GDE_HUMAN
ID GDE_HUMAN Reviewed; 1532 AA.
AC P35573; A6NCX7; A6NEK2; D3DT51; P78354; P78544; Q59H92; Q6AZ90; Q9UF08;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Glycogen debranching enzyme;
DE AltName: Full=Glycogen debrancher;
DE Includes:
DE RecName: Full=4-alpha-glucanotransferase;
DE EC=2.4.1.25;
DE AltName: Full=Oligo-1,4-1,4-glucantransferase;
DE Includes:
DE RecName: Full=Amylo-alpha-1,6-glucosidase;
DE Short=Amylo-1,6-glucosidase;
DE EC=3.2.1.33;
DE AltName: Full=Dextrin 6-alpha-D-glucosidase;
GN Name=AGL; Synonyms=GDE;
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], AND PARTIAL PROTEIN SEQUENCE (ISOFORM 5).
RC TISSUE=Muscle;
RX PubMed=1374391; DOI=10.1016/s0021-9258(19)50422-7;
RA Yang B.-Z., Ding J.-H., Enghild J.J., Bao Y., Chen Y.-T.;
RT "Molecular cloning and nucleotide sequence of cDNA encoding human muscle
RT glycogen debranching enzyme.";
RL J. Biol. Chem. 267:9294-9299(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=8954797; DOI=10.1006/geno.1996.0611;
RA Bao Y., Dawson T.L. Jr., Chen Y.-T.;
RT "Human glycogen debranching enzyme gene (AGL): complete structural
RT organization and characterization of the 5' flanking region.";
RL Genomics 38:155-165(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Liver;
RX PubMed=9332391; DOI=10.1016/s0378-1119(97)00291-6;
RA Bao Y., Yang B.-Z., Dawson T.L. Jr., Chen Y.-T.;
RT "Isolation and nucleotide sequence of human liver glycogen debranching
RT enzyme mRNA: identification of multiple tissue-specific isoforms.";
RL Gene 197:389-398(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS.
RX PubMed=10982190; DOI=10.1007/s004390051017;
RA Okubo M., Horinishi A., Takeuchi M., Suzuki Y., Sakura N., Hasegawa Y.,
RA Igarashi T., Goto K., Tahara H., Uchimoto S., Omichi K., Kanno H.,
RA Hayasaka K., Murase T.;
RT "Heterogeneous mutations in the glycogen-debranching enzyme gene are
RT responsible for glycogen storage disease type IIIa in Japan.";
RL Hum. Genet. 106:108-115(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [9]
RP UBIQUITINATION, CHARACTERIZATION OF VARIANT GSD3 ARG-1448, INTERACTION WITH
RP NHLRC1, AND SUBCELLULAR LOCATION.
RX PubMed=17908927; DOI=10.1101/gad.1553207;
RA Cheng A., Zhang M., Gentry M.S., Worby C.A., Dixon J.E., Saltiel A.R.;
RT "A role for AGL ubiquitination in the glycogen storage disorders of Lafora
RT and Cori's disease.";
RL Genes Dev. 21:2399-2409(2007).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP 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 [12]
RP VARIANT GSD3 ARG-1448, AND VARIANT ARG-1115.
RX PubMed=10571954;
RX DOI=10.1002/(sici)1098-1004(199912)14:6<542::aid-humu15>3.0.co;2-0;
RA Okubo M., Kanda F., Horinishi A., Takahashi K., Okuda S., Chihara K.,
RA Murase T.;
RT "Glycogen storage disease type IIIa: first report of a causative missense
RT mutation (G1448R) of the glycogen debranching enzyme gene found in a
RT homozygous patient.";
RL Hum. Mutat. 14:542-543(1999).
CC -!- FUNCTION: Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4-
CC alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase
CC in glycogen degradation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Transfers a segment of a (1->4)-alpha-D-glucan to a new
CC position in an acceptor, which may be glucose or a (1->4)-alpha-D-
CC glucan.; EC=2.4.1.25;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in
CC glycogen phosphorylase limit dextrin.; EC=3.2.1.33;
CC -!- SUBUNIT: Monomer. Interacts with NHLRC1/malin.
CC {ECO:0000269|PubMed:17908927}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17908927}.
CC Note=Under glycogenolytic conditions localizes to the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=2, 3, 4;
CC IsoId=P35573-1; Sequence=Displayed;
CC Name=5;
CC IsoId=P35573-2; Sequence=VSP_004270;
CC Name=6;
CC IsoId=P35573-3; Sequence=VSP_004271;
CC -!- TISSUE SPECIFICITY: Liver, kidney and lymphoblastoid cells express
CC predominantly isoform 1; whereas muscle and heart express not only
CC isoform 1, but also muscle-specific isoform mRNAs (isoforms 2, 3 and
CC 4). Isoforms 5 and 6 are present in both liver and muscle.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:17908927}.
