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Glucosylceramidase (EC 3.2.1.45) (Acid beta-glucosidase) (Alglucerase) (Beta-glucocerebrosidase) (Beta-GC) (D-glucosyl-N-acylsphingosine glucohydrolase) (Imiglucerase)

 GLCM_HUMAN              Reviewed;         536 AA.
P04062; A8K796; B7Z5G2; B7Z6S1; J3KQG4; J3KQK9; Q16545; Q4VX22;
Q6I9R6; Q9UMJ8;
01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
09-NOV-2004, sequence version 3.
22-NOV-2017, entry version 224.
RecName: Full=Glucosylceramidase;
EC=3.2.1.45;
AltName: Full=Acid beta-glucosidase;
AltName: Full=Alglucerase;
AltName: Full=Beta-glucocerebrosidase;
Short=Beta-GC;
AltName: Full=D-glucosyl-N-acylsphingosine glucohydrolase;
AltName: Full=Imiglucerase;
Flags: Precursor;
Name=GBA; Synonyms=GC, GLUC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
TISSUE=Placenta;
PubMed=3864160; DOI=10.1073/pnas.82.21.7289;
Sorge J., West C., Westwood B., Beutler E.;
"Molecular cloning and nucleotide sequence of human glucocerebrosidase
cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 82:7289-7293(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND VARIANT LEU-298.
TISSUE=Hepatoma;
PubMed=3001061;
Tsuji S., Choudary P.V., Martin B.M., Winfield S., Barranger J.A.,
Ginns E.I.;
"Nucleotide sequence of cDNA containing the complete coding sequence
for human lysosomal glucocerebrosidase.";
J. Biol. Chem. 261:50-53(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=2914709; DOI=10.1016/0888-7543(89)90319-4;
Horowitz M., Wilder S., Horowitz Z., Reiner O., Gelbart T.,
Beutler E.;
"The human glucocerebrosidase gene and pseudogene: structure and
evolution.";
Genomics 4:87-96(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=1572652; DOI=10.1016/0888-7543(92)90311-F;
Beutler E., West C., Gelbart T.;
"Polymorphisms in the human glucocerebrosidase gene.";
Genomics 12:795-800(1992).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND 3), VARIANTS GD ARG-223;
GLY-230; PRO-235; ARG-241; ILE-252 AND ARG-364, AND VARIANTS GLY-310
AND HIS-368.
PubMed=8294033; DOI=10.1016/0378-1119(93)90497-Q;
Imai K., Nakamura M., Yamada M., Asano A., Yokoyama S., Tsuji S.,
Ginns E.I.;
"A novel transcript from a pseudogene for human glucocerebrosidase in
non-Gaucher disease cells.";
Gene 136:365-368(1993).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9331372;
Winfield S.L., Tayebi N., Martin B.M., Ginns E.I., Sidransky E.;
"Identification of three additional genes contiguous to the
glucocerebrosidase locus on chromosome 1q21: implications for Gaucher
disease.";
Genome Res. 7:1020-1026(1997).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG; 4 AND 5), AND
VARIANT MET-408.
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-11.
PubMed=3359914; DOI=10.1089/dna.1988.7.107;
Reiner O., Wigderson M., Horowitz M.;
"Structural analysis of the human glucocerebrosidase genes.";
DNA 7:107-116(1988).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
PubMed=3687939;
Sorge J.A., West C., Kuhl W., Treger L., Beutler E.;
"The human glucocerebrosidase gene has two functional ATG initiator
codons.";
Am. J. Hum. Genet. 41:1016-1024(1987).
[12]
PROTEIN SEQUENCE OF 40-44.
TISSUE=Placenta;
Martin B.M., Murray G.J., Coligan J.E., Raum M., Brady R.O.,
Barranger J.A.;
"Structural studies of human placental glucocerebrosidase.";
Fed. Proc. 43:1869-1869(1984).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 403-416.
PubMed=6091633; DOI=10.1016/0006-291X(84)90268-7;
Ginns E.I., Choudary P.V., Martin B.M., Winfield S., Stubblefield B.,
Mayor J., Merkle-Lehman D., Murray G.J., Bowers L.A., Barranger J.A.;
"Isolation of cDNA clones for human beta-glucocerebrosidase using the
lambda gt11 expression system.";
Biochem. Biophys. Res. Commun. 123:574-580(1984).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 409-462, AND VARIANT GD1 SER-409.
TISSUE=Skin;
Tsuji S., Martin B.M., Barranger J.A., Stubblefield B.K.,
LaMarca M.E., Ginns E.I.;
"Genetic heterogeneity in type 1 Gaucher disease: multiple genotypes
in Ashkenazic and non-Ashkenazic individuals.";
Proc. Natl. Acad. Sci. U.S.A. 85:2349-2352(1988).
[15]
PROTEIN SEQUENCE OF 469-520.
TISSUE=Placenta;
PubMed=3456607; DOI=10.1073/pnas.83.6.1660;
Dinur T., Osiecki K.M., Legler G., Gatt S., Desnick R.J.,
Grabowski G.A.;
"Human acid beta-glucosidase: isolation and amino acid sequence of a
peptide containing the catalytic site.";
Proc. Natl. Acad. Sci. U.S.A. 83:1660-1664(1986).
[16]
MUTAGENESIS OF GLU-379, ACTIVE SITE, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=7908905;
Miao S., McCarter J.D., Grace M.E., Grabowski G.A., Aebersold R.,
Withers S.G.;
"Identification of Glu340 as the active-site nucleophile in human
glucocerebrosidase by use of electrospray tandem mass spectrometry.";
J. Biol. Chem. 269:10975-10978(1994).
[17]
INTERACTION WITH SAPOSIN-C AND MEMBRANES CONTAINING ANIONIC
PHOSPHOLIPIDS.
PubMed=10781797; DOI=10.1016/S0014-5793(00)01417-4;
Salvioli R., Tatti M., Ciaffoni F., Vaccaro A.M.;
"Further studies on the reconstitution of glucosylceramidase activity
by Sap C and anionic phospholipids.";
FEBS Lett. 472:17-21(2000).
[18]
GLYCOSYLATION AT ASN-98; ASN-185 AND ASN-309.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[19]
SUBCELLULAR LOCATION, AND INTERACTION WITH SCARB2.
PubMed=18022370; DOI=10.1016/j.cell.2007.10.018;
Reczek D., Schwake M., Schroder J., Hughes H., Blanz J., Jin X.,
Brondyk W., Van Patten S., Edmunds T., Saftig P.;
"LIMP-2 is a receptor for lysosomal mannose-6-phosphate-independent
targeting of beta-glucocerebrosidase.";
Cell 131:770-783(2007).
[20]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Placenta;
PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B.,
Schaefer H., Elsaesser H.-P., Mann M., Hasilik A.;
"Integral and associated lysosomal membrane proteins.";
Traffic 8:1676-1686(2007).
[21]
INVOLVEMENT IN PARKINSON DISEASE, AND VARIANTS GLU-46; CYS-170;
GLU-232; GLN-296; SER-409; ALA-419; HIS-448; ASN-482; PRO-483;
PRO-495; LEU-497 AND CYS-502.
PubMed=19286695; DOI=10.1093/brain/awp044;
Neumann J., Bras J., Deas E., O'Sullivan S.S., Parkkinen L.,
Lachmann R.H., Li A., Holton J., Guerreiro R., Paudel R., Segarane B.,
Singleton A., Lees A., Hardy J., Houlden H., Revesz T., Wood N.W.;
"Glucocerebrosidase mutations in clinical and pathologically proven
Parkinson's disease.";
Brain 132:1783-1794(2009).
[22]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98 AND ASN-309.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[24]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 40-536, GLYCOSYLATION AT
ASN-58, AND DISULFIDE BONDS.
PubMed=12792654; DOI=10.1038/sj.embor.embor873;
Dvir H., Harel M., McCarthy A.A., Toker L., Silman I., Futerman A.H.,
Sussman J.L.;
"X-ray structure of human acid-beta-glucosidase, the defective enzyme
in Gaucher disease.";
EMBO Rep. 4:704-709(2003).
[25]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 40-536 IN COMPLEX WITH
SYNTHETIC INHIBITOR, AND ACTIVE SITE.
PubMed=15817452; DOI=10.1074/jbc.M502799200;
Premkumar L., Sawkar A.R., Boldin-Adamsky S., Toker L., Silman I.,
Kelly J.W., Futerman A.H., Sussman J.L.;
"X-ray structure of human acid-beta-glucosidase covalently bound to
conduritol-B-epoxide. Implications for Gaucher disease.";
J. Biol. Chem. 280:23815-23819(2005).
[26]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 40-536, CHARACTERIZATION OF
VARIANTS GD SER-55; GLN-87; ASN-118; GLN-159; LEU-161; VAL-162;
VAL-166; ASN-200; PHE-213; PHE-224; GLU-232; GLU-237; LEU-298;
ILE-303; CYS-343; ILE-362; LYS-365; GLY-381; LYS-388; TRP-392;
CYS-402; SER-409; VAL-410; HIS-419; LYS-421; ARG-429; LEU-433;
SER-436; ASN-438; HIS-448; VAL-455; PRO-483; PRO-500 AND PRO-502, AND
MUTAGENESIS OF CYS-43; CYS-57 AND CYS-62.
PubMed=16293621; DOI=10.1074/jbc.M511110200;
Liou B., Kazimierczuk A., Zhang M., Scott C.R., Hegde R.S.,
Grabowski G.A.;
"Analyses of variant acid beta-glucosidases: effects of Gaucher
disease mutations.";
J. Biol. Chem. 281:4242-4253(2006).
[27]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 40-536, AND GLYCOSYLATION AT
ASN-58; ASN-98 AND ASN-185.
PubMed=17139081; DOI=10.1107/S0907444906038303;
Brumshtein B., Wormald M.R., Silman I., Futerman A.H., Sussman J.L.;
"Structural comparison of differently glycosylated forms of acid-beta-
glucosidase, the defective enzyme in Gaucher disease.";
Acta Crystallogr. D 62:1458-1465(2006).
[28]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 40-536 IN COMPLEXES WITH
ISOFAGOMINE, AND SUBCELLULAR LOCATION.
PubMed=17187079; DOI=10.1038/nchembio850;
Lieberman R.L., Wustman B.A., Huertas P., Powe A.C. Jr., Pine C.W.,
Khanna R., Schlossmacher M.G., Ringe D., Petsko G.A.;
"Structure of acid beta-glucosidase with pharmacological chaperone
provides insight into Gaucher disease.";
Nat. Chem. Biol. 3:101-107(2007).
[29]
REVIEW ON GD VARIANTS.
PubMed=8118460; DOI=10.1002/humu.1380030102;
Horowitz M., Zimran A.;
"Mutations causing Gaucher disease.";
Hum. Mutat. 3:1-11(1994).
