, AND RP FUNCTION. RX PubMed=19472408; DOI=10.1002/humu.21031; RA Hofer D., Paul K., Fantur K., Beck M., Buerger F., Caillaud C., Fumic K., RA Ledvinova J., Lugowska A., Michelakakis H., Radeva B., Ramaswami U., RA Plecko B., Paschke E.; RT "GM1 gangliosidosis and Morquio B disease: expression analysis of missense RT mutations affecting the catalytic site of acid beta-galactosidase."; RL Hum. Mutat. 30:1214-1221(2009). RN [50] RP VARIANTS GM1G2 CYS-49; ARG-134; CYS-148; GLU-262; LEU-314; PRO-337; RP VAL-414; ASN-493; LEU-597 AND ILE-600, CHARACTERIZATION OF VARIANTS GM1G2 RP CYS-49; GLU-262; LEU-314; PRO-337; VAL-414; ASN-493; LEU-597 AND ILE-600, RP VARIANTS GM1G1 TRP-68; ARG-123; PRO-236; CYS-331; ASN-332; PRO-337; HIS-482 RP AND PRO-514, CHARACTERIZATION OF VARIANTS GM1G1 TRP-68; ARG-123; PRO-236; RP ASN-332; PRO-337; HIS-482 AND PRO-514, VARIANT GM1G3 PHE-297, RP CHARACTERIZATION OF VARIANT GM1G3 PHE-297, VARIANTS GLN-129 AND CYS-521, RP CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=25936995; DOI=10.1016/j.gene.2015.04.078; RA Bidchol A.M., Dalal A., Trivedi R., Shukla A., Nampoothiri S., Sankar V.H., RA Danda S., Gupta N., Kabra M., Hebbar S.A., Bhat R.Y., Matta D., RA Ekbote A.V., Puri R.D., Phadke S.R., Gowrishankar K., Aggarwal S., RA Ranganath P., Sharda S., Kamate M., Datar C.A., Bhat K., Kamath N., RA Shah H., Krishna S., Gopinath P.M., Verma I.C., Nagarajaram H.A., RA Satyamoorthy K., Girisha K.M.; RT "Recurrent and novel GLB1 mutations in India."; RL Gene 567:173-181(2015). CC -!- FUNCTION: [Isoform 1]: Cleaves beta-linked terminal galactosyl residues CC from gangliosides, glycoproteins, and glycosaminoglycans. CC {ECO:0000269|PubMed:15714521, ECO:0000269|PubMed:19472408, CC ECO:0000269|PubMed:2511208, ECO:0000269|PubMed:25936995, CC ECO:0000269|PubMed:8200356}. CC -!- FUNCTION: [Isoform 2]: Has no beta-galactosidase catalytic activity, CC but plays functional roles in the formation of extracellular elastic CC fibers (elastogenesis) and in the development of connective tissue. CC Seems to be identical to the elastin-binding protein (EBP), a major CC component of the non-integrin cell surface receptor expressed on CC fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and CC certain cancer cell types. In elastin producing cells, associates with CC tropoelastin intracellularly and functions as a recycling molecular CC chaperone which facilitates the secretions of tropoelastin and its CC assembly into elastic fibers. {ECO:0000269|PubMed:10841810, CC ECO:0000269|PubMed:8922281}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues CC in beta-D-galactosides.; EC=3.2.1.23; CC Evidence={ECO:0000269|PubMed:15714521, ECO:0000269|PubMed:19472408, CC ECO:0000269|PubMed:24737316, ECO:0000269|PubMed:2511208, CC ECO:0000269|PubMed:25936995, ECO:0000269|PubMed:3143362, CC ECO:0000269|PubMed:8200356}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 4.5-5.5.; CC -!- SUBUNIT: Homodimer (PubMed:22128166). May form higher multimers CC (Probable). {ECO:0000269|PubMed:22128166, ECO:0000305|PubMed:3084261}. CC -!- INTERACTION: CC P16278; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-989638, EBI-712073; CC P16278; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-989638, EBI-18159983; CC P16278; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-989638, EBI-8644112; CC P16278; P30825: SLC7A1; NbExp=3; IntAct=EBI-989638, EBI-4289564; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Lysosome CC {ECO:0000269|PubMed:2511208, ECO:0000269|PubMed:3084261}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, perinuclear region CC {ECO:0000269|PubMed:2511208}. Note=Localized to the perinuclear area of CC the cytoplasm but not to lysosomes. {ECO:0000269|PubMed:2511208}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P16278-1; Sequence=Displayed; CC Name=2; Synonyms=Beta-galactosidase-related protein CC {ECO:0000303|PubMed:2511208}, Beta-galactosidase-like protein, S-Gal CC {ECO:0000303|PubMed:8383699}, Elastin-binding protein, EBP CC {ECO:0000303|PubMed:9497360}; CC IsoId=P16278-2, P16279-1; Sequence=VSP_031241; CC Name=3; CC IsoId=P16278-3; Sequence=VSP_039974; CC -!- TISSUE SPECIFICITY: Detected in placenta (at protein level) CC (PubMed:8383699). Detected in fibroblasts and testis (PubMed:2511208). CC {ECO:0000269|PubMed:2511208, ECO:0000269|PubMed:8383699}. CC -!