CC -!- DISEASE: Glycogen storage disease 3 (GSD3) [MIM:232400]: A metabolic
CC disorder associated with an accumulation of abnormal glycogen with
CC short outer chains. It is clinically characterized by hepatomegaly,
CC hypoglycemia, short stature, and variable myopathy. Glycogen storage
CC disease type 3 includes different forms: GSD type 3A patients lack
CC glycogen debrancher enzyme activity in both liver and muscle, while GSD
CC type 3B patients are enzyme-deficient in liver only. In rare cases,
CC selective loss of only 1 of the 2 debranching activities, glucosidase
CC or transferase, results in GSD type 3C or type 3D, respectively.
CC {ECO:0000269|PubMed:10571954, ECO:0000269|PubMed:17908927}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 1]: The products of the mRNAs termed isoforms 1
CC to 4 are identical.
CC -!- SIMILARITY: Belongs to the glycogen debranching enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92104.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M85168; AAB41040.1; -; mRNA.
DR EMBL; U84007; AAB48466.1; -; mRNA.
DR EMBL; U84008; AAB48467.1; -; mRNA.
DR EMBL; U84009; AAB48468.1; -; mRNA.
DR EMBL; U84010; AAB48469.1; -; mRNA.
DR EMBL; U84011; AAB48470.1; -; mRNA.
DR EMBL; AB035443; BAA88405.1; -; Genomic_DNA.
DR EMBL; AB208867; BAD92104.1; ALT_INIT; mRNA.
DR EMBL; AC096949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW72985.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW72982.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW72983.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW72987.1; -; Genomic_DNA.
DR EMBL; BC078663; AAH78663.1; -; mRNA.
DR CCDS; CCDS759.1; -. [P35573-1]
DR CCDS; CCDS760.1; -. [P35573-3]
DR RefSeq; NP_000019.2; NM_000028.2. [P35573-1]
DR RefSeq; NP_000633.2; NM_000642.2. [P35573-1]
DR RefSeq; NP_000634.2; NM_000643.2. [P35573-1]
DR RefSeq; NP_000635.2; NM_000644.2. [P35573-1]
DR RefSeq; NP_000637.2; NM_000646.2. [P35573-3]
DR RefSeq; XP_005270614.1; XM_005270557.2. [P35573-1]
DR AlphaFoldDB; P35573; -.
DR SMR; P35573; -.
DR BioGRID; 106686; 75.
DR IntAct; P35573; 28.
DR MINT; P35573; -.
DR STRING; 9606.ENSP00000294724; -.
DR BindingDB; P35573; -.
DR ChEMBL; CHEMBL5272; -.
DR DrugCentral; P35573; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR CAZy; GH133; Glycoside Hydrolase Family 133.
DR GlyGen; P35573; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P35573; -.
DR PhosphoSitePlus; P35573; -.
DR BioMuta; AGL; -.
DR DMDM; 116242491; -.
DR EPD; P35573; -.
DR jPOST; P35573; -.
DR MassIVE; P35573; -.
DR MaxQB; P35573; -.
DR PaxDb; P35573; -.
DR PeptideAtlas; P35573; -.
DR PRIDE; P35573; -.
DR ProteomicsDB; 55089; -. [P35573-1]
DR ProteomicsDB; 55090; -. [P35573-2]
DR ProteomicsDB; 55091; -. [P35573-3]
DR Antibodypedia; 33684; 169 antibodies from 25 providers.
DR DNASU; 178; -.
DR Ensembl; ENST00000294724.8; ENSP00000294724.4; ENSG00000162688.17. [P35573-1]
DR Ensembl; ENST00000361915.8; ENSP00000355106.3; ENSG00000162688.17. [P35573-1]
DR Ensembl; ENST00000370161.6; ENSP00000359180.2; ENSG00000162688.17. [P35573-3]
DR Ensembl; ENST00000370163.7; ENSP00000359182.3; ENSG00000162688.17. [P35573-1]
DR Ensembl; ENST00000370165.7; ENSP00000359184.3; ENSG00000162688.17. [P35573-1]
DR GeneID; 178; -.
DR KEGG; hsa:178; -.
DR MANE-Select; ENST00000361915.8; ENSP00000355106.3; NM_000642.3; NP_000633.2.
DR UCSC; uc001dsi.2; human. [P35573-1]
DR CTD; 178; -.
DR DisGeNET; 178; -.
DR GeneCards; AGL; -.
DR GeneReviews; AGL; -.
DR HGNC; HGNC:321; AGL.
DR HPA; ENSG00000162688; Group enriched (skeletal muscle, tongue).
DR MalaCards; AGL; -.
DR MIM; 232400; phenotype.
DR MIM; 610860; gene.
DR neXtProt; NX_P35573; -.
DR OpenTargets; ENSG00000162688; -.