[30]
REVIEW ON GD VARIANTS.
PubMed=8889578;
DOI=10.1002/(SICI)1098-1004(1996)8:3<207::AID-HUMU2>3.3.CO;2-5;
Beutler E., Gelbart T.;
"Glucocerebrosidase (Gaucher disease).";
Hum. Mutat. 8:207-213(1996).
[31]
REVIEW ON GD VARIANTS.
PubMed=10527671; DOI=10.1006/mgme.1999.2918;
Tayebi N., Stone D.L., Sidransky E.;
"Type 2 Gaucher disease: an expanding phenotype.";
Mol. Genet. Metab. 68:209-219(1999).
[32]
REVIEW ON GD VARIANTS.
PubMed=10649495;
DOI=10.1002/(SICI)1098-1004(200002)15:2<181::AID-HUMU7>3.3.CO;2-J;
Stone D.L., Tayebi N., Orvisky E., Stubblefield B., Madike V.,
Sidransky E.;
"Glucocerebrosidase gene mutations in patients with type 2 Gaucher
disease.";
Hum. Mutat. 15:181-188(2000).
[33]
VARIANT GD TYR-255.
PubMed=1974409; DOI=10.1111/j.1469-1809.1990.tb00371.x;
Beutler E., Gelbart T.;
"Gaucher disease associated with a unique KpnI restriction site:
identification of the amino-acid substitution.";
Ann. Hum. Genet. 54:149-153(1990).
[34]
VARIANT GD CYS-502, AND CHARACTERIZATION OF VARIANT GD CYS-502.
PubMed=1972019; DOI=10.1089/dna.1990.9.233;
Hong C.M., Ohashi T., Yu X.J., Weiler S., Barranger J.A.;
"Sequence of two alleles responsible for Gaucher disease.";
DNA Cell Biol. 9:233-241(1990).
[35]
VARIANTS GD.
PubMed=8432537; DOI=10.1006/geno.1993.1035;
Beutler E., Gelbart T., West C.;
"Identification of six new Gaucher disease mutations.";
Genomics 15:203-205(1993).
[36]
VARIANT GD HIS-535.
PubMed=7916532; DOI=10.1002/ajmg.1320510216;
Choy F.Y.M., Wei C., Applegarth D.A., McGillivray B.C.;
"DNA analysis of an uncommon missense mutation in a Gaucher disease
patient of Jewish-Polish-Russian descent.";
Am. J. Med. Genet. 51:156-160(1994).
[37]
VARIANT GD ASN-438.
PubMed=8112750; DOI=10.1007/BF00210614;
Beutler E., Gelbart T.;
"Two new Gaucher disease mutations.";
Hum. Genet. 93:209-210(1994).
[38]
VARIANTS GD SER-409 AND CYS-457.
PubMed=8076951; DOI=10.1007/BF00208292;
Tuteja R., Tuteja N., Lilliu F., Bembi B., Galanello R., Cao A.,
Baralle F.E.;
"Y418C: a novel mutation in exon 9 of the glucocerebrosidase gene of a
patient with Gaucher disease creates a new Bgl I site.";
Hum. Genet. 94:314-315(1994).
[39]
VARIANTS GD ASP-215; THR-221; ARG-241; GLN-296; CYS-324; GLY-417 AND
ASN-419.
PubMed=8790604;
Beutler E., Demina A., Gelbart T.;
"Glucocerebrosidase mutations in Gaucher disease.";
Mol. Med. 1:82-92(1994).
[40]
VARIANTS GD SER-409; HIS-448; PRO-483 AND CYS-502.
PubMed=7627184; DOI=10.1002/humu.1380050406;
Cormand B., Vilageliu L., Burguera J.M., Balcells S.,
Gonzalez-Duarte R., Grinberg D., Chabas A.;
"Gaucher disease in Spanish patients: analysis of eight mutations.";
Hum. Mutat. 5:303-309(1995).
[41]
VARIANT GD SER-217.
PubMed=7627192; DOI=10.1002/humu.1380050414;
Choy F.Y.M., Wei C.;
"Identification of a new mutation (P178S) in an African-American
patient with type 2 Gaucher disease.";
Hum. Mutat. 5:345-347(1995).
[42]
VARIANTS GD SER-409; LEU-426; LEU-433 AND PRO-483.
PubMed=8937765;
Morar B., Lane A.B.;
"The molecular characterization of Gaucher disease in South Africa.";
Clin. Genet. 50:78-84(1996).
[43]
VARIANTS GD LEU-54; GLU-85 AND SER-227.
PubMed=8829654;
DOI=10.1002/(SICI)1098-1004(1996)7:3<214::AID-HUMU5>3.0.CO;2-A;
Kim J.-W., Liou B.B., Lai M.-Y., Ponce E., Grabowski G.A.;
"Gaucher disease: identification of three new mutations in the Korean
and Chinese (Taiwanese) populations.";
Hum. Mutat. 7:214-218(1996).
[44]
VARIANTS GD HIS-352 AND GLN-398.
PubMed=8829663;
DOI=10.1002/(SICI)1098-1004(1996)7:3<272::AID-HUMU14>3.3.CO;2-7;
Cormand B., Vilageliu L., Balcells S., Gonzalez-Duatre R., Chabas A.,
Grinberg D.;
"Two novel (1098insA and Y313H) and one rare (R359Q) mutations
detected in exon 8 of the beta-glucocerebrosidase gene in Gaucher's
disease patients.";
Hum. Mutat. 7:272-274(1996).
[45]
VARIANT GD1 THR-435.
PubMed=8889591;
DOI=10.1002/(SICI)1098-1004(1996)8:3<280::AID-HUMU15>3.3.CO;2-6;
Amaral O., Pinto E., Fortuna M., Lacerda L., Sa Miranda M.C.;
"Type 1 Gaucher disease: identification of N396T and prevalence of
glucocerebrosidase mutations in the Portuguese.";
Hum. Mutat. 8:280-281(1996).
[46]
VARIANTS GD3 LEU-437 AND ILE-530.
PubMed=8780099; DOI=10.1212/WNL.46.4.1102;
Seeman P.J.V., Finckh U., Hoeppner J., Lakner V., Liebisch I.,
Grau G., Rolfs A.;
"Two new missense mutations in a non-Jewish Caucasian family with type
3 Gaucher disease.";
Neurology 46:1102-1107(1996).
[47]
VARIANTS GD LEU-414 AND THR-441.
PubMed=9182788;
DOI=10.1002/(SICI)1096-8628(19970627)70:4<437::AID-AJMG19>3.0.CO;2-I;
Cormand B., Grinberg D., Gort L., Fiumara A., Barone R., Vilageliu L.,
Chabas A.;
"Two new mild homozygous mutations in Gaucher disease patients:
clinical signs and biochemical analyses.";
Am. J. Med. Genet. 70:437-443(1997).
[48]
VARIANTS GD VAL-76; GLU-85; TRP-87; TRP-159; SER-227; ILE-252 AND
PRO-483.
PubMed=9217217;
DOI=10.1002/(SICI)1096-8628(19970808)71:2<172::AID-AJMG10>3.0.CO;2-B;
Choy F.Y.M., Humphries M.L., Shi H.;
"Identification of two novel and four uncommon missense mutations
among Chinese Gaucher disease patients.";
Am. J. Med. Genet. 71:172-178(1997).
[49]
VARIANT GD LYS-501.
PubMed=9279145; DOI=10.1136/adc.77.1.17;
Hatton C.E., Cooper A., Whitehouse C., Wraith J.E.;
"Mutation analysis in 46 British and Irish patients with Gaucher's
disease.";
Arch. Dis. Child. 77:17-22(1997).
[50]
VARIANTS GD TRP-87; GLU-234; ARG-241; ILE-252; ASN-310; LEU-391 AND
SER-409.
PubMed=9153297; DOI=10.1172/JCI119437;
Grace M.E., Desnick R.J., Pastores G.M.;
"Identification and expression of acid beta-glucosidase mutations
causing severe type 1 and neurologic type 2 Gaucher disease in non-
Jewish patients.";
J. Clin. Invest. 99:2530-2537(1997).
[51]
VARIANTS GD VAL-228; ILE-252; GLY-405; HIS-448; GLN-452; PRO-483 AND
CYS-535.
PubMed=9061570; DOI=10.1023/A:1005313724361;
Ida H., Rennert O.M., Kawame H., Maekawa K., Eto Y.;
"Mutation prevalence among 47 unrelated Japanese patients with Gaucher
disease: identification of four novel mutations.";
J. Inherit. Metab. Dis. 20:67-73(1997).
[52]
VARIANT PSEUDO-GAUCHER HIS-448.
PubMed=9040001; DOI=10.1136/jmg.34.2.175;
Uyama E., Uchino M., Ida H., Eto Y., Owada M.;
"D409H/D409H genotype in Gaucher-like disease.";
J. Med. Genet. 34:175-175(1997).
[53]
VARIANTS GD LEU-146; LEU-198; THR-380; ASN-405 AND ARG-432.
PubMed=9554454; DOI=10.1159/000040815;
Demina A., Beutler E.;
"Six new Gaucher disease mutations.";
Acta Haematol. 99:80-82(1998).
[54]
VARIANTS GD.
PubMed=9683600; DOI=10.1086/301969;
Germain D.P., Puech J.-P., Caillaud C., Kahn A., Poenaru L.;
"Exhaustive screening of the acid beta-glucosidase gene, by
fluorescence-assisted mismatch analysis using universal primers:
mutation profile and genotype/phenotype correlations in Gaucher
disease.";
Am. J. Hum. Genet. 63:415-427(1998).
[55]
VARIANT GD2 TYR-513.
PubMed=9637431;
DOI=10.1002/(SICI)1096-8628(19980616)78:1<92::AID-AJMG19>3.0.CO;2-J;
Choy F.Y.M., Humphries M.L., Ben-Yoseph Y.;
"Gaucher type 2 disease: identification of a novel transversion
mutation in a French-Irish patient.";
Am. J. Med. Genet. 78:92-93(1998).
[56]
VARIANTS GD.
PubMed=9516376; DOI=10.1006/bcmd.1998.0165;
Beutler E., Gelbart T.;
"Hematologically important mutations: Gaucher disease.";
Blood Cells Mol. Dis. 24:2-8(1998).
[57]
VARIANTS GD2 LYS-80; CYS-170 AND PRO-483.
PubMed=9851895; DOI=10.1006/bcmd.1998.0210;
Sinclair G., Choy F.Y.M., Humphries L.;
"A novel complex allele and two new point mutations in type 2 (acute
neuronopathic) Gaucher disease.";
Blood Cells Mol. Dis. 24:420-427(1998).
[58]
VARIANT GD GLY-392.
