LYAG_HUMAN
ID LYAG_HUMAN Reviewed; 952 AA.
AC P10253; Q09GN4; Q14351; Q16302; Q8IWE7;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 4.
DT 03-AUG-2022, entry version 236.
DE RecName: Full=Lysosomal alpha-glucosidase;
DE EC=3.2.1.20 {ECO:0000269|PubMed:18429042, ECO:0000269|PubMed:1856189, ECO:0000269|PubMed:29061980, ECO:0000269|PubMed:7717400};
DE AltName: Full=Acid maltase;
DE AltName: Full=Aglucosidase alfa;
DE Contains:
DE RecName: Full=76 kDa lysosomal alpha-glucosidase;
DE Contains:
DE RecName: Full=70 kDa lysosomal alpha-glucosidase;
DE Flags: Precursor;
GN Name=GAA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 70-89; 123-145; 204-215;
RP 230-249; 332-345; 349-370; 394-409; 480-513; 520-545; 703-719; 726-731 AND
RP 795-803, AND VARIANTS ARG-199; HIS-223 AND ILE-780.
RC TISSUE=Placenta, Testis, and Urine;
RX PubMed=3049072; DOI=10.1002/j.1460-2075.1988.tb02998.x;
RA Hoefsloot L.H., Hoogeveen-Westerveld M., Kroos M.A., van Beeumen J.,
RA Reuser A.J.J., Oostra B.A.;
RT "Primary structure and processing of lysosomal alpha-glucosidase; homology
RT with the intestinal sucrase-isomaltase complex.";
RL EMBO J. 7:1697-1704(1988).
RN [2]
RP SEQUENCE REVISION.
RA Reuser A.J.J.;
RL Submitted (JUN-1990) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-780.
RX PubMed=2268276; DOI=10.1042/bj2720493;
RA Hoefsloot L.H., Hoogeveen-Westerveld M., Reuser A.J.J., Oostra B.A.;
RT "Characterization of the human lysosomal alpha-glucosidase gene.";
RL Biochem. J. 272:493-497(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ILE-780.
RX PubMed=2111708; DOI=10.1089/dna.1990.9.85;
RA Martiniuk F., Mehler M., Tzall S., Meredith G., Hirschhorn R.;
RT "Sequence of the cDNA and 5'-flanking region for human acid alpha-
RT glucosidase, detection of an intron in the 5' untranslated leader sequence,
RT definition of 18-bp polymorphisms, and differences with previous cDNA and
RT amino acid sequences.";
RL DNA Cell Biol. 9:85-94(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT GSD2 LEU-457, AND VARIANTS ARG-199;
RP HIS-223 AND ILE-780.
RA Ghaffari S.R., Sabokbar T., Tahmasebi S., Dastan J.;
RT "Identification of a novel mutation in the acid alpha glucosidase gene
RT causing juvenile form of Pompe disease in Iranian population.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Duodenum;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 631-680, AND VARIANT GSD2 HIS-645.
RX PubMed=7695647; DOI=10.1006/bbrc.1995.1418;
RA Lin C.-Y., Shieh J.-J.;
RT "Identification of a de novo point mutation resulting in infantile form of
RT Pompe's disease.";
RL Biochem. Biophys. Res. Commun. 208:886-893(1995).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF TRP-516 AND ASP-518, AND
RP ACTIVE SITE.
RX PubMed=1856189; DOI=10.1016/s0021-9258(18)92727-4;
RA Hermans M.M.P., Kroos M.A., van Beeumen J., Oostra B.A., Reuser A.J.J.;
RT "Human lysosomal alpha-glucosidase. Characterization of the catalytic
RT site.";
RL J. Biol. Chem. 266:13507-13512(1991).
RN [10]
RP GLYCOSYLATION AT ASN-140; ASN-233; ASN-390; ASN-470; ASN-652; ASN-882 AND
RP ASN-925.
RX PubMed=8435067; DOI=10.1042/bj2890681;
RA Hermans M.M.P., Wisselaar H.A., Kroos M.A., Oostra B.A., Reuser A.J.J.;
RT "Human lysosomal alpha-glucosidase: functional characterization of the
RT glycosylation sites.";
RL Biochem. J. 289:681-686(1993).
RN [11]
RP GLYCOSYLATION AT ASN-470.
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 [12]
RP REVIEW ON VARIANTS.
RX PubMed=7603530; DOI=10.1002/mus.880181414;
RA Reuser A.J.J., Kroos M.A., Hermans M.M.P., Bijvoet A.G.A., Verbeet M.P.,
RA van Diggelen O.P., Kleijer W.J., van der Ploeg A.T.;
RT "Glycogenosis type II (acid maltase deficiency).";
RL Muscle Nerve 3:S61-S69(1995).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-390.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [14]
RP 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., Schaefer H.,
RA Elsaesser H.-P., Mann M., Hasilik A.;
RT "Integral and associated lysosomal membrane proteins.";
RL Traffic 8:1676-1686(2007).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-140; ASN-470; ASN-882 AND
RP ASN-925.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [19] {ECO:0007744|PDB:5KZW, ECO:0007744|PDB:5KZX}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 79-952, GLYCOSYLATION AT ASN-140;
RP ASN-233; ASN-390; ASN-470; ASN-652 AND ASN-882, AND DISULFIDE BONDS.
RA Deming D.T., Garman S.C.;
RT "The structure of human GAA: structural basis of Pompe disease.";
RL Submitted (JUL-2016) to the PDB data bank.
RN [20] {ECO:0007744|PDB:5NN3, ECO:0007744|PDB:5NN4, ECO:0007744|PDB:5NN5, ECO:0007744|PDB:5NN6, ECO:0007744|PDB:5NN8}
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 81-952 IN COMPLEXES WITH
RP SUBSTRATE ANALOGS, FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT ASN-140;
RP ASN-233; ASN-390; ASN-470; ASN-652 AND ASN-882, AND DISULFIDE BONDS.
RX PubMed=29061980; DOI=10.1038/s41467-017-01263-3;
RA Roig-Zamboni V., Cobucci-Ponzano B., Iacono R., Ferrara M.C., Germany S.,
RA Bourne Y., Parenti G., Moracci M., Sulzenbacher G.;
RT "Structure of human lysosomal acid alpha-glucosidase-a guide for the
RT treatment of Pompe disease.";
RL Nat. Commun. 8:1111-1111(2017).
RN [21]
RP VARIANT ASN-91.
RX PubMed=2203258;
RA Martiniuk F., Bodkin M., Tzall S., Hirschhorn R.;
RT "Identification of the base-pair substitution responsible for a human acid
RT alpha glucosidase allele with lower 'affinity' for glycogen (GAA 2) and
RT transient gene expression in deficient cells.";
RL Am. J. Hum. Genet. 47:440-445(1990).
RN [22]
RP VARIANT GSD2 THR-318.
RX PubMed=1652892;
RA Zhong N., Martiniuk F., Tzall S., Hirschhorn R.;
RT "Identification of a missense mutation in one allele of a patient with
RT Pompe disease, and use of endonuclease digestion of PCR-amplified RNA to
RT demonstrate lack of mRNA expression from the second allele.";
RL Am. J. Hum. Genet. 49:635-645(1991).
RN [23]
RP VARIANT GSD2 LYS-521.
RX PubMed=1898413; DOI=10.1016/0006-291x(91)91906-s;
RA Hermans M.M.P., de Graaff E., Kroos M.A., Wisselaar H.A., Oostra B.A.,
RA Reuser A.J.J.;
RT "Identification of a point mutation in the human lysosomal alpha-
RT glucosidase gene causing infantile glycogenosis type II.";
RL Biochem. Biophys. Res. Commun. 179:919-926(1991).
RN [24]
RP VARIANTS GSD2 ARG-643 AND TRP-725.
RX PubMed=8401535; DOI=10.1002/humu.1380020406;
RA Hermans M.M.P., Kroos M.A., de Graaff E., Oostra B.A., Reuser A.J.J.;
RT "Two mutations affecting the transport and maturation of lysosomal alpha-
RT glucosidase in an adult case of glycogen storage disease type II.";
RL Hum. Mutat. 2:268-273(1993).
RN [25]
RP VARIANT GSD2 GLU-645, AND VARIANTS ILE-816 AND ILE-927.
RX PubMed=8094613; DOI=10.1042/bj2890687;
RA Hermans M.M.P., de Graaff E., Kroos M.A., Wisselaar H.A., Willemsen R.,
RA Oostra B.A., Reuser A.J.J.;
RT "The conservative substitution Asp-645-->Glu in lysosomal alpha-glucosidase
RT affects transport and phosphorylation of the enzyme in an adult patient
RT with glycogen-storage disease type II.";
RL Biochem. J. 289:687-693(1993).
RN [26]
RP VARIANT GSD2 GLU-645, AND VARIANTS ILE-816 AND ILE-927.
RX PubMed=1684505; DOI=10.1089/dna.1991.10.681;
RA Martiniuk F., Mehler M., Bodkin M., Tzall S., Hirschhorn K., Zhong N.,
RA Hirschhorn R.;
RT "Identification of a missense mutation in an adult-onset patient with
RT glycogenosis type II expressing only one allele.";
RL DNA Cell Biol. 10:681-687(1991).
RN [27]
RP VARIANTS ILE-816 AND ILE-927.
RX PubMed=8486380; DOI=10.1006/geno.1993.1185;
RA Hermans M.M.P., Svetkey L.P., Oostra B.A., Chen Y.T., Reuser A.J.J.;
RT "The loss of a polymorphic glycosylation site caused by Thr-927-->Ile is
RT linked to a second polymorphic Val-816-->Ile substitution in lysosomal
RT alpha-glucosidase of American blacks.";
RL Genomics 16:300-301(1993).
RN [28]
RP VARIANT GSD2 VAL-519.
RX PubMed=7866409; DOI=10.1002/humu.1380040410;
RA Huie M.L., Hirschhorn R., Chen A.S., Martiniuk F., Zhong N.;
RT "Mutation at the catalytic site (M519V) in glycogen storage disease type II
RT (Pompe disease).";
RL Hum. Mutat. 4:291-293(1994).
RN [29]
RP VARIANT GSD2 TRP-647.
RX PubMed=7981676; DOI=10.1093/hmg/3.7.1081;
RA Huie M.L., Chen A.S., Brooks S.S., Grix A., Hirschhorn R.;
RT "A de novo 13 nt deletion, a newly identified C647W missense mutation and a
RT deletion of exon 18 in infantile onset glycogen storage disease type II
RT (GSDII).";
RL Hum. Mol. Genet. 3:1081-1087(1994).
RN [30]
RP VARIANT GSD2 LEU-545.
RX PubMed=7881422; DOI=10.1093/hmg/3.12.2213;
RA Hermans M.M.P., de Graaff E., Kroos M.A., Mohkamsing S., Eussen B.J.,
RA Joosse M., Willemsen R., Kleijer W.J., Oostra B.A., Reuser A.J.J.;
RT "The effect of a single base pair deletion (delta T525) and a C1634T
RT missense mutation (Pro545Leu) on the expression of lysosomal alpha-
RT glucosidase in patients with glycogen storage disease type II.";
RL Hum. Mol. Genet. 3:2213-2218(1994).