DR Orphanet; 366; Glycogen storage disease due to glycogen debranching enzyme deficiency.
DR PharmGKB; PA24618; -.
DR VEuPathDB; HostDB:ENSG00000162688; -.
DR eggNOG; KOG3625; Eukaryota.
DR GeneTree; ENSGT00390000012596; -.
DR HOGENOM; CLU_001517_2_0_1; -.
DR InParanoid; P35573; -.
DR OMA; DKMGEST; -.
DR PhylomeDB; P35573; -.
DR TreeFam; TF300697; -.
DR BioCyc; MetaCyc:HS08717-MON; -.
DR BRENDA; 3.2.1.33; 2681.
DR PathwayCommons; P35573; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-70221; Glycogen breakdown (glycogenolysis).
DR SignaLink; P35573; -.
DR BioGRID-ORCS; 178; 28 hits in 1083 CRISPR screens.
DR GeneWiki; Glycogen_debranching_enzyme; -.
DR GenomeRNAi; 178; -.
DR Pharos; P35573; Tbio.
DR PRO; PR:P35573; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P35573; protein.
DR Bgee; ENSG00000162688; Expressed in vastus lateralis and 213 other tissues.
DR ExpressionAtlas; P35573; baseline and differential.
DR Genevisible; P35573; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0016234; C:inclusion body; IEA:Ensembl.
DR GO; GO:0043033; C:isoamylase complex; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0004134; F:4-alpha-glucanotransferase activity; EXP:Reactome.
DR GO; GO:0004135; F:amylo-alpha-1,6-glucosidase activity; EXP:Reactome.
DR GO; GO:0102500; F:beta-maltose 4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004133; F:glycogen debranching enzyme activity; TAS:ProtInc.
DR GO; GO:0030247; F:polysaccharide binding; IEA:Ensembl.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IEA:Ensembl.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0005980; P:glycogen catabolic process; IBA:GO_Central.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR CDD; cd11327; AmyAc_Glg_debranch_2; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR010401; AGL/Gdb1.
DR InterPro; IPR032788; AGL_central.
DR InterPro; IPR029436; AGL_euk_N.
DR InterPro; IPR032792; AGL_glucanoTrfase.
DR InterPro; IPR032790; GDE_C.
DR InterPro; IPR006421; Glycogen_debranch_met.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10569; PTHR10569; 1.
DR Pfam; PF06202; GDE_C; 1.
DR Pfam; PF14701; hDGE_amylase; 1.
DR Pfam; PF14702; hGDE_central; 1.
DR Pfam; PF14699; hGDE_N; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR TIGRFAMs; TIGR01531; glyc_debranch; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Disease variant; Glycogen biosynthesis; Glycogen storage disease;
KW Glycosidase; Glycosyltransferase; Hydrolase; Multifunctional enzyme;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation.
FT CHAIN 1..1532
FT /note="Glycogen debranching enzyme"
FT /id="PRO_0000087450"
FT REGION 1..?
FT /note="4-alpha-glucanotransferase"
FT REGION ?..1532
FT /note="Amylo-1,6-glucosidase"
FT ACT_SITE 526
FT /evidence="ECO:0000250"
FT ACT_SITE 529
FT /evidence="ECO:0000250"
FT ACT_SITE 627
FT /evidence="ECO:0000250"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..27
FT /note="MGHSKQIRILLLNEMEKLEKTLFRLEQ -> MSLLTCAFYL (in
FT isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_004270"
FT VAR_SEQ 1..27
FT /note="MGHSKQIRILLLNEMEKLEKTLFRLEQ -> MAPILSINLFI (in
FT isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_004271"
FT VARIANT 38