PubMed=9650766;
Parenti G., Filocamo M., Titomanlio L., Rizzolo G., Silvestro E.,
Perretti A., Gatti R., Andria G.;
"A novel mutation of the beta-glucocerebrosidase gene associated with
neurologic manifestations in three sibs.";
Clin. Genet. 53:281-285(1998).
[59]
VARIANTS GD GLU-152; PRO-173; GLU-428; LEU-430; ILE-431 AND HIS-451.
PubMed=9554746;
DOI=10.1002/(SICI)1098-1004(1998)11:4<295::AID-HUMU7>3.0.CO;2-6;
Cormand B., Grinberg D., Gort L., Chabas A., Vilageliu L.;
"Molecular analysis and clinical findings in the Spanish Gaucher
disease population: putative haplotype of the N370S ancestral
chromosome.";
Hum. Mutat. 11:295-305(1998).
[60]
VARIANTS GD1 GLY-230 AND SER-409.
PubMed=10206680;
DOI=10.1002/(SICI)1098-1004(1998)11:5<411::AID-HUMU13>3.0.CO;2-X;
Choy F.Y.M., Humphries M.L., Ben-Yoseph Y.;
"A novel mutation (V191G) in a German-British type 1 Gaucher disease
patient.";
Hum. Mutat. 11:411-412(1998).
[61]
VARIANTS GD1 SER-409 AND LEU-440.
PubMed=10340647;
DOI=10.1002/(SICI)1096-8628(19990604)84:4<334::AID-AJMG5>3.3.CO;2-G;
Wasserstein M.P., Martignetti J.A., Zeitlin R., Lumerman H.,
Solomon M., Grace M.E., Desnick R.J.;
"Type 1 Gaucher disease presenting with extensive mandibular lytic
lesions: identification and expression of a novel acid beta-
glucosidase mutation.";
Am. J. Med. Genet. 84:334-339(1999).
[62]
VARIANTS GD ARG-241; CYS-244; ILE-252; HIS-448 AND PRO-483.
PubMed=10360404;
DOI=10.1002/(SICI)1096-8628(19990611)84:5<484::AID-AJMG14>3.0.CO;2-W;
Choy F.Y.M., Wong K., Shi H.P.;
"Glucocerebrosidase mutations among Chinese neuronopathic and non-
neuronopathic Gaucher disease patients.";
Am. J. Med. Genet. 84:484-486(1999).
[63]
VARIANTS GD.
PubMed=10744424;
Hodanov K., Hrebicek M., Cervenkov M., Mrzov L., Veprekov L.,
Zemen J.;
"Analysis of the beta-glucocerebrosidase gene in Czech and Slovak
Gaucher patients: mutation profile and description of six novel mutant
alleles.";
Blood Cells Mol. Dis. 25:287-298(1999).
[64]
VARIANTS PERINATAL LETHAL GD ARG-350 AND PHE-437.
PubMed=10352942; DOI=10.1038/sj.ejhg.5200315;
Stone D.L., van Diggelen O.P., de Klerk J.B.C., Gaillard J.L.J.,
Niermeijer M.F., Willemsen R., Tayebi N., Sidransky E.;
"Is the perinatal lethal form of Gaucher disease more common than
classic type 2 Gaucher disease?";
Eur. J. Hum. Genet. 7:505-509(1999).
[65]
VARIANTS GD PRO-173; TRP-234; SER-409; SER-416; HIS-448 AND PRO-483.
PubMed=10447266;
DOI=10.1002/(SICI)1098-1004(1999)14:1<88::AID-HUMU16>3.0.CO;2-E;
Sarria A.J., Giraldo P., Perez-Calvo J.I., Pocovi M.;
"Detection of three rare (G377S, T134P and 1451delAC), and two novel
mutations (G195W and Rec[1263del55;1342G>C]] in Spanish Gaucher
disease patients.";
Hum. Mutat. 14:88-88(1999).
[66]
VARIANTS GD TRP-87; ASN-118; THR-129; ASP-156; GLN-159; TRP-159;
LEU-170; ILE-173; CYS-209; PRO-209; SER-227; THR-229; PRO-235;
ARG-241; ILE-252; GLN-296; CYS-324; THR-380; MET-408; SER-409;
SER-416; LEU-433; TYR-438; HIS-448; PRO-483 AND CYS-502, AND VARIANT
LYS-365.
PubMed=10796875; DOI=10.1086/302925;
Koprivica V., Stone D.L., Park J.K., Callahan M., Frisch A.,
Cohen I.J., Tayebi N., Sidransky E.;
"Analysis and classification of 304 mutant alleles in patients with
type 1 and type 3 Gaucher disease.";
Am. J. Hum. Genet. 66:1777-1786(2000).
[67]
VARIANTS GD SER-55 AND HIS-448.
PubMed=11992489; DOI=10.1002/ajmg.10385;
Bodamer O.A.F., Church H.J., Cooper A., Wraith J.E., Scott C.R.,
Scaglia F.;
"Variant Gaucher disease characterized by dysmorphic features, absence
of cardiovascular involvement, laryngospasm, and compound
heterozygosity for a novel mutation (D409H/C16S).";
Am. J. Med. Genet. 109:328-331(2002).
[68]
VARIANTS GD GLU-175; PRO-201; GLU-237; LEU-290 AND PHE-441.
PubMed=11933202; DOI=10.1002/humu.9024;
Orvisky E., Park J.K., Parker A., Walker J.M., Martin B.M.,
Stubblefield B.K., Uyama E., Tayebi N., Sidransky E.;
"The identification of eight novel glucocerebrosidase (GBA) mutations
in patients with Gaucher disease.";
Hum. Mutat. 19:458-459(2002).
[69]
VARIANTS GD THR-198; ARG-241; ARG-270; ILE-400 AND ARG-490.
PubMed=12204005; DOI=10.1002/humu.9058;
Filocamo M., Mazzotti R., Stroppiano M., Seri M., Giona F.,
Parenti G., Regis S., Corsolini F., Zoboli S., Gatti R.;
"Analysis of the glucocerebrosidase gene and mutation profile in 144
Italian Gaucher patients.";
Hum. Mutat. 20:234-235(2002).
[70]
POSSIBLE INVOLVEMENT IN PARKINSON DISEASE.
PubMed=12847165; DOI=10.1212/01.WNL.0000072482.70963.D7;
Bembi B., Zambito Marsala S., Sidransky E., Ciana G., Carrozzi M.,
Zorzon M., Martini C., Gioulis M., Pittis M.G., Capus L.;
"Gaucher's disease with Parkinson's disease: clinical and pathological
aspects.";
Neurology 61:99-101(2003).
[71]
VARIANT GD SER-55.
PubMed=15292921; DOI=10.1038/sj.ejhg.5201251;
Church H.J., Cooper A., Stewart F., Thornton C.M., Wraith J.E.;
"Homozygous loss of a cysteine residue in the glucocerebrosidase gene
results in Gaucher's disease with a hydropic phenotype.";
Eur. J. Hum. Genet. 12:975-978(2004).
[72]
CHARACTERIZATION OF VARIANT GD SER-409.
PubMed=15826241; DOI=10.1042/BJ20050325;
Salvioli R., Tatti M., Scarpa S., Moavero S.M., Ciaffoni F.,
Felicetti F., Kaneski C.R., Brady R.O., Vaccaro A.M.;
"The N370S (Asn370->Ser) mutation affects the capacity of
glucosylceramidase to interact with anionic phospholipid-containing
membranes and saposin C.";
Biochem. J. 390:95-103(2005).
[73]
VARIANTS GD1 ASN-63; SER-158; TRP-159; CYS-170; LEU-221; GLU-230;
ARG-241; GLN-294; CYS-324; SER-409; ASN-438; LEU-440; HIS-448;
CYS-457; ASP-460; PRO-483 AND ARG-490, AND CHARACTERIZATION OF
VARIANTS GD1 ASN-63; SER-158; LEU-221; GLU-230 AND ASP-460.
PubMed=15605411; DOI=10.1002/humu.9301;
Miocic S., Filocamo M., Dominissini S., Montalvo A.L., Vlahovicek K.,
Deganuto M., Mazzotti R., Cariati R., Bembi B., Pittis M.G.;
"Identification and functional characterization of five novel mutant
alleles in 58 Italian patients with Gaucher disease type 1.";
Hum. Mutat. 25:100-100(2005).
[74]
POSSIBLE INVOLVEMENT IN PARKINSON DISEASE.
PubMed=16148263; DOI=10.1212/01.wnl.0000176987.47875.28;
Aharon-Peretz J., Badarny S., Rosenbaum H., Gershoni-Baruch R.;
"Mutations in the glucocerebrosidase gene and Parkinson disease:
phenotype-genotype correlation.";
Neurology 65:1460-1461(2005).
[75]
INVOLVEMENT OF VARIANT GD PRO-483 IN SUSCEPTIBILITY TO PARKINSON
DISEASE.
PubMed=17620502; DOI=10.1001/archneur.64.7.1056;
Tan E.K., Tong J., Fook-Chong S., Yih Y., Wong M.C., Pavanni R.,
Zhao Y.;
"Glucocerebrosidase mutations and risk of Parkinson disease in Chinese
patients.";
Arch. Neurol. 64:1056-1058(2007).
[76]
INVOLVEMENT OF VARIANTS GD SER-409 AND PRO-483 IN SUSCEPTIBILITY TO
PARKINSON DISEASE.
PubMed=18332251; DOI=10.1001/archneurol.2007.68;
Mata I.F., Samii A., Schneer S.H., Roberts J.W., Griffith A.,
Leis B.C., Schellenberg G.D., Sidransky E., Bird T.D., Leverenz J.B.,
Tsuang D., Zabetian C.P.;
"Glucocerebrosidase gene mutations: a risk factor for Lewy body
disorders.";
Arch. Neurol. 65:379-382(2008).
[77]
INVOLVEMENT OF VARIANTS GD SER-409 AND PRO-483 IN SUSCEPTIBILITY TO
PARKINSON DISEASE.
PubMed=19846850; DOI=10.1056/NEJMoa0901281;
Sidransky E., Nalls M.A., Aasly J.O., Aharon-Peretz J., Annesi G.,
Barbosa E.R., Bar-Shira A., Berg D., Bras J., Brice A., Chen C.M.,
Clark L.N., Condroyer C., De Marco E.V., Durr A., Eblan M.J., Fahn S.,
Farrer M.J., Fung H.C., Gan-Or Z., Gasser T., Gershoni-Baruch R.,
Giladi N., Griffith A., Gurevich T., Januario C., Kropp P., Lang A.E.,
Lee-Chen G.J., Lesage S., Marder K., Mata I.F., Mirelman A.,
Mitsui J., Mizuta I., Nicoletti G., Oliveira C., Ottman R.,
Orr-Urtreger A., Pereira L.V., Quattrone A., Rogaeva E., Rolfs A.,
Rosenbaum H., Rozenberg R., Samii A., Samaddar T., Schulte C.,
Sharma M., Singleton A., Spitz M., Tan E.K., Tayebi N., Toda T.,
Troiano A.R., Tsuji S., Wittstock M., Wolfsberg T.G., Wu Y.R.,
Zabetian C.P., Zhao Y., Ziegler S.G.;
"Multicenter analysis of glucocerebrosidase mutations in Parkinson's
disease.";
N. Engl. J. Med. 361:1651-1661(2009).
[78]
VARIANT PRO-363.