RN [31]
RP VARIANTS GSD2 ARG-299 AND LYS-903 DEL, VARIANTS ARG-199; HIS-223 AND
RP ILE-780, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7717400;
RA Boerkoel C.F., Exelbert R., Nicastri C., Nichols R.C., Miller F.W.,
RA Plotz P.H., Raben N.;
RT "Leaky splicing mutation in the acid maltase gene is associated with
RT delayed onset of glycogenosis type II.";
RL Am. J. Hum. Genet. 56:887-897(1995).
RN [32]
RP VARIANT LYS-689.
RX PubMed=8912788; DOI=10.1111/j.1469-1809.1996.tb00433.x;
RA Huie M.L., Menaker M., McAlpine P.J., Hirschhorn R.;
RT "Identification of an E689K substitution as the molecular basis of the
RT human acid alpha-glucosidase type 4 allozyme (GAA*4).";
RL Ann. Hum. Genet. 60:365-368(1996).
RN [33]
RP VARIANT GSD2 VAL-529.
RX PubMed=8834250; DOI=10.1007/bf02267074;
RA Tsunoda H., Ohshima T., Tohyama J., Sasaki M., Sakuragawa N., Martiniuk F.;
RT "Acid alpha-glucosidase deficiency: identification and expression of a
RT missense mutation (S529V) in a Japanese adult phenotype.";
RL Hum. Genet. 97:496-499(1996).
RN [34]
RP VARIANTS GSD2 ASN-645; TRP-647; SER-648; GLN-672 AND TRP-672.
RX PubMed=9535769; DOI=10.1006/bbrc.1998.8255;
RA Huie M.L., Tsujino S., Brooks S.S., Engel A., Elias E., Bonthron D.T.,
RA Bessley C., Shanske S., Dimauro S., Goto Y., Hirschhorn R.;
RT "Glycogen storage disease type II: identification of four novel missense
RT mutations (D645N, G648S, R672W, R672Q) and two insertions/deletions in the
RT acid alpha-glucosidase locus of patients of differing phenotype.";
RL Biochem. Biophys. Res. Commun. 244:921-927(1998).
RN [35]
RP VARIANT GSD2 ARG-309.
RX PubMed=9660056; DOI=10.1111/j.1399-0004.1998.tb02749.x;
RA Kroos M.A., van Leenen D., Verbiest J., Reuser A.J.J., Hermans M.M.P.;
RT "Glycogen storage disease type II: identification of a dinucleotide
RT deletion and a common missense mutation in the lysosomal alpha-glucosidase
RT gene.";
RL Clin. Genet. 53:379-382(1998).
RN [36]
RP VARIANTS GSD2 PRO-566; ARG-643 AND ARG-768, AND VARIANTS ASN-91; ARG-199
RP AND HIS-223.
RX PubMed=9521422;
RX DOI=10.1002/(sici)1098-1004(1998)11:3<209::aid-humu5>3.0.co;2-c;
RA Hermans M.M.P., Kroos M.A., Smeitink J.A.M., van der Ploeg A.T.,
RA Kleijer W.J., Reuser A.J.J.;
RT "Glycogen storage disease type II: genetic and biochemical analysis of
RT novel mutations in infantile patients from Turkish ancestry.";
RL Hum. Mutat. 11:209-215(1998).
RN [37]
RP VARIANT GSD2 GLY-VAL-PRO-VAL-SER-ASN-925 INS.
RX PubMed=10206684;
RX DOI=10.1002/(sici)1098-1004(1998)11:5<413::aid-humu16>3.0.co;2-i;
RA Beesley C.E., Child A.H., Yacoub M.Y.;
RT "The identification of five novel mutations in the lysosomal acid alpha-
RT (1,4) glucosidase gene from patients with glycogen storage disease type
RT II.";
RL Hum. Mutat. 11:413-413(1998).
RN [38]
RP VARIANTS GSD2 LEU-545 AND TRP-638.
RX PubMed=10737124; DOI=10.1007/s100480050030;
RA Vorgerd M., Burwinkel B., Reichmann H., Malin J.-P., Kilimann M.W.;
RT "Adult-onset glycogen storage disease type II: phenotypic and allelic
RT heterogeneity in German patients.";
RL Neurogenetics 1:205-211(1998).
RN [39]
RP VARIANT GSD2 ARG-481.
RX PubMed=10189220;
RX DOI=10.1002/(sici)1098-1004(1999)13:1<83::aid-humu13>3.0.co;2-2;
RA Raben N., Lee E., Lee L., Hirschhorn R., Plotz P.H.;
RT "Novel mutations in African American patients with glycogen storage disease
RT Type II.";
RL Hum. Mutat. 13:83-84(1999).
RN [40]
RP VARIANTS GSD2, AND VARIANTS.
RX PubMed=10338092;
RX DOI=10.1002/(sici)1098-1004(1999)13:5<380::aid-humu6>3.0.co;2-a;
RA Ko T.-M., Hwu W.-L., Lin Y.-W., Tseng L.-H., Hwa H.-L., Wang T.-R.,
RA Chuang S.-M.;
RT "Molecular genetic study of Pompe disease in Chinese patients in Taiwan.";
RL Hum. Mutat. 13:380-384(1999).
RN [41]
RP VARIANTS GSD2 PRO-208; LEU-308; LEU-324; MET-585; 607-GLY--HIS-612 DEL;
RP ARG-643 AND THR-672.
RX PubMed=11071489; DOI=10.1212/wnl.55.8.1122;
RA Laforet P., Nicolino M., Eymard P.B., Puech J.P., Caillaud C., Poenaru L.,
RA Fardeau M.;
RT "Juvenile and adult-onset acid maltase deficiency in France: genotype-
RT phenotype correlation.";
RL Neurology 55:1122-1128(2000).
RN [42]
RP VARIANTS GSD2 ARG-219; LYS-262 AND VAL-408.
RX PubMed=11738358; DOI=10.1016/s0960-8966(01)00247-4;
RA Fernandez-Hojas R., Huie M.L., Navarro C., Dominguez C., Roig M.,
RA Lopez-Coronas D., Teijeira S., Anyane-Yeboa K., Hirschhorn R.;
RT "Identification of six novel mutations in the acid alpha-glucosidase gene
RT in three Spanish patients with infantile onset glycogen storage disease
RT type II (Pompe disease).";
RL Neuromuscul. Disord. 12:159-166(2002).
RN [43]
RP VARIANT GSD2 TRP-224, AND CHARACTERIZATION OF VARIANT GSD2 TRP-224.
RX PubMed=12923862; DOI=10.1002/ajmg.a.20164;
RA Pittis M.G., Montalvo A.L., Miocic S., Martini C., Deganuto M.,
RA Candusso M., Ciana G., Bembi B.;
RT "Identification of four novel mutations in the alpha glucosidase gene in
RT five Italian patients with infantile onset glycogen storage disease type
RT II.";
RL Am. J. Med. Genet. A 121:225-230(2003).
RN [44]
RP VARIANTS GSD2 LEU-361 AND CYS-437.
RX PubMed=12601120; DOI=10.1212/01.wnl.0000048661.95327.bf;
RA Lam C.W., Yuen Y.P., Chan K.Y., Tong S.F., Lai C.K., Chow T.C., Lee K.C.,
RA Chan Y.W., Martiniuk F.;
RT "Juvenile-onset glycogen storage disease type II with novel mutations in
RT acid alpha-glucosidase gene.";
RL Neurology 60:715-717(2003).
RN [45]
RP VARIANTS GSD2 TRP-224; CYS-600; ARG-619 AND HIS-660, CHARACTERIZATION OF
RP VARIANTS GSD2 TRP-224; ARG-619 AND HIS-660, AND CHARACTERIZATION OF VARIANT
RP SER-576.
RX PubMed=14643388; DOI=10.1016/s0887-8994(03)00267-4;
RA Pipo J.R., Feng J.-H., Yamamoto T., Ohsaki Y., Nanba E., Tsujino S.,
RA Sakuragawa N., Martiniuk F., Ninomiya H., Oka A., Ohno K.;
RT "New GAA mutations in Japanese patients with GSDII (Pompe disease).";
RL Pediatr. Neurol. 29:284-287(2003).
RN [46]
RP VARIANTS GSD2 GLY-103; ARG-219; ARG-285; CYS-292; ARG-293; PRO-308;
RP ARG-312; PRO-355; ARG-374; PRO-405; PHE-455; ASP-459 DEL; ARG-478; ARG-481;
RP THR-519; LEU-545; ARG-549; PRO-552; SER-575; LYS-579; CYS-600; ASP-607 AND
RP ASP-880, CHARACTERIZATION OF VARIANTS, AND FUNCTION.
RX PubMed=14695532; DOI=10.1002/humu.10286;
RA Hermans M.M.P., van Leenen D., Kroos M.A., Beesley C.E.,
RA Van der Ploeg A.T., Sakuraba H., Wevers R., Kleijer W.J., Michelakakis H.,
RA Kirk E.P., Fletcher J., Bosshard N., Basel-Vanagaite L., Besley G.,
RA Reuser A.J.J.;
RT "Twenty-two novel mutations in the lysosomal alpha-glucosidase gene (GAA)
RT underscore the genotype-phenotype correlation in glycogen storage disease
RT type II.";
RL Hum. Mutat. 23:47-56(2004).
RN [47]
RP VARIANTS GSD2 PRO-355 AND CYS-702, AND CHARACTERIZATION OF VARIANTS GSD2
RP PRO-355 AND CYS-702.
RX PubMed=14972326; DOI=10.1016/j.ymgme.2003.11.011;
RA Montalvo A.L.E., Cariati R., Deganuto M., Guerci V., Garcia R., Ciana G.,
RA Bembi B., Pittis M.G.;
RT "Glycogenosis type II: identification and expression of three novel
RT mutations in the acid alpha-glucosidase gene causing the infantile form of
RT the disease.";
RL Mol. Genet. Metab. 81:203-208(2004).
RN [48]
RP VARIANT GSD2 GLN-901, AND VARIANT ASN-645.
RX PubMed=15145338; DOI=10.1016/j.nmd.2004.02.012;
RA Kroos M.A., Kirschner J., Gellerich F.N., Hermans M.M., Van der Ploeg A.T.,
RA Reuser A.J., Korinthenberg R.;
RT "A case of childhood Pompe disease demonstrating phenotypic variability of
RT p.Asp645Asn.";
RL Neuromuscul. Disord. 14:371-374(2004).
RN [49]
RP VARIANTS GSD2 VAL-237 AND ARG-293.
RX PubMed=15668445; DOI=10.1212/01.wnl.0000149528.95362.20;
RA Anneser J.M., Pongratz D.E., Podskarbi T., Shin Y.S., Schoser B.G.;
RT "Mutations in the acid alpha-glucosidase gene (M. Pompe) in a patient with
RT an unusual phenotype.";
RL Neurology 64:368-370(2005).
