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Database: UniProt
Entry: P04062
LinkDB: P04062
Original site: P04062 
ID   GLCM_HUMAN              Reviewed;         536 AA.
AC   P04062; A8K796; B7Z5G2; B7Z6S1; J3KQG4; J3KQK9; Q16545; Q4VX22;
AC   Q6I9R6; Q9UMJ8;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   09-NOV-2004, sequence version 3.
DT   20-JUN-2018, entry version 230.
DE   RecName: Full=Glucosylceramidase;
DE            EC=3.2.1.45;
DE   AltName: Full=Acid beta-glucosidase;
DE   AltName: Full=Alglucerase;
DE   AltName: Full=Beta-glucocerebrosidase;
DE            Short=Beta-GC;
DE   AltName: Full=D-glucosyl-N-acylsphingosine glucohydrolase;
DE   AltName: Full=Imiglucerase;
DE   Flags: Precursor;
GN   Name=GBA; Synonyms=GC, GLUC;
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 SHORT).
RC   TISSUE=Placenta;
RX   PubMed=3864160; DOI=10.1073/pnas.82.21.7289;
RA   Sorge J., West C., Westwood B., Beutler E.;
RT   "Molecular cloning and nucleotide sequence of human glucocerebrosidase
RT   cDNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:7289-7293(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND VARIANT LEU-298.
RC   TISSUE=Hepatoma;
RX   PubMed=3001061;
RA   Tsuji S., Choudary P.V., Martin B.M., Winfield S., Barranger J.A.,
RA   Ginns E.I.;
RT   "Nucleotide sequence of cDNA containing the complete coding sequence
RT   for human lysosomal glucocerebrosidase.";
RL   J. Biol. Chem. 261:50-53(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=2914709; DOI=10.1016/0888-7543(89)90319-4;
RA   Horowitz M., Wilder S., Horowitz Z., Reiner O., Gelbart T.,
RA   Beutler E.;
RT   "The human glucocerebrosidase gene and pseudogene: structure and
RT   evolution.";
RL   Genomics 4:87-96(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=1572652; DOI=10.1016/0888-7543(92)90311-F;
RA   Beutler E., West C., Gelbart T.;
RT   "Polymorphisms in the human glucocerebrosidase gene.";
RL   Genomics 12:795-800(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND 3), VARIANTS GD ARG-223;
RP   GLY-230; PRO-235; ARG-241; ILE-252 AND ARG-364, AND VARIANTS GLY-310
RP   AND HIS-368.
RX   PubMed=8294033; DOI=10.1016/0378-1119(93)90497-Q;
RA   Imai K., Nakamura M., Yamada M., Asano A., Yokoyama S., Tsuji S.,
RA   Ginns E.I.;
RT   "A novel transcript from a pseudogene for human glucocerebrosidase in
RT   non-Gaucher disease cells.";
RL   Gene 136:365-368(1993).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9331372;
RA   Winfield S.L., Tayebi N., Martin B.M., Ginns E.I., Sidransky E.;
RT   "Identification of three additional genes contiguous to the
RT   glucocerebrosidase locus on chromosome 1q21: implications for Gaucher
RT   disease.";
RL   Genome Res. 7:1020-1026(1997).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG; 4 AND 5), AND
RP   VARIANT MET-408.
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC   TISSUE=Placenta;
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   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-11.
RX   PubMed=3359914; DOI=10.1089/dna.1988.7.107;
RA   Reiner O., Wigderson M., Horowitz M.;
RT   "Structural analysis of the human glucocerebrosidase genes.";
RL   DNA 7:107-116(1988).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
RX   PubMed=3687939;
RA   Sorge J.A., West C., Kuhl W., Treger L., Beutler E.;
RT   "The human glucocerebrosidase gene has two functional ATG initiator
RT   codons.";
RL   Am. J. Hum. Genet. 41:1016-1024(1987).
RN   [12]
RP   PROTEIN SEQUENCE OF 40-44.
RC   TISSUE=Placenta;
RA   Martin B.M., Murray G.J., Coligan J.E., Raum M., Brady R.O.,
RA   Barranger J.A.;
RT   "Structural studies of human placental glucocerebrosidase.";
RL   Fed. Proc. 43:1869-1869(1984).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 403-416.
RX   PubMed=6091633; DOI=10.1016/0006-291X(84)90268-7;
RA   Ginns E.I., Choudary P.V., Martin B.M., Winfield S., Stubblefield B.,
RA   Mayor J., Merkle-Lehman D., Murray G.J., Bowers L.A., Barranger J.A.;
RT   "Isolation of cDNA clones for human beta-glucocerebrosidase using the
RT   lambda gt11 expression system.";
RL   Biochem. Biophys. Res. Commun. 123:574-580(1984).
RN   [14]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 409-462, AND VARIANT GD1 SER-409.
RC   TISSUE=Skin;
RA   Tsuji S., Martin B.M., Barranger J.A., Stubblefield B.K.,
RA   LaMarca M.E., Ginns E.I.;
RT   "Genetic heterogeneity in type 1 Gaucher disease: multiple genotypes
RT   in Ashkenazic and non-Ashkenazic individuals.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:2349-2352(1988).
RN   [15]
RP   PROTEIN SEQUENCE OF 469-520.
RC   TISSUE=Placenta;
RX   PubMed=3456607; DOI=10.1073/pnas.83.6.1660;
RA   Dinur T., Osiecki K.M., Legler G., Gatt S., Desnick R.J.,
RA   Grabowski G.A.;
RT   "Human acid beta-glucosidase: isolation and amino acid sequence of a
RT   peptide containing the catalytic site.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:1660-1664(1986).
RN   [16]
RP   MUTAGENESIS OF GLU-379, ACTIVE SITE, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=7908905;
RA   Miao S., McCarter J.D., Grace M.E., Grabowski G.A., Aebersold R.,
RA   Withers S.G.;
RT   "Identification of Glu340 as the active-site nucleophile in human
RT   glucocerebrosidase by use of electrospray tandem mass spectrometry.";
RL   J. Biol. Chem. 269:10975-10978(1994).
RN   [17]
RP   INTERACTION WITH SAPOSIN-C AND MEMBRANES CONTAINING ANIONIC
RP   PHOSPHOLIPIDS.
RX   PubMed=10781797; DOI=10.1016/S0014-5793(00)01417-4;
RA   Salvioli R., Tatti M., Ciaffoni F., Vaccaro A.M.;
RT   "Further studies on the reconstitution of glucosylceramidase activity
RT   by Sap C and anionic phospholipids.";
RL   FEBS Lett. 472:17-21(2000).
RN   [18]
RP   GLYCOSYLATION AT ASN-98; ASN-185 AND ASN-309.
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   [19]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH SCARB2.
RX   PubMed=18022370; DOI=10.1016/j.cell.2007.10.018;
RA   Reczek D., Schwake M., Schroder J., Hughes H., Blanz J., Jin X.,
RA   Brondyk W., Van Patten S., Edmunds T., Saftig P.;
RT   "LIMP-2 is a receptor for lysosomal mannose-6-phosphate-independent
RT   targeting of beta-glucocerebrosidase.";
RL   Cell 131:770-783(2007).
RN   [20]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Placenta;
RX   PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA   Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B.,
RA   Schaefer H., Elsaesser H.-P., Mann M., Hasilik A.;
RT   "Integral and associated lysosomal membrane proteins.";
RL   Traffic 8:1676-1686(2007).
RN   [21]
RP   INVOLVEMENT IN PARKINSON DISEASE, AND VARIANTS GLU-46; CYS-170;
RP   GLU-232; GLN-296; SER-409; ALA-419; HIS-448; ASN-482; PRO-483;
RP   PRO-495; LEU-497 AND CYS-502.
RX   PubMed=19286695; DOI=10.1093/brain/awp044;
RA   Neumann J., Bras J., Deas E., O'Sullivan S.S., Parkkinen L.,
RA   Lachmann R.H., Li A., Holton J., Guerreiro R., Paudel R., Segarane B.,
RA   Singleton A., Lees A., Hardy J., Houlden H., Revesz T., Wood N.W.;
RT   "Glucocerebrosidase mutations in clinical and pathologically proven
RT   Parkinson's disease.";
RL   Brain 132:1783-1794(2009).
RN   [22]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98 AND ASN-309.
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   [23]
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.,
RA   Buerckstuemmer T., 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   [24]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 40-536, GLYCOSYLATION AT
RP   ASN-58, AND DISULFIDE BONDS.
RX   PubMed=12792654; DOI=10.1038/sj.embor.embor873;
RA   Dvir H., Harel M., McCarthy A.A., Toker L., Silman I., Futerman A.H.,
RA   Sussman J.L.;
RT   "X-ray structure of human acid-beta-glucosidase, the defective enzyme
RT   in Gaucher disease.";
RL   EMBO Rep. 4:704-709(2003).
RN   [25]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 40-536 IN COMPLEX WITH
RP   SYNTHETIC INHIBITOR, AND ACTIVE SITE.
RX   PubMed=15817452; DOI=10.1074/jbc.M502799200;
RA   Premkumar L., Sawkar A.R., Boldin-Adamsky S., Toker L., Silman I.,
RA   Kelly J.W., Futerman A.H., Sussman J.L.;
RT   "X-ray structure of human acid-beta-glucosidase covalently bound to
RT   conduritol-B-epoxide. Implications for Gaucher disease.";
RL   J. Biol. Chem. 280:23815-23819(2005).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 40-536, CHARACTERIZATION OF
RP   VARIANTS GD SER-55; GLN-87; ASN-118; GLN-159; LEU-161; VAL-162;
RP   VAL-166; ASN-200; PHE-213; PHE-224; GLU-232; GLU-237; LEU-298;
RP   ILE-303; CYS-343; ILE-362; LYS-365; GLY-381; LYS-388; TRP-392;
RP   CYS-402; SER-409; VAL-410; HIS-419; LYS-421; ARG-429; LEU-433;
RP   SER-436; ASN-438; HIS-448; VAL-455; PRO-483; PRO-500 AND PRO-502, AND
RP   MUTAGENESIS OF CYS-43; CYS-57 AND CYS-62.
RX   PubMed=16293621; DOI=10.1074/jbc.M511110200;
RA   Liou B., Kazimierczuk A., Zhang M., Scott C.R., Hegde R.S.,
RA   Grabowski G.A.;
RT   "Analyses of variant acid beta-glucosidases: effects of Gaucher
RT   disease mutations.";
RL   J. Biol. Chem. 281:4242-4253(2006).
RN   [27]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 40-536, AND GLYCOSYLATION AT
RP   ASN-58; ASN-98 AND ASN-185.
RX   PubMed=17139081; DOI=10.1107/S0907444906038303;
RA   Brumshtein B., Wormald M.R., Silman I., Futerman A.H., Sussman J.L.;
RT   "Structural comparison of differently glycosylated forms of acid-beta-
RT   glucosidase, the defective enzyme in Gaucher disease.";
RL   Acta Crystallogr. D 62:1458-1465(2006).
RN   [28]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 40-536 IN COMPLEXES WITH
RP   ISOFAGOMINE, AND SUBCELLULAR LOCATION.
RX   PubMed=17187079; DOI=10.1038/nchembio850;
RA   Lieberman R.L., Wustman B.A., Huertas P., Powe A.C. Jr., Pine C.W.,
RA   Khanna R., Schlossmacher M.G., Ringe D., Petsko G.A.;
RT   "Structure of acid beta-glucosidase with pharmacological chaperone
RT   provides insight into Gaucher disease.";
RL   Nat. Chem. Biol. 3:101-107(2007).
RN   [29]
RP   REVIEW ON GD VARIANTS.
RX   PubMed=8118460; DOI=10.1002/humu.1380030102;
RA   Horowitz M., Zimran A.;
RT   "Mutations causing Gaucher disease.";
RL   Hum. Mutat. 3:1-11(1994).
RN   [30]
RP   REVIEW ON GD VARIANTS.
RX   PubMed=8889578;
RX   DOI=10.1002/(SICI)1098-1004(1996)8:3<207::AID-HUMU2>3.3.CO;2-5;
RA   Beutler E., Gelbart T.;
RT   "Glucocerebrosidase (Gaucher disease).";
RL   Hum. Mutat. 8:207-213(1996).
RN   [31]
RP   REVIEW ON GD VARIANTS.