PubMed=26528954; DOI=10.1002/ana.24553;
International Parkinsonism Genetics Network;
Olgiati S., Quadri M., Fang M., Rood J.P., Saute J.A., Chien H.F.,
Bouwkamp C.G., Graafland J., Minneboo M., Breedveld G.J., Zhang J.,
Verheijen F.W., Boon A.J., Kievit A.J., Jardim L.B., Mandemakers W.,
Barbosa E.R., Rieder C.R., Leenders K.L., Wang J., Bonifati V.;
"DNAJC6 mutations associated with early-onset Parkinson's disease.";
Ann. Neurol. 79:244-256(2016).
-!- CATALYTIC ACTIVITY: D-glucosyl-N-acylsphingosine + H(2)O = D-
glucose + N-acylsphingosine.
-!- ENZYME REGULATION: Requires saposin-C and anionic phospholipids
for activity.
-!- SUBUNIT: Interacts with saposin-C. Interacts with SCARB2.
{ECO:0000269|PubMed:10781797, ECO:0000269|PubMed:15817452,
ECO:0000269|PubMed:18022370}.
-!- INTERACTION:
P17987:TCP1; NbExp=2; IntAct=EBI-1564609, EBI-356553;
-!- SUBCELLULAR LOCATION: Lysosome membrane
{ECO:0000269|PubMed:17187079, ECO:0000269|PubMed:17897319,
ECO:0000269|PubMed:18022370}; Peripheral membrane protein
{ECO:0000269|PubMed:17187079, ECO:0000269|PubMed:17897319,
ECO:0000269|PubMed:18022370}; Lumenal side
{ECO:0000269|PubMed:17187079, ECO:0000269|PubMed:17897319,
ECO:0000269|PubMed:18022370}. Note=Interaction with saposin-C
promotes membrane association. Targeting to lysosomes occurs
through an alternative MPR-independent mechanism via SCARB2.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=5;
Name=Long;
IsoId=P04062-1; Sequence=Displayed;
Note=Has a 39 residue signal sequence. The upstream initiation
site produces two to three times as much protein as does the
downstream initiation codon.;
Name=Short;
IsoId=P04062-2; Sequence=VSP_018800;
Note=Has a 19 residue signal sequence.;
Name=3;
IsoId=P04062-3; Sequence=VSP_025216, VSP_025217, VSP_025218;
Note=Produced by alternative splicing.;
Name=4;
IsoId=P04062-4; Sequence=VSP_054655;
Note=No experimental confirmation available.;
Name=5;
IsoId=P04062-5; Sequence=VSP_054656;
Note=No experimental confirmation available.;
-!- DISEASE: Gaucher disease (GD) [MIM:230800]: A lysosomal storage
disease due to deficient activity of beta-glucocerebrosidase and
characterized by accumulation of glucosylceramide in the reticulo-
endothelial system. Different clinical forms are recognized
depending on the presence (neuronopathic forms) or absence of
central nervous system involvement, severity and age of onset.
{ECO:0000269|PubMed:10352942, ECO:0000269|PubMed:10360404,
ECO:0000269|PubMed:10447266, ECO:0000269|PubMed:10744424,
ECO:0000269|PubMed:10796875, ECO:0000269|PubMed:11933202,
ECO:0000269|PubMed:11992489, ECO:0000269|PubMed:12204005,
ECO:0000269|PubMed:15292921, ECO:0000269|PubMed:15826241,
ECO:0000269|PubMed:16293621, ECO:0000269|PubMed:17620502,
ECO:0000269|PubMed:18332251, ECO:0000269|PubMed:1972019,
ECO:0000269|PubMed:1974409, ECO:0000269|PubMed:19846850,
ECO:0000269|PubMed:7627184, ECO:0000269|PubMed:7627192,
ECO:0000269|PubMed:7916532, ECO:0000269|PubMed:8076951,
ECO:0000269|PubMed:8112750, ECO:0000269|PubMed:8294033,
ECO:0000269|PubMed:8432537, ECO:0000269|PubMed:8790604,
ECO:0000269|PubMed:8829654, ECO:0000269|PubMed:8829663,
ECO:0000269|PubMed:8937765, ECO:0000269|PubMed:9061570,
ECO:0000269|PubMed:9153297, ECO:0000269|PubMed:9182788,
ECO:0000269|PubMed:9217217, ECO:0000269|PubMed:9279145,
ECO:0000269|PubMed:9516376, ECO:0000269|PubMed:9554454,
ECO:0000269|PubMed:9554746, ECO:0000269|PubMed:9650766,
ECO:0000269|PubMed:9683600}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Gaucher disease 1 (GD1) [MIM:230800]: A form of Gaucher
disease characterized by hepatosplenomegaly with consequent anemia
and thrombopenia, and bone involvement. The central nervous system
is not involved. {ECO:0000269|PubMed:10206680,
ECO:0000269|PubMed:10340647, ECO:0000269|PubMed:15605411,
ECO:0000269|PubMed:8889591, ECO:0000269|Ref.14}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Gaucher disease 2 (GD2) [MIM:230900]: The most severe
form of Gaucher disease. It manifests soon after birth, with death
generally occurring before patients reach two years of age.
{ECO:0000269|PubMed:9637431, ECO:0000269|PubMed:9851895}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Gaucher disease 3 (GD3) [MIM:231000]: A subacute form of
neuronopathic Gaucher disease. It has later onset and slower
progression compared to the acute form of neuronopathic Gaucher
disease 2. {ECO:0000269|PubMed:8780099}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Gaucher disease 3C (GD3C) [MIM:231005]: A variant of
subacute neuronopathic Gaucher disease 3 associated with
cardiovascular calcifications. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Gaucher disease perinatal lethal (GDPL) [MIM:608013]:
Distinct form of Gaucher disease type 2, characterized by fetal
onset. Hydrops fetalis, in utero fetal death and neonatal distress
are prominent features. When hydrops is absent, neurologic
involvement begins in the first week and leads to death within 3
months. Hepatosplenomegaly is a major sign, and is associated with
ichthyosis, arthrogryposis, and facial dysmorphism. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Note=Perinatal lethal Gaucher disease is associated with
non-immune hydrops fetalis, a generalized edema of the fetus with
fluid accumulation in the body cavities due to non-immune causes.
Non-immune hydrops fetalis is not a diagnosis in itself but a
symptom, a feature of many genetic disorders, and the end-stage of
a wide variety of disorders.
-!- DISEASE: Parkinson disease (PARK) [MIM:168600]: A complex
neurodegenerative disorder characterized by bradykinesia, resting
tremor, muscular rigidity and postural instability. Additional
features are characteristic postural abnormalities, dysautonomia,
dystonic cramps, and dementia. The pathology of Parkinson disease
involves the loss of dopaminergic neurons in the substantia nigra
and the presence of Lewy bodies (intraneuronal accumulations of
aggregated proteins), in surviving neurons in various areas of the
brain. The disease is progressive and usually manifests after the
age of 50 years, although early-onset cases (before 50 years) are
known. The majority of the cases are sporadic suggesting a
multifactorial etiology based on environmental and genetic
factors. However, some patients present with a positive family
history for the disease. Familial forms of the disease usually
begin at earlier ages and are associated with atypical clinical
features. {ECO:0000269|PubMed:12847165,
ECO:0000269|PubMed:16148263, ECO:0000269|PubMed:19286695}.
Note=Disease susceptibility may be associated with variations
affecting the gene represented in this entry.
-!- PHARMACEUTICAL: Available under the names Ceredase and Cerezyme
(Genzyme). Used to treat Gaucher's disease.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 30 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Ceredase; Note=Clinical information on
Ceredase;
URL="http://www.rxlist.com/ceredase-drug.htm";
-!- WEB RESOURCE: Name=Cerezyme; Note=Clinical information on
Cerezyme;
URL="https://www.rxlist.com/cerezyme-drug.htm";
-----------------------------------------------------------------------
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EMBL; M16328; AAA35873.1; -; mRNA.
EMBL; K02920; AAA35877.1; -; mRNA.
EMBL; J03059; AAC63056.1; -; Genomic_DNA.
EMBL; D13286; BAA02545.1; -; mRNA.
EMBL; D13287; BAA02546.1; -; mRNA.
EMBL; AF023268; AAC51820.1; -; Genomic_DNA.
EMBL; AK291911; BAF84600.1; -; mRNA.
EMBL; AK298900; BAH12898.1; -; mRNA.
EMBL; AK300829; BAH13357.1; -; mRNA.
EMBL; AL713999; CAI95090.1; -; Genomic_DNA.
EMBL; BC003356; AAH03356.1; -; mRNA.
EMBL; M19285; AAA35880.1; -; mRNA.
EMBL; M18916; AAA35878.1; ALT_SEQ; Genomic_DNA.
EMBL; M18917; AAA35879.1; ALT_SEQ; Genomic_DNA.
EMBL; M20248; AAA35874.1; -; Genomic_DNA.
EMBL; M20282; AAA35876.1; -; Genomic_DNA.
CCDS; CCDS1102.1; -. [P04062-1]
CCDS; CCDS53373.1; -. [P04062-4]
CCDS; CCDS53374.1; -. [P04062-5]
PIR; A94068; EUHUGC.
PIR; I52980; I52980.
PIR; I67792; I67792.
RefSeq; NP_000148.2; NM_000157.3. [P04062-1]
RefSeq; NP_001005741.1; NM_001005741.2. [P04062-1]
RefSeq; NP_001005742.1; NM_001005742.2. [P04062-1]
RefSeq; NP_001165282.1; NM_001171811.1. [P04062-4]
RefSeq; NP_001165283.1; NM_001171812.1. [P04062-5]
UniGene; Hs.282997; -.
PDB; 1OGS; X-ray; 2.00 A; A/B=40-536.
PDB; 1Y7V; X-ray; 2.40 A; A/B=40-536.
PDB; 2F61; X-ray; 2.50 A; A/B=40-536.
PDB; 2J25; X-ray; 2.90 A; A/B=40-536.
PDB; 2NSX; X-ray; 2.11 A; A/B/C/D=40-536.
PDB; 2NT0; X-ray; 1.79 A; A/B/C/D=40-536.
PDB; 2NT1; X-ray; 2.30 A; A/B/C/D=40-536.
PDB; 2V3D; X-ray; 1.96 A; A/B=40-536.
PDB; 2V3E; X-ray; 2.00 A; A/B=40-536.