RN [50]
RP VARIANT GSD2 GLY-330.
RX PubMed=16782080; DOI=10.1016/j.cca.2006.04.007;
RA Dou W., Gu X., Fu L., Peng C., Zheng J., Martiniuk F., Sheng H.Z.;
RT "A novel missense mutation in the acid alpha-glucosidase gene causing the
RT classic infantile form of Pompe disease.";
RL Clin. Chim. Acta 374:145-146(2006).
RN [51]
RP VARIANT GSD2 GLY-ASN-404.
RX PubMed=16433701; DOI=10.1111/j.1399-0004.2005.00557.x;
RA Amartino H., Painceira D., Pomponio R.J., Niizawa G., Sabio Paz V.,
RA Blanco M., Chamoles N.;
RT "Two clinical forms of glycogen-storage disease type II in two generations
RT of the same family.";
RL Clin. Genet. 69:187-188(2006).
RN [52]
RP VARIANTS GSD2 ARG-309; PRO-355; LEU-361; PRO-445; ASN-489; ARG-549;
RP GLN-612; ARG-643; TRP-672 AND CYS-746.
RX PubMed=16917947; DOI=10.1002/humu.20374;
RA Montalvo A.L., Bembi B., Donnarumma M., Filocamo M., Parenti G., Rossi M.,
RA Merlini L., Buratti E., De Filippi P., Dardis A., Stroppiano M., Ciana G.,
RA Pittis M.G.;
RT "Mutation profile of the GAA gene in 40 Italian patients with late onset
RT glycogen storage disease type II.";
RL Hum. Mutat. 27:999-1006(2006).
RN [53]
RP VARIANTS GSD2 PRO-355; ALA-522 AND VAL-610, AND VARIANT ARG-359.
RX PubMed=17643989; DOI=10.1016/j.nmd.2007.06.002;
RA Muller-Felber W., Horvath R., Gempel K., Podskarbi T., Shin Y.,
RA Pongratz D., Walter M.C., Baethmann M., Schlotter-Weigel B., Lochmuller H.,
RA Schoser B.;
RT "Late onset Pompe disease: clinical and neurophysiological spectrum of 38
RT patients including long-term follow-up in 18 patients.";
RL Neuromuscul. Disord. 17:698-706(2007).
RN [54]
RP VARIANTS GSD2 HIS-190; SER-285; PHE-291; PRO-291; LYS-318; ARG-335;
RP ARG-347; ARG-482; VAL-483; GLN-521; SER-522; LYS-570; GLN-572; PRO-594;
RP LYS-614; ASN-737; SER-746 AND PRO-935, AND VARIANT LYS-585.
RX PubMed=18425781; DOI=10.1002/humu.20745;
RA Kroos M., Pomponio R.J., van Vliet L., Palmer R.E., Phipps M.,
RA Van der Helm R., Halley D., Reuser A.;
RT "Update of the Pompe disease mutation database with 107 sequence variants
RT and a format for severity rating.";
RL Hum. Mutat. 29:E13-E26(2008).
RN [55]
RP VARIANTS GSD2 GLY-103; CYS-191; ARG-219; TRP-224; LYS-262; ARG-293;
RP PRO-355; LEU-375; ARG-401; ASN-489; ALA-522; PRO-552; TYR-599; TRP-638;
RP ARG-643 AND ASN-645, CHARACTERIZATION OF VARIANTS GSD2 CYS-191; LEU-375;
RP ARG-401; ALA-522 AND TYR-599, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18429042; DOI=10.1002/humu.20753;
RA Pittis M.G., Donnarumma M., Montalvo A.L.E., Dominissini S., Kroos M.,
RA Rosano C., Stroppiano M., Bianco M.G., Donati M.A., Parenti G., D'Amico A.,
RA Ciana G., Di Rocco M., Reuser A., Bembi B., Filocamo M.;
RT "Molecular and functional characterization of eight novel GAA mutations in
RT Italian infants with Pompe disease.";
RL Hum. Mutat. 29:E27-E36(2008).
RN [56]
RP VARIANTS GSD2 PRO-46; LEU-217; PRO-486; PRO-594; TYR-612; LYS-635 AND
RP VAL-638.
RX PubMed=19588081; DOI=10.1007/s00415-009-5219-y;
RA Oba-Shinjo S.M., da Silva R., Andrade F.G., Palmer R.E., Pomponio R.J.,
RA Ciociola K.M., Carvalho S.M., Gutierrez P.S., Porta G., Marrone C.D.,
RA Munoz V., Grzesiuk A.K., Llerena J.C. Jr., Berditchevsky C.R., Sobreira C.,
RA Horovitz D., Hatem T.P., Frota E.R., Pecchini R., Kouyoumdjian J.A.,
RA Werneck L., Amado V.M., Camelo J.S. Jr., Mattaliano R.J., Marie S.K.;
RT "Pompe disease in a Brazilian series: clinical and molecular analyses with
RT identification of nine new mutations.";
RL J. Neurol. 256:1881-1890(2009).
RN [57]
RP VARIANT GSD2 SER-558.
RX PubMed=20350966; DOI=10.1177/0883073809356035;
RA Alcantara-Ortigoza M.A., Gonzalez-del Angel A., Barrientos-Rios R.,
RA Cupples C., Garrido-Garcia L.M., de Leon-Bojorge B., Alva-Chaire Adel C.;
RT "Screening of late-onset Pompe disease in a sample of Mexican patients with
RT myopathies of unknown etiology: identification of a novel mutation in the
RT acid alpha-glucosidase gene.";
RL J. Child Neurol. 25:1034-1037(2010).
RN [58]
RP VARIANTS GSD2 PRO-224; LEU-251; LEU-254; LYS-262; SER-266; PRO-291;
RP VAL-408; ARG-478; TYR-525; LEU-545; PHE-557; ARG-615; GLU-645; GLY-746 AND
RP CYS-746, AND VARIANTS ALA-271 AND ARG-711.
RX PubMed=20080426; DOI=10.1016/j.ymgme.2009.12.014;
RA Labrousse P., Chien Y.H., Pomponio R.J., Keutzer J., Lee N.C., Akmaev V.R.,
RA Scholl T., Hwu W.L.;
RT "Genetic heterozygosity and pseudodeficiency in the Pompe disease newborn
RT screening pilot program.";
RL Mol. Genet. Metab. 99:379-383(2010).
RN [59]
RP VARIANT GSD2 GLY-103, AND VARIANT ASN-91.
RX PubMed=21109266; DOI=10.1016/j.jns.2010.10.031;
RA Fidzianska A., Lugowska A., Tylki-Szymanska A.;
RT "Late form of Pompe disease with glycogen storage in peripheral nerves
RT axons.";
RL J. Neurol. Sci. 301:59-62(2011).
RN [60]
RP VARIANTS HIS-74; HIS-89; LEU-220; MET-222; ASP-290; GLY-310; VAL-391;
RP CYS-458; ASP-611; LEU-629; 700-THR-LEU-701 DEL AND ILE-718, AND VARIANTS
RP GSD2 ARG-103; GLY-108; PHE-127; GLN-224; ARG-234; LYS-234; ILE-316;
RP GLU-335; LEU-361; LEU-397; VAL-419; HIS-457; TYR-523; SER-558; CYS-575;
RP ARG-576; HIS-594; LEU-601; ALA-602; PRO-627; ASP-648; LEU-702; LYS-743;
RP PRO-819 AND PHE-916.
RX PubMed=22644586; DOI=10.1002/humu.22108;
RA Kroos M., Hoogeveen-Westerveld M., Michelakakis H., Pomponio R.,
RA Van der Ploeg A., Halley D., Reuser A., Augoustides-Savvopoulou P.,
RA Ausems M., Llona J.B., Bautista Lorite J., van der Beek N., Bonafe L.,
RA Cuk M., D'Hooghe M., Engelen B., Farouk A., Fumic K., Garcia-Delgado E.,
RA Herzog A., Hurst J., Jones S., Kariminejad M.H., Kucukcongar A.,
RA Lissens W., Lund A., Majoor-Krakauer D., Kumamoto S., Maravi E., Marie S.,
RA Mengel E., Mavridou I., Munteis Olivas E., Najmabadi H., Okumiya T.,
RA Peric S., Paschke E., Plecko B., Robberecht W., Serdaroglu P., Shboul M.,
RA Tansek M.Z., Tarnutzer A., Stojanovic V.R., Tylki-Szymanska A.,
RA Venancio M., Verhoeven K.;
RT "Update of the pompe disease mutation database with 60 novel GAA sequence
RT variants and additional studies on the functional effect of 34 previously
RT reported variants.";
RL Hum. Mutat. 33:1161-1165(2012).
RN [61]
RP VARIANTS GSD2 LYS-234; 431-LEU--GLN-433 DEL; LEU-568; LEU-601; CYS-766 AND
RP ARG-913.
RX PubMed=22676651; DOI=10.1186/1750-1172-7-35;
RA Herzog A., Hartung R., Reuser A.J., Hermanns P., Runz H., Karabul N.,
RA Goekce S., Pohlenz J., Kampmann C., Lampe C., Beck M., Mengel E.;
RT "A cross-sectional single-centre study on the spectrum of Pompe disease,
RT German patients: molecular analysis of the GAA gene, manifestation and
RT genotype-phenotype correlations.";
RL Orphanet J. Rare Dis. 7:35-35(2012).
RN [62]
RP VARIANTS GSD2 VAL-391; HIS-437; PRO-552; ASP-611; VAL-641; TRP-647 AND
RP PRO-705, AND VARIANTS ASN-91; ARG-199; HIS-223; SER-576; LYS-689; ILE-780
RP AND ILE-816.
RX PubMed=25681614; DOI=10.1016/j.gene.2015.02.023;
RA Turaca L.T., de Faria D.O., Kyosen S.O., Teixeira V.D., Motta F.L.,
RA Pessoa J.G., Rodrigues E Silva M., de Almeida S.S., D'Almeida V.,
RA Munoz Rojas M.V., Martins A.M., Pesquero J.B.;
RT "Novel GAA mutations in patients with Pompe disease.";
RL Gene 561:124-131(2015).
CC -!- FUNCTION: Essential for the degradation of glycogen in lysosomes
CC (PubMed:1856189, PubMed:7717400, PubMed:14695532, PubMed:18429042). Has
CC highest activity on alpha-1,4-linked glycosidic linkages, but can also
CC hydrolyze alpha-1,6-linked glucans (PubMed:29061980).
CC {ECO:0000269|PubMed:14695532, ECO:0000269|PubMed:18429042,
CC ECO:0000269|PubMed:1856189, ECO:0000269|PubMed:29061980,
CC ECO:0000269|PubMed:7717400}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-
CC glucose residues with release of alpha-D-glucose.; EC=3.2.1.20;
CC Evidence={ECO:0000269|PubMed:18429042, ECO:0000269|PubMed:1856189,
CC ECO:0000269|PubMed:29061980, ECO:0000269|PubMed:7717400};
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:17897319}. Lysosome
CC membrane {ECO:0000269|PubMed:17897319}.