- DISEASE: GM1-gangliosidosis 1 (GM1G1) [MIM:230500]: An autosomal CC recessive lysosomal storage disease marked by the accumulation of GM1 CC gangliosides, glycoproteins and keratan sulfate primarily in neurons of CC the central nervous system. GM1-gangliosidosis type 1 is characterized CC by onset within the first three months of life, central nervous system CC degeneration, coarse facial features, hepatosplenomegaly, skeletal CC dysmorphology reminiscent of Hurler syndrome, and rapidly progressive CC psychomotor deterioration. Urinary oligosaccharide levels are high. It CC leads to death usually between the first and second year of life. CC {ECO:0000269|PubMed:10338095, ECO:0000269|PubMed:10737981, CC ECO:0000269|PubMed:10839995, ECO:0000269|PubMed:1487238, CC ECO:0000269|PubMed:15365997, ECO:0000269|PubMed:15714521, CC ECO:0000269|PubMed:15791924, ECO:0000269|PubMed:16538002, CC ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:17309651, CC ECO:0000269|PubMed:17664528, ECO:0000269|PubMed:1907800, CC ECO:0000269|PubMed:1909089, ECO:0000269|PubMed:1928092, CC ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:24737316, CC ECO:0000269|PubMed:25936995, ECO:0000269|PubMed:8213816, CC ECO:0000269|Ref.28, ECO:0000269|Ref.31}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- DISEASE: GM1-gangliosidosis 2 (GM1G2) [MIM:230600]: A gangliosidosis CC characterized by onset between ages 1 and 5. The main symptom is CC locomotor ataxia, ultimately leading to a state of decerebration with CC epileptic seizures. Patients do not display the skeletal changes CC associated with the infantile form, but they nonetheless excrete CC elevated amounts of beta-linked galactose-terminal oligosaccharides. CC Inheritance is autosomal recessive. {ECO:0000269|PubMed:10737981, CC ECO:0000269|PubMed:12644936, ECO:0000269|PubMed:15714521, CC ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:17309651, CC ECO:0000269|PubMed:1907800, ECO:0000269|PubMed:1909089, CC ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:24737316, CC ECO:0000269|PubMed:25936995, ECO:0000269|PubMed:8213816}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: GM1-gangliosidosis 3 (GM1G3) [MIM:230650]: A gangliosidosis CC with a variable phenotype. Patients show mild skeletal abnormalities, CC dysarthria, gait disturbance, dystonia and visual impairment. CC Visceromegaly is absent. Intellectual deficit can initially be mild or CC absent but progresses over time. Inheritance is autosomal recessive. CC {ECO:0000269|PubMed:11511921, ECO:0000269|PubMed:15714521, CC ECO:0000269|PubMed:15986423, ECO:0000269|PubMed:16941474, CC ECO:0000269|PubMed:17309651, ECO:0000269|PubMed:17664528, CC ECO:0000269|PubMed:1907800, ECO:0000269|PubMed:1909089, CC ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:24737316, CC ECO:0000269|PubMed:25936995, ECO:0000269|PubMed:8198123, CC ECO:0000269|Ref.28, ECO:0000269|Ref.30}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- DISEASE: Mucopolysaccharidosis 4B (MPS4B) [MIM:253010]: A form of CC mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage CC disease characterized by intracellular accumulation of keratan sulfate CC and chondroitin-6-sulfate. Key clinical features include short stature, CC skeletal dysplasia, dental anomalies, and corneal clouding. CC Intelligence is normal and there is no direct central nervous system CC involvement, although the skeletal changes may result in neurologic CC complications. There is variable severity, but patients with the severe CC phenotype usually do not survive past the second or third decade of CC life. {ECO:0000269|PubMed:11511921, ECO:0000269|PubMed:12393180, CC ECO:0000269|PubMed:16538002, ECO:0000269|PubMed:16941474, CC ECO:0000269|PubMed:17664528, ECO:0000269|PubMed:1928092, CC ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:7586649}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Beta-galactosidase entry; CC URL="https://en.wikipedia.org/wiki/Beta-galactosidase"; 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; M22590; AAA51822.1; -; mRNA. DR EMBL; M27507; AAA51819.1; -; mRNA. DR EMBL; M27508; AAA35599.1; -; mRNA. DR EMBL; M34423; AAA51823.1; -; mRNA. DR EMBL; AK300021; BAH13196.1; -; mRNA. DR EMBL; AK312988; BAG35825.1; -; mRNA. DR EMBL; BT007147; AAP35811.1; -; mRNA. DR EMBL; AC112211; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC007493; AAH07493.1; -; mRNA. DR CCDS; CCDS43061.1; -. [P16278-1] DR CCDS; CCDS43062.1; -. [P16278-3] DR CCDS; CCDS46785.1; -. [P16278-2] DR PIR; A32688; A32611. DR PIR; B32688; B32688. DR RefSeq; NP_000395.2; NM_000404.3. DR RefSeq; NP_001073279.1; NM_001079811.2. DR RefSeq; NP_001129074.1; NM_001135602.2. DR RefSeq; NP_001303969.1; NM_001317040.1. DR PDB; 3THC; X-ray; 1.80 A; A/B/C/D=24-677. DR PDB; 3THD; X-ray; 1.79 A; A/B/C/D=24-677. DR PDB; 3WEZ; X-ray; 2.11 A; A/B/C/D=24-677. DR PDB; 3WF0; X-ray; 2.20 A; A/B/C/D=24-677. DR PDB; 3WF1; X-ray; 2.00 A; A/B/C/D=24-677. DR PDB; 3WF2; X-ray; 2.30 A; A/B/C/D=24-677. DR PDB; 3WF3; X-ray; 2.15 A; A/B/C/D=24-677. DR PDB; 3WF4; X-ray; 2.30 A; A/B/C/D=24-677. DR PDBsum; 3THC; -. DR PDBsum; 3THD; -. DR PDBsum; 3WEZ; -. DR PDBsum; 3WF0; -. DR PDBsum; 3WF1; -. DR PDBsum; 3WF2; -. DR PDBsum; 3WF3; -. DR PDBsum; 3WF4; -. DR AlphaFoldDB; P16278; -. DR SMR; P16278; -. DR BioGRID; 108984; 116. DR CORUM; P16278; -. DR IntAct; P16278; 49. DR MINT; P16278; -. DR STRING; 9606.ENSP00000306920; -. DR BindingDB; P16278; -. DR ChEMBL; CHEMBL2522; -. DR DrugBank; DB04465; Lactose. DR DrugCentral; P16278; -. DR CAZy; GH35; Glycoside Hydrolase Family 35. DR GlyConnect; 1036; 15 N-Linked glycans (3 sites). DR GlyCosmos; P16278; 7 sites, 14 glycans. DR GlyGen; P16278; 8 sites, 14 N-linked glycans (3 sites), 1 O-linked glycan (1 site). DR iPTMnet; P16278; -. DR PhosphoSitePlus; P16278; -. DR SwissPalm; P16278; -. DR BioMuta; GLB1; -. DR DMDM; 215273939; -. DR