PDB; 2V3F; X-ray; 1.95 A; A/B=40-536.
PDB; 2VT0; X-ray; 2.15 A; A/B=40-536.
PDB; 2WCG; X-ray; 2.30 A; A/B=40-536.
PDB; 2WKL; X-ray; 2.70 A; A/B=40-536.
PDB; 2XWD; X-ray; 2.66 A; A/B=40-536.
PDB; 2XWE; X-ray; 2.31 A; A/B=40-536.
PDB; 3GXD; X-ray; 2.50 A; A/B/C/D=40-536.
PDB; 3GXF; X-ray; 2.40 A; A/B/C/D=40-536.
PDB; 3GXI; X-ray; 1.84 A; A/B/C/D=40-536.
PDB; 3GXM; X-ray; 2.20 A; A/B/C/D=40-536.
PDB; 3KE0; X-ray; 2.70 A; A/B=40-536.
PDB; 3KEH; X-ray; 2.80 A; A/B=40-536.
PDB; 3RIK; X-ray; 2.48 A; A/B/C/D=40-536.
PDB; 3RIL; X-ray; 2.40 A; A/B/C/D=40-536.
PDBsum; 1OGS; -.
PDBsum; 1Y7V; -.
PDBsum; 2F61; -.
PDBsum; 2J25; -.
PDBsum; 2NSX; -.
PDBsum; 2NT0; -.
PDBsum; 2NT1; -.
PDBsum; 2V3D; -.
PDBsum; 2V3E; -.
PDBsum; 2V3F; -.
PDBsum; 2VT0; -.
PDBsum; 2WCG; -.
PDBsum; 2WKL; -.
PDBsum; 2XWD; -.
PDBsum; 2XWE; -.
PDBsum; 3GXD; -.
PDBsum; 3GXF; -.
PDBsum; 3GXI; -.
PDBsum; 3GXM; -.
PDBsum; 3KE0; -.
PDBsum; 3KEH; -.
PDBsum; 3RIK; -.
PDBsum; 3RIL; -.
ProteinModelPortal; P04062; -.
SMR; P04062; -.
BioGrid; 108899; 48.
DIP; DIP-38645N; -.
IntAct; P04062; 32.
MINT; MINT-3004354; -.
STRING; 9606.ENSP00000314508; -.
BindingDB; P04062; -.
ChEMBL; CHEMBL2179; -.
DrugBank; DB03106; Myo-Inositol.
DrugBank; DB03740; N-acetyl-alpha-D-glucosamine.
DrugBank; DB06720; Velaglucerase alfa.
SwissLipids; SLP:000001387; -.
Allergome; 8244; Hom s Glucocerebrosidase.
CAZy; GH30; Glycoside Hydrolase Family 30.
iPTMnet; P04062; -.
PhosphoSitePlus; P04062; -.
SwissPalm; P04062; -.
BioMuta; GBA; -.
DMDM; 55584151; -.
EPD; P04062; -.
MaxQB; P04062; -.
PaxDb; P04062; -.
PeptideAtlas; P04062; -.
PRIDE; P04062; -.
DNASU; 2629; -.
Ensembl; ENST00000327247; ENSP00000314508; ENSG00000177628. [P04062-1]
Ensembl; ENST00000368373; ENSP00000357357; ENSG00000177628. [P04062-1]
Ensembl; ENST00000427500; ENSP00000402577; ENSG00000177628. [P04062-5]
Ensembl; ENST00000428024; ENSP00000397986; ENSG00000177628. [P04062-4]
GeneID; 2629; -.
KEGG; hsa:2629; -.
UCSC; uc001fjh.4; human. [P04062-1]
CTD; 2629; -.
DisGeNET; 2629; -.
EuPathDB; HostDB:ENSG00000177628.15; -.
GeneCards; GBA; -.
GeneReviews; GBA; -.
H-InvDB; HIX0001123; -.
HGNC; HGNC:4177; GBA.
HPA; CAB037171; -.
HPA; CAB037289; -.
HPA; HPA006667; -.
MalaCards; GBA; -.
MIM; 168600; phenotype.
MIM; 230800; phenotype.
MIM; 230900; phenotype.
MIM; 231000; phenotype.
MIM; 231005; phenotype.
MIM; 606463; gene.
MIM; 608013; phenotype.
neXtProt; NX_P04062; -.
OpenTargets; ENSG00000177628; -.
Orphanet; 1648; Dementia with Lewy body.
Orphanet; 85212; Fetal Gaucher disease.
Orphanet; 2072; Gaucher disease - ophthalmoplegia - cardiovascular calcification.
Orphanet; 77259; Gaucher disease type 1.
Orphanet; 77260; Gaucher disease type 2.
Orphanet; 77261; Gaucher disease type 3.
Orphanet; 319705; Parkinson disease.
Orphanet; 2828; Young adult-onset Parkinsonism.
PharmGKB; PA28591; -.
eggNOG; KOG2566; Eukaryota.
eggNOG; COG5520; LUCA.
GeneTree; ENSGT00390000009464; -.
HOVERGEN; HBG002285; -.
InParanoid; P04062; -.
KO; K01201; -.
OMA; TYCDSLD; -.
OrthoDB; EOG091G06I4; -.
PhylomeDB; P04062; -.
TreeFam; TF314254; -.
BRENDA; 3.2.1.45; 2681.
Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
EvolutionaryTrace; P04062; -.
GeneWiki; Glucocerebrosidase; -.
GenomeRNAi; 2629; -.
PRO; PR:P04062; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000177628; -.
CleanEx; HS_GBA; -.
CleanEx; HS_GC; -.
ExpressionAtlas; P04062; baseline and differential.
Genevisible; P04062; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0043202; C:lysosomal lumen; ISS:BHF-UCL.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0004348; F:glucosylceramidase activity; IDA:BHF-UCL.
GO; GO:0005102; F:receptor binding; ISS:BHF-UCL.
GO; GO:1905037; P:autophagosome organization; IEA:Ensembl.
GO; GO:1901805; P:beta-glucoside catabolic process; IEA:Ensembl.
GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IMP:BHF-UCL.
GO; GO:0046513; P:ceramide biosynthetic process; IMP:BHF-UCL.
GO; GO:0006680; P:glucosylceramide catabolic process; IMP:BHF-UCL.
GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:Reactome.
GO; GO:0050728; P:negative regulation of inflammatory response; IC:BHF-UCL.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:BHF-UCL.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:BHF-UCL.
GO; GO:1901215; P:negative regulation of neuron death; IGI:ParkinsonsUK-UCL.
GO; GO:0032463; P:negative regulation of protein homooligomerization; IDA:ParkinsonsUK-UCL.
GO; GO:1904925; P:positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization; IEA:Ensembl.
GO; GO:1904457; P:positive regulation of neuronal action potential; IMP:ParkinsonsUK-UCL.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:0043243; P:positive regulation of protein complex disassembly; IDA:ParkinsonsUK-UCL.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; IMP:BHF-UCL.
GO; GO:1903061; P:positive regulation of protein lipidation; IGI:ParkinsonsUK-UCL.
GO; GO:0051247; P:positive regulation of protein metabolic process; IGI:ParkinsonsUK-UCL.
GO; GO:1903052; P:positive regulation of proteolysis involved in cellular protein catabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:0032268; P:regulation of cellular protein metabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:1905165; P:regulation of lysosomal protein catabolic process; TAS:ParkinsonsUK-UCL.
GO; GO:0016241; P:regulation of macroautophagy; TAS:ParkinsonsUK-UCL.
GO; GO:0033561; P:regulation of water loss via skin; IEA:Ensembl.
GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0009268; P:response to pH; IEA:Ensembl.
GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
GO; GO:0097066; P:response to thyroid hormone; IEA:Ensembl.
GO; GO:0043589; P:skin morphogenesis; IEA:Ensembl.
GO; GO:0046512; P:sphingosine biosynthetic process; IMP:BHF-UCL.
GO; GO:0023021; P:termination of signal transduction; IMP:BHF-UCL.
InterPro; IPR033452; GH30_C.
InterPro; IPR001139; Glyco_hydro_30.
InterPro; IPR033453; Glyco_hydro_30_TIM-barrel.
InterPro; IPR017853; Glycoside_hydrolase_SF.
PANTHER; PTHR11069; PTHR11069; 1.
Pfam; PF02055; Glyco_hydro_30; 1.
Pfam; PF17189; Glyco_hydro_30C; 1.
PRINTS; PR00843; GLHYDRLASE30.
SUPFAM; SSF51445; SSF51445; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; Alternative splicing;
Complete proteome; Direct protein sequencing; Disease mutation;
Disulfide bond; Gaucher disease; Glycoprotein; Glycosidase; Hydrolase;
Ichthyosis; Lipid metabolism; Lysosome; Membrane; Neurodegeneration;
Parkinson disease; Parkinsonism; Pharmaceutical; Polymorphism;
Reference proteome; Signal; Sphingolipid metabolism.
SIGNAL 1 39 In isoform Long. {ECO:0000269|Ref.12}.
SIGNAL 21 39 In isoform Short. {ECO:0000269|Ref.12}.
CHAIN 40 536 Glucosylceramidase.
/FTId=PRO_0000012177.
ACT_SITE 274 274 Proton donor.
{ECO:0000269|PubMed:15817452}.
ACT_SITE 379 379 Nucleophile.
{ECO:0000269|PubMed:15817452}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12792654,
ECO:0000269|PubMed:17139081}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:17139081,
ECO:0000269|PubMed:19159218}.
CARBOHYD 185 185 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:17139081}.
CARBOHYD 309 309 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218}.
CARBOHYD 501 501 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 43 55 {ECO:0000269|PubMed:12792654}.
DISULFID 57 62 {ECO:0000269|PubMed:12792654}.
VAR_SEQ 1 161 Missing (in isoform 3).
{ECO:0000303|PubMed:8294033}.
/FTId=VSP_025216.
VAR_SEQ 1 87 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054655.
VAR_SEQ 1 20 Missing (in isoform Short).
{ECO:0000303|PubMed:3001061,
ECO:0000303|PubMed:3864160}.
/FTId=VSP_018800.
VAR_SEQ 103 151 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054656.
VAR_SEQ 422 423 LA -> PS (in isoform 3).
{ECO:0000303|PubMed:8294033}.
/FTId=VSP_025217.
VAR_SEQ 425 536 Missing (in isoform 3).
{ECO:0000303|PubMed:8294033}.
/FTId=VSP_025218.
VARIANT 46 46 K -> E (in a patient with Parkinson
disease; dbSNP:rs142761046).
{ECO:0000269|PubMed:19286695}.
/FTId=VAR_063066.
VARIANT 54 54 V -> L (in GD; dbSNP:rs121908302).
{ECO:0000269|PubMed:8829654}.
/FTId=VAR_003255.
VARIANT 55 55 C -> S (in GD; neuronopathic and
perinatal lethal forms; loss of activity;
dbSNP:rs773007510).