CC -!- PTM: The different forms of acid glucosidase are obtained by
CC proteolytic processing. {ECO:0000269|PubMed:3049072}.
CC -!- PTM: Phosphorylation of mannose residues ensures efficient transport of
CC the enzyme to the lysosomes via the mannose 6-phosphate receptor.
CC -!- POLYMORPHISM: There are three common alleles of GAA: GAA*1, GAA*2 and
CC GAA*4. The sequence shown is that of allele GAA*1, which is the most
CC common. Alleles GAA*2 and GAA*4 are much rarer.
CC {ECO:0000269|PubMed:21109266, ECO:0000269|PubMed:2203258,
CC ECO:0000269|PubMed:25681614, ECO:0000269|PubMed:8912788,
CC ECO:0000269|PubMed:9521422}.
CC -!- DISEASE: Glycogen storage disease 2 (GSD2) [MIM:232300]: A metabolic
CC disorder with a broad clinical spectrum. The severe infantile form, or
CC Pompe disease, presents at birth with massive accumulation of glycogen
CC in muscle, heart and liver. Cardiomyopathy and muscular hypotonia are
CC the cardinal features of this form whose life expectancy is less than
CC two years. The juvenile and adult forms present as limb-girdle muscular
CC dystrophy beginning in the lower limbs. Final outcome depends on
CC respiratory muscle failure. Patients with the adult form can be free of
CC clinical symptoms for most of their life but finally develop a slowly
CC progressive myopathy. {ECO:0000269|PubMed:10189220,
CC ECO:0000269|PubMed:10206684, ECO:0000269|PubMed:10338092,
CC ECO:0000269|PubMed:10737124, ECO:0000269|PubMed:11071489,
CC ECO:0000269|PubMed:11738358, ECO:0000269|PubMed:12601120,
CC ECO:0000269|PubMed:12923862, ECO:0000269|PubMed:14643388,
CC ECO:0000269|PubMed:14695532, ECO:0000269|PubMed:14972326,
CC ECO:0000269|PubMed:15145338, ECO:0000269|PubMed:15668445,
CC ECO:0000269|PubMed:16433701, ECO:0000269|PubMed:1652892,
CC ECO:0000269|PubMed:16782080, ECO:0000269|PubMed:1684505,
CC ECO:0000269|PubMed:16917947, ECO:0000269|PubMed:17643989,
CC ECO:0000269|PubMed:18425781, ECO:0000269|PubMed:18429042,
CC ECO:0000269|PubMed:1898413, ECO:0000269|PubMed:19588081,
CC ECO:0000269|PubMed:20080426, ECO:0000269|PubMed:20350966,
CC ECO:0000269|PubMed:21109266, ECO:0000269|PubMed:22644586,
CC ECO:0000269|PubMed:22676651, ECO:0000269|PubMed:25681614,
CC ECO:0000269|PubMed:7695647, ECO:0000269|PubMed:7717400,
CC ECO:0000269|PubMed:7866409, ECO:0000269|PubMed:7881422,
CC ECO:0000269|PubMed:7981676, ECO:0000269|PubMed:8094613,
CC ECO:0000269|PubMed:8401535, ECO:0000269|PubMed:8834250,
CC ECO:0000269|PubMed:9521422, ECO:0000269|PubMed:9535769,
CC ECO:0000269|PubMed:9660056, ECO:0000269|Ref.5}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=GAA; Note=Mutations in alpha-glucosidase;
CC URL="https://medlineplus.gov/genetics/gene/gaa/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Alpha-glucosidase entry;
CC URL="https://en.wikipedia.org/wiki/Alpha-glucosidase";
CC -!- WEB RESOURCE: Name=Glucosidase, alpha, acid (Pompe disease) (GAA);
CC Note=Leiden Open Variation Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/GAA";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
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DR EMBL; Y00839; CAA68763.1; -; mRNA.
DR EMBL; Y00839; CAA68764.1; -; mRNA.
DR EMBL; X55080; CAC12967.1; -; Genomic_DNA.
DR EMBL; X55081; CAC12967.1; JOINED; Genomic_DNA.
DR EMBL; X55095; CAC12967.1; JOINED; Genomic_DNA.
DR EMBL; X55082; CAC12967.1; JOINED; Genomic_DNA.
DR EMBL; X55084; CAC12967.1; JOINED; Genomic_DNA.
DR EMBL; X55083; CAC12967.1; JOINED; Genomic_DNA.
DR EMBL; X55098; CAC12967.1; JOINED; Genomic_DNA.
DR EMBL; X55085; CAC12967.1; JOINED; Genomic_DNA.
DR EMBL; X55086; CAC12967.1; JOINED; Genomic_DNA.
DR EMBL; X55087; CAC12967.1; JOINED; Genomic_DNA.
DR EMBL; X55088; CAC12967.1; JOINED; Genomic_DNA.
DR EMBL; X55089; CAC12967.1; JOINED; Genomic_DNA.
DR EMBL; X55090; CAC12967.1; JOINED; Genomic_DNA.
DR EMBL; X55096; CAC12967.1; JOINED; Genomic_DNA.
DR EMBL; X55091; CAC12967.1; JOINED; Genomic_DNA.
DR EMBL; X55092; CAC12967.1; JOINED; Genomic_DNA.
DR EMBL; X55093; CAC12967.1; JOINED; Genomic_DNA.
DR EMBL; X55094; CAC12967.1; JOINED; Genomic_DNA.
DR EMBL; X55097; CAC12967.1; JOINED; Genomic_DNA.
DR EMBL; M34424; AAA52506.1; -; mRNA.
DR EMBL; DQ907243; ABI53718.1; -; mRNA.
DR EMBL; AC087741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040431; AAH40431.1; -; mRNA.
DR EMBL; S76893; AAB33842.1; -; mRNA.
DR CCDS; CCDS32760.1; -.
DR PIR; A40577; A32609.
DR RefSeq; NP_000143.2; NM_000152.4.
DR RefSeq; NP_001073271.1; NM_001079803.2.
DR RefSeq; NP_001073272.1; NM_001079804.2.
DR RefSeq; XP_005257250.1; XM_005257193.2.
DR RefSeq; XP_005257251.1; XM_005257194.4.
DR PDB; 5KZW; X-ray; 2.00 A; A=79-952.
DR PDB; 5KZX; X-ray; 2.00 A; A=79-952.
DR PDB; 5NN3; X-ray; 1.90 A; A=81-952.
DR PDB; 5NN4; X-ray; 1.83 A; A=81-952.
DR PDB; 5NN5; X-ray; 2.00 A; A=81-952.
DR PDB; 5NN6; X-ray; 2.00 A; A=81-952.
DR PDB; 5NN8; X-ray; 2.45 A; A=81-952.
DR PDBsum; 5KZW; -.
DR PDBsum; 5KZX; -.
DR PDBsum; 5NN3; -.
DR PDBsum; 5NN4; -.
DR PDBsum; 5NN5; -.
DR PDBsum; 5NN6; -.
DR PDBsum; 5NN8; -.
DR AlphaFoldDB; P10253; -.
DR SMR; P10253; -.
DR BioGRID; 108823; 126.
DR IntAct; P10253; 30.
DR MINT; P10253; -.
DR STRING; 9606.ENSP00000305692; -.
DR BindingDB; P10253; -.
DR ChEMBL; CHEMBL2608; -.
DR DrugBank; DB00284; Acarbose.
DR DrugBank; DB05200; AT2220.
DR DrugBank; DB00491; Miglitol.
DR DrugBank; DB14962; Trastuzumab deruxtecan.
DR DrugCentral; P10253; -.
DR GuidetoPHARMACOLOGY; 2611; -.
DR Allergome; 9614; Hom s Glucosidase.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR GlyConnect; 723; 17 N-Linked glycans (7 sites).
DR GlyGen; P10253; 11 sites, 28 N-linked glycans (7 sites), 1 O-linked glycan (3 sites).
DR iPTMnet; P10253; -.
DR MetOSite; P10253; -.
DR PhosphoSitePlus; P10253; -.
DR BioMuta; GAA; -.
DR DMDM; 317373572; -.
DR CPTAC; CPTAC-2224; -.
DR EPD; P10253; -.
DR jPOST; P10253; -.
DR MassIVE; P10253; -.
DR MaxQB; P10253; -.
DR PaxDb; P10253; -.
DR PeptideAtlas; P10253; -.
DR PRIDE; P10253; -.
DR ProteomicsDB; 52587; -.
DR Antibodypedia; 32676; 337 antibodies from 33 providers.
DR DNASU; 2548; -.
DR Ensembl; ENST00000302262.8; ENSP00000305692.3; ENSG00000171298.13.
DR Ensembl; ENST00000390015.7; ENSP00000374665.3; ENSG00000171298.13.
DR GeneID; 2548; -.
DR KEGG; hsa:2548; -.
DR MANE-Select; ENST00000302262.8; ENSP00000305692.3; NM_000152.5; NP_000143.2.
DR UCSC; uc002jxo.4; human.
DR CTD; 2548; -.
DR DisGeNET; 2548; -.
DR GeneCards; GAA; -.
DR GeneReviews; GAA; -.
DR HGNC; HGNC:4065; GAA.
DR HPA; ENSG00000171298; Low tissue specificity.
DR MalaCards; GAA; -.
DR MIM; 232300; phenotype.
DR MIM; 606800; gene.
DR neXtProt; NX_P10253; -.
DR OpenTargets; ENSG00000171298; -.
DR Orphanet; 308552; Glycogen storage disease due to acid maltase deficiency, infantile onset.
DR Orphanet; 420429; Glycogen storage disease due to acid maltase deficiency, late-onset.
DR PharmGKB; PA28476; -.
DR VEuPathDB; HostDB:ENSG00000171298; -.
DR eggNOG; KOG1065; Eukaryota.
DR GeneTree; ENSGT00940000159355; -.
DR HOGENOM; CLU_000631_11_2_1; -.
DR InParanoid; P10253; -.
DR OMA; YDTYTRG; -.
DR OrthoDB; 151244at2759; -.
DR PhylomeDB; P10253; -.
DR TreeFam; TF314577; -.
DR BRENDA; 3.2.1.20; 2681.
DR PathwayCommons; P10253; -.
DR Reactome; R-HSA-5357609; Glycogen storage disease type II (GAA).
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-70221; Glycogen breakdown (glycogenolysis).
DR SignaLink; P10253; -.
DR BioGRID-ORCS; 2548; 12 hits in 1069 CRISPR screens.
DR ChiTaRS; GAA; human.
DR GeneWiki; Acid_alpha-glucosidase; -.
DR GenomeRNAi; 2548; -.
DR Pharos; P10253; Tclin.
DR PRO; PR:P10253; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P10253; protein.
DR Bgee; ENSG00000171298; Expressed in granulocyte and 175 other tissues.
DR ExpressionAtlas; P10253; baseline and differential.
DR Genevisible; P10253; HS.