RX   PubMed=10527671; DOI=10.1006/mgme.1999.2918;
RA   Tayebi N., Stone D.L., Sidransky E.;
RT   "Type 2 Gaucher disease: an expanding phenotype.";
RL   Mol. Genet. Metab. 68:209-219(1999).
RN   [32]
RP   REVIEW ON GD VARIANTS.
RX   PubMed=10649495;
RX   DOI=10.1002/(SICI)1098-1004(200002)15:2<181::AID-HUMU7>3.3.CO;2-J;
RA   Stone D.L., Tayebi N., Orvisky E., Stubblefield B., Madike V.,
RA   Sidransky E.;
RT   "Glucocerebrosidase gene mutations in patients with type 2 Gaucher
RT   disease.";
RL   Hum. Mutat. 15:181-188(2000).
RN   [33]
RP   VARIANT GD TYR-255.
RX   PubMed=1974409; DOI=10.1111/j.1469-1809.1990.tb00371.x;
RA   Beutler E., Gelbart T.;
RT   "Gaucher disease associated with a unique KpnI restriction site:
RT   identification of the amino-acid substitution.";
RL   Ann. Hum. Genet. 54:149-153(1990).
RN   [34]
RP   VARIANT GD CYS-502, AND CHARACTERIZATION OF VARIANT GD CYS-502.
RX   PubMed=1972019; DOI=10.1089/dna.1990.9.233;
RA   Hong C.M., Ohashi T., Yu X.J., Weiler S., Barranger J.A.;
RT   "Sequence of two alleles responsible for Gaucher disease.";
RL   DNA Cell Biol. 9:233-241(1990).
RN   [35]
RP   VARIANTS GD.
RX   PubMed=8432537; DOI=10.1006/geno.1993.1035;
RA   Beutler E., Gelbart T., West C.;
RT   "Identification of six new Gaucher disease mutations.";
RL   Genomics 15:203-205(1993).
RN   [36]
RP   VARIANT GD HIS-535.
RX   PubMed=7916532; DOI=10.1002/ajmg.1320510216;
RA   Choy F.Y.M., Wei C., Applegarth D.A., McGillivray B.C.;
RT   "DNA analysis of an uncommon missense mutation in a Gaucher disease
RT   patient of Jewish-Polish-Russian descent.";
RL   Am. J. Med. Genet. 51:156-160(1994).
RN   [37]
RP   VARIANT GD ASN-438.
RX   PubMed=8112750; DOI=10.1007/BF00210614;
RA   Beutler E., Gelbart T.;
RT   "Two new Gaucher disease mutations.";
RL   Hum. Genet. 93:209-210(1994).
RN   [38]
RP   VARIANTS GD SER-409 AND CYS-457.
RX   PubMed=8076951; DOI=10.1007/BF00208292;
RA   Tuteja R., Tuteja N., Lilliu F., Bembi B., Galanello R., Cao A.,
RA   Baralle F.E.;
RT   "Y418C: a novel mutation in exon 9 of the glucocerebrosidase gene of a
RT   patient with Gaucher disease creates a new Bgl I site.";
RL   Hum. Genet. 94:314-315(1994).
RN   [39]
RP   VARIANTS GD ASP-215; THR-221; ARG-241; GLN-296; CYS-324; GLY-417 AND
RP   ASN-419.
RX   PubMed=8790604;
RA   Beutler E., Demina A., Gelbart T.;
RT   "Glucocerebrosidase mutations in Gaucher disease.";
RL   Mol. Med. 1:82-92(1994).
RN   [40]
RP   VARIANTS GD SER-409; HIS-448; PRO-483 AND CYS-502.
RX   PubMed=7627184; DOI=10.1002/humu.1380050406;
RA   Cormand B., Vilageliu L., Burguera J.M., Balcells S.,
RA   Gonzalez-Duarte R., Grinberg D., Chabas A.;
RT   "Gaucher disease in Spanish patients: analysis of eight mutations.";
RL   Hum. Mutat. 5:303-309(1995).
RN   [41]
RP   VARIANT GD SER-217.
RX   PubMed=7627192; DOI=10.1002/humu.1380050414;
RA   Choy F.Y.M., Wei C.;
RT   "Identification of a new mutation (P178S) in an African-American
RT   patient with type 2 Gaucher disease.";
RL   Hum. Mutat. 5:345-347(1995).
RN   [42]
RP   VARIANTS GD SER-409; LEU-426; LEU-433 AND PRO-483.
RX   PubMed=8937765;
RA   Morar B., Lane A.B.;
RT   "The molecular characterization of Gaucher disease in South Africa.";
RL   Clin. Genet. 50:78-84(1996).
RN   [43]
RP   VARIANTS GD LEU-54; GLU-85 AND SER-227.
RX   PubMed=8829654;
RX   DOI=10.1002/(SICI)1098-1004(1996)7:3<214::AID-HUMU5>3.0.CO;2-A;
RA   Kim J.-W., Liou B.B., Lai M.-Y., Ponce E., Grabowski G.A.;
RT   "Gaucher disease: identification of three new mutations in the Korean
RT   and Chinese (Taiwanese) populations.";
RL   Hum. Mutat. 7:214-218(1996).
RN   [44]
RP   VARIANTS GD HIS-352 AND GLN-398.
RX   PubMed=8829663;
RX   DOI=10.1002/(SICI)1098-1004(1996)7:3<272::AID-HUMU14>3.3.CO;2-7;
RA   Cormand B., Vilageliu L., Balcells S., Gonzalez-Duatre R., Chabas A.,
RA   Grinberg D.;
RT   "Two novel (1098insA and Y313H) and one rare (R359Q) mutations
RT   detected in exon 8 of the beta-glucocerebrosidase gene in Gaucher's
RT   disease patients.";
RL   Hum. Mutat. 7:272-274(1996).
RN   [45]
RP   VARIANT GD1 THR-435.
RX   PubMed=8889591;
RX   DOI=10.1002/(SICI)1098-1004(1996)8:3<280::AID-HUMU15>3.3.CO;2-6;
RA   Amaral O., Pinto E., Fortuna M., Lacerda L., Sa Miranda M.C.;
RT   "Type 1 Gaucher disease: identification of N396T and prevalence of
RT   glucocerebrosidase mutations in the Portuguese.";
RL   Hum. Mutat. 8:280-281(1996).
RN   [46]
RP   VARIANTS GD3 LEU-437 AND ILE-530.
RX   PubMed=8780099; DOI=10.1212/WNL.46.4.1102;
RA   Seeman P.J.V., Finckh U., Hoeppner J., Lakner V., Liebisch I.,
RA   Grau G., Rolfs A.;
RT   "Two new missense mutations in a non-Jewish Caucasian family with type
RT   3 Gaucher disease.";
RL   Neurology 46:1102-1107(1996).
RN   [47]
RP   VARIANTS GD LEU-414 AND THR-441.
RX   PubMed=9182788;
RX   DOI=10.1002/(SICI)1096-8628(19970627)70:4<437::AID-AJMG19>3.0.CO;2-I;
RA   Cormand B., Grinberg D., Gort L., Fiumara A., Barone R., Vilageliu L.,
RA   Chabas A.;
RT   "Two new mild homozygous mutations in Gaucher disease patients:
RT   clinical signs and biochemical analyses.";
RL   Am. J. Med. Genet. 70:437-443(1997).
RN   [48]
RP   VARIANTS GD VAL-76; GLU-85; TRP-87; TRP-159; SER-227; ILE-252 AND
RP   PRO-483.
RX   PubMed=9217217;
RX   DOI=10.1002/(SICI)1096-8628(19970808)71:2<172::AID-AJMG10>3.0.CO;2-B;
RA   Choy F.Y.M., Humphries M.L., Shi H.;
RT   "Identification of two novel and four uncommon missense mutations
RT   among Chinese Gaucher disease patients.";
RL   Am. J. Med. Genet. 71:172-178(1997).
RN   [49]
RP   VARIANT GD LYS-501.
RX   PubMed=9279145; DOI=10.1136/adc.77.1.17;
RA   Hatton C.E., Cooper A., Whitehouse C., Wraith J.E.;
RT   "Mutation analysis in 46 British and Irish patients with Gaucher's
RT   disease.";
RL   Arch. Dis. Child. 77:17-22(1997).
RN   [50]
RP   VARIANTS GD TRP-87; GLU-234; ARG-241; ILE-252; ASN-310; LEU-391 AND
RP   SER-409.
RX   PubMed=9153297; DOI=10.1172/JCI119437;
RA   Grace M.E., Desnick R.J., Pastores G.M.;
RT   "Identification and expression of acid beta-glucosidase mutations
RT   causing severe type 1 and neurologic type 2 Gaucher disease in non-
RT   Jewish patients.";
RL   J. Clin. Invest. 99:2530-2537(1997).
RN   [51]
RP   VARIANTS GD VAL-228; ILE-252; GLY-405; HIS-448; GLN-452; PRO-483 AND
RP   CYS-535.
RX   PubMed=9061570; DOI=10.1023/A:1005313724361;
RA   Ida H., Rennert O.M., Kawame H., Maekawa K., Eto Y.;
RT   "Mutation prevalence among 47 unrelated Japanese patients with Gaucher
RT   disease: identification of four novel mutations.";
RL   J. Inherit. Metab. Dis. 20:67-73(1997).
RN   [52]
RP   VARIANT PSEUDO-GAUCHER HIS-448.
RX   PubMed=9040001; DOI=10.1136/jmg.34.2.175;
RA   Uyama E., Uchino M., Ida H., Eto Y., Owada M.;
RT   "D409H/D409H genotype in Gaucher-like disease.";
RL   J. Med. Genet. 34:175-175(1997).
RN   [53]
RP   VARIANTS GD LEU-146; LEU-198; THR-380; ASN-405 AND ARG-432.
RX   PubMed=9554454; DOI=10.1159/000040815;
RA   Demina A., Beutler E.;
RT   "Six new Gaucher disease mutations.";
RL   Acta Haematol. 99:80-82(1998).
RN   [54]
RP   VARIANTS GD.
RX   PubMed=9683600; DOI=10.1086/301969;
RA   Germain D.P., Puech J.-P., Caillaud C., Kahn A., Poenaru L.;
RT   "Exhaustive screening of the acid beta-glucosidase gene, by
RT   fluorescence-assisted mismatch analysis using universal primers:
RT   mutation profile and genotype/phenotype correlations in Gaucher
RT   disease.";
RL   Am. J. Hum. Genet. 63:415-427(1998).
RN   [55]
RP   VARIANT GD2 TYR-513.
RX   PubMed=9637431;
RX   DOI=10.1002/(SICI)1096-8628(19980616)78:1<92::AID-AJMG19>3.0.CO;2-J;
RA   Choy F.Y.M., Humphries M.L., Ben-Yoseph Y.;
RT   "Gaucher type 2 disease: identification of a novel transversion
RT   mutation in a French-Irish patient.";
RL   Am. J. Med. Genet. 78:92-93(1998).
RN   [56]
RP   VARIANTS GD.
RX   PubMed=9516376; DOI=10.1006/bcmd.1998.0165;
RA   Beutler E., Gelbart T.;
RT   "Hematologically important mutations: Gaucher disease.";
RL   Blood Cells Mol. Dis. 24:2-8(1998).
RN   [57]
RP   VARIANTS GD2 LYS-80; CYS-170 AND PRO-483.
RX   PubMed=9851895; DOI=10.1006/bcmd.1998.0210;
RA   Sinclair G., Choy F.Y.M., Humphries L.;
RT   "A novel complex allele and two new point mutations in type 2 (acute
RT   neuronopathic) Gaucher disease.";
RL   Blood Cells Mol. Dis. 24:420-427(1998).
RN   [58]
RP   VARIANT GD GLY-392.
RX   PubMed=9650766;
RA   Parenti G., Filocamo M., Titomanlio L., Rizzolo G., Silvestro E.,
RA   Perretti A., Gatti R., Andria G.;
RT   "A novel mutation of the beta-glucocerebrosidase gene associated with
RT   neurologic manifestations in three sibs.";
RL   Clin. Genet. 53:281-285(1998).
RN   [59]
RP   VARIANTS GD GLU-152; PRO-173; GLU-428; LEU-430; ILE-431 AND HIS-451.