EPD; P16278; -. DR jPOST; P16278; -. DR MassIVE; P16278; -. DR MaxQB; P16278; -. DR PaxDb; 9606-ENSP00000306920; -. DR PeptideAtlas; P16278; -. DR ProteomicsDB; 53332; -. [P16278-1] DR ProteomicsDB; 53333; -. [P16278-2] DR ProteomicsDB; 53334; -. [P16278-3] DR Pumba; P16278; -. DR Antibodypedia; 3647; 839 antibodies from 38 providers. DR DNASU; 2720; -. DR Ensembl; ENST00000307363.10; ENSP00000306920.4; ENSG00000170266.16. DR Ensembl; ENST00000399402.7; ENSP00000382333.2; ENSG00000170266.16. DR GeneID; 2720; -. DR KEGG; hsa:2720; -. DR MANE-Select; ENST00000307363.10; ENSP00000306920.4; NM_000404.4; NP_000395.3. DR UCSC; uc003cfh.2; human. [P16278-1] DR AGR; HGNC:4298; -. DR CTD; 2720; -. DR DisGeNET; 2720; -. DR GeneCards; GLB1; -. DR GeneReviews; GLB1; -. DR HGNC; HGNC:4298; GLB1. DR HPA; ENSG00000170266; Low tissue specificity. DR MalaCards; GLB1; -. DR MIM; 230500; phenotype. DR MIM; 230600; phenotype. DR MIM; 230650; phenotype. DR MIM; 253010; phenotype. DR MIM; 611458; gene. DR neXtProt; NX_P16278; -. DR Orphanet; 79255; GM1 gangliosidosis type 1. DR Orphanet; 79256; GM1 gangliosidosis type 2. DR Orphanet; 79257; GM1 gangliosidosis type 3. DR Orphanet; 309310; Mucopolysaccharidosis type 4B. DR PharmGKB; PA28709; -. DR VEuPathDB; HostDB:ENSG00000170266; -. DR eggNOG; KOG0496; Eukaryota. DR HOGENOM; CLU_007853_7_2_1; -. DR InParanoid; P16278; -. DR OrthoDB; 5489808at2759; -. DR PhylomeDB; P16278; -. DR TreeFam; TF314816; -. DR PathwayCommons; P16278; -. DR Reactome; R-HSA-2022857; Keratan sulfate degradation. DR Reactome; R-HSA-2024096; HS-GAG degradation. DR Reactome; R-HSA-2206308; MPS IV - Morquio syndrome B. DR Reactome; R-HSA-4085001; Sialic acid metabolism. DR Reactome; R-HSA-4341670; Defective NEU1 causes sialidosis. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-9840310; Glycosphingolipid catabolism. DR SABIO-RK; P16278; -. DR SignaLink; P16278; -. DR BioGRID-ORCS; 2720; 12 hits in 1163 CRISPR screens. DR ChiTaRS; GLB1; human. DR GeneWiki; GLB1; -. DR GenomeRNAi; 2720; -. DR Pharos; P16278; Tchem. DR PRO; PR:P16278; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P16278; Protein. DR Bgee; ENSG00000170266; Expressed in monocyte and 180 other cell types or tissues. DR ExpressionAtlas; P16278; baseline and differential. DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome. DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005773; C:vacuole; IBA:GO_Central. DR GO; GO:0004565; F:beta-galactosidase activity; IDA:UniProtKB. DR GO; GO:0016936; F:galactoside binding; IEA:Ensembl. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:BHF-UCL. DR GO; GO:0019388; P:galactose catabolic process; IEA:Ensembl. DR GO; GO:0046479; P:glycosphingolipid catabolic process; TAS:Reactome. DR GO; GO:0030200; P:heparan sulfate proteoglycan catabolic process; TAS:Reactome. DR GO; GO:0042340; P:keratan sulfate catabolic process; TAS:Reactome. DR GO; GO:0051413; P:response to cortisone; IEA:Ensembl. DR GO; GO:1904016; P:response to Thyroglobulin triiodothyronine; IEA:Ensembl. DR DisProt; DP02785; -. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR026283; B-gal_1-like. DR InterPro; IPR048912; BetaGal1-like_ABD1. DR InterPro; IPR048913; BetaGal_gal-bd. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR031330; Gly_Hdrlase_35_cat. DR InterPro; IPR019801; Glyco_hydro_35_CS. DR InterPro; IPR001944; Glycoside_Hdrlase_35. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR23421:SF172; BETA-GALACTOSIDASE; 1. DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1. DR Pfam; PF21317; BetaGal_ABD_1; 1. DR Pfam; PF21467; BetaGal_gal-bd; 1. DR Pfam; PF01301; Glyco_hydro_35; 1. DR PIRSF; PIRSF006336; B-gal; 1. DR PRINTS; PR00742; GLHYDRLASE35. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF49785; Galactose-binding domain-like; 1. DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1. DR Genevisible; P16278; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing; KW Disease variant; Disulfide bond; Gangliosidosis; Glycoprotein; Glycosidase; KW Hydrolase; Lysosome; Mucopolysaccharidosis; Reference proteome; Signal; KW Zymogen. FT SIGNAL 1..23 FT PROPEP 24..28 FT /evidence="ECO:0000305|PubMed:2511208" FT /id="PRO_0000012185" FT CHAIN 29..677 FT /note="Beta-galactosidase" FT /id="PRO_0000012186" FT REGION 650..677 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 188 FT /note="Proton donor" FT /evidence="ECO:0000305|PubMed:22128166" FT ACT_SITE 268 FT /note="Nucleophile" FT /evidence="ECO:0000305|PubMed:22128166" FT BINDING 83 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:22128166, FT ECO:0000269|PubMed:24737316, ECO:0007744|PDB:3THC, FT ECO:0007744|PDB:3WF3" FT BINDING 129 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:22128166, FT ECO:0000269|PubMed:24737316, ECO:0007744|PDB:3THC, FT ECO:0007744|PDB:3WF3" FT BINDING 187 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:22128166, FT ECO:0000269|PubMed:24737316, ECO:0007744|PDB:3THC, FT ECO:0007744|PDB:3WF3" FT BINDING 333 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:22128166, FT ECO:0000269|PubMed:24737316, ECO:0007744|PDB:3THC, FT