DR GO; GO:0120282; C:autolysosome lumen; IEA:Ensembl.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0004558; F:alpha-1,4-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0090599; F:alpha-glucosidase activity; EXP:Reactome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL.
DR GO; GO:0002086; P:diaphragm contraction; IMP:BHF-UCL.
DR GO; GO:0006006; P:glucose metabolic process; IC:BHF-UCL.
DR GO; GO:0005980; P:glycogen catabolic process; IDA:UniProtKB.
DR GO; GO:0061723; P:glycophagy; IEA:Ensembl.
DR GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0007040; P:lysosome organization; IMP:BHF-UCL.
DR GO; GO:0000023; P:maltose metabolic process; IC:BHF-UCL.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR GO; GO:0050884; P:neuromuscular process controlling posture; IEA:Ensembl.
DR GO; GO:0002026; P:regulation of the force of heart contraction; IEA:Ensembl.
DR GO; GO:0005985; P:sucrose metabolic process; IC:BHF-UCL.
DR GO; GO:0009888; P:tissue development; IEA:Ensembl.
DR GO; GO:0043181; P:vacuolar sequestering; IMP:BHF-UCL.
DR CDD; cd00111; Trefoil; 1.
DR Gene3D; 2.60.40.1180; -; 2.
DR Gene3D; 4.10.110.10; -; 1.
DR InterPro; IPR031727; Gal_mutarotase_N.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR030459; Glyco_hydro_31_CS.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR017957; P_trefoil_CS.
DR InterPro; IPR000519; P_trefoil_dom.
DR InterPro; IPR044913; P_trefoil_dom_sf.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR Pfam; PF16863; NtCtMGAM_N; 1.
DR Pfam; PF00088; Trefoil; 1.
DR SMART; SM00018; PD; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF57492; SSF57492; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
DR PROSITE; PS00025; P_TREFOIL_1; 1.
DR PROSITE; PS51448; P_TREFOIL_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disease variant; Disulfide bond;
KW Glycogen storage disease; Glycoprotein; Glycosidase; Hydrolase; Lysosome;
KW Membrane; Phosphoprotein; Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..69
FT /evidence="ECO:0000269|PubMed:3049072"
FT /id="PRO_0000018565"
FT CHAIN 70..952
FT /note="Lysosomal alpha-glucosidase"
FT /id="PRO_0000018566"
FT CHAIN 123..952
FT /note="76 kDa lysosomal alpha-glucosidase"
FT /id="PRO_0000018567"
FT CHAIN 204..952
FT /note="70 kDa lysosomal alpha-glucosidase"
FT /id="PRO_0000018568"
FT DOMAIN 80..131
FT /note="P-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT REGION 47..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 518
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10066,
FT ECO:0000269|PubMed:1856189, ECO:0000305|PubMed:29061980"
FT ACT_SITE 521
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:29061980"
FT BINDING 600
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:29061980"
FT BINDING 616
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:29061980"
FT BINDING 674
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:29061980"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:29061980, ECO:0000269|PubMed:8435067,
FT ECO:0000269|Ref.19, ECO:0007744|PDB:5KZW,
FT ECO:0007744|PDB:5NN3"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29061980,
FT ECO:0000269|PubMed:8435067, ECO:0000269|Ref.19,
FT ECO:0007744|PDB:5KZW, ECO:0007744|PDB:5NN3"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:29061980, ECO:0000269|PubMed:8435067,
FT ECO:0000269|Ref.19, ECO:0007744|PDB:5KZW,
FT ECO:0007744|PDB:5NN3"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:29061980,
FT ECO:0000269|PubMed:8435067, ECO:0000269|Ref.19,
FT ECO:0007744|PDB:5KZW, ECO:0007744|PDB:5NN3"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29061980,
FT ECO:0000269|PubMed:8435067, ECO:0000269|Ref.19,
FT ECO:0007744|PDB:5KZW, ECO:0007744|PDB:5NN3"
FT CARBOHYD 882
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:29061980, ECO:0000269|PubMed:8435067,
FT ECO:0000269|Ref.19, ECO:0007744|PDB:5KZW,
FT ECO:0007744|PDB:5NN3"
FT CARBOHYD 925
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:8435067"
FT DISULFID 82..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779,
FT ECO:0000269|PubMed:29061980, ECO:0000269|Ref.19,
FT ECO:0007744|PDB:5KZW, ECO:0007744|PDB:5KZX,
FT ECO:0007744|PDB:5NN3, ECO:0007744|PDB:5NN4,
FT ECO:0007744|PDB:5NN5, ECO:0007744|PDB:5NN6,
FT ECO:0007744|PDB:5NN8"
FT DISULFID 92..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779,
FT ECO:0000269|PubMed:29061980, ECO:0000269|Ref.19,
FT ECO:0007744|PDB:5KZW, ECO:0007744|PDB:5KZX,
FT ECO:0007744|PDB:5NN3, ECO:0007744|PDB:5NN4,
FT ECO:0007744|PDB:5NN5, ECO:0007744|PDB:5NN6,
FT ECO:0007744|PDB:5NN8"
FT DISULFID 103..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779,
FT ECO:0000269|PubMed:29061980, ECO:0000269|Ref.19,
FT ECO:0007744|PDB:5KZW, ECO:0007744|PDB:5KZX,
FT ECO:0007744|PDB:5NN3, ECO:0007744|PDB:5NN4,
FT ECO:0007744|PDB:5NN5, ECO:0007744|PDB:5NN6,
FT ECO:0007744|PDB:5NN8"
FT DISULFID 533..558
FT /evidence="ECO:0000269|PubMed:29061980, ECO:0000269|Ref.19,
FT ECO:0007744|PDB:5KZW, ECO:0007744|PDB:5KZX,
FT ECO:0007744|PDB:5NN3, ECO:0007744|PDB:5NN4,
FT ECO:0007744|PDB:5NN5, ECO:0007744|PDB:5NN6,
FT ECO:0007744|PDB:5NN8"
FT DISULFID 647..658
FT /evidence="ECO:0000269|PubMed:29061980, ECO:0000269|Ref.19,
FT ECO:0007744|PDB:5KZW, ECO:0007744|PDB:5KZX,
FT ECO:0007744|PDB:5NN3, ECO:0007744|PDB:5NN4,
FT ECO:0007744|PDB:5NN5, ECO:0007744|PDB:5NN6,
FT ECO:0007744|PDB:5NN8"
FT VARIANT 46
FT /note="S -> P (in GSD2; dbSNP:rs777215354)"
FT /evidence="ECO:0000269|PubMed:19588081"
FT /id="VAR_068564"
FT VARIANT 74
FT /note="R -> H (in dbSNP:rs764797280)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068565"
FT VARIANT 89
FT /note="R -> H (in dbSNP:rs200586324)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068566"
FT VARIANT 91
FT /note="D -> N (in allele GAA*2; lower affinity for glycogen
FT and starch but not for lower-molecular weight substrates;
FT dbSNP:rs1800299)"
FT /evidence="ECO:0000269|PubMed:21109266,
FT ECO:0000269|PubMed:2203258, ECO:0000269|PubMed:25681614,
FT ECO:0000269|PubMed:9521422"
FT /id="VAR_004285"
FT VARIANT 103
FT /note="C -> G (in GSD2; infantile form; severe; loss of
FT activity; shows enzyme localization primarily in the ER-
FT Golgi compartment suggesting that mutation could affect the
FT normal processing and stability of the enzyme;
FT dbSNP:rs398123174)"
FT /evidence="ECO:0000269|PubMed:14695532,
FT ECO:0000269|PubMed:18429042, ECO:0000269|PubMed:21109266"
FT /id="VAR_018078"
FT VARIANT 103
FT /note="C -> R (in GSD2)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068567"
FT VARIANT 108
FT /note="C -> G (in GSD2)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068568"
FT VARIANT 127
FT /note="C -> F (in GSD2)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068569"
FT VARIANT 190
FT /note="R -> H (in GSD2; dbSNP:rs528367092)"
FT /evidence="ECO:0000269|PubMed:18425781"
FT /id="VAR_068570"
FT VARIANT 191
FT /note="Y -> C (in GSD2; extremely low residual enzymatic
FT activity)"
FT /evidence="ECO:0000269|PubMed:18429042"
FT /id="VAR_046467"
FT VARIANT 199
FT /note="H -> R (in dbSNP:rs1042393)"
FT /evidence="ECO:0000269|PubMed:25681614,
FT ECO:0000269|PubMed:3049072, ECO:0000269|PubMed:7717400,
FT ECO:0000269|PubMed:9521422, ECO:0000269|Ref.5"
FT /id="VAR_004286"
FT VARIANT 208
FT /note="L -> P (in GSD2)"
FT /evidence="ECO:0000269|PubMed:11071489"
FT /id="VAR_029025"
FT VARIANT 217
FT /note="P -> L (in GSD2)"
FT /evidence="ECO:0000269|PubMed:19588081"
FT /id="VAR_068571"
FT VARIANT 219
FT /note="G -> R (in GSD2; infantile form; severe; loss of
FT activity; dbSNP:rs370950728)"
FT /evidence="ECO:0000269|PubMed:11738358,
FT ECO:0000269|PubMed:14695532, ECO:0000269|PubMed:18429042"
FT /id="VAR_018079"
FT VARIANT 220
FT /note="V -> L (in dbSNP:rs530478036)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068572"
FT VARIANT 222
FT /note="V -> M (in dbSNP:rs374569672)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068573"
FT VARIANT 223
FT /note="R -> H (in dbSNP:rs1042395)"
FT /evidence="ECO:0000269|PubMed:25681614,
FT ECO:0000269|PubMed:3049072, ECO:0000269|PubMed:7717400,
FT ECO:0000269|PubMed:9521422, ECO:0000269|Ref.5"
FT /id="VAR_004287"
FT VARIANT 224
FT /note="R -> P (in GSD2; dbSNP:rs200210219)"
FT /evidence="ECO:0000269|PubMed:20080426"
FT /id="VAR_068574"
FT VARIANT 224
FT /note="R -> Q (in GSD2; dbSNP:rs200210219)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068575"
FT VARIANT 224
FT /note="R -> W (in GSD2; infantile; mild partial loss of
FT activity; dbSNP:rs757700700)"
FT /evidence="ECO:0000269|PubMed:12923862,
FT ECO:0000269|PubMed:14643388, ECO:0000269|PubMed:18429042"
FT /id="VAR_029026"