RX   PubMed=9554746;
RX   DOI=10.1002/(SICI)1098-1004(1998)11:4<295::AID-HUMU7>3.0.CO;2-6;
RA   Cormand B., Grinberg D., Gort L., Chabas A., Vilageliu L.;
RT   "Molecular analysis and clinical findings in the Spanish Gaucher
RT   disease population: putative haplotype of the N370S ancestral
RT   chromosome.";
RL   Hum. Mutat. 11:295-305(1998).
RN   [60]
RP   VARIANTS GD1 GLY-230 AND SER-409.
RX   PubMed=10206680;
RX   DOI=10.1002/(SICI)1098-1004(1998)11:5<411::AID-HUMU13>3.0.CO;2-X;
RA   Choy F.Y.M., Humphries M.L., Ben-Yoseph Y.;
RT   "A novel mutation (V191G) in a German-British type 1 Gaucher disease
RT   patient.";
RL   Hum. Mutat. 11:411-412(1998).
RN   [61]
RP   VARIANTS GD1 SER-409 AND LEU-440.
RX   PubMed=10340647;
RX   DOI=10.1002/(SICI)1096-8628(19990604)84:4<334::AID-AJMG5>3.3.CO;2-G;
RA   Wasserstein M.P., Martignetti J.A., Zeitlin R., Lumerman H.,
RA   Solomon M., Grace M.E., Desnick R.J.;
RT   "Type 1 Gaucher disease presenting with extensive mandibular lytic
RT   lesions: identification and expression of a novel acid beta-
RT   glucosidase mutation.";
RL   Am. J. Med. Genet. 84:334-339(1999).
RN   [62]
RP   VARIANTS GD ARG-241; CYS-244; ILE-252; HIS-448 AND PRO-483.
RX   PubMed=10360404;
RX   DOI=10.1002/(SICI)1096-8628(19990611)84:5<484::AID-AJMG14>3.0.CO;2-W;
RA   Choy F.Y.M., Wong K., Shi H.P.;
RT   "Glucocerebrosidase mutations among Chinese neuronopathic and non-
RT   neuronopathic Gaucher disease patients.";
RL   Am. J. Med. Genet. 84:484-486(1999).
RN   [63]
RP   VARIANTS GD.
RX   PubMed=10744424;
RA   Hodanov K., Hrebicek M., Cervenkov M., Mrzov L., Veprekov L.,
RA   Zemen J.;
RT   "Analysis of the beta-glucocerebrosidase gene in Czech and Slovak
RT   Gaucher patients: mutation profile and description of six novel mutant
RT   alleles.";
RL   Blood Cells Mol. Dis. 25:287-298(1999).
RN   [64]
RP   VARIANTS PERINATAL LETHAL GD ARG-350 AND PHE-437.
RX   PubMed=10352942; DOI=10.1038/sj.ejhg.5200315;
RA   Stone D.L., van Diggelen O.P., de Klerk J.B.C., Gaillard J.L.J.,
RA   Niermeijer M.F., Willemsen R., Tayebi N., Sidransky E.;
RT   "Is the perinatal lethal form of Gaucher disease more common than
RT   classic type 2 Gaucher disease?";
RL   Eur. J. Hum. Genet. 7:505-509(1999).
RN   [65]
RP   VARIANTS GD PRO-173; TRP-234; SER-409; SER-416; HIS-448 AND PRO-483.
RX   PubMed=10447266;
RX   DOI=10.1002/(SICI)1098-1004(1999)14:1<88::AID-HUMU16>3.0.CO;2-E;
RA   Sarria A.J., Giraldo P., Perez-Calvo J.I., Pocovi M.;
RT   "Detection of three rare (G377S, T134P and 1451delAC), and two novel
RT   mutations (G195W and Rec[1263del55;1342G>C]] in Spanish Gaucher
RT   disease patients.";
RL   Hum. Mutat. 14:88-88(1999).
RN   [66]
RP   VARIANTS GD TRP-87; ASN-118; THR-129; ASP-156; GLN-159; TRP-159;
RP   LEU-170; ILE-173; CYS-209; PRO-209; SER-227; THR-229; PRO-235;
RP   ARG-241; ILE-252; GLN-296; CYS-324; THR-380; MET-408; SER-409;
RP   SER-416; LEU-433; TYR-438; HIS-448; PRO-483 AND CYS-502, AND VARIANT
RP   LYS-365.
RX   PubMed=10796875; DOI=10.1086/302925;
RA   Koprivica V., Stone D.L., Park J.K., Callahan M., Frisch A.,
RA   Cohen I.J., Tayebi N., Sidransky E.;
RT   "Analysis and classification of 304 mutant alleles in patients with
RT   type 1 and type 3 Gaucher disease.";
RL   Am. J. Hum. Genet. 66:1777-1786(2000).
RN   [67]
RP   VARIANTS GD SER-55 AND HIS-448.
RX   PubMed=11992489; DOI=10.1002/ajmg.10385;
RA   Bodamer O.A.F., Church H.J., Cooper A., Wraith J.E., Scott C.R.,
RA   Scaglia F.;
RT   "Variant Gaucher disease characterized by dysmorphic features, absence
RT   of cardiovascular involvement, laryngospasm, and compound
RT   heterozygosity for a novel mutation (D409H/C16S).";
RL   Am. J. Med. Genet. 109:328-331(2002).
RN   [68]
RP   VARIANTS GD GLU-175; PRO-201; GLU-237; LEU-290 AND PHE-441.
RX   PubMed=11933202; DOI=10.1002/humu.9024;
RA   Orvisky E., Park J.K., Parker A., Walker J.M., Martin B.M.,
RA   Stubblefield B.K., Uyama E., Tayebi N., Sidransky E.;
RT   "The identification of eight novel glucocerebrosidase (GBA) mutations
RT   in patients with Gaucher disease.";
RL   Hum. Mutat. 19:458-459(2002).
RN   [69]
RP   VARIANTS GD THR-198; ARG-241; ARG-270; ILE-400 AND ARG-490.
RX   PubMed=12204005; DOI=10.1002/humu.9058;
RA   Filocamo M., Mazzotti R., Stroppiano M., Seri M., Giona F.,
RA   Parenti G., Regis S., Corsolini F., Zoboli S., Gatti R.;
RT   "Analysis of the glucocerebrosidase gene and mutation profile in 144
RT   Italian Gaucher patients.";
RL   Hum. Mutat. 20:234-235(2002).
RN   [70]
RP   POSSIBLE INVOLVEMENT IN PARKINSON DISEASE.
RX   PubMed=12847165; DOI=10.1212/01.WNL.0000072482.70963.D7;
RA   Bembi B., Zambito Marsala S., Sidransky E., Ciana G., Carrozzi M.,
RA   Zorzon M., Martini C., Gioulis M., Pittis M.G., Capus L.;
RT   "Gaucher's disease with Parkinson's disease: clinical and pathological
RT   aspects.";
RL   Neurology 61:99-101(2003).
RN   [71]
RP   VARIANT GD SER-55.
RX   PubMed=15292921; DOI=10.1038/sj.ejhg.5201251;
RA   Church H.J., Cooper A., Stewart F., Thornton C.M., Wraith J.E.;
RT   "Homozygous loss of a cysteine residue in the glucocerebrosidase gene
RT   results in Gaucher's disease with a hydropic phenotype.";
RL   Eur. J. Hum. Genet. 12:975-978(2004).
RN   [72]
RP   CHARACTERIZATION OF VARIANT GD SER-409.
RX   PubMed=15826241; DOI=10.1042/BJ20050325;
RA   Salvioli R., Tatti M., Scarpa S., Moavero S.M., Ciaffoni F.,
RA   Felicetti F., Kaneski C.R., Brady R.O., Vaccaro A.M.;
RT   "The N370S (Asn370->Ser) mutation affects the capacity of
RT   glucosylceramidase to interact with anionic phospholipid-containing
RT   membranes and saposin C.";
RL   Biochem. J. 390:95-103(2005).
RN   [73]
RP   VARIANTS GD1 ASN-63; SER-158; TRP-159; CYS-170; LEU-221; GLU-230;
RP   ARG-241; GLN-294; CYS-324; SER-409; ASN-438; LEU-440; HIS-448;
RP   CYS-457; ASP-460; PRO-483 AND ARG-490, AND CHARACTERIZATION OF
RP   VARIANTS GD1 ASN-63; SER-158; LEU-221; GLU-230 AND ASP-460.
RX   PubMed=15605411; DOI=10.1002/humu.9301;
RA   Miocic S., Filocamo M., Dominissini S., Montalvo A.L., Vlahovicek K.,
RA   Deganuto M., Mazzotti R., Cariati R., Bembi B., Pittis M.G.;
RT   "Identification and functional characterization of five novel mutant
RT   alleles in 58 Italian patients with Gaucher disease type 1.";
RL   Hum. Mutat. 25:100-100(2005).
RN   [74]
RP   POSSIBLE INVOLVEMENT IN PARKINSON DISEASE.
RX   PubMed=16148263; DOI=10.1212/01.wnl.0000176987.47875.28;
RA   Aharon-Peretz J., Badarny S., Rosenbaum H., Gershoni-Baruch R.;
RT   "Mutations in the glucocerebrosidase gene and Parkinson disease:
RT   phenotype-genotype correlation.";
RL   Neurology 65:1460-1461(2005).
RN   [75]
RP   INVOLVEMENT OF VARIANT GD PRO-483 IN SUSCEPTIBILITY TO PARKINSON
RP   DISEASE.
RX   PubMed=17620502; DOI=10.1001/archneur.64.7.1056;
RA   Tan E.K., Tong J., Fook-Chong S., Yih Y., Wong M.C., Pavanni R.,
RA   Zhao Y.;
RT   "Glucocerebrosidase mutations and risk of Parkinson disease in Chinese
RT   patients.";
RL   Arch. Neurol. 64:1056-1058(2007).
RN   [76]
RP   INVOLVEMENT OF VARIANTS GD SER-409 AND PRO-483 IN SUSCEPTIBILITY TO
RP   PARKINSON DISEASE.
RX   PubMed=18332251; DOI=10.1001/archneurol.2007.68;
RA   Mata I.F., Samii A., Schneer S.H., Roberts J.W., Griffith A.,
RA   Leis B.C., Schellenberg G.D., Sidransky E., Bird T.D., Leverenz J.B.,
RA   Tsuang D., Zabetian C.P.;
RT   "Glucocerebrosidase gene mutations: a risk factor for Lewy body
RT   disorders.";
RL   Arch. Neurol. 65:379-382(2008).
RN   [77]
RP   INVOLVEMENT OF VARIANTS GD SER-409 AND PRO-483 IN SUSCEPTIBILITY TO
RP   PARKINSON DISEASE.
RX   PubMed=19846850; DOI=10.1056/NEJMoa0901281;
RA   Sidransky E., Nalls M.A., Aasly J.O., Aharon-Peretz J., Annesi G.,
RA   Barbosa E.R., Bar-Shira A., Berg D., Bras J., Brice A., Chen C.M.,
RA   Clark L.N., Condroyer C., De Marco E.V., Durr A., Eblan M.J., Fahn S.,
RA   Farrer M.J., Fung H.C., Gan-Or Z., Gasser T., Gershoni-Baruch R.,
RA   Giladi N., Griffith A., Gurevich T., Januario C., Kropp P., Lang A.E.,
RA   Lee-Chen G.J., Lesage S., Marder K., Mata I.F., Mirelman A.,
RA   Mitsui J., Mizuta I., Nicoletti G., Oliveira C., Ottman R.,
RA   Orr-Urtreger A., Pereira L.V., Quattrone A., Rogaeva E., Rolfs A.,
RA   Rosenbaum H., Rozenberg R., Samii A., Samaddar T., Schulte C.,
RA   Sharma M., Singleton A., Spitz M., Tan E.K., Tayebi N., Toda T.,
RA   Troiano A.R., Tsuji S., Wittstock M., Wolfsberg T.G., Wu Y.R.,
RA   Zabetian C.P., Zhao Y., Ziegler S.G.;
RT   "Multicenter analysis of glucocerebrosidase mutations in Parkinson's
RT   disease.";
RL   N. Engl. J. Med. 361:1651-1661(2009).
RN   [78]
RP   VARIANT PRO-363.