{ECO:0000269|PubMed:11992489,
ECO:0000269|PubMed:15292921,
ECO:0000269|PubMed:16293621}.
/FTId=VAR_032394.
VARIANT 63 63 D -> N (in GD1; very low activity).
{ECO:0000269|PubMed:15605411}.
/FTId=VAR_032395.
VARIANT 76 76 F -> V (in GD).
{ECO:0000269|PubMed:9217217}.
/FTId=VAR_003256.
VARIANT 80 80 E -> K (in GD2).
{ECO:0000269|PubMed:9851895}.
/FTId=VAR_009033.
VARIANT 82 82 T -> I (in GD; dbSNP:rs1141811).
/FTId=VAR_003257.
VARIANT 85 85 G -> E (in GD; dbSNP:rs77829017).
{ECO:0000269|PubMed:8829654,
ECO:0000269|PubMed:9217217}.
/FTId=VAR_003258.
VARIANT 87 87 R -> Q (in GD; 20% of normal activity;
dbSNP:rs78769774).
{ECO:0000269|PubMed:16293621}.
/FTId=VAR_032197.
VARIANT 87 87 R -> W (in GD; mild; dbSNP:rs1141814).
{ECO:0000269|PubMed:10796875,
ECO:0000269|PubMed:9153297,
ECO:0000269|PubMed:9217217}.
/FTId=VAR_003259.
VARIANT 92 92 M -> T (in dbSNP:rs3205619).
/FTId=VAR_032396.
VARIANT 118 118 K -> N (in GD; mild; 8% of normal
activity; increases susceptibility to
proteolytic degradation;
dbSNP:rs121908312).
{ECO:0000269|PubMed:10796875,
ECO:0000269|PubMed:16293621}.
/FTId=VAR_003260.
VARIANT 129 129 A -> T (in GD).
{ECO:0000269|PubMed:10796875}.
/FTId=VAR_032397.
VARIANT 146 146 S -> L (in GD; type 2;
dbSNP:rs758447515).
{ECO:0000269|PubMed:9554454}.
/FTId=VAR_009034.
VARIANT 152 152 G -> E (in GD).
{ECO:0000269|PubMed:9554746}.
/FTId=VAR_003261.
VARIANT 156 156 N -> D (in GD).
{ECO:0000269|PubMed:10796875}.
/FTId=VAR_032398.
VARIANT 158 158 I -> S (in GD1; very low activity;
dbSNP:rs77834747).
{ECO:0000269|PubMed:15605411}.
/FTId=VAR_032399.
VARIANT 158 158 I -> T (in GD).
/FTId=VAR_003262.
VARIANT 159 159 R -> Q (in GD; type 2; 13% of normal
activity; dbSNP:rs79653797).
{ECO:0000269|PubMed:10796875,
ECO:0000269|PubMed:16293621}.
/FTId=VAR_003263.
VARIANT 159 159 R -> W (in GD; severe;
dbSNP:rs397515515).
{ECO:0000269|PubMed:10796875,
ECO:0000269|PubMed:15605411,
ECO:0000269|PubMed:9217217}.
/FTId=VAR_003264.
VARIANT 161 161 P -> L (in GD; 16% of normal activity;
dbSNP:rs79637617).
{ECO:0000269|PubMed:16293621}.
/FTId=VAR_032198.
VARIANT 161 161 P -> S (in GD; mild; dbSNP:rs121908299).
/FTId=VAR_003265.
VARIANT 162 162 M -> V (in GD; loss of activity;
increases susceptibility to proteolytic
degradation; dbSNP:rs377325220).
{ECO:0000269|PubMed:16293621}.
/FTId=VAR_032199.
VARIANT 166 166 D -> V (in GD; 9% of normal activity;
increases susceptibility to proteolytic
degradation; dbSNP:rs79796061).
{ECO:0000269|PubMed:16293621}.
/FTId=VAR_032200.
VARIANT 170 170 R -> C (in GD1 and GD2; also found in a
patient with Parkinson disease;
dbSNP:rs398123530).
{ECO:0000269|PubMed:15605411,
ECO:0000269|PubMed:19286695,
ECO:0000269|PubMed:9851895}.
/FTId=VAR_009035.
VARIANT 170 170 R -> L (in GD; dbSNP:rs80356763).
{ECO:0000269|PubMed:10796875}.
/FTId=VAR_009036.
VARIANT 173 173 T -> I (in GD; dbSNP:rs78657146).
{ECO:0000269|PubMed:10796875}.
/FTId=VAR_032400.
VARIANT 173 173 T -> P (in GD).
{ECO:0000269|PubMed:10447266,
ECO:0000269|PubMed:9554746}.
/FTId=VAR_003266.
VARIANT 175 175 A -> E (in GD; dbSNP:rs79660787).
{ECO:0000269|PubMed:11933202}.
/FTId=VAR_032401.
VARIANT 179 179 D -> H (in GD; dbSNP:rs147138516).
/FTId=VAR_003267.
VARIANT 196 196 K -> Q (in GD; severe;
dbSNP:rs121908297).
/FTId=VAR_003268.
VARIANT 198 198 P -> L (in GD; dbSNP:rs80222298).
{ECO:0000269|PubMed:9554454}.
/FTId=VAR_009037.
VARIANT 198 198 P -> T (in GD).
{ECO:0000269|PubMed:12204005}.
/FTId=VAR_032402.
VARIANT 200 200 I -> N (in GD; 5% of normal activity;
dbSNP:rs77933015).
{ECO:0000269|PubMed:16293621}.
/FTId=VAR_032201.
VARIANT 200 200 I -> S (in GD; dbSNP:rs77933015).
/FTId=VAR_010059.
VARIANT 201 201 H -> P (in GD; dbSNP:rs76500263).
{ECO:0000269|PubMed:11933202}.
/FTId=VAR_032403.
VARIANT 209 209 R -> C (in GD; dbSNP:rs398123532).
{ECO:0000269|PubMed:10796875}.
/FTId=VAR_032404.
VARIANT 209 209 R -> P (in GD).
{ECO:0000269|PubMed:10796875}.
/FTId=VAR_003269.
VARIANT 213 213 L -> F (in GD; 12% of normal activity;
dbSNP:rs374591570).
{ECO:0000269|PubMed:16293621}.
/FTId=VAR_032202.
VARIANT 215 215 A -> D (in GD).
{ECO:0000269|PubMed:8790604}.
/FTId=VAR_003270.
VARIANT 217 217 P -> S (in GD; type 2).
{ECO:0000269|PubMed:7627192}.
/FTId=VAR_003271.
VARIANT 221 221 P -> L (in GD1; very low activity;
dbSNP:rs80205046).
{ECO:0000269|PubMed:15605411}.
/FTId=VAR_032405.
VARIANT 221 221 P -> T (in GD; dbSNP:rs866075757).
{ECO:0000269|PubMed:8790604}.
/FTId=VAR_003272.
VARIANT 223 223 W -> R (in GD; gene conversion;
dbSNP:rs61748906).
{ECO:0000269|PubMed:8294033}.
/FTId=VAR_003273.
VARIANT 224 224 L -> F (in GD; 4% of normal activity;
increases susceptibility to proteolytic
degradation).
{ECO:0000269|PubMed:16293621}.
/FTId=VAR_032203.
VARIANT 227 227 N -> K (in GD; gene conversion;
dbSNP:rs381418).
/FTId=VAR_003275.
VARIANT 227 227 N -> S (in GD; type 2; dbSNP:rs364897).
{ECO:0000269|PubMed:10796875,
ECO:0000269|PubMed:8829654,
ECO:0000269|PubMed:9217217}.
/FTId=VAR_003274.
VARIANT 228 228 G -> V (in GD; dbSNP:rs78911246).
{ECO:0000269|PubMed:9061570}.
/FTId=VAR_010060.
VARIANT 229 229 A -> E (in GD; type 2; dbSNP:rs75636769).
/FTId=VAR_009038.
VARIANT 229 229 A -> T (in GD).
{ECO:0000269|PubMed:10796875}.
/FTId=VAR_032406.
VARIANT 230 230 V -> E (in GD1; very low activity;
dbSNP:rs381427).
{ECO:0000269|PubMed:15605411}.
/FTId=VAR_032407.
VARIANT 230 230 V -> G (in GD1; gene conversion;
dbSNP:rs381427).
{ECO:0000269|PubMed:10206680,
ECO:0000269|PubMed:8294033}.
/FTId=VAR_003276.
VARIANT 232 232 G -> E (in GD; also found in a patient
with Parkinson disease; 7% of normal
activity). {ECO:0000269|PubMed:16293621,
ECO:0000269|PubMed:19286695}.
/FTId=VAR_032204.
VARIANT 234 234 G -> E (in GD; severe; dbSNP:rs74462743).
{ECO:0000269|PubMed:9153297}.
/FTId=VAR_003277.
VARIANT 234 234 G -> W (in GD).
{ECO:0000269|PubMed:10447266}.
/FTId=VAR_009039.
VARIANT 235 235 S -> P (in GD; type 2; gene conversion;
dbSNP:rs1064644).
{ECO:0000269|PubMed:10796875,
ECO:0000269|PubMed:8294033}.
/FTId=VAR_003278.
VARIANT 237 237 K -> E (in GD; severe; loss of activity;
increases susceptibility to proteolytic
degradation; dbSNP:rs773409311).
{ECO:0000269|PubMed:11933202,
ECO:0000269|PubMed:16293621}.
/FTId=VAR_032205.
VARIANT 241 241 G -> E (in GD; dbSNP:rs77451368).
/FTId=VAR_010061.
VARIANT 241 241 G -> R (in GD; type 1 and type 2; gene
conversion; dbSNP:rs398123534).
{ECO:0000269|PubMed:10360404,
ECO:0000269|PubMed:10796875,
ECO:0000269|PubMed:12204005,
ECO:0000269|PubMed:15605411,
ECO:0000269|PubMed:8294033,
ECO:0000269|PubMed:8790604,
ECO:0000269|PubMed:9153297}.
/FTId=VAR_003279.
VARIANT 244 244 Y -> C (in GD; dbSNP:rs76026102).
{ECO:0000269|PubMed:10360404}.
/FTId=VAR_010062.
VARIANT 251 251 Y -> H (in GD; dbSNP:rs121908300).
/FTId=VAR_003280.
VARIANT 252 252 F -> I (in GD; type 2; gene conversion;
dbSNP:rs381737).
{ECO:0000269|PubMed:10360404,
ECO:0000269|PubMed:10796875,
ECO:0000269|PubMed:8294033,
ECO:0000269|PubMed:9061570,
ECO:0000269|PubMed:9153297,
ECO:0000269|PubMed:9217217}.
/FTId=VAR_003281.
VARIANT 255 255 F -> Y (in GD; mild; dbSNP:rs74500255).