FT VARIANT 234
FT /note="T -> K (in GSD2)"
FT /evidence="ECO:0000269|PubMed:22644586,
FT ECO:0000269|PubMed:22676651"
FT /id="VAR_068576"
FT VARIANT 234
FT /note="T -> R (in GSD2)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068577"
FT VARIANT 237
FT /note="A -> V (in GSD2; dbSNP:rs121907944)"
FT /evidence="ECO:0000269|PubMed:15668445"
FT /id="VAR_029027"
FT VARIANT 251
FT /note="S -> L (in GSD2; dbSNP:rs200856561)"
FT /evidence="ECO:0000269|PubMed:20080426"
FT /id="VAR_068578"
FT VARIANT 254
FT /note="S -> L (in GSD2; dbSNP:rs577915581)"
FT /evidence="ECO:0000269|PubMed:20080426"
FT /id="VAR_068579"
FT VARIANT 262
FT /note="E -> K (in GSD2; infantile; severe;
FT dbSNP:rs201896815)"
FT /evidence="ECO:0000269|PubMed:11738358,
FT ECO:0000269|PubMed:18429042, ECO:0000269|PubMed:20080426"
FT /id="VAR_029028"
FT VARIANT 266
FT /note="P -> S (in GSD2; dbSNP:rs1555599667)"
FT /evidence="ECO:0000269|PubMed:20080426"
FT /id="VAR_068580"
FT VARIANT 271
FT /note="T -> A"
FT /evidence="ECO:0000269|PubMed:20080426"
FT /id="VAR_068581"
FT VARIANT 285
FT /note="P -> R (in GSD2; juvenile form; mild; partial loss
FT of activity; dbSNP:rs764622267)"
FT /evidence="ECO:0000269|PubMed:14695532"
FT /id="VAR_018080"
FT VARIANT 285
FT /note="P -> S (in GSD2; dbSNP:rs886042086)"
FT /evidence="ECO:0000269|PubMed:18425781"
FT /id="VAR_068582"
FT VARIANT 290
FT /note="N -> D (in dbSNP:rs552929702)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068583"
FT VARIANT 291
FT /note="L -> F (in GSD2; dbSNP:rs773417785)"
FT /evidence="ECO:0000269|PubMed:18425781"
FT /id="VAR_068584"
FT VARIANT 291
FT /note="L -> P (in GSD2)"
FT /evidence="ECO:0000269|PubMed:18425781,
FT ECO:0000269|PubMed:20080426"
FT /id="VAR_068585"
FT VARIANT 292
FT /note="Y -> C (in GSD2; juvenile form; mild; partial loss
FT of activity; dbSNP:rs1057516600)"
FT /evidence="ECO:0000269|PubMed:14695532"
FT /id="VAR_018081"
FT VARIANT 293
FT /note="G -> R (in GSD2; infantile form; severe; almost
FT complete loss of activity; dbSNP:rs121907945)"
FT /evidence="ECO:0000269|PubMed:14695532,
FT ECO:0000269|PubMed:15668445, ECO:0000269|PubMed:18429042"
FT /id="VAR_018082"
FT VARIANT 299
FT /note="L -> R (in GSD2; infantile form; dbSNP:rs121907940)"
FT /evidence="ECO:0000269|PubMed:7717400"
FT /id="VAR_004288"
FT VARIANT 308
FT /note="H -> L (in GSD2)"
FT /evidence="ECO:0000269|PubMed:11071489"
FT /id="VAR_046468"
FT VARIANT 308
FT /note="H -> P (in GSD2; infantile form; severe; complete
FT loss of activity)"
FT /evidence="ECO:0000269|PubMed:14695532"
FT /id="VAR_018083"
FT VARIANT 309
FT /note="G -> R (in GSD2; severe; dbSNP:rs543300039)"
FT /evidence="ECO:0000269|PubMed:16917947,
FT ECO:0000269|PubMed:9660056"
FT /id="VAR_018084"
FT VARIANT 310
FT /note="V -> G (found in a patient with GSD2; unknown
FT pathological significance; dbSNP:rs763091901)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068586"
FT VARIANT 312
FT /note="L -> R (in GSD2; infantile form; severe; loss of
FT activity)"
FT /evidence="ECO:0000269|PubMed:14695532"
FT /id="VAR_018085"
FT VARIANT 316
FT /note="N -> I (in GSD2)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068587"
FT VARIANT 318
FT /note="M -> K (in GSD2)"
FT /evidence="ECO:0000269|PubMed:18425781"
FT /id="VAR_068588"
FT VARIANT 318
FT /note="M -> T (in GSD2; severe; dbSNP:rs121907936)"
FT /evidence="ECO:0000269|PubMed:1652892"
FT /id="VAR_004289"
FT VARIANT 324
FT /note="P -> L (in GSD2; dbSNP:rs750030887)"
FT /evidence="ECO:0000269|PubMed:11071489"
FT /id="VAR_029029"
FT VARIANT 330
FT /note="W -> G (in GSD2; infantile form; severe)"
FT /evidence="ECO:0000269|PubMed:16782080"
FT /id="VAR_029030"
FT VARIANT 335
FT /note="G -> E (in GSD2; dbSNP:rs730880022)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068589"
FT VARIANT 335
FT /note="G -> R (in GSD2; dbSNP:rs202095215)"
FT /evidence="ECO:0000269|PubMed:18425781"
FT /id="VAR_068590"
FT VARIANT 347
FT /note="P -> R (in GSD2)"
FT /evidence="ECO:0000269|PubMed:18425781"
FT /id="VAR_068591"
FT VARIANT 355
FT /note="L -> P (in GSD2; infantile form; severe; loss of
FT activity; dbSNP:rs766074609)"
FT /evidence="ECO:0000269|PubMed:14695532,
FT ECO:0000269|PubMed:14972326, ECO:0000269|PubMed:16917947,
FT ECO:0000269|PubMed:17643989, ECO:0000269|PubMed:18429042"
FT /id="VAR_018086"
FT VARIANT 359
FT /note="G -> R"
FT /evidence="ECO:0000269|PubMed:17643989"
FT /id="VAR_068592"
FT VARIANT 361
FT /note="P -> L (in GSD2; juvenile form; severe;
FT dbSNP:rs755253527)"
FT /evidence="ECO:0000269|PubMed:12601120,
FT ECO:0000269|PubMed:16917947, ECO:0000269|PubMed:22644586"
FT /id="VAR_029031"
FT VARIANT 374
FT /note="C -> R (in GSD2; infantile form; severe; loss of
FT activity)"
FT /evidence="ECO:0000269|PubMed:14695532"
FT /id="VAR_018087"
FT VARIANT 375
FT /note="R -> L (in GSD2; extremely low residual enzymatic
FT activity; dbSNP:rs142752477)"
FT /evidence="ECO:0000269|PubMed:18429042"
FT /id="VAR_046469"
FT VARIANT 377
FT /note="G -> R (in GSD2; severe; dbSNP:rs752002666)"
FT /id="VAR_029032"
FT VARIANT 391
FT /note="M -> V (found in a patient with GSD2; unknown
FT pathological significance; dbSNP:rs778634337)"
FT /evidence="ECO:0000269|PubMed:22644586,
FT ECO:0000269|PubMed:25681614"
FT /id="VAR_068593"
FT VARIANT 397
FT /note="P -> L (in GSD2; dbSNP:rs776008078)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068594"
FT VARIANT 401
FT /note="Q -> R (in GSD2; extremely low residual enzymatic
FT activity)"
FT /evidence="ECO:0000269|PubMed:18429042"
FT /id="VAR_046470"
FT VARIANT 402
FT /note="W -> R (in GSD2; severe)"
FT /id="VAR_004290"
FT VARIANT 404
FT /note="D -> N (in GSD2; severe; dbSNP:rs141533320)"
FT /id="VAR_029033"
FT VARIANT 405
FT /note="L -> P (in GSD2; infantile form; severe; loss of
FT activity)"
FT /evidence="ECO:0000269|PubMed:14695532"
FT /id="VAR_018088"
FT VARIANT 408
FT /note="M -> V (in GSD2; juvenile form; severe;
FT dbSNP:rs560575383)"
FT /evidence="ECO:0000269|PubMed:11738358,
FT ECO:0000269|PubMed:20080426"
FT /id="VAR_029034"
FT VARIANT 419
FT /note="D -> V (in GSD2)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068595"
FT VARIANT 431..433
FT /note="Missing (in GSD2)"
FT /evidence="ECO:0000269|PubMed:22676651"
FT /id="VAR_070017"
FT VARIANT 437
FT /note="R -> C (in GSD2; juvenile form; severe;
FT dbSNP:rs770610356)"
FT /evidence="ECO:0000269|PubMed:12601120"
FT /id="VAR_029035"
FT VARIANT 437
FT /note="R -> H (in GSD2; unknown pathological significance;
FT dbSNP:rs150868652)"
FT /evidence="ECO:0000269|PubMed:25681614"
FT /id="VAR_074277"
FT VARIANT 445
FT /note="A -> P (in GSD2)"
FT /evidence="ECO:0000269|PubMed:16917947"
FT /id="VAR_029036"
FT VARIANT 455
FT /note="Y -> F (in GSD2; juvenile form; almost complete loss
FT of activity)"
FT /evidence="ECO:0000269|PubMed:14695532"
FT /id="VAR_018089"
FT VARIANT 457
FT /note="P -> H (in GSD2)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068596"
FT VARIANT 457
FT /note="P -> L (in GSD2; juvenile form)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_029040"
FT VARIANT 458
FT /note="Y -> C (in dbSNP:rs1358826817)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068597"
FT VARIANT 459
FT /note="Missing (in GSD2; infantile form; severe)"
FT /evidence="ECO:0000269|PubMed:14695532"
FT /id="VAR_018090"
FT VARIANT 478
FT /note="G -> R (in GSD2; severe; loss of activity;
FT dbSNP:rs778068209)"
FT /evidence="ECO:0000269|PubMed:14695532,
FT ECO:0000269|PubMed:20080426"
FT /id="VAR_004291"
FT VARIANT 481
FT /note="W -> R (in GSD2; severe; loss of activity;
FT dbSNP:rs772883420)"
FT /evidence="ECO:0000269|PubMed:10189220,
FT ECO:0000269|PubMed:14695532"
FT /id="VAR_004292"
FT VARIANT 482
FT /note="P -> R (in GSD2)"
FT /evidence="ECO:0000269|PubMed:18425781"
FT /id="VAR_068598"
FT VARIANT 483
FT /note="G -> V (in GSD2)"
FT /evidence="ECO:0000269|PubMed:18425781"
FT /id="VAR_068599"
FT VARIANT 486
FT /note="A -> P (in GSD2)"
FT /evidence="ECO:0000269|PubMed:19588081"
FT /id="VAR_068600"
FT VARIANT 489
FT /note="D -> N (in GSD2; severe; dbSNP:rs398123169)"
FT /evidence="ECO:0000269|PubMed:16917947,
FT ECO:0000269|PubMed:18429042"
FT /id="VAR_029037"
FT VARIANT 519
FT /note="M -> T (in GSD2; severe; loss of activity;
FT dbSNP:rs786204720)"
FT /evidence="ECO:0000269|PubMed:14695532"
FT /id="VAR_004293"
FT VARIANT 519
FT /note="M -> V (in GSD2)"
FT /evidence="ECO:0000269|PubMed:7866409"
FT /id="VAR_004294"
FT VARIANT 521
FT /note="E -> K (in GSD2; severe; dbSNP:rs121907937)"
FT /evidence="ECO:0000269|PubMed:1898413"
FT /id="VAR_004295"
FT VARIANT 521
FT /note="E -> Q (in GSD2)"
FT /evidence="ECO:0000269|PubMed:18425781"