RX   PubMed=26528954; DOI=10.1002/ana.24553;
RG   International Parkinsonism Genetics Network;
RA   Olgiati S., Quadri M., Fang M., Rood J.P., Saute J.A., Chien H.F.,
RA   Bouwkamp C.G., Graafland J., Minneboo M., Breedveld G.J., Zhang J.,
RA   Verheijen F.W., Boon A.J., Kievit A.J., Jardim L.B., Mandemakers W.,
RA   Barbosa E.R., Rieder C.R., Leenders K.L., Wang J., Bonifati V.;
RT   "DNAJC6 mutations associated with early-onset Parkinson's disease.";
RL   Ann. Neurol. 79:244-256(2016).
CC   -!- CATALYTIC ACTIVITY: D-glucosyl-N-acylsphingosine + H(2)O = D-
CC       glucose + N-acylsphingosine.
CC   -!- ENZYME REGULATION: Requires saposin-C and anionic phospholipids
CC       for activity.
CC   -!- SUBUNIT: Interacts with saposin-C. Interacts with SCARB2.
CC       {ECO:0000269|PubMed:10781797, ECO:0000269|PubMed:15817452,
CC       ECO:0000269|PubMed:18022370}.
CC   -!- INTERACTION:
CC       P17987:TCP1; NbExp=2; IntAct=EBI-1564609, EBI-356553;
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane
CC       {ECO:0000269|PubMed:17187079, ECO:0000269|PubMed:17897319,
CC       ECO:0000269|PubMed:18022370}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:17187079, ECO:0000269|PubMed:17897319,
CC       ECO:0000269|PubMed:18022370}; Lumenal side
CC       {ECO:0000269|PubMed:17187079, ECO:0000269|PubMed:17897319,
CC       ECO:0000269|PubMed:18022370}. Note=Interaction with saposin-C
CC       promotes membrane association. Targeting to lysosomes occurs
CC       through an alternative MPR-independent mechanism via SCARB2.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing, Alternative initiation; Named isoforms=5;
CC       Name=Long;
CC         IsoId=P04062-1; Sequence=Displayed;
CC         Note=Has a 39 residue signal sequence. The upstream initiation
CC         site produces two to three times as much protein as does the
CC         downstream initiation codon.;
CC       Name=Short;
CC         IsoId=P04062-2; Sequence=VSP_018800;
CC         Note=Has a 19 residue signal sequence.;
CC       Name=3;
CC         IsoId=P04062-3; Sequence=VSP_025216, VSP_025217, VSP_025218;
CC         Note=Produced by alternative splicing.;
CC       Name=4;
CC         IsoId=P04062-4; Sequence=VSP_054655;
CC         Note=No experimental confirmation available.;
CC       Name=5;
CC         IsoId=P04062-5; Sequence=VSP_054656;
CC         Note=No experimental confirmation available.;
CC   -!- DISEASE: Gaucher disease (GD) [MIM:230800]: A lysosomal storage
CC       disease due to deficient activity of beta-glucocerebrosidase and
CC       characterized by accumulation of glucosylceramide in the reticulo-
CC       endothelial system. Different clinical forms are recognized
CC       depending on the presence (neuronopathic forms) or absence of
CC       central nervous system involvement, severity and age of onset.
CC       {ECO:0000269|PubMed:10352942, ECO:0000269|PubMed:10360404,
CC       ECO:0000269|PubMed:10447266, ECO:0000269|PubMed:10744424,
CC       ECO:0000269|PubMed:10796875, ECO:0000269|PubMed:11933202,
CC       ECO:0000269|PubMed:11992489, ECO:0000269|PubMed:12204005,
CC       ECO:0000269|PubMed:15292921, ECO:0000269|PubMed:15826241,
CC       ECO:0000269|PubMed:16293621, ECO:0000269|PubMed:17620502,
CC       ECO:0000269|PubMed:18332251, ECO:0000269|PubMed:1972019,
CC       ECO:0000269|PubMed:1974409, ECO:0000269|PubMed:19846850,
CC       ECO:0000269|PubMed:7627184, ECO:0000269|PubMed:7627192,
CC       ECO:0000269|PubMed:7916532, ECO:0000269|PubMed:8076951,
CC       ECO:0000269|PubMed:8112750, ECO:0000269|PubMed:8294033,
CC       ECO:0000269|PubMed:8432537, ECO:0000269|PubMed:8790604,
CC       ECO:0000269|PubMed:8829654, ECO:0000269|PubMed:8829663,
CC       ECO:0000269|PubMed:8937765, ECO:0000269|PubMed:9061570,
CC       ECO:0000269|PubMed:9153297, ECO:0000269|PubMed:9182788,
CC       ECO:0000269|PubMed:9217217, ECO:0000269|PubMed:9279145,
CC       ECO:0000269|PubMed:9516376, ECO:0000269|PubMed:9554454,
CC       ECO:0000269|PubMed:9554746, ECO:0000269|PubMed:9650766,
CC       ECO:0000269|PubMed:9683600}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Gaucher disease 1 (GD1) [MIM:230800]: A form of Gaucher
CC       disease characterized by hepatosplenomegaly with consequent anemia
CC       and thrombopenia, and bone involvement. The central nervous system
CC       is not involved. {ECO:0000269|PubMed:10206680,
CC       ECO:0000269|PubMed:10340647, ECO:0000269|PubMed:15605411,
CC       ECO:0000269|PubMed:8889591, ECO:0000269|Ref.14}. Note=The disease
CC       is caused by mutations affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Gaucher disease 2 (GD2) [MIM:230900]: The most severe
CC       form of Gaucher disease. It manifests soon after birth, with death
CC       generally occurring before patients reach two years of age.
CC       {ECO:0000269|PubMed:9637431, ECO:0000269|PubMed:9851895}. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       this entry.
CC   -!- DISEASE: Gaucher disease 3 (GD3) [MIM:231000]: A subacute form of
CC       neuronopathic Gaucher disease. It has later onset and slower
CC       progression compared to the acute form of neuronopathic Gaucher
CC       disease 2. {ECO:0000269|PubMed:8780099}. Note=The disease is
CC       caused by mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Gaucher disease 3C (GD3C) [MIM:231005]: A variant of
CC       subacute neuronopathic Gaucher disease 3 associated with
CC       cardiovascular calcifications. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Gaucher disease perinatal lethal (GDPL) [MIM:608013]:
CC       Distinct form of Gaucher disease type 2, characterized by fetal
CC       onset. Hydrops fetalis, in utero fetal death and neonatal distress
CC       are prominent features. When hydrops is absent, neurologic
CC       involvement begins in the first week and leads to death within 3
CC       months. Hepatosplenomegaly is a major sign, and is associated with
CC       ichthyosis, arthrogryposis, and facial dysmorphism. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       this entry.
CC   -!- DISEASE: Note=Perinatal lethal Gaucher disease is associated with
CC       non-immune hydrops fetalis, a generalized edema of the fetus with
CC       fluid accumulation in the body cavities due to non-immune causes.
CC       Non-immune hydrops fetalis is not a diagnosis in itself but a
CC       symptom, a feature of many genetic disorders, and the end-stage of
CC       a wide variety of disorders.
CC   -!- DISEASE: Parkinson disease (PARK) [MIM:168600]: A complex
CC       neurodegenerative disorder characterized by bradykinesia, resting
CC       tremor, muscular rigidity and postural instability. Additional
CC       features are characteristic postural abnormalities, dysautonomia,
CC       dystonic cramps, and dementia. The pathology of Parkinson disease
CC       involves the loss of dopaminergic neurons in the substantia nigra
CC       and the presence of Lewy bodies (intraneuronal accumulations of
CC       aggregated proteins), in surviving neurons in various areas of the
CC       brain. The disease is progressive and usually manifests after the
CC       age of 50 years, although early-onset cases (before 50 years) are
CC       known. The majority of the cases are sporadic suggesting a
CC       multifactorial etiology based on environmental and genetic
CC       factors. However, some patients present with a positive family
CC       history for the disease. Familial forms of the disease usually
CC       begin at earlier ages and are associated with atypical clinical
CC       features. {ECO:0000269|PubMed:12847165,
CC       ECO:0000269|PubMed:16148263, ECO:0000269|PubMed:19286695}.
CC       Note=Disease susceptibility may be associated with variations
CC       affecting the gene represented in this entry.
CC   -!- PHARMACEUTICAL: Available under the names Ceredase and Cerezyme
CC       (Genzyme). Used to treat Gaucher's disease.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 30 family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Ceredase; Note=Clinical information on
CC       Ceredase;
CC       URL="https://www.rxlist.com/ceredase-drug.htm";
CC   -!- WEB RESOURCE: Name=Cerezyme; Note=Clinical information on
CC       Cerezyme;
CC       URL="https://www.rxlist.com/cerezyme-drug.htm";
DR   EMBL; M16328; AAA35873.1; -; mRNA.
DR   EMBL; K02920; AAA35877.1; -; mRNA.
DR   EMBL; J03059; AAC63056.1; -; Genomic_DNA.
DR   EMBL; D13286; BAA02545.1; -; mRNA.
DR   EMBL; D13287; BAA02546.1; -; mRNA.
DR   EMBL; AF023268; AAC51820.1; -; Genomic_DNA.
DR   EMBL; AK291911; BAF84600.1; -; mRNA.
DR   EMBL; AK298900; BAH12898.1; -; mRNA.
DR   EMBL; AK300829; BAH13357.1; -; mRNA.
DR   EMBL; AL713999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC003356; AAH03356.1; -; mRNA.
DR   EMBL; M19285; AAA35880.1; -; mRNA.
DR   EMBL; M18916; AAA35878.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; M18917; AAA35879.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; M20248; AAA35874.1; -; Genomic_DNA.
DR   EMBL; M20282; AAA35876.1; -; Genomic_DNA.
DR   CCDS; CCDS1102.1; -. [P04062-1]
DR   CCDS; CCDS53373.1; -. [P04062-4]
DR   CCDS; CCDS53374.1; -. [P04062-5]
DR   PIR; A94068; EUHUGC.
DR   PIR; I52980; I52980.
DR   PIR; I67792; I67792.
DR   RefSeq; NP_000148.2; NM_000157.3. [P04062-1]
DR   RefSeq; NP_001005741.1; NM_001005741.2. [P04062-1]
DR   RefSeq; NP_001005742.1; NM_001005742.2. [P04062-1]
DR   RefSeq; NP_001165282.1; NM_001171811.1. [P04062-4]
DR   RefSeq; NP_001165283.1; NM_001171812.1. [P04062-5]
DR   UniGene; Hs.282997; -.
DR   PDB; 1OGS; X-ray; 2.00 A; A/B=40-536.
DR   PDB; 1Y7V; X-ray; 2.40 A; A/B=40-536.
DR   PDB; 2F61; X-ray; 2.50 A; A/B=40-536.
DR   PDB; 2J25; X-ray; 2.90 A; A/B=40-536.
DR   PDB; 2NSX; X-ray; 2.11 A; A/B/C/D=40-536.
DR   PDB; 2NT0; X-ray; 1.79 A; A/B/C/D=40-536.
DR   PDB; 2NT1; X-ray; 2.30 A; A/B/C/D=40-536.
DR   PDB; 2V3D; X-ray; 1.96 A; A/B=40-536.
DR   PDB; 2V3E; X-ray; 2.00 A; A/B=40-536.
DR   PDB; 2V3F; X-ray; 1.95 A; A/B=40-536.
DR   PDB; 2VT0; X-ray; 2.15 A; A/B=40-536.
DR   PDB; 2WCG; X-ray; 2.30 A; A/B=40-536.
DR   PDB; 2WKL; X-ray; 2.70 A; A/B=40-536.
DR   PDB; 2XWD; X-ray; 2.66 A; A/B=40-536.
DR   PDB; 2XWE; X-ray; 2.31 A; A/B=40-536.
DR   PDB; 3GXD; X-ray; 2.50 A; A/B/C/D=40-536.
DR   PDB; 3GXF; X-ray; 2.40 A; A/B/C/D=40-536.
DR   PDB; 3GXI; X-ray; 1.84 A; A/B/C/D=40-536.
DR   PDB; 3GXM; X-ray; 2.20 A; A/B/C/D=40-536.
DR   PDB; 3KE0; X-ray; 2.70 A; A/B=40-536.
DR   PDB; 3KEH; X-ray; 2.80 A; A/B=40-536.
DR   PDB; 3RIK; X-ray; 2.48 A; A/B/C/D=40-536.
DR   PDB; 3RIL; X-ray; 2.40 A; A/B/C/D=40-536.