ECO:0007744|PDB:3WF3" FT CARBOHYD 26 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 247 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:22128166, FT ECO:0000269|PubMed:24737316, ECO:0007744|PDB:3THC, FT ECO:0007744|PDB:3THD, ECO:0007744|PDB:3WEZ, FT ECO:0007744|PDB:3WF0, ECO:0007744|PDB:3WF1, FT ECO:0007744|PDB:3WF2, ECO:0007744|PDB:3WF3, FT ECO:0007744|PDB:3WF4" FT CARBOHYD 464 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16263699, FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22128166, FT ECO:0000269|PubMed:24737316, ECO:0007744|PDB:3THC, FT ECO:0007744|PDB:3THD, ECO:0007744|PDB:3WEZ, FT ECO:0007744|PDB:3WF0, ECO:0007744|PDB:3WF1, FT ECO:0007744|PDB:3WF2, ECO:0007744|PDB:3WF3, FT ECO:0007744|PDB:3WF4" FT CARBOHYD 498 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:22128166, FT ECO:0000269|PubMed:24737316, ECO:0007744|PDB:3THC, FT ECO:0007744|PDB:3THD, ECO:0007744|PDB:3WEZ, FT ECO:0007744|PDB:3WF0, ECO:0007744|PDB:3WF1, FT ECO:0007744|PDB:3WF2, ECO:0007744|PDB:3WF3, FT ECO:0007744|PDB:3WF4" FT CARBOHYD 542 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 545 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 555 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:22128166, ECO:0000269|PubMed:24737316, FT ECO:0007744|PDB:3THC, ECO:0007744|PDB:3THD, FT ECO:0007744|PDB:3WEZ, ECO:0007744|PDB:3WF0, FT ECO:0007744|PDB:3WF1, ECO:0007744|PDB:3WF2, FT ECO:0007744|PDB:3WF3, ECO:0007744|PDB:3WF4" FT DISULFID 195..230 FT /evidence="ECO:0000269|PubMed:22128166, FT ECO:0000269|PubMed:24737316, ECO:0007744|PDB:3THC, FT ECO:0007744|PDB:3THD, ECO:0007744|PDB:3WEZ, FT ECO:0007744|PDB:3WF0, ECO:0007744|PDB:3WF1, FT ECO:0007744|PDB:3WF2, ECO:0007744|PDB:3WF3, FT ECO:0007744|PDB:3WF4" FT DISULFID 626..634 FT /evidence="ECO:0000269|PubMed:22128166, FT ECO:0000269|PubMed:24737316, ECO:0007744|PDB:3THC, FT ECO:0007744|PDB:3THD, ECO:0007744|PDB:3WEZ, FT ECO:0007744|PDB:3WF0, ECO:0007744|PDB:3WF1, FT ECO:0007744|PDB:3WF2, ECO:0007744|PDB:3WF3, FT ECO:0007744|PDB:3WF4" FT VAR_SEQ 1..30 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_039974" FT VAR_SEQ 83..244 FT /note="YVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVILRPGPYICAEWEMGG FT LPAWLLEKESILLRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPVITVQVENEYGSYF FT ACDFDYLRFLQKRFRHHLGDDVVLFTTDGAHKTFLKCGALQGLYTTVDFGT -> LPGS FT CGQVVGSPSAQDEASPLSEWRASYNSA (in isoform 2)" FT /evidence="ECO:0000303|PubMed:2511208" FT /id="VSP_031241" FT VARIANT 10 FT /note="P -> L (in dbSNP:rs7637099)" FT /evidence="ECO:0000269|PubMed:10338095, FT ECO:0000269|PubMed:11511921, ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15791924, FT ECO:0000269|PubMed:2111707, ECO:0000269|PubMed:2511208, FT ECO:0000269|Ref.5" FT /id="VAR_008671" FT VARIANT 49 FT /note="R -> C (in GM1G1 and GM1G2; decrease in FT galactosidase activity; dbSNP:rs72555358)" FT /evidence="ECO:0000269|PubMed:1909089, FT ECO:0000269|PubMed:25936995" FT /id="VAR_003329" FT VARIANT 49 FT /note="R -> H (in GM1G3; dbSNP:rs780523881)" FT /evidence="ECO:0000269|PubMed:15986423" FT /id="VAR_062340" FT VARIANT 51 FT /note="I -> T (in GM1G3; no effect on catalytic activity; FT decreased protein stability; dbSNP:rs72555390)" FT /evidence="ECO:0000269|PubMed:1907800, FT ECO:0000269|PubMed:1909089, ECO:0000269|PubMed:24737316" FT /id="VAR_003330" FT VARIANT 59 FT /note="R -> C (in GM1G1; loss of galactosidase activity; FT severe mutation; dbSNP:rs756878418)" FT /evidence="ECO:0000269|PubMed:15714521, FT ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:17309651" FT /id="VAR_026129" FT VARIANT 59 FT /note="R -> H (in GM1G1; with cardiac involvement in some FT patients; loss of galactosidase activity; severe mutation; FT dbSNP:rs72555392)" FT /evidence="ECO:0000269|PubMed:10338095, FT ECO:0000269|PubMed:10737981, ECO:0000269|PubMed:15714521, FT ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:17309651, FT ECO:0000269|PubMed:17664528, ECO:0000269|PubMed:19472408, FT ECO:0000269|Ref.31" FT /id="VAR_008672" FT VARIANT 68 FT /note="R -> Q (in GM1G2; 7.4% of wild-type galactosidase FT activity; dbSNP:rs572237881)" FT /evidence="ECO:0000269|PubMed:19472408" FT /id="VAR_062341" FT VARIANT 68 FT /note="R -> W (in GM1G2 and GM1G1; loss of galactosidase FT activity; dbSNP:rs72555370)" FT /evidence="ECO:0000269|PubMed:12644936, FT ECO:0000269|PubMed:25936995" FT /id="VAR_026130" FT VARIANT 73 FT /note="K -> E (in GM1G3)" FT /evidence="ECO:0000269|PubMed:15986423" FT /id="VAR_062342" FT VARIANT 82 FT /note="T -> M (in GM1G3; mild phenotype; dbSNP:rs72555393)" FT /evidence="ECO:0000269|PubMed:11511921, FT ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:8198123" FT /id="VAR_008673" FT VARIANT 83 FT /note="Y -> C (in MPS4B; decrease in galactosidase FT activity; dbSNP:rs1553612220)" FT /evidence="ECO:0000269|PubMed:16941474, FT ECO:0000269|PubMed:17664528" FT /id="VAR_062343" FT VARIANT 83 FT /note="Y -> H (in MPS4B; 2-5% of wild-type galactosidase FT activity; dbSNP:rs72555364)" FT /evidence="ECO:0000269|PubMed:7586649" FT /id="VAR_008674" FT VARIANT 109 FT /note="R -> W (in dbSNP:rs35289681)" FT /id="VAR_053875" FT