FT /id="VAR_068601"
FT VARIANT 522
FT /note="P -> A (in GSD2; no residual enzymatic activity;
FT dbSNP:rs1057517146)"
FT /evidence="ECO:0000269|PubMed:17643989,
FT ECO:0000269|PubMed:18429042"
FT /id="VAR_046471"
FT VARIANT 522
FT /note="P -> S (in GSD2; dbSNP:rs892129065)"
FT /evidence="ECO:0000269|PubMed:18425781"
FT /id="VAR_068602"
FT VARIANT 523
FT /note="S -> Y (in GSD2)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068603"
FT VARIANT 525
FT /note="F -> Y (in GSD2)"
FT /evidence="ECO:0000269|PubMed:20080426"
FT /id="VAR_068604"
FT VARIANT 529
FT /note="S -> V (in GSD2; mild; requires 2 nucleotide
FT substitutions; dbSNP:rs121907941)"
FT /evidence="ECO:0000269|PubMed:8834250"
FT /id="VAR_004296"
FT VARIANT 545
FT /note="P -> L (in GSD2; mild; partial loss of activity;
FT dbSNP:rs121907942)"
FT /evidence="ECO:0000269|PubMed:10737124,
FT ECO:0000269|PubMed:14695532, ECO:0000269|PubMed:20080426,
FT ECO:0000269|PubMed:7881422"
FT /id="VAR_004297"
FT VARIANT 549
FT /note="G -> R (in GSD2; juvenile form; mild; partial loss
FT of activity)"
FT /evidence="ECO:0000269|PubMed:14695532,
FT ECO:0000269|PubMed:16917947"
FT /id="VAR_018091"
FT VARIANT 552
FT /note="L -> P (in GSD2; infantile/juvenile form; severe;
FT loss of activity; dbSNP:rs779556619)"
FT /evidence="ECO:0000269|PubMed:14695532,
FT ECO:0000269|PubMed:18429042, ECO:0000269|PubMed:25681614"
FT /id="VAR_018092"
FT VARIANT 557
FT /note="I -> F (in GSD2; dbSNP:rs747150965)"
FT /evidence="ECO:0000269|PubMed:20080426"
FT /id="VAR_068605"
FT VARIANT 558
FT /note="C -> S (in GSD2)"
FT /evidence="ECO:0000269|PubMed:20350966,
FT ECO:0000269|PubMed:22644586"
FT /id="VAR_068606"
FT VARIANT 566
FT /note="S -> P (in GSD2; infantile form)"
FT /evidence="ECO:0000269|PubMed:9521422"
FT /id="VAR_004298"
FT VARIANT 568
FT /note="H -> L (in GSD2)"
FT /evidence="ECO:0000269|PubMed:22676651"
FT /id="VAR_070018"
FT VARIANT 570
FT /note="N -> K (in GSD2; dbSNP:rs765362308)"
FT /evidence="ECO:0000269|PubMed:18425781"
FT /id="VAR_068607"
FT VARIANT 572
FT /note="H -> Q (in GSD2; dbSNP:rs772962666)"
FT /evidence="ECO:0000269|PubMed:18425781"
FT /id="VAR_068608"
FT VARIANT 575
FT /note="Y -> C (in GSD2)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068609"
FT VARIANT 575
FT /note="Y -> S (in GSD2; juvenile form)"
FT /evidence="ECO:0000269|PubMed:14695532"
FT /id="VAR_018093"
FT VARIANT 576
FT /note="G -> A"
FT /id="VAR_004299"
FT VARIANT 576
FT /note="G -> R (in GSD2)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068610"
FT VARIANT 576
FT /note="G -> S (retains about half of the activity compared
FT with the wild-type; dbSNP:rs1800307)"
FT /evidence="ECO:0000269|PubMed:14643388,
FT ECO:0000269|PubMed:25681614"
FT /id="VAR_004300"
FT VARIANT 579
FT /note="E -> K (in GSD2; infantile form; severe; loss of
FT activity; dbSNP:rs991082382)"
FT /evidence="ECO:0000269|PubMed:14695532"
FT /id="VAR_018094"
FT VARIANT 585
FT /note="R -> K (in dbSNP:rs747373179)"
FT /evidence="ECO:0000269|PubMed:18425781"
FT /id="VAR_068611"
FT VARIANT 585
FT /note="R -> M (in GSD2)"
FT /evidence="ECO:0000269|PubMed:11071489"
FT /id="VAR_046472"
FT VARIANT 594
FT /note="R -> H (in GSD2; dbSNP:rs775450536)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068612"
FT VARIANT 594
FT /note="R -> P (in GSD2; dbSNP:rs775450536)"
FT /evidence="ECO:0000269|PubMed:18425781,
FT ECO:0000269|PubMed:19588081"
FT /id="VAR_068613"
FT VARIANT 599
FT /note="S -> Y (in GSD2; no residual enzymatic activity;
FT dbSNP:rs753505203)"
FT /evidence="ECO:0000269|PubMed:18429042"
FT /id="VAR_046473"
FT VARIANT 600
FT /note="R -> C (in GSD2; juvenile form; loss of activity;
FT dbSNP:rs764670084)"
FT /evidence="ECO:0000269|PubMed:14643388,
FT ECO:0000269|PubMed:14695532"
FT /id="VAR_018095"
FT VARIANT 600
FT /note="R -> H (in GSD2; infantile form; dbSNP:rs377544304)"
FT /id="VAR_008689"
FT VARIANT 601
FT /note="S -> L (in GSD2; dbSNP:rs374470794)"
FT /evidence="ECO:0000269|PubMed:22644586,
FT ECO:0000269|PubMed:22676651"
FT /id="VAR_068614"
FT VARIANT 602
FT /note="T -> A (in GSD2; dbSNP:rs781484283)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068615"
FT VARIANT 607..612
FT /note="Missing (in GSD2)"
FT /evidence="ECO:0000269|PubMed:11071489"
FT /id="VAR_046474"
FT VARIANT 607
FT /note="G -> D (in GSD2; infantile form; severe; loss of
FT activity; dbSNP:rs1393386120)"
FT /evidence="ECO:0000269|PubMed:14695532"
FT /id="VAR_018096"
FT VARIANT 610
FT /note="A -> V (in GSD2)"
FT /evidence="ECO:0000269|PubMed:17643989"
FT /id="VAR_068616"
FT VARIANT 611
FT /note="G -> D (found in a patient with GSD2; unknown
FT pathological significance; dbSNP:rs1057517105)"
FT /evidence="ECO:0000269|PubMed:22644586,
FT ECO:0000269|PubMed:25681614"
FT /id="VAR_068617"
FT VARIANT 612
FT /note="H -> Q (in GSD2; dbSNP:rs768397968)"
FT /evidence="ECO:0000269|PubMed:16917947"
FT /id="VAR_029038"
FT VARIANT 612
FT /note="H -> Y (in GSD2)"
FT /evidence="ECO:0000269|PubMed:19588081"
FT /id="VAR_068618"
FT VARIANT 614
FT /note="T -> K (in GSD2; dbSNP:rs369531647)"
FT /evidence="ECO:0000269|PubMed:18425781"
FT /id="VAR_068619"
FT VARIANT 615
FT /note="G -> R (in GSD2; infantile/adult form;
FT dbSNP:rs549029029)"
FT /evidence="ECO:0000269|PubMed:20080426"
FT /id="VAR_008690"
FT VARIANT 619
FT /note="S -> R (in GSD2; loss of function of the mutant
FT enzyme; dbSNP:rs914396317)"
FT /evidence="ECO:0000269|PubMed:14643388"
FT /id="VAR_046475"
FT VARIANT 627
FT /note="S -> P (in GSD2)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068620"
FT VARIANT 629
FT /note="P -> L (in dbSNP:rs746961289)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068621"
FT VARIANT 635
FT /note="N -> K (in GSD2; dbSNP:rs1414146587)"
FT /evidence="ECO:0000269|PubMed:19588081"
FT /id="VAR_068622"
FT VARIANT 638
FT /note="G -> V (in GSD2)"
FT /evidence="ECO:0000269|PubMed:19588081"
FT /id="VAR_068623"
FT VARIANT 638
FT /note="G -> W (in GSD2; dbSNP:rs757617999)"
FT /evidence="ECO:0000269|PubMed:10737124,
FT ECO:0000269|PubMed:18429042"
FT /id="VAR_046476"
FT VARIANT 641
FT /note="L -> V (in GSD2; unknown pathological significance;
FT dbSNP:rs1420043899)"
FT /evidence="ECO:0000269|PubMed:25681614"
FT /id="VAR_074278"
FT VARIANT 643
FT /note="G -> R (in GSD2; infantile form; dbSNP:rs28937909)"
FT /evidence="ECO:0000269|PubMed:11071489,
FT ECO:0000269|PubMed:16917947, ECO:0000269|PubMed:18429042,
FT ECO:0000269|PubMed:8401535, ECO:0000269|PubMed:9521422"
FT /id="VAR_004301"
FT VARIANT 645
FT /note="D -> E (in GSD2; infantile form; most common
FT mutation; deficient in phosphorylation and in proteolytic
FT processing; dbSNP:rs28940868)"
FT /evidence="ECO:0000269|PubMed:1684505,
FT ECO:0000269|PubMed:20080426, ECO:0000269|PubMed:8094613"
FT /id="VAR_004302"
FT VARIANT 645
FT /note="D -> H (in GSD2; almost complete loss of activity;
FT dbSNP:rs368438393)"
FT /evidence="ECO:0000269|PubMed:7695647"
FT /id="VAR_004303"
FT VARIANT 645
FT /note="D -> N (in GSD2; dbSNP:rs368438393)"
FT /evidence="ECO:0000269|PubMed:15145338,
FT ECO:0000269|PubMed:18429042, ECO:0000269|PubMed:9535769"
FT /id="VAR_004304"
FT VARIANT 647
FT /note="C -> W (in GSD2; dbSNP:rs776948121)"
FT /evidence="ECO:0000269|PubMed:25681614,
FT ECO:0000269|PubMed:7981676, ECO:0000269|PubMed:9535769"
FT /id="VAR_004305"
FT VARIANT 648
FT /note="G -> D (in GSD2; dbSNP:rs1448515860)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068624"
FT VARIANT 648
FT /note="G -> S (in GSD2; dbSNP:rs536906561)"
FT /evidence="ECO:0000269|PubMed:9535769"
FT /id="VAR_004306"
FT VARIANT 660
FT /note="R -> H (in GSD2; loss of function of the mutant
FT enzyme; dbSNP:rs374143224)"
FT /evidence="ECO:0000269|PubMed:14643388"
FT /id="VAR_046477"
FT VARIANT 672
FT /note="R -> Q (in GSD2; dbSNP:rs778418246)"
FT /evidence="ECO:0000269|PubMed:9535769"
FT /id="VAR_004307"
FT VARIANT 672
FT /note="R -> T (in GSD2)"
FT /evidence="ECO:0000269|PubMed:11071489"
FT /id="VAR_046478"
FT VARIANT 672
FT /note="R -> W (in GSD2; dbSNP:rs757111744)"
FT /evidence="ECO:0000269|PubMed:16917947,
FT ECO:0000269|PubMed:9535769"
FT /id="VAR_004308"
FT VARIANT 675
FT /note="Missing (in GSD2; infantile form)"
FT /id="VAR_008692"
FT VARIANT 689
FT /note="E -> K (in allele GAA*4; dbSNP:rs1800309)"
FT /evidence="ECO:0000269|PubMed:25681614,
FT ECO:0000269|PubMed:8912788"
FT /id="VAR_004309"
FT VARIANT 700..701
FT /note="Missing (found in a patient with GSD2; unknown
FT pathological significance)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068625"
FT VARIANT 702
FT /note="R -> C (in GSD2; no enzymatic activity; shows enzyme
FT localization primarily in the ER-Golgi compartment