DR   PDB; 5LVX; X-ray; 2.20 A; A/B/C/D=40-536.
DR   PDBsum; 1OGS; -.
DR   PDBsum; 1Y7V; -.
DR   PDBsum; 2F61; -.
DR   PDBsum; 2J25; -.
DR   PDBsum; 2NSX; -.
DR   PDBsum; 2NT0; -.
DR   PDBsum; 2NT1; -.
DR   PDBsum; 2V3D; -.
DR   PDBsum; 2V3E; -.
DR   PDBsum; 2V3F; -.
DR   PDBsum; 2VT0; -.
DR   PDBsum; 2WCG; -.
DR   PDBsum; 2WKL; -.
DR   PDBsum; 2XWD; -.
DR   PDBsum; 2XWE; -.
DR   PDBsum; 3GXD; -.
DR   PDBsum; 3GXF; -.
DR   PDBsum; 3GXI; -.
DR   PDBsum; 3GXM; -.
DR   PDBsum; 3KE0; -.
DR   PDBsum; 3KEH; -.
DR   PDBsum; 3RIK; -.
DR   PDBsum; 3RIL; -.
DR   PDBsum; 5LVX; -.
DR   ProteinModelPortal; P04062; -.
DR   SMR; P04062; -.
DR   BioGrid; 108899; 48.
DR   DIP; DIP-38645N; -.
DR   IntAct; P04062; 32.
DR   MINT; P04062; -.
DR   STRING; 9606.ENSP00000314508; -.
DR   BindingDB; P04062; -.
DR   ChEMBL; CHEMBL2179; -.
DR   DrugBank; DB03106; Myo-Inositol.
DR   DrugBank; DB03740; N-acetyl-alpha-D-glucosamine.
DR   DrugBank; DB06720; Velaglucerase alfa.
DR   SwissLipids; SLP:000001387; -.
DR   Allergome; 8244; Hom s Glucocerebrosidase.
DR   CAZy; GH30; Glycoside Hydrolase Family 30.
DR   iPTMnet; P04062; -.
DR   PhosphoSitePlus; P04062; -.
DR   SwissPalm; P04062; -.
DR   BioMuta; GBA; -.
DR   DMDM; 55584151; -.
DR   EPD; P04062; -.
DR   MaxQB; P04062; -.
DR   PaxDb; P04062; -.
DR   PeptideAtlas; P04062; -.
DR   PRIDE; P04062; -.
DR   ProteomicsDB; 51642; -.
DR   ProteomicsDB; 51643; -. [P04062-2]
DR   ProteomicsDB; 51644; -. [P04062-3]
DR   DNASU; 2629; -.
DR   Ensembl; ENST00000327247; ENSP00000314508; ENSG00000177628. [P04062-1]
DR   Ensembl; ENST00000368373; ENSP00000357357; ENSG00000177628. [P04062-1]
DR   Ensembl; ENST00000427500; ENSP00000402577; ENSG00000177628. [P04062-5]
DR   Ensembl; ENST00000428024; ENSP00000397986; ENSG00000177628. [P04062-4]
DR   GeneID; 2629; -.
DR   KEGG; hsa:2629; -.
DR   UCSC; uc001fjh.4; human. [P04062-1]
DR   CTD; 2629; -.
DR   DisGeNET; 2629; -.
DR   EuPathDB; HostDB:ENSG00000177628.15; -.
DR   GeneCards; GBA; -.
DR   GeneReviews; GBA; -.
DR   H-InvDB; HIX0001123; -.
DR   HGNC; HGNC:4177; GBA.
DR   HPA; CAB037171; -.
DR   HPA; CAB037289; -.
DR   HPA; HPA006667; -.
DR   MalaCards; GBA; -.
DR   MIM; 168600; phenotype.
DR   MIM; 230800; phenotype.
DR   MIM; 230900; phenotype.
DR   MIM; 231000; phenotype.
DR   MIM; 231005; phenotype.
DR   MIM; 606463; gene.
DR   MIM; 608013; phenotype.
DR   neXtProt; NX_P04062; -.
DR   OpenTargets; ENSG00000177628; -.
DR   Orphanet; 1648; Dementia with Lewy body.
DR   Orphanet; 85212; Fetal Gaucher disease.
DR   Orphanet; 2072; Gaucher disease - ophthalmoplegia - cardiovascular calcification.
DR   Orphanet; 77259; Gaucher disease type 1.
DR   Orphanet; 77260; Gaucher disease type 2.
DR   Orphanet; 77261; Gaucher disease type 3.
DR   Orphanet; 319705; Parkinson disease.
DR   Orphanet; 2828; Young adult-onset Parkinsonism.
DR   PharmGKB; PA28591; -.
DR   eggNOG; KOG2566; Eukaryota.
DR   eggNOG; COG5520; LUCA.
DR   GeneTree; ENSGT00390000009464; -.
DR   HOVERGEN; HBG002285; -.
DR   InParanoid; P04062; -.
DR   KO; K01201; -.
DR   OMA; TYCDSLD; -.
DR   OrthoDB; EOG091G06I4; -.
DR   PhylomeDB; P04062; -.
DR   TreeFam; TF314254; -.
DR   BRENDA; 3.2.1.45; 2681.
DR   Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
DR   Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR   EvolutionaryTrace; P04062; -.
DR   GeneWiki; Glucocerebrosidase; -.
DR   GenomeRNAi; 2629; -.
DR   PRO; PR:P04062; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000177628; -.
DR   CleanEx; HS_GBA; -.
DR   CleanEx; HS_GC; -.
DR   ExpressionAtlas; P04062; baseline and differential.
DR   Genevisible; P04062; HS.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0019898; C:extrinsic component of membrane; NAS:ARUK-UCL.
DR   GO; GO:0043202; C:lysosomal lumen; ISS:BHF-UCL.
DR   GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR   GO; GO:0005764; C:lysosome; IMP:ARUK-UCL.
DR   GO; GO:0004348; F:glucosylceramidase activity; IDA:BHF-UCL.
DR   GO; GO:0005124; F:scavenger receptor binding; IPI:ARUK-UCL.
DR   GO; GO:0005102; F:signaling receptor binding; ISS:BHF-UCL.
DR   GO; GO:1905037; P:autophagosome organization; IEA:Ensembl.
DR   GO; GO:1901805; P:beta-glucoside catabolic process; IEA:Ensembl.
DR   GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IMP:BHF-UCL.
DR   GO; GO:0046513; P:ceramide biosynthetic process; IMP:BHF-UCL.
DR   GO; GO:0006680; P:glucosylceramide catabolic process; IMP:BHF-UCL.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IC:BHF-UCL.
DR   GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:BHF-UCL.
DR   GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:BHF-UCL.
DR   GO; GO:1901215; P:negative regulation of neuron death; IGI:ParkinsonsUK-UCL.
DR   GO; GO:0032463; P:negative regulation of protein homooligomerization; IDA:ParkinsonsUK-UCL.
DR   GO; GO:1904925; P:positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization; IEA:Ensembl.
DR   GO; GO:1904457; P:positive regulation of neuronal action potential; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR   GO; GO:0043243; P:positive regulation of protein complex disassembly; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0035307; P:positive regulation of protein dephosphorylation; IMP:BHF-UCL.
DR   GO; GO:1903061; P:positive regulation of protein lipidation; IGI:ParkinsonsUK-UCL.
DR   GO; GO:0051247; P:positive regulation of protein metabolic process; IGI:ParkinsonsUK-UCL.
DR   GO; GO:1903052; P:positive regulation of proteolysis involved in cellular protein catabolic process; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0032268; P:regulation of cellular protein metabolic process; IMP:ParkinsonsUK-UCL.
DR   GO; GO:1905165; P:regulation of lysosomal protein catabolic process; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0016241; P:regulation of macroautophagy; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0033561; P:regulation of water loss via skin; IEA:Ensembl.
DR   GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl.
DR   GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR   GO; GO:0009268; P:response to pH; IEA:Ensembl.
DR   GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR   GO; GO:0097066; P:response to thyroid hormone; IEA:Ensembl.
DR   GO; GO:0043589; P:skin morphogenesis; IEA:Ensembl.
DR   GO; GO:0046512; P:sphingosine biosynthetic process; IMP:BHF-UCL.
DR   GO; GO:0023021; P:termination of signal transduction; IMP:BHF-UCL.
DR   Gene3D; 2.60.40.1180; -; 2.
DR   InterPro; IPR033452; GH30_C.
DR   InterPro; IPR001139; Glyco_hydro_30.
DR   InterPro; IPR033453; Glyco_hydro_30_TIM-barrel.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR11069; PTHR11069; 1.
DR   Pfam; PF02055; Glyco_hydro_30; 1.
DR   Pfam; PF17189; Glyco_hydro_30C; 1.
DR   PRINTS; PR00843; GLHYDRLASE30.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative initiation; Alternative splicing;
KW   Complete proteome; Direct protein sequencing; Disease mutation;
KW   Disulfide bond; Gaucher disease; Glycoprotein; Glycosidase; Hydrolase;
KW   Ichthyosis; Lipid metabolism; Lysosome; Membrane; Neurodegeneration;
KW   Parkinson disease; Parkinsonism; Pharmaceutical; Polymorphism;
KW   Reference proteome; Signal; Sphingolipid metabolism.
FT   SIGNAL        1     39       In isoform Long. {ECO:0000269|Ref.12}.
FT   SIGNAL       21     39       In isoform Short. {ECO:0000269|Ref.12}.
FT   CHAIN        40    536       Glucosylceramidase.
FT                                /FTId=PRO_0000012177.
FT   ACT_SITE    274    274       Proton donor.
FT                                {ECO:0000269|PubMed:15817452}.
FT   ACT_SITE    379    379       Nucleophile.
FT                                {ECO:0000269|PubMed:15817452}.
FT   CARBOHYD     58     58       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:12792654,
FT                                ECO:0000269|PubMed:17139081}.
FT   CARBOHYD     98     98       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:12754519,
FT                                ECO:0000269|PubMed:17139081,
FT                                ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    185    185       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:12754519,
FT                                ECO:0000269|PubMed:17139081}.
FT   CARBOHYD    309    309       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:12754519,
FT                                ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    501    501       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     43     55       {ECO:0000269|PubMed:12792654}.
FT   DISULFID     57     62       {ECO:0000269|PubMed:12792654}.
FT   VAR_SEQ       1    161       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:8294033}.
FT                                /FTId=VSP_025216.
FT   VAR_SEQ       1     87       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_054655.
FT   VAR_SEQ       1     20       Missing (in isoform Short).
FT                                {ECO:0000303|PubMed:3001061,
FT                                ECO:0000303|PubMed:3864160}.
FT                                /FTId=VSP_018800.
FT   VAR_SEQ     103    151       Missing (in isoform 5).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_054656.
FT   VAR_SEQ     422    423       LA -> PS (in isoform 3).
FT                                {ECO:0000303|PubMed:8294033}.
FT                                /FTId=VSP_025217.
FT   VAR_SEQ     425    536       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:8294033}.
FT                                /FTId=VSP_025218.
FT   VARIANT      46     46       K -> E (in a patient with Parkinson
FT                                disease; dbSNP:rs142761046).
FT                                {ECO:0000269|PubMed:19286695}.
FT                                /FTId=VAR_063066.
FT   VARIANT      54     54       V -> L (in GD; dbSNP:rs121908302).
FT                                {ECO:0000269|PubMed:8829654}.
FT                                /FTId=VAR_003255.
FT   VARIANT      55     55       C -> S (in GD; neuronopathic and
FT                                perinatal lethal forms; loss of activity;
FT                                dbSNP:rs773007510).
FT                                {ECO:0000269|PubMed:11992489,
FT                                ECO:0000269|PubMed:15292921,
FT                                ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_032394.
FT   VARIANT      63     63       D -> N (in GD1; very low activity).
FT                                {ECO:0000269|PubMed:15605411}.
FT                                /FTId=VAR_032395.
FT   VARIANT      76     76       F -> V (in GD).
FT                                {ECO:0000269|PubMed:9217217}.
FT                                /FTId=VAR_003256.
FT   VARIANT      80     80       E -> K (in GD2).
FT                                {ECO:0000269|PubMed:9851895}.
FT                                /FTId=VAR_009033.
FT   VARIANT      82     82       T -> I (in GD; dbSNP:rs1141811).
FT                                /FTId=VAR_003257.