VARIANT 121 FT /note="R -> S (in GM1G1; dbSNP:rs879050821)" FT /evidence="ECO:0000269|PubMed:10338095" FT /id="VAR_008675" FT VARIANT 123 FT /note="G -> R (in GM1G1; decrease in galactosidase FT activity; dbSNP:rs28934274)" FT /evidence="ECO:0000269|PubMed:1907800, FT ECO:0000269|PubMed:25936995" FT /id="VAR_003331" FT VARIANT 129 FT /note="E -> Q (in dbSNP:rs886042079)" FT /evidence="ECO:0000269|PubMed:25936995" FT /id="VAR_074054" FT VARIANT 132 FT /note="M -> T (in GM1G1; 4.3% of wild-type galactosidase FT activity; dbSNP:rs1553612189)" FT /evidence="ECO:0000269|PubMed:19472408" FT /id="VAR_062344" FT VARIANT 134 FT /note="G -> R (in GM1G2; uncertain significance)" FT /evidence="ECO:0000269|PubMed:25936995" FT /id="VAR_074055" FT VARIANT 134 FT /note="G -> V (in GM1G1; dbSNP:rs773562141)" FT /evidence="ECO:0000269|PubMed:17309651" FT /id="VAR_037937" FT VARIANT 136 FT /note="P -> S (in GM1G1; dbSNP:rs747305905)" FT /evidence="ECO:0000269|PubMed:16941474" FT /id="VAR_062345" FT VARIANT 147 FT /note="Missing (in GM1G1)" FT /evidence="ECO:0000269|PubMed:17309651" FT /id="VAR_037938" FT VARIANT 148 FT /note="R -> C (in GM1G3 and GM1G2; dbSNP:rs192732174)" FT /evidence="ECO:0000269|PubMed:15986423, FT ECO:0000269|PubMed:25936995" FT /id="VAR_062346" FT VARIANT 148 FT /note="R -> S (in GM1G1; dbSNP:rs192732174)" FT /evidence="ECO:0000269|PubMed:10839995, ECO:0000269|Ref.28" FT /id="VAR_013541" FT VARIANT 149 FT /note="S -> F (in MPS4B; 2.0% of wild-type galactosidase FT activity; dbSNP:rs778700089)" FT /evidence="ECO:0000269|PubMed:19472408" FT /id="VAR_062347" FT VARIANT 151 FT /note="D -> V (in GM1G1)" FT /evidence="ECO:0000269|PubMed:16941474" FT /id="VAR_062348" FT VARIANT 151 FT /note="D -> Y (in GM1G1; complete lack of protein; loss of FT galactosidase activity)" FT /evidence="ECO:0000269|PubMed:15365997, FT ECO:0000269|PubMed:15791924" FT /id="VAR_026131" FT VARIANT 155 FT /note="L -> R (in GM1G2 and GM1G3; 6.7% of wild-type FT galactosidase activity; dbSNP:rs376710410)" FT /evidence="ECO:0000269|PubMed:17309651, FT ECO:0000269|PubMed:19472408" FT /id="VAR_037939" FT VARIANT 162 FT /note="L -> S (in GM1G1; loss of galactosidase activity)" FT /evidence="ECO:0000269|PubMed:17309651, FT ECO:0000269|PubMed:17664528" FT /id="VAR_037940" FT VARIANT 173 FT /note="L -> P (in GM1G1; loss of galactosidase activity; FT dbSNP:rs397515617)" FT /evidence="ECO:0000269|PubMed:16941474, FT ECO:0000269|PubMed:17664528" FT /id="VAR_062349" FT VARIANT 184 FT /note="Q -> R (in GM1G1; loss of galactosidase activity)" FT /evidence="ECO:0000269|PubMed:19472408" FT /id="VAR_062350" FT VARIANT 190 FT /note="G -> D (in GM1G1; 3.4% of wild-type galactosidase FT activity; dbSNP:rs756575833)" FT /evidence="ECO:0000269|PubMed:19472408" FT /id="VAR_062351" FT VARIANT 198 FT /note="D -> Y (in MPS4B; 17.4% of wild-type galactosidase FT activity)" FT /evidence="ECO:0000269|PubMed:19472408" FT /id="VAR_062352" FT VARIANT 199 FT /note="Y -> C (in GM1G1)" FT /evidence="ECO:0000269|PubMed:16941474" FT /id="VAR_062353" FT VARIANT 201 FT /note="R -> C (in GM1G1 and GM1G2; no effect on intrinsic FT catalytic activity; decreased protein stability; 8.4% of FT wild-type galactosidase activity; activity severely reduced FT in transfection with variant F-436; dbSNP:rs72555360)" FT /evidence="ECO:0000269|PubMed:12644936, FT ECO:0000269|PubMed:16538002, ECO:0000269|PubMed:1907800, FT ECO:0000269|PubMed:1909089, ECO:0000269|PubMed:19472408, FT ECO:0000269|PubMed:24737316" FT /id="VAR_003332" FT VARIANT 201 FT /note="R -> H (in GM1G1 and GM1G2; also in a patient with a FT slowly progressive GM1-gangliosidosis form; 36.2% of FT wild-type galactosidase activity; dbSNP:rs189115557)" FT /evidence="ECO:0000269|PubMed:10737981, FT ECO:0000269|PubMed:15714521, ECO:0000269|PubMed:16538002, FT ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:17309651, FT ECO:0000269|PubMed:17664528, ECO:0000269|PubMed:19472408, FT ECO:0000269|PubMed:9203065" FT /id="VAR_013542" FT VARIANT 208 FT /note="R -> C (in GM1G1; dbSNP:rs72555366)" FT /evidence="ECO:0000269|PubMed:10338095, FT ECO:0000269|PubMed:15714521, ECO:0000269|PubMed:17309651, FT ECO:0000269|PubMed:8213816" FT /id="VAR_008676" FT VARIANT 214 FT /note="D -> Y (in GM1G3)" FT /evidence="ECO:0000269|Ref.28" FT /id="VAR_013543" FT VARIANT 216 FT /note="V -> A (in GM1G1; dbSNP:rs886042815)" FT /evidence="ECO:0000269|Ref.28" FT /id="VAR_013544" FT VARIANT 236 FT /note="L -> P (in GM1G1; decrease in galactosidase FT activity)" FT /evidence="ECO:0000269|PubMed:25936995" FT /id="VAR_074056" FT VARIANT 239 FT /note="T -> M (in GM1G1; loss of galactosidase activity; FT severe mutation; causes a rapid degradation of the protein FT precursor; dbSNP:rs746766232)" FT /evidence="ECO:0000269|PubMed:15714521, FT ECO:0000269|PubMed:19472408" FT /id="VAR_026132" FT VARIANT 240 FT /note="V -> M (in GM1G1)" FT /evidence="ECO:0000269|PubMed:10338095" FT /id="VAR_008677" FT VARIANT 255 FT /note="Q -> H (in GM1G1; 2.4% of wild-type galactosidase FT activity; dbSNP:rs1553610553)" FT /evidence="ECO:0000269|PubMed:19472408" FT /id="VAR_062354" FT