{ECO:0000269|PubMed:1974409}.
/FTId=VAR_003282.
VARIANT 270 270 T -> R (in GD; dbSNP:rs76725886).
{ECO:0000269|PubMed:12204005}.
/FTId=VAR_032408.
VARIANT 276 276 S -> P (in GD).
/FTId=VAR_003283.
VARIANT 290 290 F -> L (in GD; perinatal lethal form;
dbSNP:rs121908313).
{ECO:0000269|PubMed:11933202}.
/FTId=VAR_032409.
VARIANT 294 294 H -> Q (in GD1; also found in Gaucher
disease type 2; dbSNP:rs367968666).
{ECO:0000269|PubMed:15605411}.
/FTId=VAR_009040.
VARIANT 296 296 R -> Q (in GD; type 2; also found in a
patient with Parkinson disease;
dbSNP:rs78973108).
{ECO:0000269|PubMed:10796875,
ECO:0000269|PubMed:19286695,
ECO:0000269|PubMed:8790604}.
/FTId=VAR_003284.
VARIANT 298 298 F -> L (in GD; type 2; 4% of normal
activity). {ECO:0000269|PubMed:16293621,
ECO:0000269|PubMed:3001061}.
/FTId=VAR_009041.
VARIANT 303 303 L -> I (in GD; 5% of normal activity).
{ECO:0000269|PubMed:16293621}.
/FTId=VAR_032206.
VARIANT 304 304 G -> D (in GD; dbSNP:rs80116658).
/FTId=VAR_010063.
VARIANT 305 305 P -> R (in GD; mild; dbSNP:rs79215220).
/FTId=VAR_003285.
VARIANT 310 310 S -> G (in dbSNP:rs1057942).
{ECO:0000269|PubMed:8294033}.
/FTId=VAR_032410.
VARIANT 310 310 S -> N (in GD; less than 5% of normal
activity; dbSNP:rs74731340).
{ECO:0000269|PubMed:9153297}.
/FTId=VAR_010064.
VARIANT 324 324 R -> C (in GD; type 1;
dbSNP:rs765633380).
{ECO:0000269|PubMed:10796875,
ECO:0000269|PubMed:15605411,
ECO:0000269|PubMed:8790604}.
/FTId=VAR_003286.
VARIANT 324 324 R -> H (in GD; type 2; dbSNP:rs79696831).
/FTId=VAR_009042.
VARIANT 328 328 P -> L (in GD; mild; dbSNP:rs121908298).
/FTId=VAR_003287.
VARIANT 342 342 K -> I (in GD; dbSNP:rs77714449).
/FTId=VAR_003288.
VARIANT 343 343 Y -> C (in GD; type 2; 16% of normal
activity; increases susceptibility to
proteolytic degradation;
dbSNP:rs77321207).
{ECO:0000269|PubMed:16293621}.
/FTId=VAR_009043.
VARIANT 348 348 A -> V (in GD; dbSNP:rs78396650).
/FTId=VAR_003289.
VARIANT 350 350 H -> R (in perinatal lethal GD;
dbSNP:rs78198234).
{ECO:0000269|PubMed:10352942}.
/FTId=VAR_009044.
VARIANT 351 351 W -> C (in GD; mild; dbSNP:rs121908304).
/FTId=VAR_003290.
VARIANT 352 352 Y -> H (in GD).
{ECO:0000269|PubMed:8829663}.
/FTId=VAR_003291.
VARIANT 354 354 D -> H (in GD; dbSNP:rs398123526).
/FTId=VAR_003292.
VARIANT 357 357 A -> D (in GD; dbSNP:rs78188205).
/FTId=VAR_003293.
VARIANT 362 362 T -> I (in GD; 6% of normal activity;
dbSNP:rs76539814).
{ECO:0000269|PubMed:16293621}.
/FTId=VAR_003294.
VARIANT 363 363 L -> P (in GD; unknown pathological
significance).
{ECO:0000269|PubMed:26528954}.
/FTId=VAR_003295.
VARIANT 364 364 G -> R (in GD; type 2;
dbSNP:rs121908305).
{ECO:0000269|PubMed:8294033}.
/FTId=VAR_003296.
VARIANT 365 365 E -> K (in GD; mild; 42% of normal
activity; dbSNP:rs2230288).
{ECO:0000269|PubMed:10796875,
ECO:0000269|PubMed:16293621}.
/FTId=VAR_003297.
VARIANT 368 368 R -> H (in dbSNP:rs1064648).
{ECO:0000269|PubMed:8294033}.
/FTId=VAR_032411.
VARIANT 380 380 A -> T (in GD; dbSNP:rs781306264).
{ECO:0000269|PubMed:10796875,
ECO:0000269|PubMed:9554454}.
/FTId=VAR_009045.
VARIANT 381 381 C -> G (in GD; type 2; loss of activity;
dbSNP:rs121908306).
{ECO:0000269|PubMed:16293621}.
/FTId=VAR_003298.
VARIANT 388 388 E -> K (in GD; 12% of normal activity).
{ECO:0000269|PubMed:16293621}.
/FTId=VAR_032207.
VARIANT 391 391 V -> L (in GD; dbSNP:rs398123527).
{ECO:0000269|PubMed:9153297}.
/FTId=VAR_010065.
VARIANT 392 392 R -> G (in GD; dbSNP:rs121908308).
{ECO:0000269|PubMed:9650766}.
/FTId=VAR_010066.
VARIANT 392 392 R -> W (in GD; 5% of normal activity).
{ECO:0000269|PubMed:16293621}.
/FTId=VAR_032208.
VARIANT 398 398 R -> Q (in GD; mild; dbSNP:rs74979486).
{ECO:0000269|PubMed:8829663}.
/FTId=VAR_003299.
VARIANT 400 400 M -> I (in GD; dbSNP:rs149487315).
{ECO:0000269|PubMed:12204005}.
/FTId=VAR_032412.
VARIANT 402 402 Y -> C (in GD; 8% of normal activity;
increases susceptibility to proteolytic
degradation; dbSNP:rs76228122).
{ECO:0000269|PubMed:16293621}.
/FTId=VAR_032209.
VARIANT 403 403 S -> T (in GD; mild; dbSNP:rs121908307).
/FTId=VAR_003300.
VARIANT 405 405 S -> G (in GD).
{ECO:0000269|PubMed:9061570}.
/FTId=VAR_010067.
VARIANT 405 405 S -> N (in GD).
{ECO:0000269|PubMed:9554454}.
/FTId=VAR_009046.
VARIANT 408 408 T -> M (in GD; dbSNP:rs75548401).
{ECO:0000269|PubMed:10796875,
ECO:0000269|PubMed:14702039}.
/FTId=VAR_003301.
VARIANT 409 409 N -> S (in GD1; common mutation;
associated with susceptibility to
Parkinson disease; alters interaction
with saposin-C; mild; dbSNP:rs76763715).
{ECO:0000269|PubMed:10206680,
ECO:0000269|PubMed:10340647,
ECO:0000269|PubMed:10447266,
ECO:0000269|PubMed:10796875,
ECO:0000269|PubMed:15605411,
ECO:0000269|PubMed:15826241,
ECO:0000269|PubMed:16293621,
ECO:0000269|PubMed:18332251,
ECO:0000269|PubMed:19286695,
ECO:0000269|PubMed:19846850,
ECO:0000269|PubMed:7627184,
ECO:0000269|PubMed:8076951,
ECO:0000269|PubMed:8937765,
ECO:0000269|PubMed:9153297,
ECO:0000269|Ref.14}.
/FTId=VAR_003302.
VARIANT 410 410 L -> V (in GD; 15% of normal activity;
increases susceptibility to proteolytic
degradation; dbSNP:rs121908314).
{ECO:0000269|PubMed:16293621}.
/FTId=VAR_032210.
VARIANT 414 414 V -> L (in GD; mild; dbSNP:rs398123528).
{ECO:0000269|PubMed:9182788}.
/FTId=VAR_010068.
VARIANT 416 416 G -> S (in GD; mild; dbSNP:rs121908311).
{ECO:0000269|PubMed:10447266,
ECO:0000269|PubMed:10796875}.
/FTId=VAR_003303.
VARIANT 417 417 W -> G (in GD).
{ECO:0000269|PubMed:8790604}.
/FTId=VAR_003304.
VARIANT 419 419 D -> A (in GD; type 2; also found in a
patient with Parkinson disease;
dbSNP:rs77284004).
{ECO:0000269|PubMed:19286695}.
/FTId=VAR_003305.
VARIANT 419 419 D -> H (in GD; 4% of normal activity).
{ECO:0000269|PubMed:16293621}.
/FTId=VAR_032211.
VARIANT 419 419 D -> N (in GD).
{ECO:0000269|PubMed:8790604}.
/FTId=VAR_003306.
VARIANT 421 421 N -> K (in GD; 22% of normal activity).
{ECO:0000269|PubMed:16293621}.
/FTId=VAR_032212.
VARIANT 426 426 P -> L (in GD).
{ECO:0000269|PubMed:8937765}.
/FTId=VAR_010069.
VARIANT 428 428 G -> E (in GD; type 2).
{ECO:0000269|PubMed:9554746}.
/FTId=VAR_003307.
VARIANT 429 429 G -> R (in GD; 17% of normal activity).
{ECO:0000269|PubMed:16293621}.
/FTId=VAR_032213.
VARIANT 430 430 P -> L (in GD; dbSNP:rs76910485).
{ECO:0000269|PubMed:9554746}.
/FTId=VAR_003308.
VARIANT 431 431 N -> I (in GD; type 2; dbSNP:rs77738682).
{ECO:0000269|PubMed:9554746}.
/FTId=VAR_003309.
VARIANT 432 432 W -> R (in GD).
{ECO:0000269|PubMed:9554454}.
/FTId=VAR_009047.
VARIANT 433 433 V -> L (in GD; severe; 12% of normal
activity; dbSNP:rs80356769).
{ECO:0000269|PubMed:10796875,
ECO:0000269|PubMed:16293621,
ECO:0000269|PubMed:8937765}.
/FTId=VAR_003310.
VARIANT 435 435 N -> T (in GD1; mild; dbSNP:rs75385858).
{ECO:0000269|PubMed:8889591}.
/FTId=VAR_003311.
VARIANT 436 436 F -> S (in GD; 6% of normal activity;
alters protein stability and increases
susceptibility to proteolytic
degradation; dbSNP:rs75243000).
{ECO:0000269|PubMed:16293621}.
/FTId=VAR_032214.
VARIANT 437 437 V -> F (in perinatal lethal GD;
dbSNP:rs121908310).
{ECO:0000269|PubMed:10352942}.
/FTId=VAR_009048.
VARIANT 437 437 V -> L (in GD3).
{ECO:0000269|PubMed:8780099}.
/FTId=VAR_010070.