FT   VARIANT      85     85       G -> E (in GD; dbSNP:rs77829017).
FT                                {ECO:0000269|PubMed:8829654,
FT                                ECO:0000269|PubMed:9217217}.
FT                                /FTId=VAR_003258.
FT   VARIANT      87     87       R -> Q (in GD; 20% of normal activity;
FT                                dbSNP:rs78769774).
FT                                {ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_032197.
FT   VARIANT      87     87       R -> W (in GD; mild; dbSNP:rs1141814).
FT                                {ECO:0000269|PubMed:10796875,
FT                                ECO:0000269|PubMed:9153297,
FT                                ECO:0000269|PubMed:9217217}.
FT                                /FTId=VAR_003259.
FT   VARIANT      92     92       M -> T (in dbSNP:rs1141815).
FT                                /FTId=VAR_032396.
FT   VARIANT     118    118       K -> N (in GD; mild; 8% of normal
FT                                activity; increases susceptibility to
FT                                proteolytic degradation;
FT                                dbSNP:rs121908312).
FT                                {ECO:0000269|PubMed:10796875,
FT                                ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_003260.
FT   VARIANT     129    129       A -> T (in GD).
FT                                {ECO:0000269|PubMed:10796875}.
FT                                /FTId=VAR_032397.
FT   VARIANT     146    146       S -> L (in GD; type 2;
FT                                dbSNP:rs758447515).
FT                                {ECO:0000269|PubMed:9554454}.
FT                                /FTId=VAR_009034.
FT   VARIANT     152    152       G -> E (in GD).
FT                                {ECO:0000269|PubMed:9554746}.
FT                                /FTId=VAR_003261.
FT   VARIANT     156    156       N -> D (in GD).
FT                                {ECO:0000269|PubMed:10796875}.
FT                                /FTId=VAR_032398.
FT   VARIANT     158    158       I -> S (in GD1; very low activity;
FT                                dbSNP:rs77834747).
FT                                {ECO:0000269|PubMed:15605411}.
FT                                /FTId=VAR_032399.
FT   VARIANT     158    158       I -> T (in GD).
FT                                /FTId=VAR_003262.
FT   VARIANT     159    159       R -> Q (in GD; type 2; 13% of normal
FT                                activity; dbSNP:rs79653797).
FT                                {ECO:0000269|PubMed:10796875,
FT                                ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_003263.
FT   VARIANT     159    159       R -> W (in GD; severe; dbSNP:rs439898).
FT                                {ECO:0000269|PubMed:10796875,
FT                                ECO:0000269|PubMed:15605411,
FT                                ECO:0000269|PubMed:9217217}.
FT                                /FTId=VAR_003264.
FT   VARIANT     161    161       P -> L (in GD; 16% of normal activity;
FT                                dbSNP:rs79637617).
FT                                {ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_032198.
FT   VARIANT     161    161       P -> S (in GD; mild; dbSNP:rs121908299).
FT                                /FTId=VAR_003265.
FT   VARIANT     162    162       M -> V (in GD; loss of activity;
FT                                increases susceptibility to proteolytic
FT                                degradation; dbSNP:rs377325220).
FT                                {ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_032199.
FT   VARIANT     166    166       D -> V (in GD; 9% of normal activity;
FT                                increases susceptibility to proteolytic
FT                                degradation; dbSNP:rs79796061).
FT                                {ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_032200.
FT   VARIANT     170    170       R -> C (in GD1 and GD2; also found in a
FT                                patient with Parkinson disease;
FT                                dbSNP:rs398123530).
FT                                {ECO:0000269|PubMed:15605411,
FT                                ECO:0000269|PubMed:19286695,
FT                                ECO:0000269|PubMed:9851895}.
FT                                /FTId=VAR_009035.
FT   VARIANT     170    170       R -> L (in GD; dbSNP:rs80356763).
FT                                {ECO:0000269|PubMed:10796875}.
FT                                /FTId=VAR_009036.
FT   VARIANT     173    173       T -> I (in GD; dbSNP:rs78657146).
FT                                {ECO:0000269|PubMed:10796875}.
FT                                /FTId=VAR_032400.
FT   VARIANT     173    173       T -> P (in GD).
FT                                {ECO:0000269|PubMed:10447266,
FT                                ECO:0000269|PubMed:9554746}.
FT                                /FTId=VAR_003266.
FT   VARIANT     175    175       A -> E (in GD; dbSNP:rs79660787).
FT                                {ECO:0000269|PubMed:11933202}.
FT                                /FTId=VAR_032401.
FT   VARIANT     179    179       D -> H (in GD; dbSNP:rs147138516).
FT                                /FTId=VAR_003267.
FT   VARIANT     196    196       K -> Q (in GD; severe;
FT                                dbSNP:rs121908297).
FT                                /FTId=VAR_003268.
FT   VARIANT     198    198       P -> L (in GD; dbSNP:rs80222298).
FT                                {ECO:0000269|PubMed:9554454}.
FT                                /FTId=VAR_009037.
FT   VARIANT     198    198       P -> T (in GD).
FT                                {ECO:0000269|PubMed:12204005}.
FT                                /FTId=VAR_032402.
FT   VARIANT     200    200       I -> N (in GD; 5% of normal activity;
FT                                dbSNP:rs77933015).
FT                                {ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_032201.
FT   VARIANT     200    200       I -> S (in GD; dbSNP:rs77933015).
FT                                /FTId=VAR_010059.
FT   VARIANT     201    201       H -> P (in GD; dbSNP:rs76500263).
FT                                {ECO:0000269|PubMed:11933202}.
FT                                /FTId=VAR_032403.
FT   VARIANT     209    209       R -> C (in GD; dbSNP:rs398123532).
FT                                {ECO:0000269|PubMed:10796875}.
FT                                /FTId=VAR_032404.
FT   VARIANT     209    209       R -> P (in GD).
FT                                {ECO:0000269|PubMed:10796875}.
FT                                /FTId=VAR_003269.
FT   VARIANT     213    213       L -> F (in GD; 12% of normal activity;
FT                                dbSNP:rs374591570).
FT                                {ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_032202.
FT   VARIANT     215    215       A -> D (in GD).
FT                                {ECO:0000269|PubMed:8790604}.
FT                                /FTId=VAR_003270.
FT   VARIANT     217    217       P -> S (in GD; type 2).
FT                                {ECO:0000269|PubMed:7627192}.
FT                                /FTId=VAR_003271.
FT   VARIANT     221    221       P -> L (in GD1; very low activity;
FT                                dbSNP:rs80205046).
FT                                {ECO:0000269|PubMed:15605411}.
FT                                /FTId=VAR_032405.
FT   VARIANT     221    221       P -> T (in GD; dbSNP:rs866075757).
FT                                {ECO:0000269|PubMed:8790604}.
FT                                /FTId=VAR_003272.
FT   VARIANT     223    223       W -> R (in GD; gene conversion;
FT                                dbSNP:rs61748906).
FT                                {ECO:0000269|PubMed:8294033}.
FT                                /FTId=VAR_003273.
FT   VARIANT     224    224       L -> F (in GD; 4% of normal activity;
FT                                increases susceptibility to proteolytic
FT                                degradation).
FT                                {ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_032203.
FT   VARIANT     227    227       N -> K (in GD; gene conversion;
FT                                dbSNP:rs381418).
FT                                /FTId=VAR_003275.
FT   VARIANT     227    227       N -> S (in GD; type 2; dbSNP:rs364897).
FT                                {ECO:0000269|PubMed:10796875,
FT                                ECO:0000269|PubMed:8829654,
FT                                ECO:0000269|PubMed:9217217}.
FT                                /FTId=VAR_003274.
FT   VARIANT     228    228       G -> V (in GD; dbSNP:rs78911246).
FT                                {ECO:0000269|PubMed:9061570}.
FT                                /FTId=VAR_010060.
FT   VARIANT     229    229       A -> E (in GD; type 2; dbSNP:rs75636769).
FT                                /FTId=VAR_009038.
FT   VARIANT     229    229       A -> T (in GD).
FT                                {ECO:0000269|PubMed:10796875}.
FT                                /FTId=VAR_032406.
FT   VARIANT     230    230       V -> E (in GD1; very low activity;
FT                                dbSNP:rs381427).
FT                                {ECO:0000269|PubMed:15605411}.
FT                                /FTId=VAR_032407.
FT   VARIANT     230    230       V -> G (in GD1; gene conversion;
FT                                dbSNP:rs381427).
FT                                {ECO:0000269|PubMed:10206680,
FT                                ECO:0000269|PubMed:8294033}.
FT                                /FTId=VAR_003276.
FT   VARIANT     232    232       G -> E (in GD; also found in a patient
FT                                with Parkinson disease; 7% of normal
FT                                activity). {ECO:0000269|PubMed:16293621,
FT                                ECO:0000269|PubMed:19286695}.
FT                                /FTId=VAR_032204.
FT   VARIANT     234    234       G -> E (in GD; severe; dbSNP:rs74462743).
FT                                {ECO:0000269|PubMed:9153297}.
FT                                /FTId=VAR_003277.
FT   VARIANT     234    234       G -> W (in GD).
FT                                {ECO:0000269|PubMed:10447266}.
FT                                /FTId=VAR_009039.
FT   VARIANT     235    235       S -> P (in GD; type 2; gene conversion;
FT                                dbSNP:rs1064644).
FT                                {ECO:0000269|PubMed:10796875,
FT                                ECO:0000269|PubMed:8294033}.
FT                                /FTId=VAR_003278.
FT   VARIANT     237    237       K -> E (in GD; severe; loss of activity;
FT                                increases susceptibility to proteolytic
FT                                degradation; dbSNP:rs773409311).
FT                                {ECO:0000269|PubMed:11933202,
FT                                ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_032205.
FT   VARIANT     241    241       G -> E (in GD; dbSNP:rs77451368).
FT                                /FTId=VAR_010061.
FT   VARIANT     241    241       G -> R (in GD; type 1 and type 2; gene
FT                                conversion; dbSNP:rs409652).
FT                                {ECO:0000269|PubMed:10360404,
FT                                ECO:0000269|PubMed:10796875,
FT                                ECO:0000269|PubMed:12204005,
FT                                ECO:0000269|PubMed:15605411,
FT                                ECO:0000269|PubMed:8294033,
FT                                ECO:0000269|PubMed:8790604,
FT                                ECO:0000269|PubMed:9153297}.
FT                                /FTId=VAR_003279.
FT   VARIANT     244    244       Y -> C (in GD; dbSNP:rs76026102).
FT                                {ECO:0000269|PubMed:10360404}.
FT                                /FTId=VAR_010062.
FT   VARIANT     251    251       Y -> H (in GD; dbSNP:rs121908300).
FT                                /FTId=VAR_003280.
FT   VARIANT     252    252       F -> I (in GD; type 2; gene conversion;
FT                                dbSNP:rs381737).
FT                                {ECO:0000269|PubMed:10360404,
FT                                ECO:0000269|PubMed:10796875,
FT                                ECO:0000269|PubMed:8294033,
FT                                ECO:0000269|PubMed:9061570,
FT                                ECO:0000269|PubMed:9153297,
FT                                ECO:0000269|PubMed:9217217}.
FT                                /FTId=VAR_003281.
FT   VARIANT     255    255       F -> Y (in GD; mild; dbSNP:rs74500255).
FT                                {ECO:0000269|PubMed:1974409}.
FT                                /FTId=VAR_003282.
FT   VARIANT     270    270       T -> R (in GD; dbSNP:rs76725886).
FT                                {ECO:0000269|PubMed:12204005}.
FT                                /FTId=VAR_032408.
FT   VARIANT     276    276       S -> P (in GD).
FT                                /FTId=VAR_003283.
FT   VARIANT     290    290       F -> L (in GD; perinatal lethal form;
FT                                dbSNP:rs121908313).
FT                                {ECO:0000269|PubMed:11933202}.
FT                                /FTId=VAR_032409.
FT   VARIANT     294    294       H -> Q (in GD1; also found in Gaucher
FT                                disease type 2; dbSNP:rs367968666).
FT                                {ECO:0000269|PubMed:15605411}.
FT                                /FTId=VAR_009040.
FT   VARIANT     296    296       R -> Q (in GD; type 2; also found in a
FT                                patient with Parkinson disease;
FT                                dbSNP:rs78973108).