FT suggesting that mutation could affect the normal processing
FT and stability of the enzyme; dbSNP:rs786204645)"
FT /evidence="ECO:0000269|PubMed:14972326"
FT /id="VAR_046479"
FT VARIANT 702
FT /note="R -> L (in GSD2; dbSNP:rs398123172)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068626"
FT VARIANT 705
FT /note="L -> P (in GSD2; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:25681614"
FT /id="VAR_074279"
FT VARIANT 711
FT /note="T -> R (in dbSNP:rs759292700)"
FT /evidence="ECO:0000269|PubMed:20080426"
FT /id="VAR_068627"
FT VARIANT 718
FT /note="V -> I (in dbSNP:rs141017311)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068628"
FT VARIANT 725
FT /note="R -> W (in GSD2; adult form; dbSNP:rs121907938)"
FT /evidence="ECO:0000269|PubMed:8401535"
FT /id="VAR_004310"
FT VARIANT 737
FT /note="T -> N (in GSD2; dbSNP:rs1381005435)"
FT /evidence="ECO:0000269|PubMed:18425781"
FT /id="VAR_068629"
FT VARIANT 743
FT /note="Q -> K (in GSD2)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068630"
FT VARIANT 746
FT /note="W -> C (in GSD2; dbSNP:rs1800312)"
FT /evidence="ECO:0000269|PubMed:16917947,
FT ECO:0000269|PubMed:20080426"
FT /id="VAR_004311"
FT VARIANT 746
FT /note="W -> G (in GSD2; dbSNP:rs1479740763)"
FT /evidence="ECO:0000269|PubMed:20080426"
FT /id="VAR_068631"
FT VARIANT 746
FT /note="W -> S (in GSD2; dbSNP:rs752921215)"
FT /evidence="ECO:0000269|PubMed:18425781"
FT /id="VAR_068632"
FT VARIANT 766
FT /note="Y -> C (in GSD2; dbSNP:rs144016984)"
FT /evidence="ECO:0000269|PubMed:22676651"
FT /id="VAR_070019"
FT VARIANT 768
FT /note="P -> R (in GSD2; infantile form)"
FT /evidence="ECO:0000269|PubMed:9521422"
FT /id="VAR_004312"
FT VARIANT 780
FT /note="V -> I (in dbSNP:rs1126690)"
FT /evidence="ECO:0000269|PubMed:2111708,
FT ECO:0000269|PubMed:2268276, ECO:0000269|PubMed:25681614,
FT ECO:0000269|PubMed:3049072, ECO:0000269|PubMed:7717400,
FT ECO:0000269|Ref.5"
FT /id="VAR_004313"
FT VARIANT 816
FT /note="V -> I (in dbSNP:rs1800314)"
FT /evidence="ECO:0000269|PubMed:1684505,
FT ECO:0000269|PubMed:25681614, ECO:0000269|PubMed:8094613,
FT ECO:0000269|PubMed:8486380"
FT /id="VAR_004314"
FT VARIANT 819
FT /note="R -> P (in GSD2)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068633"
FT VARIANT 880
FT /note="A -> D (in GSD2; infantile form; severe; loss of
FT activity)"
FT /evidence="ECO:0000269|PubMed:14695532"
FT /id="VAR_018097"
FT VARIANT 901
FT /note="L -> Q (in GSD2; infantile form; severe)"
FT /evidence="ECO:0000269|PubMed:15145338"
FT /id="VAR_029039"
FT VARIANT 903
FT /note="Missing (in GSD2; infantile form; severe; loss of
FT activity)"
FT /evidence="ECO:0000269|PubMed:7717400"
FT /id="VAR_004315"
FT VARIANT 913
FT /note="P -> R (in GSD2; dbSNP:rs1480070037)"
FT /evidence="ECO:0000269|PubMed:22676651"
FT /id="VAR_070020"
FT VARIANT 916
FT /note="V -> F (in GSD2; dbSNP:rs1221948995)"
FT /evidence="ECO:0000269|PubMed:22644586"
FT /id="VAR_068634"
FT VARIANT 925
FT /note="N -> NGVPVSN (in GSD2)"
FT /evidence="ECO:0000269|PubMed:10206684"
FT /id="VAR_004316"
FT VARIANT 927
FT /note="T -> I (loss of glycosylation site;
FT dbSNP:rs1800315)"
FT /evidence="ECO:0000269|PubMed:1684505,
FT ECO:0000269|PubMed:8094613, ECO:0000269|PubMed:8486380"
FT /id="VAR_004317"
FT VARIANT 935
FT /note="L -> P (in GSD2)"
FT /evidence="ECO:0000269|PubMed:18425781"
FT /id="VAR_068635"
FT VARIANT 949
FT /note="V -> D (in GSD2; dbSNP:rs1245412108)"
FT /id="VAR_004318"
FT MUTAGEN 516
FT /note="W->R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1856189"
FT MUTAGEN 518
FT /note="D->G,N,E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1856189"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:5KZW"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:5NN3"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 145..153
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 175..184
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:5NN4"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:5NN4"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:5NN4"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:5NN4"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 327..335
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:5NN4"
FT HELIX 347..358
FT /evidence="ECO:0007829|PDB:5NN4"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:5NN4"
FT HELIX 381..393
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 399..403
FT /evidence="ECO:0007829|PDB:5NN4"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:5NN4"
FT TURN 420..423
FT /evidence="ECO:0007829|PDB:5NN4"
FT HELIX 424..433
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 437..442
FT /evidence="ECO:0007829|PDB:5NN4"
FT HELIX 456..464
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:5NN4"
FT HELIX 493..509
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 514..517
FT /evidence="ECO:0007829|PDB:5NN4"
FT TURN 520..522
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 525..528
FT /evidence="ECO:0007829|PDB:5NN4"
FT TURN 537..539
FT /evidence="ECO:0007829|PDB:5NN4"
FT TURN 552..555
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 564..567
FT /evidence="ECO:0007829|PDB:5NN4"
FT HELIX 568..571
FT /evidence="ECO:0007829|PDB:5NN4"
FT HELIX 572..574
FT /evidence="ECO:0007829|PDB:5NN4"
FT HELIX 575..591
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 597..601
FT /evidence="ECO:0007829|PDB:5NN4"
FT HELIX 606..608
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 611..613
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 618..620
FT /evidence="ECO:0007829|PDB:5NN4"
FT HELIX 621..636
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:5NN4"
FT HELIX 655..665
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 668..670
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 677..679
FT /evidence="ECO:0007829|PDB:5NN8"
FT HELIX 684..686
FT /evidence="ECO:0007829|PDB:5NN4"
FT HELIX 689..704
FT /evidence="ECO:0007829|PDB:5NN4"
FT HELIX 706..719
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 723..725
FT /evidence="ECO:0007829|PDB:5NN4"
FT HELIX 727..730
FT /evidence="ECO:0007829|PDB:5NN4"
FT HELIX 735..737
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 742..746
FT /evidence="ECO:0007829|PDB:5NN4"
FT TURN 747..749
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 750..753
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 761..767
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 769..774
FT /evidence="ECO:0007829|PDB:5NN4"
FT HELIX 775..777
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 796..808
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 815..819
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 822..827
FT /evidence="ECO:0007829|PDB:5NN4"
FT HELIX 833..836
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 841..846
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 853..859
FT /evidence="ECO:0007829|PDB:5NN4"
FT HELIX 867..870
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 874..881
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 884..891
FT /evidence="ECO:0007829|PDB:5NN4"
FT HELIX 894..896
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 900..907
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 916..918
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 926..929
FT /evidence="ECO:0007829|PDB:5NN4"
FT TURN 930..933
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 934..942
FT /evidence="ECO:0007829|PDB:5NN4"
FT STRAND 948..951
FT /evidence="ECO:0007829|PDB:5NN4"
SQ SEQUENCE 952 AA; 105324 MW; 6E2717BF7201F469 CRC64;
MGVRHPPCSH RLLAVCALVS LATAALLGHI LLHDFLLVPR ELSGSSPVLE ETHPAHQQGA
SRPGPRDAQA HPGRPRAVPT QCDVPPNSRF DCAPDKAITQ EQCEARGCCY IPAKQGLQGA
QMGQPWCFFP PSYPSYKLEN LSSSEMGYTA TLTRTTPTFF PKDILTLRLD VMMETENRLH
FTIKDPANRR YEVPLETPHV HSRAPSPLYS VEFSEEPFGV IVRRQLDGRV LLNTTVAPLF
FADQFLQLST SLPSQYITGL AEHLSPLMLS TSWTRITLWN RDLAPTPGAN LYGSHPFYLA
LEDGGSAHGV FLLNSNAMDV VLQPSPALSW RSTGGILDVY IFLGPEPKSV VQQYLDVVGY
PFMPPYWGLG FHLCRWGYSS TAITRQVVEN MTRAHFPLDV QWNDLDYMDS RRDFTFNKDG
FRDFPAMVQE LHQGGRRYMM IVDPAISSSG PAGSYRPYDE GLRRGVFITN ETGQPLIGKV
WPGSTAFPDF TNPTALAWWE DMVAEFHDQV PFDGMWIDMN EPSNFIRGSE DGCPNNELEN
PPYVPGVVGG TLQAATICAS SHQFLSTHYN LHNLYGLTEA IASHRALVKA RGTRPFVISR
STFAGHGRYA GHWTGDVWSS WEQLASSVPE ILQFNLLGVP LVGADVCGFL GNTSEELCVR
WTQLGAFYPF MRNHNSLLSL PQEPYSFSEP AQQAMRKALT LRYALLPHLY TLFHQAHVAG
ETVARPLFLE FPKDSSTWTV DHQLLWGEAL LITPVLQAGK AEVTGYFPLG TWYDLQTVPV
EALGSLPPPP AAPREPAIHS EGQWVTLPAP LDTINVHLRA GYIIPLQGPG LTTTESRQQP
MALAVALTKG GEARGELFWD DGESLEVLER GAYTQVIFLA RNNTIVNELV RVTSEGAGLQ
LQKVTVLGVA TAPQQVLSNG VPVSNFTYSP DTKVLDICVS LLMGEQFLVS WC