VARIANT 262 FT /note="G -> E (in GM1G2; decrease in galactosidase FT activity; dbSNP:rs377174858)" FT /evidence="ECO:0000269|PubMed:25936995" FT /id="VAR_074057" FT VARIANT 263 FT /note="P -> S (in GM1G3)" FT /evidence="ECO:0000269|Ref.30" FT /id="VAR_013545" FT VARIANT 264 FT /note="L -> S (in GM1G2)" FT /evidence="ECO:0000269|PubMed:16941474" FT /id="VAR_062355" FT VARIANT 266 FT /note="N -> S (in GM1G3; dbSNP:rs1214295886)" FT /evidence="ECO:0000269|PubMed:9203065" FT /id="VAR_013546" FT VARIANT 270 FT /note="Y -> D (in GM1G3; originally classified as Morquio FT syndrome; dbSNP:rs376663785)" FT /evidence="ECO:0000269|PubMed:11511921, FT ECO:0000269|PubMed:19472408" FT /id="VAR_013547" FT VARIANT 272 FT /note="G -> D (in GM1G1)" FT /evidence="ECO:0000269|PubMed:16941474, FT ECO:0000269|PubMed:17309651" FT /id="VAR_038346" FT VARIANT 273 FT /note="W -> L (in MPS4B; decreased galactosidase activity; FT dbSNP:rs72555362)" FT /evidence="ECO:0000269|PubMed:11511921, FT ECO:0000269|PubMed:16538002, ECO:0000269|PubMed:1928092, FT ECO:0000269|PubMed:19472408" FT /id="VAR_003333" FT VARIANT 281 FT /note="H -> Y (in GM1G1 and GM1G3; dbSNP:rs745386663)" FT /evidence="ECO:0000269|PubMed:11511921, FT ECO:0000269|PubMed:15714521" FT /id="VAR_013548" FT VARIANT 297 FT /note="L -> F (in GM1G3; decrease in galactosidase FT activity)" FT /evidence="ECO:0000269|PubMed:25936995" FT /id="VAR_074058" FT VARIANT 314 FT /note="F -> L (in GM1G2; decrease in galactosidase FT activity)" FT /evidence="ECO:0000269|PubMed:25936995" FT /id="VAR_074059" FT VARIANT 316 FT /note="Y -> C (in GM1G1; dbSNP:rs72555361)" FT /evidence="ECO:0000269|PubMed:1907800" FT /id="VAR_003334" FT VARIANT 318 FT /note="N -> H (in GM1G1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:16538002" FT /id="VAR_062356" FT VARIANT 329 FT /note="T -> I (in GM1G1; 5.0% of wild-type galactosidase FT activity)" FT /evidence="ECO:0000269|PubMed:19472408" FT /id="VAR_062357" FT VARIANT 331 FT /note="Y -> C (in GM1G1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:25936995" FT /id="VAR_074060" FT VARIANT 332 FT /note="D -> E (in GM1G1; 2.3% of wild-type galactosidase FT activity)" FT /evidence="ECO:0000269|PubMed:19472408" FT /id="VAR_062358" FT VARIANT 332 FT /note="D -> N (in GM1G1; decrease in galactosidase FT activity; dbSNP:rs781658798)" FT /evidence="ECO:0000269|PubMed:10839995, FT ECO:0000269|PubMed:25936995" FT /id="VAR_013549" FT VARIANT 333 FT /note="Y -> H (in GM1G2; 3.0% of wild-type galactosidase FT activity; the mutant protein is localized in the FT lysosomal-endosomal compartment)" FT /evidence="ECO:0000269|PubMed:19472408" FT /id="VAR_062359" FT VARIANT 337 FT /note="L -> P (in GM1G1 and GM1G2; loss of galactosidase FT activity; dbSNP:rs752177002)" FT /evidence="ECO:0000269|PubMed:25936995" FT /id="VAR_074061" FT VARIANT 346 FT /note="K -> N (in GM1G1; dbSNP:rs749980306)" FT /evidence="ECO:0000269|PubMed:16941474, FT ECO:0000269|PubMed:19472408" FT /id="VAR_062360" FT VARIANT 347 FT /note="Y -> C (in GM1G1)" FT /evidence="ECO:0000269|PubMed:16941474" FT /id="VAR_062361" FT VARIANT 377..381 FT /note="Missing (in GM1G1)" FT /evidence="ECO:0000269|PubMed:17309651" FT /id="VAR_037941" FT VARIANT 397 FT /note="P -> A (in MPS4B; 24.0% of wild-type galactosidase FT activity)" FT /evidence="ECO:0000269|PubMed:19472408" FT /id="VAR_062362" FT VARIANT 408 FT /note="Q -> P (in MPS4B; 1.1% of wild-type galactosidase FT activity; dbSNP:rs72555369)" FT /evidence="ECO:0000269|PubMed:11511921, FT ECO:0000269|PubMed:19472408" FT /id="VAR_013550" FT VARIANT 414 FT /note="G -> V (in GM1G2; decrease in galactosidase FT activity)" FT /evidence="ECO:0000269|PubMed:25936995" FT /id="VAR_074062" FT VARIANT 420 FT /note="T -> K (in GM1G3; decrease in galactosidase FT activity)" FT /evidence="ECO:0000269|PubMed:16941474, FT ECO:0000269|PubMed:17664528" FT /id="VAR_062363" FT VARIANT 420 FT /note="T -> P (in GM1G1; loss of galactosidase activity; FT dbSNP:rs200181401)" FT /evidence="ECO:0000269|PubMed:16941474, FT ECO:0000269|PubMed:17664528" FT /id="VAR_062364" FT VARIANT 422 FT /note="L -> R (in GM1G1; dbSNP:rs758203004)" FT /evidence="ECO:0000269|PubMed:16941474" FT /id="VAR_062365" FT VARIANT 434 FT /note="S -> L (in GM1-gangliosidosis; unclassified clinical FT type; dbSNP:rs267599773)" FT /evidence="ECO:0000269|PubMed:17309651" FT /id="VAR_037942" FT VARIANT 436 FT /note="L -> F (seems to have a modulating action in the FT expression of the severity of other mutations; FT dbSNP:rs34421970)" FT /evidence="ECO:0000269|PubMed:12644936, FT ECO:0000269|PubMed:16941474" FT /id="VAR_026133" FT VARIANT 438 FT /note="G -> E (in GM1G3 and MPS4B; mild form; 5.7% of FT wild-type galactosidase activity; dbSNP:rs72555367)" FT /evidence="ECO:0000269|PubMed:12393180, FT ECO:0000269|PubMed:15986423, ECO:0000269|PubMed:19472408" FT /id="VAR_013551" FT VARIANT 441 FT /note="D -> N (in GM1G1; loss of galactosidase activity; FT dbSNP:rs780724173)" FT /evidence="ECO:0000269|PubMed:16941474, FT ECO:0000269|PubMed:17664528" FT /id="VAR_062366" FT VARIANT 442 FT /note="R -> Q (in GM1G1; dbSNP:rs564428355)" FT /evidence="ECO:0000269|PubMed:19472408" FT /id="VAR_062367" FT VARIANT 444 FT /note="Y -> C (in MPS4B; loss of galactosidase activity)" FT /evidence="ECO:0000269|PubMed:16941474, FT ECO:0000269|PubMed:17664528" FT /id="VAR_062368" FT VARIANT 457 FT /note="R -> Q (in GM1G3; dbSNP:rs28934886)" FT /evidence="ECO:0000269|PubMed:1907800" FT /id="VAR_003335" FT VARIANT 482 FT /note="R -> C (in MPS4B; loss of galactosidase activity; FT dbSNP:rs72555365)" FT /evidence="ECO:0000269|PubMed:7586649" FT /id="VAR_008678" FT VARIANT 482 FT /note="R -> H (in MPS4B and GM1G1; severe decrease in FT galactosidase activity; dbSNP:rs72555391)" FT /evidence="ECO:0000269|PubMed:10737981, FT ECO:0000269|PubMed:1487238, ECO:0000269|PubMed:15714521, FT ECO:0000269|PubMed:16538002, ECO:0000269|PubMed:1928092, FT ECO:0000269|PubMed:25936995" FT /id="VAR_003336" FT VARIANT 484 FT /note="N -> K (in MPS4B; mild form; fibroblasts from MPS4B FT compound heterozygotes for K-484 and A-500 have 1.9% of FT wild-type galactosidase activity; dbSNP:rs968221254)" FT /evidence="ECO:0000269|PubMed:12393180" FT /id="VAR_013552" FT VARIANT 491 FT /note="D -> N (in GM1G1; dbSNP:rs780232995)" FT /evidence="ECO:0000269|PubMed:10338095" FT /id="VAR_008679" FT VARIANT 491 FT /note="D -> Y (in GM1G1)" FT /evidence="ECO:0000269|PubMed:17309651" FT /id="VAR_037943" FT VARIANT 493 FT /note="K -> N (in GM1G2; decrease in galactosidase FT activity; dbSNP:rs1172435886)" FT /evidence="ECO:0000269|PubMed:25936995" FT /id="VAR_074063" FT VARIANT 494 FT /note="G -> C (in GM1G1; dbSNP:rs1312626201)" FT /evidence="ECO:0000269|PubMed:1928092" FT /id="VAR_013553" FT VARIANT 494 FT /note="G -> S (in MPS4B; loss of galactosidase activity)" FT /evidence="ECO:0000269|PubMed:16941474, FT ECO:0000269|PubMed:17664528" FT /id="VAR_062369" FT VARIANT 500 FT /note="T -> A (in MPS4B; mild form; 2.1% of wild-type FT galactosidase activity; dbSNP:rs72555368)" FT /evidence="ECO:0000269|PubMed:11511921, FT ECO:0000269|PubMed:12393180, ECO:0000269|PubMed:16941474, FT ECO:0000269|PubMed:19472408" FT /id="VAR_013554" FT VARIANT 509 FT /note="W -> C (in MPS4B; also in a patient with a slowly FT progressive form of GM1-gangliosidosis; loss of FT galactosidase activity; dbSNP:rs72555363)" FT /evidence="ECO:0000269|PubMed:16538002, FT ECO:0000269|PubMed:1928092, ECO:0000269|PubMed:9203065" FT /id="VAR_003337" FT VARIANT 514 FT /note="L -> P (in GM1G1; decrease in galactosidase FT activity)" FT /evidence="ECO:0000269|PubMed:25936995" FT /id="VAR_074064" FT VARIANT 521 FT /note="R -> C (in GM1G3; likely benign; galactosidase FT activity is reduced in homozygous patient fibroblasts to FT 30% of control values; has 25% of wild-type galactosidase FT activity when expressed in a heterologous system; FT dbSNP:rs4302331)" FT /evidence="ECO:0000269|PubMed:10338095, FT ECO:0000269|PubMed:15714521, ECO:0000269|PubMed:16641997, FT ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:17664528, FT ECO:0000269|PubMed:25936995" FT /id="VAR_008680" FT VARIANT 532 FT /note="S -> G (results in near-normal activity FT corresponding to 60%-100% of the wild-type depending on the FT expression system; dbSNP:rs73826339)" FT /evidence="ECO:0000269|PubMed:10338095, FT ECO:0000269|PubMed:10839995, ECO:0000269|PubMed:16941474, FT ECO:0000269|PubMed:17664528, ECO:0000269|Ref.28" FT /id="VAR_008681" FT VARIANT 549 FT /note="P -> L (in GM1G1; dbSNP:rs776327443)" FT /evidence="ECO:0000269|PubMed:17309651" FT /id="VAR_037944" FT VARIANT 554 FT /note="G -> E (in GM1-gangliosidosis; unclassified clinical FT type)" FT /evidence="ECO:0000269|PubMed:17309651" FT /id="VAR_037945" FT VARIANT 578 FT /note="K -> R (in GM1G1; dbSNP:rs371582179)" FT /evidence="ECO:0000269|PubMed:8213816" FT /id="VAR_008682" FT VARIANT 579 FT /note="G -> D (in GM1G1 and GM1G2; loss of galactosidase FT activity; severe mutation; dbSNP:rs746350513)" FT /evidence="ECO:0000269|PubMed:10737981, FT ECO:0000269|PubMed:15714521" FT /id="VAR_013555" FT VARIANT 590 FT /note="R -> C (in GM1G1; loss of galactosidase activity; FT dbSNP:rs794727165)" FT /evidence="ECO:0000269|PubMed:16941474, FT ECO:0000269|PubMed:17309651, ECO:0000269|PubMed:17664528" FT /id="VAR_037946" FT VARIANT 590 FT /note="R -> H (in GM1G2; dbSNP:rs398123351)" FT /evidence="ECO:0000269|PubMed:8213816" FT /id="VAR_008683" FT VARIANT 591 FT /note="Y -> C (in GM1G1; with cardiac involvement in some FT patients; loss of galactosidase activity; severe mutation; FT causes a rapid degradation of the protein precursor; FT dbSNP:rs72555371)" FT /evidence="ECO:0000269|PubMed:10737981, FT ECO:0000269|PubMed:15714521, ECO:0000269|Ref.31" FT /id="VAR_008684" FT VARIANT 591 FT /note="Y -> N (in GM1G1; with cardiac involvement in some FT patients; loss of galactosidase activity; severe mutation; FT causes a rapid degradation of the protein precursor; FT dbSNP:rs72555373)" FT /evidence="ECO:0000269|PubMed:10737981, FT ECO:0000269|PubMed:15714521, ECO:0000269|Ref.31" FT /id="VAR_008685" FT VARIANT 595 FT /note="R -> W (reduction of galactosidase activity; FT dbSNP:rs201807974)" FT /evidence="ECO:0000269|PubMed:17661814" FT /id="VAR_037947" FT VARIANT 597 FT /note="P -> L (in GM1G2; decrease in galactosidase FT activity)" FT /evidence="ECO:0000269|PubMed:25936995" FT /id="VAR_074065" FT VARIANT 597 FT /note="P -> S (in GM1G1; 2.1% of wild-type galactosidase FT activity)" FT /evidence="ECO:0000269|PubMed:19472408" FT /id="VAR_062370" FT VARIANT 600 FT /note="T -> I (in GM1G2; decrease in galactosidase FT activity)" FT /evidence="ECO:0000269|PubMed:25936995" FT /id="VAR_074066" FT VARIANT 632 FT /note="E -> G (in GM1G2)" FT /evidence="ECO:0000269|PubMed:8213816" FT /id="VAR_008686" FT CONFLICT 89 FT /note="H -> Y (in Ref. 4; BAH13196)" FT /evidence="ECO:0000305" FT CONFLICT 201 FT /note="R -> A (in Ref. 1; AAA51822)" FT /evidence="ECO:0000305" FT STRAND 32..35 FT /evidence="ECO:0007829|PDB:3THD" FT TURN 36..39 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 40..43 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 51..54 FT /evidence="ECO:0007829|PDB:3THD" FT HELIX 57..59 FT /evidence="ECO:0007829|PDB:3THD" FT HELIX 62..64 FT /evidence="ECO:0007829|PDB:3THD" FT HELIX 65..74 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 78..83 FT /evidence="ECO:0007829|PDB:3THD" FT HELIX 86..89 FT /evidence="ECO:0007829|PDB:3THD" FT HELIX 100..102 FT /evidence="ECO:0007829|PDB:3THD" FT HELIX 104..113 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 117..121 FT /evidence="ECO:0007829|PDB:3THD" FT HELIX 131..134 FT /evidence="ECO:0007829|PDB:3THD" FT HELIX 137..141 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 147..149 FT /evidence="ECO:0007829|PDB:3THD" FT HELIX 152..169 FT /evidence="ECO:0007829|PDB:3THD" FT HELIX 170..172 FT /evidence="ECO:0007829|PDB:3THD" FT HELIX 174..176 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 178..184 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 186..188 FT /evidence="ECO:0007829|PDB:3WF0" FT HELIX 189..191 FT /evidence="ECO:0007829|PDB:3THD" FT HELIX 197..211 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 213..224 FT /evidence="ECO:0007829|PDB:3THD" FT HELIX 225..231 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 236..241 FT /evidence="ECO:0007829|PDB:3THD" FT HELIX 248..258 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 260..262 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 265..272 FT /evidence="ECO:0007829|PDB:3THD" FT HELIX 286..298 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 302..306 FT /evidence="ECO:0007829|PDB:3THD" FT TURN 322..324 FT /evidence="ECO:0007829|PDB:3THD" FT HELIX 345..354 FT /evidence="ECO:0007829|PDB:3THD" FT TURN 355..357 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 375..378 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 380..384 FT /evidence="ECO:0007829|PDB:3THD" FT TURN 385..388 FT /evidence="ECO:0007829|PDB:3THD" FT HELIX 389..392 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 398..402 FT /evidence="ECO:0007829|PDB:3THD" FT HELIX 407..409 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 413..421 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 426..433 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 439..447 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 450..456 FT /evidence="ECO:0007829|PDB:3THD" FT TURN 457..459 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 462..467 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 472..478 FT /evidence="ECO:0007829|PDB:3THD" FT HELIX 487..489 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 509..513 FT /evidence="ECO:0007829|PDB:3THD" FT HELIX 516..521 FT /evidence="ECO:0007829|PDB:3THD" FT TURN 522..527 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 550..556 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 568..572 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 578..583 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 586..591 FT /evidence="ECO:0007829|PDB:3THD" FT TURN 593..595 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 601..603 FT /evidence="ECO:0007829|PDB:3THD" FT HELIX 605..607 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 610..612 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 614..622 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 627..629 FT /evidence="ECO:0007829|PDB:3THD" FT HELIX 631..633 FT /evidence="ECO:0007829|PDB:3THD" FT STRAND 634..641 FT /evidence="ECO:0007829|PDB:3THD" SQ SEQUENCE 677 AA; 76075 MW; 74421586B1BCFECA CRC64; MPGFLVRILP LLLVLLLLGP TRGLRNATQR MFEIDYSRDS FLKDGQPFRY ISGSIHYSRV PRFYWKDRLL KMKMAGLNAI QTYVPWNFHE PWPGQYQFSE DHDVEYFLRL AHELGLLVIL RPGPYICAEW EMGGLPAWLL EKESILLRSS DPDYLAAVDK WLGVLLPKMK PLLYQNGGPV ITVQVENEYG SYFACDFDYL RFLQKRFRHH LGDDVVLFTT DGAHKTFLKC GALQGLYTTV DFGTGSNITD AFLSQRKCEP KGPLINSEFY TGWLDHWGQP HSTIKTEAVA SSLYDILARG ASVNLYMFIG GTNFAYWNGA NSPYAAQPTS YDYDAPLSEA GDLTEKYFAL RNIIQKFEKV PEGPIPPSTP KFAYGKVTLE KLKTVGAALD ILCPSGPIKS LYPLTFIQVK QHYGFVLYRT TLPQDCSNPA PLSSPLNGVH DRAYVAVDGI PQGVLERNNV ITLNITGKAG ATLDLLVENM GRVNYGAYIN DFKGLVSNLT LSSNILTDWT IFPLDTEDAV RSHLGGWGHR DSGHHDEAWA HNSSNYTLPA FYMGNFSIPS GIPDLPQDTF IQFPGWTKGQ VWINGFNLGR YWPARGPQLT LFVPQHILMT SAPNTITVLE LEWAPCSSDD PELCAVTFVD RPVIGSSVTY DHPSKPVEKR LMPPPPQKNK DSWLDHV //