FT                                {ECO:0000269|PubMed:10796875,
FT                                ECO:0000269|PubMed:19286695,
FT                                ECO:0000269|PubMed:8790604}.
FT                                /FTId=VAR_003284.
FT   VARIANT     298    298       F -> L (in GD; type 2; 4% of normal
FT                                activity). {ECO:0000269|PubMed:16293621,
FT                                ECO:0000269|PubMed:3001061}.
FT                                /FTId=VAR_009041.
FT   VARIANT     303    303       L -> I (in GD; 5% of normal activity).
FT                                {ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_032206.
FT   VARIANT     304    304       G -> D (in GD; dbSNP:rs80116658).
FT                                /FTId=VAR_010063.
FT   VARIANT     305    305       P -> R (in GD; mild; dbSNP:rs79215220).
FT                                /FTId=VAR_003285.
FT   VARIANT     310    310       S -> G (in dbSNP:rs1057942).
FT                                {ECO:0000269|PubMed:8294033}.
FT                                /FTId=VAR_032410.
FT   VARIANT     310    310       S -> N (in GD; less than 5% of normal
FT                                activity; dbSNP:rs74731340).
FT                                {ECO:0000269|PubMed:9153297}.
FT                                /FTId=VAR_010064.
FT   VARIANT     324    324       R -> C (in GD; type 1;
FT                                dbSNP:rs765633380).
FT                                {ECO:0000269|PubMed:10796875,
FT                                ECO:0000269|PubMed:15605411,
FT                                ECO:0000269|PubMed:8790604}.
FT                                /FTId=VAR_003286.
FT   VARIANT     324    324       R -> H (in GD; type 2; dbSNP:rs79696831).
FT                                /FTId=VAR_009042.
FT   VARIANT     328    328       P -> L (in GD; mild; dbSNP:rs121908298).
FT                                /FTId=VAR_003287.
FT   VARIANT     342    342       K -> I (in GD; dbSNP:rs77714449).
FT                                /FTId=VAR_003288.
FT   VARIANT     343    343       Y -> C (in GD; type 2; 16% of normal
FT                                activity; increases susceptibility to
FT                                proteolytic degradation;
FT                                dbSNP:rs77321207).
FT                                {ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_009043.
FT   VARIANT     348    348       A -> V (in GD; dbSNP:rs78396650).
FT                                /FTId=VAR_003289.
FT   VARIANT     350    350       H -> R (in perinatal lethal GD;
FT                                dbSNP:rs78198234).
FT                                {ECO:0000269|PubMed:10352942}.
FT                                /FTId=VAR_009044.
FT   VARIANT     351    351       W -> C (in GD; mild; dbSNP:rs121908304).
FT                                /FTId=VAR_003290.
FT   VARIANT     352    352       Y -> H (in GD).
FT                                {ECO:0000269|PubMed:8829663}.
FT                                /FTId=VAR_003291.
FT   VARIANT     354    354       D -> H (in GD; dbSNP:rs398123526).
FT                                /FTId=VAR_003292.
FT   VARIANT     357    357       A -> D (in GD; dbSNP:rs78188205).
FT                                /FTId=VAR_003293.
FT   VARIANT     362    362       T -> I (in GD; 6% of normal activity;
FT                                dbSNP:rs76539814).
FT                                {ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_003294.
FT   VARIANT     363    363       L -> P (in GD; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:26528954}.
FT                                /FTId=VAR_003295.
FT   VARIANT     364    364       G -> R (in GD; type 2;
FT                                dbSNP:rs121908305).
FT                                {ECO:0000269|PubMed:8294033}.
FT                                /FTId=VAR_003296.
FT   VARIANT     365    365       E -> K (in GD; mild; 42% of normal
FT                                activity; dbSNP:rs2230288).
FT                                {ECO:0000269|PubMed:10796875,
FT                                ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_003297.
FT   VARIANT     368    368       R -> H (in dbSNP:rs1064648).
FT                                {ECO:0000269|PubMed:8294033}.
FT                                /FTId=VAR_032411.
FT   VARIANT     380    380       A -> T (in GD; dbSNP:rs781306264).
FT                                {ECO:0000269|PubMed:10796875,
FT                                ECO:0000269|PubMed:9554454}.
FT                                /FTId=VAR_009045.
FT   VARIANT     381    381       C -> G (in GD; type 2; loss of activity;
FT                                dbSNP:rs121908306).
FT                                {ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_003298.
FT   VARIANT     388    388       E -> K (in GD; 12% of normal activity).
FT                                {ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_032207.
FT   VARIANT     391    391       V -> L (in GD; dbSNP:rs398123527).
FT                                {ECO:0000269|PubMed:9153297}.
FT                                /FTId=VAR_010065.
FT   VARIANT     392    392       R -> G (in GD; dbSNP:rs121908308).
FT                                {ECO:0000269|PubMed:9650766}.
FT                                /FTId=VAR_010066.
FT   VARIANT     392    392       R -> W (in GD; 5% of normal activity).
FT                                {ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_032208.
FT   VARIANT     398    398       R -> Q (in GD; mild; dbSNP:rs74979486).
FT                                {ECO:0000269|PubMed:8829663}.
FT                                /FTId=VAR_003299.
FT   VARIANT     400    400       M -> I (in GD; dbSNP:rs149487315).
FT                                {ECO:0000269|PubMed:12204005}.
FT                                /FTId=VAR_032412.
FT   VARIANT     402    402       Y -> C (in GD; 8% of normal activity;
FT                                increases susceptibility to proteolytic
FT                                degradation; dbSNP:rs76228122).
FT                                {ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_032209.
FT   VARIANT     403    403       S -> T (in GD; mild; dbSNP:rs121908307).
FT                                /FTId=VAR_003300.
FT   VARIANT     405    405       S -> G (in GD).
FT                                {ECO:0000269|PubMed:9061570}.
FT                                /FTId=VAR_010067.
FT   VARIANT     405    405       S -> N (in GD).
FT                                {ECO:0000269|PubMed:9554454}.
FT                                /FTId=VAR_009046.
FT   VARIANT     408    408       T -> M (in GD; dbSNP:rs75548401).
FT                                {ECO:0000269|PubMed:10796875,
FT                                ECO:0000269|PubMed:14702039}.
FT                                /FTId=VAR_003301.
FT   VARIANT     409    409       N -> S (in GD1; common mutation;
FT                                associated with susceptibility to
FT                                Parkinson disease; alters interaction
FT                                with saposin-C; mild; dbSNP:rs76763715).
FT                                {ECO:0000269|PubMed:10206680,
FT                                ECO:0000269|PubMed:10340647,
FT                                ECO:0000269|PubMed:10447266,
FT                                ECO:0000269|PubMed:10796875,
FT                                ECO:0000269|PubMed:15605411,
FT                                ECO:0000269|PubMed:15826241,
FT                                ECO:0000269|PubMed:16293621,
FT                                ECO:0000269|PubMed:18332251,
FT                                ECO:0000269|PubMed:19286695,
FT                                ECO:0000269|PubMed:19846850,
FT                                ECO:0000269|PubMed:7627184,
FT                                ECO:0000269|PubMed:8076951,
FT                                ECO:0000269|PubMed:8937765,
FT                                ECO:0000269|PubMed:9153297,
FT                                ECO:0000269|Ref.14}.
FT                                /FTId=VAR_003302.
FT   VARIANT     410    410       L -> V (in GD; 15% of normal activity;
FT                                increases susceptibility to proteolytic
FT                                degradation; dbSNP:rs121908314).
FT                                {ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_032210.
FT   VARIANT     414    414       V -> L (in GD; mild; dbSNP:rs398123528).
FT                                {ECO:0000269|PubMed:9182788}.
FT                                /FTId=VAR_010068.
FT   VARIANT     416    416       G -> S (in GD; mild; dbSNP:rs121908311).
FT                                {ECO:0000269|PubMed:10447266,
FT                                ECO:0000269|PubMed:10796875}.
FT                                /FTId=VAR_003303.
FT   VARIANT     417    417       W -> G (in GD).
FT                                {ECO:0000269|PubMed:8790604}.
FT                                /FTId=VAR_003304.
FT   VARIANT     419    419       D -> A (in GD; type 2; also found in a
FT                                patient with Parkinson disease;
FT                                dbSNP:rs77284004).
FT                                {ECO:0000269|PubMed:19286695}.
FT                                /FTId=VAR_003305.
FT   VARIANT     419    419       D -> H (in GD; 4% of normal activity).
FT                                {ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_032211.
FT   VARIANT     419    419       D -> N (in GD).
FT                                {ECO:0000269|PubMed:8790604}.
FT                                /FTId=VAR_003306.
FT   VARIANT     421    421       N -> K (in GD; 22% of normal activity).
FT                                {ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_032212.
FT   VARIANT     426    426       P -> L (in GD; dbSNP:rs1057519357 and
FT                                dbSNP:rs994723035).
FT                                {ECO:0000269|PubMed:8937765}.
FT                                /FTId=VAR_010069.
FT   VARIANT     428    428       G -> E (in GD; type 2).
FT                                {ECO:0000269|PubMed:9554746}.
FT                                /FTId=VAR_003307.
FT   VARIANT     429    429       G -> R (in GD; 17% of normal activity).
FT                                {ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_032213.
FT   VARIANT     430    430       P -> L (in GD; dbSNP:rs76910485).
FT                                {ECO:0000269|PubMed:9554746}.
FT                                /FTId=VAR_003308.
FT   VARIANT     431    431       N -> I (in GD; type 2; dbSNP:rs77738682).
FT                                {ECO:0000269|PubMed:9554746}.
FT                                /FTId=VAR_003309.
FT   VARIANT     432    432       W -> R (in GD).
FT                                {ECO:0000269|PubMed:9554454}.
FT                                /FTId=VAR_009047.
FT   VARIANT     433    433       V -> L (in GD; severe; 12% of normal
FT                                activity; dbSNP:rs80356769).
FT                                {ECO:0000269|PubMed:10796875,
FT                                ECO:0000269|PubMed:16293621,
FT                                ECO:0000269|PubMed:8937765}.
FT                                /FTId=VAR_003310.
FT   VARIANT     435    435       N -> T (in GD1; mild; dbSNP:rs75385858).
FT                                {ECO:0000269|PubMed:8889591}.
FT                                /FTId=VAR_003311.
FT   VARIANT     436    436       F -> S (in GD; 6% of normal activity;
FT                                alters protein stability and increases
FT                                susceptibility to proteolytic
FT                                degradation; dbSNP:rs75243000).
FT                                {ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_032214.
FT   VARIANT     437    437       V -> F (in perinatal lethal GD;
FT                                dbSNP:rs121908310).
FT                                {ECO:0000269|PubMed:10352942}.
FT                                /FTId=VAR_009048.
FT   VARIANT     437    437       V -> L (in GD3).
FT                                {ECO:0000269|PubMed:8780099}.
FT                                /FTId=VAR_010070.
FT   VARIANT     438    438       D -> N (in GD; type 1 and type 2; 14% of
FT                                normal activity; increases susceptibility
FT                                to proteolytic degradation).
FT                                {ECO:0000269|PubMed:15605411,
FT                                ECO:0000269|PubMed:16293621,
FT                                ECO:0000269|PubMed:8112750}.
FT                                /FTId=VAR_003312.
FT   VARIANT     438    438       D -> Y (in GD).
FT                                {ECO:0000269|PubMed:10796875}.
FT                                /FTId=VAR_032413.
FT   VARIANT     440    440       P -> L (in GD1; dbSNP:rs74598136).
FT                                {ECO:0000269|PubMed:10340647,
FT                                ECO:0000269|PubMed:15605411}.
FT                                /FTId=VAR_010071.
FT   VARIANT     441    441       I -> F (in GD; type 3).
FT                                {ECO:0000269|PubMed:11933202}.
FT                                /FTId=VAR_032414.
FT   VARIANT     441    441       I -> T (in GD; mild; dbSNP:rs75564605).
FT                                {ECO:0000269|PubMed:9182788}.
FT                                /FTId=VAR_010072.
FT   VARIANT     448    448       D -> H (in GD; type 1 and type
FT                                neuronopathic; at homozygosity it causes
FT                                GD3C; also found in a patient with
FT                                Parkinson disease; gene conversion; very
FT                                low activity; alters protein stability;
FT                                dbSNP:rs1064651).