FT /note="T -> A (in dbSNP:rs35278779)"
FT /id="VAR_032084"
FT VARIANT 229
FT /note="Q -> R (in dbSNP:rs17121403)"
FT /id="VAR_028051"
FT VARIANT 387
FT /note="R -> Q (in dbSNP:rs17121464)"
FT /id="VAR_009621"
FT VARIANT 701
FT /note="A -> S (in dbSNP:rs3736297)"
FT /id="VAR_028052"
FT VARIANT 962
FT /note="S -> C (in dbSNP:rs34714252)"
FT /id="VAR_032085"
FT VARIANT 1067
FT /note="P -> S (in dbSNP:rs3753494)"
FT /id="VAR_020389"
FT VARIANT 1115
FT /note="G -> R (in dbSNP:rs2230307)"
FT /evidence="ECO:0000269|PubMed:10571954"
FT /id="VAR_009230"
FT VARIANT 1144
FT /note="I -> N (in dbSNP:rs2230308)"
FT /id="VAR_028053"
FT VARIANT 1207
FT /note="A -> T (in dbSNP:rs11807956)"
FT /id="VAR_051010"
FT VARIANT 1253
FT /note="R -> H (in dbSNP:rs12043139)"
FT /id="VAR_028054"
FT VARIANT 1343
FT /note="E -> K (in dbSNP:rs112795811)"
FT /id="VAR_009622"
FT VARIANT 1448
FT /note="G -> R (in GSD3; deficient in ability to bind
FT glycogen; unstable due to enhanced ubiquitination; forms
FT aggresomes upon proteasome impairment; dbSNP:rs118203964)"
FT /evidence="ECO:0000269|PubMed:10571954,
FT ECO:0000269|PubMed:17908927"
FT /id="VAR_009231"
FT VARIANT 1487
FT /note="R -> G (in dbSNP:rs12118058)"
FT /id="VAR_028055"
FT CONFLICT 1398
FT /note="W -> G (in Ref. 1; AAB41040, 2; AAB48466/AAB48467/
FT AAB48468/AAB48469/AAB48470 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT P35573-3:4
FT /note="I -> L (in Ref. 2; AAB48470)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1532 AA; 174764 MW; 9BF1BCC43B7904D3 CRC64;
MGHSKQIRIL LLNEMEKLEK TLFRLEQGYE LQFRLGPTLQ GKAVTVYTNY PFPGETFNRE
KFRSLDWENP TEREDDSDKY CKLNLQQSGS FQYYFLQGNE KSGGGYIVVD PILRVGADNH
VLPLDCVTLQ TFLAKCLGPF DEWESRLRVA KESGYNMIHF TPLQTLGLSR SCYSLANQLE
LNPDFSRPNR KYTWNDVGQL VEKLKKEWNV ICITDVVYNH TAANSKWIQE HPECAYNLVN
SPHLKPAWVL DRALWRFSCD VAEGKYKEKG IPALIENDHH MNSIRKIIWE DIFPKLKLWE
FFQVDVNKAV EQFRRLLTQE NRRVTKSDPN QHLTIIQDPE YRRFGCTVDM NIALTTFIPH
DKGPAAIEEC CNWFHKRMEE LNSEKHRLIN YHQEQAVNCL LGNVFYERLA GHGPKLGPVT
RKHPLVTRYF TFPFEEIDFS MEESMIHLPN KACFLMAHNG WVMGDDPLRN FAEPGSEVYL
RRELICWGDS VKLRYGNKPE DCPYLWAHMK KYTEITATYF QGVRLDNCHS TPLHVAEYML
DAARNLQPNL YVVAELFTGS EDLDNVFVTR LGISSLIREA MSAYNSHEEG RLVYRYGGEP
VGSFVQPCLR PLMPAIAHAL FMDITHDNEC PIVHRSAYDA LPSTTIVSMA CCASGSTRGY
DELVPHQISV VSEERFYTKW NPEALPSNTG EVNFQSGIIA ARCAISKLHQ ELGAKGFIQV
YVDQVDEDIV AVTRHSPSIH QSVVAVSRTA FRNPKTSFYS KEVPQMCIPG KIEEVVLEAR
TIERNTKPYR KDENSINGTP DITVEIREHI QLNESKIVKQ AGVATKGPNE YIQEIEFENL
SPGSVIIFRV SLDPHAQVAV GILRNHLTQF SPHFKSGSLA VDNADPILKI PFASLASRLT
LAELNQILYR CESEEKEDGG GCYDIPNWSA LKYAGLQGLM SVLAEIRPKN DLGHPFCNNL
RSGDWMIDYV SNRLISRSGT IAEVGKWLQA MFFYLKQIPR YLIPCYFDAI LIGAYTTLLD
TAWKQMSSFV QNGSTFVKHL SLGSVQLCGV GKFPSLPILS PALMDVPYRL NEITKEKEQC
CVSLAAGLPH FSSGIFRCWG RDTFIALRGI LLITGRYVEA RNIILAFAGT LRHGLIPNLL
GEGIYARYNC RDAVWWWLQC IQDYCKMVPN GLDILKCPVS RMYPTDDSAP LPAGTLDQPL
FEVIQEAMQK HMQGIQFRER NAGPQIDRNM KDEGFNITAG VDEETGFVYG GNRFNCGTWM
DKMGESDRAR NRGIPATPRD GSAVEIVGLS KSAVRWLLEL SKKNIFPYHE VTVKRHGKAI
KVSYDEWNRK IQDNFEKLFH VSEDPSDLNE KHPNLVHKRG IYKDSYGASS PWCDYQLRPN
FTIAMVVAPE LFTTEKAWKA LEIAEKKLLG PLGMKTLDPD DMVYCGIYDN ALDNDNYNLA
KGFNYHQGPE WLWPIGYFLR AKLYFSRLMG PETTAKTIVL VKNVLSRHYV HLERSPWKGL
PELTNENAQY CPFSCETQAW SIATILETLY DL