VARIANT 438 438 D -> N (in GD; type 1 and type 2; 14% of
normal activity; increases susceptibility
to proteolytic degradation).
{ECO:0000269|PubMed:15605411,
ECO:0000269|PubMed:16293621,
ECO:0000269|PubMed:8112750}.
/FTId=VAR_003312.
VARIANT 438 438 D -> Y (in GD).
{ECO:0000269|PubMed:10796875}.
/FTId=VAR_032413.
VARIANT 440 440 P -> L (in GD1; dbSNP:rs74598136).
{ECO:0000269|PubMed:10340647,
ECO:0000269|PubMed:15605411}.
/FTId=VAR_010071.
VARIANT 441 441 I -> F (in GD; type 3).
{ECO:0000269|PubMed:11933202}.
/FTId=VAR_032414.
VARIANT 441 441 I -> T (in GD; mild; dbSNP:rs75564605).
{ECO:0000269|PubMed:9182788}.
/FTId=VAR_010072.
VARIANT 448 448 D -> H (in GD; type 1 and type
neuronopathic; at homozygosity it causes
GD3C; also found in a patient with
Parkinson disease; gene conversion; very
low activity; alters protein stability;
dbSNP:rs1064651).
{ECO:0000269|PubMed:10360404,
ECO:0000269|PubMed:10447266,
ECO:0000269|PubMed:10796875,
ECO:0000269|PubMed:11992489,
ECO:0000269|PubMed:15605411,
ECO:0000269|PubMed:16293621,
ECO:0000269|PubMed:19286695,
ECO:0000269|PubMed:7627184,
ECO:0000269|PubMed:9040001,
ECO:0000269|PubMed:9061570}.
/FTId=VAR_003313.
VARIANT 448 448 D -> V (in GD; severe; very low activity;
alters protein stability;
dbSNP:rs77369218).
/FTId=VAR_003314.
VARIANT 450 450 F -> I (in GD).
/FTId=VAR_010073.
VARIANT 451 451 Y -> H (in GD).
{ECO:0000269|PubMed:9554746}.
/FTId=VAR_003315.
VARIANT 452 452 K -> Q (in GD).
{ECO:0000269|PubMed:9061570}.
/FTId=VAR_010074.
VARIANT 454 454 P -> R (in GD; type 2;
dbSNP:rs121908295).
/FTId=VAR_003316.
VARIANT 455 455 M -> V (in GD; loss of activity;
increases susceptibility to proteolytic
degradation).
{ECO:0000269|PubMed:16293621}.
/FTId=VAR_032215.
VARIANT 456 456 F -> V (in GD).
/FTId=VAR_003317.
VARIANT 457 457 Y -> C (in GD; dbSNP:rs74752878).
{ECO:0000269|PubMed:15605411,
ECO:0000269|PubMed:8076951}.
/FTId=VAR_003318.
VARIANT 460 460 G -> D (in GD1; associated with R-490;
loss of activity).
{ECO:0000269|PubMed:15605411}.
/FTId=VAR_032415.
VARIANT 464 464 K -> E (in GD; severe).
/FTId=VAR_003319.
VARIANT 482 482 D -> N (in a patient with Parkinson
disease; dbSNP:rs75671029).
{ECO:0000269|PubMed:19286695}.
/FTId=VAR_063067.
VARIANT 483 483 L -> P (in GD1 and GD2; common mutation;
associated with susceptibility to
Parkinson disease; gene conversion; very
low activity; alters protein stability;
dbSNP:rs421016).
{ECO:0000269|PubMed:10360404,
ECO:0000269|PubMed:10447266,
ECO:0000269|PubMed:10796875,
ECO:0000269|PubMed:15605411,
ECO:0000269|PubMed:16293621,
ECO:0000269|PubMed:19286695,
ECO:0000269|PubMed:7627184,
ECO:0000269|PubMed:8937765,
ECO:0000269|PubMed:9061570,
ECO:0000269|PubMed:9217217,
ECO:0000269|PubMed:9851895}.
/FTId=VAR_003321.
VARIANT 483 483 L -> R (in GD; severe; dbSNP:rs421016).
/FTId=VAR_003320.
VARIANT 485 485 A -> P (in GD).
/FTId=VAR_003322.
VARIANT 490 490 H -> R (in GD; type 1; associated with D-
460; dbSNP:rs76071730).
{ECO:0000269|PubMed:12204005,
ECO:0000269|PubMed:15605411}.
/FTId=VAR_032416.
VARIANT 495 495 A -> P (in GD; gene conversion;
dbSNP:rs368060).
{ECO:0000269|PubMed:19286695}.
/FTId=VAR_003323.
VARIANT 497 497 V -> L. {ECO:0000269|PubMed:19286695}.
/FTId=VAR_063068.
VARIANT 500 500 L -> P (in GD; 10% of normal activity;
increases susceptibility to proteolytic
degradation).
{ECO:0000269|PubMed:16293621}.
/FTId=VAR_032216.
VARIANT 501 501 N -> K (in GD; type 2).
{ECO:0000269|PubMed:9279145}.
/FTId=VAR_009049.
VARIANT 502 502 R -> C (in GD; 37% of normal activity;
also found in patients with Parkinson
disease; dbSNP:rs80356771).
{ECO:0000269|PubMed:10796875,
ECO:0000269|PubMed:19286695,
ECO:0000269|PubMed:1972019,
ECO:0000269|PubMed:7627184}.
/FTId=VAR_003324.
VARIANT 502 502 R -> P (in GD; loss of activity;
increases susceptibility to proteolytic
degradation).
{ECO:0000269|PubMed:16293621}.
/FTId=VAR_032217.
VARIANT 509 509 L -> P.
/FTId=VAR_003325.
VARIANT 513 513 D -> Y (in GD2).
{ECO:0000269|PubMed:9637431}.
/FTId=VAR_009050.
VARIANT 517 517 G -> S (in GD; dbSNP:rs121908301).
/FTId=VAR_003326.
VARIANT 530 530 T -> I (in GD3; dbSNP:rs78016673).
{ECO:0000269|PubMed:8780099}.
/FTId=VAR_010075.
VARIANT 535 535 R -> C (in GD; mild; dbSNP:rs747506979).
{ECO:0000269|PubMed:9061570}.
/FTId=VAR_003327.
VARIANT 535 535 R -> H (in GD; mild; dbSNP:rs75822236).
{ECO:0000269|PubMed:7916532}.
/FTId=VAR_003328.
MUTAGEN 43 43 C->S: Loss of activity.
{ECO:0000269|PubMed:16293621}.
MUTAGEN 57 57 C->S: Loss of activity.
{ECO:0000269|PubMed:16293621}.
MUTAGEN 62 62 C->S: Loss of activity.
{ECO:0000269|PubMed:16293621}.
MUTAGEN 379 379 E->G: Decreases activity 1000-fold.
{ECO:0000269|PubMed:7908905}.
CONFLICT 176 176 D -> G (in Ref. 7; BAH13357).
{ECO:0000305}.
CONFLICT 227 227 N -> R (in Ref. 5; BAA02546).
{ECO:0000305}.
CONFLICT 470 470 S -> I (in Ref. 15; AA sequence).
{ECO:0000305}.
CONFLICT 534 534 R -> H (in Ref. 1; AAA35873).
{ECO:0000305}.
STRAND 49 52 {ECO:0000244|PDB:2NT0}.
STRAND 54 57 {ECO:0000244|PDB:2NT0}.
STRAND 75 82 {ECO:0000244|PDB:2NT0}.
STRAND 88 94 {ECO:0000244|PDB:2NT0}.
STRAND 96 98 {ECO:0000244|PDB:2NT0}.
STRAND 103 116 {ECO:0000244|PDB:2NT0}.
STRAND 119 123 {ECO:0000244|PDB:2NT0}.
HELIX 126 133 {ECO:0000244|PDB:2NT0}.
HELIX 137 148 {ECO:0000244|PDB:2NT0}.
TURN 150 153 {ECO:0000244|PDB:2NT0}.
STRAND 157 163 {ECO:0000244|PDB:2NT0}.
STRAND 166 170 {ECO:0000244|PDB:2NT0}.
STRAND 177 179 {ECO:0000244|PDB:1OGS}.
HELIX 190 193 {ECO:0000244|PDB:2NT0}.
HELIX 196 206 {ECO:0000244|PDB:2NT0}.
STRAND 212 218 {ECO:0000244|PDB:2NT0}.
HELIX 222 224 {ECO:0000244|PDB:2NT0}.
STRAND 225 227 {ECO:0000244|PDB:2J25}.
STRAND 229 233 {ECO:0000244|PDB:2NT0}.
STRAND 235 238 {ECO:0000244|PDB:2NT0}.
HELIX 243 261 {ECO:0000244|PDB:2NT0}.
STRAND 267 271 {ECO:0000244|PDB:2NT0}.
HELIX 275 279 {ECO:0000244|PDB:2NT0}.
STRAND 284 286 {ECO:0000244|PDB:3GXF}.
HELIX 292 301 {ECO:0000244|PDB:2NT0}.
HELIX 303 308 {ECO:0000244|PDB:2NT0}.
TURN 311 314 {ECO:0000244|PDB:2NT0}.
STRAND 315 323 {ECO:0000244|PDB:2NT0}.
HELIX 324 326 {ECO:0000244|PDB:2NT0}.
HELIX 329 335 {ECO:0000244|PDB:2NT0}.
HELIX 338 341 {ECO:0000244|PDB:2NT0}.
STRAND 346 352 {ECO:0000244|PDB:2NT0}.
HELIX 354 356 {ECO:0000244|PDB:3GXI}.
HELIX 359 369 {ECO:0000244|PDB:2NT0}.
STRAND 373 381 {ECO:0000244|PDB:2NT0}.
STRAND 386 388 {ECO:0000244|PDB:2J25}.
HELIX 396 411 {ECO:0000244|PDB:2NT0}.
STRAND 414 424 {ECO:0000244|PDB:2NT0}.
STRAND 426 428 {ECO:0000244|PDB:3KEH}.
STRAND 440 444 {ECO:0000244|PDB:2NT0}.
HELIX 445 447 {ECO:0000244|PDB:2NT0}.
STRAND 449 452 {ECO:0000244|PDB:2NT0}.
HELIX 454 463 {ECO:0000244|PDB:2NT0}.
STRAND 471 479 {ECO:0000244|PDB:2NT0}.
STRAND 482 489 {ECO:0000244|PDB:2NT0}.
STRAND 495 501 {ECO:0000244|PDB:2NT0}.
STRAND 503 505 {ECO:0000244|PDB:2NT0}.
STRAND 507 513 {ECO:0000244|PDB:2NT0}.
TURN 514 516 {ECO:0000244|PDB:2NT0}.
STRAND 517 523 {ECO:0000244|PDB:2NT0}.
STRAND 527 533 {ECO:0000244|PDB:2NT0}.
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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