FT                                {ECO:0000269|PubMed:10360404,
FT                                ECO:0000269|PubMed:10447266,
FT                                ECO:0000269|PubMed:10796875,
FT                                ECO:0000269|PubMed:11992489,
FT                                ECO:0000269|PubMed:15605411,
FT                                ECO:0000269|PubMed:16293621,
FT                                ECO:0000269|PubMed:19286695,
FT                                ECO:0000269|PubMed:7627184,
FT                                ECO:0000269|PubMed:9040001,
FT                                ECO:0000269|PubMed:9061570}.
FT                                /FTId=VAR_003313.
FT   VARIANT     448    448       D -> V (in GD; severe; very low activity;
FT                                alters protein stability;
FT                                dbSNP:rs77369218).
FT                                /FTId=VAR_003314.
FT   VARIANT     450    450       F -> I (in GD).
FT                                /FTId=VAR_010073.
FT   VARIANT     451    451       Y -> H (in GD).
FT                                {ECO:0000269|PubMed:9554746}.
FT                                /FTId=VAR_003315.
FT   VARIANT     452    452       K -> Q (in GD).
FT                                {ECO:0000269|PubMed:9061570}.
FT                                /FTId=VAR_010074.
FT   VARIANT     454    454       P -> R (in GD; type 2;
FT                                dbSNP:rs121908295).
FT                                /FTId=VAR_003316.
FT   VARIANT     455    455       M -> V (in GD; loss of activity;
FT                                increases susceptibility to proteolytic
FT                                degradation).
FT                                {ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_032215.
FT   VARIANT     456    456       F -> V (in GD).
FT                                /FTId=VAR_003317.
FT   VARIANT     457    457       Y -> C (in GD; dbSNP:rs74752878).
FT                                {ECO:0000269|PubMed:15605411,
FT                                ECO:0000269|PubMed:8076951}.
FT                                /FTId=VAR_003318.
FT   VARIANT     460    460       G -> D (in GD1; associated with R-490;
FT                                loss of activity).
FT                                {ECO:0000269|PubMed:15605411}.
FT                                /FTId=VAR_032415.
FT   VARIANT     464    464       K -> E (in GD; severe).
FT                                /FTId=VAR_003319.
FT   VARIANT     482    482       D -> N (in a patient with Parkinson
FT                                disease; dbSNP:rs75671029).
FT                                {ECO:0000269|PubMed:19286695}.
FT                                /FTId=VAR_063067.
FT   VARIANT     483    483       L -> P (in GD1 and GD2; common mutation;
FT                                associated with susceptibility to
FT                                Parkinson disease; gene conversion; very
FT                                low activity; alters protein stability;
FT                                dbSNP:rs421016).
FT                                {ECO:0000269|PubMed:10360404,
FT                                ECO:0000269|PubMed:10447266,
FT                                ECO:0000269|PubMed:10796875,
FT                                ECO:0000269|PubMed:15605411,
FT                                ECO:0000269|PubMed:16293621,
FT                                ECO:0000269|PubMed:19286695,
FT                                ECO:0000269|PubMed:7627184,
FT                                ECO:0000269|PubMed:8937765,
FT                                ECO:0000269|PubMed:9061570,
FT                                ECO:0000269|PubMed:9217217,
FT                                ECO:0000269|PubMed:9851895}.
FT                                /FTId=VAR_003321.
FT   VARIANT     483    483       L -> R (in GD; severe; dbSNP:rs421016).
FT                                /FTId=VAR_003320.
FT   VARIANT     485    485       A -> P (in GD).
FT                                /FTId=VAR_003322.
FT   VARIANT     490    490       H -> R (in GD; type 1; associated with D-
FT                                460; dbSNP:rs76071730).
FT                                {ECO:0000269|PubMed:12204005,
FT                                ECO:0000269|PubMed:15605411}.
FT                                /FTId=VAR_032416.
FT   VARIANT     495    495       A -> P (in GD; gene conversion;
FT                                dbSNP:rs368060).
FT                                {ECO:0000269|PubMed:19286695}.
FT                                /FTId=VAR_003323.
FT   VARIANT     497    497       V -> L. {ECO:0000269|PubMed:19286695}.
FT                                /FTId=VAR_063068.
FT   VARIANT     500    500       L -> P (in GD; 10% of normal activity;
FT                                increases susceptibility to proteolytic
FT                                degradation).
FT                                {ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_032216.
FT   VARIANT     501    501       N -> K (in GD; type 2).
FT                                {ECO:0000269|PubMed:9279145}.
FT                                /FTId=VAR_009049.
FT   VARIANT     502    502       R -> C (in GD; 37% of normal activity;
FT                                also found in patients with Parkinson
FT                                disease; dbSNP:rs80356771).
FT                                {ECO:0000269|PubMed:10796875,
FT                                ECO:0000269|PubMed:19286695,
FT                                ECO:0000269|PubMed:1972019,
FT                                ECO:0000269|PubMed:7627184}.
FT                                /FTId=VAR_003324.
FT   VARIANT     502    502       R -> P (in GD; loss of activity;
FT                                increases susceptibility to proteolytic
FT                                degradation).
FT                                {ECO:0000269|PubMed:16293621}.
FT                                /FTId=VAR_032217.
FT   VARIANT     509    509       L -> P.
FT                                /FTId=VAR_003325.
FT   VARIANT     513    513       D -> Y (in GD2).
FT                                {ECO:0000269|PubMed:9637431}.
FT                                /FTId=VAR_009050.
FT   VARIANT     517    517       G -> S (in GD; dbSNP:rs121908301).
FT                                /FTId=VAR_003326.
FT   VARIANT     530    530       T -> I (in GD3; dbSNP:rs78016673).
FT                                {ECO:0000269|PubMed:8780099}.
FT                                /FTId=VAR_010075.
FT   VARIANT     535    535       R -> C (in GD; mild; dbSNP:rs747506979).
FT                                {ECO:0000269|PubMed:9061570}.
FT                                /FTId=VAR_003327.
FT   VARIANT     535    535       R -> H (in GD; mild; dbSNP:rs75822236).
FT                                {ECO:0000269|PubMed:7916532}.
FT                                /FTId=VAR_003328.
FT   MUTAGEN      43     43       C->S: Loss of activity.
FT                                {ECO:0000269|PubMed:16293621}.
FT   MUTAGEN      57     57       C->S: Loss of activity.
FT                                {ECO:0000269|PubMed:16293621}.
FT   MUTAGEN      62     62       C->S: Loss of activity.
FT                                {ECO:0000269|PubMed:16293621}.
FT   MUTAGEN     379    379       E->G: Decreases activity 1000-fold.
FT                                {ECO:0000269|PubMed:7908905}.
FT   CONFLICT    176    176       D -> G (in Ref. 7; BAH13357).
FT                                {ECO:0000305}.
FT   CONFLICT    227    227       N -> R (in Ref. 5; BAA02546).
FT                                {ECO:0000305}.
FT   CONFLICT    470    470       S -> I (in Ref. 15; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    534    534       R -> H (in Ref. 1; AAA35873).
FT                                {ECO:0000305}.
FT   STRAND       49     52       {ECO:0000244|PDB:2NT0}.
FT   STRAND       54     57       {ECO:0000244|PDB:2NT0}.
FT   STRAND       75     82       {ECO:0000244|PDB:2NT0}.
FT   STRAND       88     94       {ECO:0000244|PDB:2NT0}.
FT   STRAND       96     98       {ECO:0000244|PDB:2NT0}.
FT   STRAND      103    116       {ECO:0000244|PDB:2NT0}.
FT   STRAND      119    123       {ECO:0000244|PDB:2NT0}.
FT   HELIX       126    133       {ECO:0000244|PDB:2NT0}.
FT   HELIX       137    148       {ECO:0000244|PDB:2NT0}.
FT   TURN        150    153       {ECO:0000244|PDB:2NT0}.
FT   STRAND      157    163       {ECO:0000244|PDB:2NT0}.
FT   STRAND      166    170       {ECO:0000244|PDB:2NT0}.
FT   STRAND      177    179       {ECO:0000244|PDB:1OGS}.
FT   HELIX       190    193       {ECO:0000244|PDB:2NT0}.
FT   HELIX       196    206       {ECO:0000244|PDB:2NT0}.
FT   STRAND      212    218       {ECO:0000244|PDB:2NT0}.
FT   HELIX       222    224       {ECO:0000244|PDB:2NT0}.
FT   STRAND      225    227       {ECO:0000244|PDB:2J25}.
FT   STRAND      229    233       {ECO:0000244|PDB:2NT0}.
FT   STRAND      235    238       {ECO:0000244|PDB:2NT0}.
FT   HELIX       243    261       {ECO:0000244|PDB:2NT0}.
FT   STRAND      267    271       {ECO:0000244|PDB:2NT0}.
FT   HELIX       275    279       {ECO:0000244|PDB:2NT0}.
FT   STRAND      284    286       {ECO:0000244|PDB:3GXF}.
FT   HELIX       292    301       {ECO:0000244|PDB:2NT0}.
FT   HELIX       303    308       {ECO:0000244|PDB:2NT0}.
FT   TURN        311    314       {ECO:0000244|PDB:2NT0}.
FT   STRAND      315    323       {ECO:0000244|PDB:2NT0}.
FT   HELIX       324    326       {ECO:0000244|PDB:2NT0}.
FT   HELIX       329    335       {ECO:0000244|PDB:2NT0}.
FT   HELIX       338    341       {ECO:0000244|PDB:2NT0}.
FT   STRAND      346    352       {ECO:0000244|PDB:2NT0}.
FT   HELIX       354    356       {ECO:0000244|PDB:3GXI}.
FT   HELIX       359    369       {ECO:0000244|PDB:2NT0}.
FT   STRAND      373    381       {ECO:0000244|PDB:2NT0}.
FT   STRAND      386    388       {ECO:0000244|PDB:2J25}.
FT   HELIX       396    411       {ECO:0000244|PDB:2NT0}.
FT   STRAND      414    424       {ECO:0000244|PDB:2NT0}.
FT   STRAND      426    428       {ECO:0000244|PDB:3KEH}.
FT   STRAND      440    444       {ECO:0000244|PDB:2NT0}.
FT   HELIX       445    447       {ECO:0000244|PDB:2NT0}.
FT   STRAND      449    452       {ECO:0000244|PDB:2NT0}.
FT   HELIX       454    463       {ECO:0000244|PDB:2NT0}.
FT   STRAND      471    479       {ECO:0000244|PDB:2NT0}.
FT   STRAND      482    489       {ECO:0000244|PDB:2NT0}.
FT   STRAND      495    501       {ECO:0000244|PDB:2NT0}.
FT   STRAND      503    505       {ECO:0000244|PDB:2NT0}.
FT   STRAND      507    513       {ECO:0000244|PDB:2NT0}.
FT   TURN        514    516       {ECO:0000244|PDB:2NT0}.
FT   STRAND      517    523       {ECO:0000244|PDB:2NT0}.
FT   STRAND      527    533       {ECO:0000244|PDB:2NT0}.
SQ   SEQUENCE   536 AA;  59716 MW;  FA1E15684344A0E6 CRC64;
     MEFSSPSREE CPKPLSRVSI MAGSLTGLLL LQAVSWASGA RPCIPKSFGY SSVVCVCNAT
     YCDSFDPPTF PALGTFSRYE STRSGRRMEL SMGPIQANHT GTGLLLTLQP EQKFQKVKGF
     GGAMTDAAAL NILALSPPAQ NLLLKSYFSE EGIGYNIIRV PMASCDFSIR TYTYADTPDD
     FQLHNFSLPE EDTKLKIPLI HRALQLAQRP VSLLASPWTS PTWLKTNGAV NGKGSLKGQP
     GDIYHQTWAR YFVKFLDAYA EHKLQFWAVT AENEPSAGLL SGYPFQCLGF TPEHQRDFIA
     RDLGPTLANS THHNVRLLML DDQRLLLPHW AKVVLTDPEA AKYVHGIAVH WYLDFLAPAK
     ATLGETHRLF PNTMLFASEA CVGSKFWEQS VRLGSWDRGM QYSHSIITNL LYHVVGWTDW
     NLALNPEGGP NWVRNFVDSP IIVDITKDTF YKQPMFYHLG HFSKFIPEGS QRVGLVASQK
     NDLDAVALMH PDGSAVVVVL NRSSKDVPLT IKDPAVGFLE TISPGYSIHT YLWRRQ
//
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