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 02-SEP-2026, entry version 224. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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_000028.3. [P35573-1] DR RefSeq; NP_000633.2; NM_000642.3. [P35573-1] DR RefSeq; NP_000634.2; NM_000643.3. [P35573-1] DR RefSeq; NP_000635.2; NM_000644.3. [P35573-1] DR RefSeq; NP_000637.2; NM_000646.3. [P35573-3] DR RefSeq; NP_001412254.1; NM_001425325.1. [P35573-1] DR RefSeq; XP_005270614.1; XM_005270557.3. [P35573-1] DR RefSeq; XP_054190771.1; XM_054334796.1. [P35573-1] DR PDB; 8ZEQ; EM; 3.36 A; A=1-1532. DR AlphaFoldDB; P35573; -. DR EMDB; EMD-60043; -. DR EMDB; EMD-63640; -. DR SMR; P35573; -. DR BioGRID; 106686; 116. DR FunCoup; P35573; 991. DR IntAct; P35573; 36. DR MINT; P35573; -. DR NDEx; IQUERY-CP-AGL; 1 NDEx IQuery Curated Pathway. 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; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P35573; -. DR PhosphoSitePlus; P35573; -. DR SwissPalm; P35573; -. DR BioMuta; AGL; -. DR DMDM; 116242491; -. DR jPOST; P35573; -. DR MassIVE; P35573; -. DR PaxDb; 9606-ENSP00000294724; -. DR PeptideAtlas; P35573; -. DR ProteomicsDB; 55089; -. [P35573-1] DR ProteomicsDB; 55090; -. [P35573-2] DR ProteomicsDB; 55091; -. [P35573-3] DR Pumba; P35573; -. DR Antibodypedia; 33684; 182 antibodies from 28 providers. DR DNASU; 178; -. DR Ensembl; ENST00000294724.8; ENSP00000294724.4; ENSG00000162688.18. [P35573-1] DR Ensembl; ENST00000361915.8; ENSP00000355106.3; ENSG00000162688.18. [P35573-1] DR Ensembl; ENST00000370161.6; ENSP00000359180.2; ENSG00000162688.18. [P35573-3] DR Ensembl; ENST00000370163.7; ENSP00000359182.3; ENSG00000162688.18. [P35573-1] DR Ensembl; ENST00000370165.7; ENSP00000359184.3; ENSG00000162688.18. [P35573-1] DR Ensembl; ENST00000881254.1; ENSP00000551313.1; ENSG00000162688.18. [P35573-1] DR Ensembl; ENST00000881255.1; ENSP00000551314.1; ENSG00000162688.18. [P35573-1] DR Ensembl; ENST00000911800.1; ENSP00000581859.1; ENSG00000162688.18. [P35573-1] DR Ensembl; ENST00000965591.1; ENSP00000635650.1; ENSG00000162688.18. [P35573-1] DR Ensembl; ENST00000965592.1; ENSP00000635651.1; ENSG00000162688.18. [P35573-1] DR Ensembl; ENST00000965593.1; ENSP00000635652.1; ENSG00000162688.18. [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 AGR; HGNC:321; -. DR ClinPGx; PA24618; -. 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 OpenTargets; ENSG00000162688; -. DR Orphanet; 366; Glycogen storage disease due to glycogen debranching enzyme deficiency. DR VEuPathDB; HostDB:ENSG00000162688; -. DR eggNOG; KOG3625; Eukaryota. DR GeneTree; ENSGT00390000012596; -. DR HOGENOM; CLU_001517_2_0_1; -. DR InParanoid; P35573; -. DR OMA; YEEGHVH; -. DR OrthoDB; 10248904at2759; -. DR PAN-GO; P35573; 3 GO annotations based on evolutionary models. DR PhylomeDB; P35573; -. DR BioCyc; MetaCyc:HS08717-MONOMER; -. 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 SIGNOR; P35573; -. DR Agora; ENSG00000162688; -. DR BioGRID-ORCS; 178; 28 hits in 1163 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 215 other cell types or tissues. DR ExpressionAtlas; P35573; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. 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:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. 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: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:InterPro. 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 FunFam; 3.20.20.80:FF:000291; Amylo-alpha-1, 6-glucosidase, 4-alpha-glucanotransferase a; 1. DR FunFam; 1.50.10.10:FF:000039; Glycogen debranching enzyme Gdb1, putative; 1. DR FunFam; 3.20.20.80:FF:000051; glycogen debranching enzyme isoform X2; 1. DR Gene3D; 3.20.20.80; Glycosidases; 2. 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; IPR017853; GH_hydrolase_sf. DR InterPro; IPR006421; Glycogen_debranch_met. DR NCBIfam; TIGR01531; glyc_debranch; 1. DR PANTHER; PTHR10569; GLYCOGEN DEBRANCHING ENZYME; 1. DR PANTHER; PTHR10569:SF2; GLYCOGEN DEBRANCHING ENZYME; 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; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1. DR PDBsum; 8ZEQ; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing; KW Disease variant; Glycogen biosynthesis; Glycogen storage disease; KW Glycosidase; Glycosyltransferase; Hydrolase; Multifunctional enzyme; KW Phosphoprotein; Proteomics identification; Reference proteome; Transferase; KW 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; FT AAB48466/AAB48467/AAB48468/AAB48469/AAB48470 and 3)" FT /evidence="ECO:0000305" FT HELIX 3..5 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 7..11 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 19..21 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 27..34 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 45..48 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 50..52 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 92..97 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 100..106 FT /evidence="ECO:0007829|PDB:8ZEQ" FT TURN 116..119 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 128..131 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 135..137 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 139..141 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 144..153 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 156..159 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 194..208 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 211..213 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 232..234 FT /evidence="ECO:0007829|PDB:8ZEQ" FT TURN 238..240 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 245..262 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 280..295 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 298..315 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 338..340 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 343..345 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 351..356 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 364..408 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 411..413 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 421..423 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 429..431 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 435..437 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 442..446 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 449..453 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 473..475 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 479..481 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 499..501 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 503..519 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 521..527 FT /evidence="ECO:0007829|PDB:8ZEQ" FT TURN 528..530 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 533..546 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 551..554 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 561..571 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 575..580 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 586..595 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 599..601 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 608..611 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 620..623 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 626..628 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 631..634 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 637..639 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 640..648 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 654..657 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 658..661 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 670..672 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 683..685 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 688..690 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 696..698 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 699..715 FT /evidence="ECO:0007829|PDB:8ZEQ" FT TURN 737..739 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 742..746 FT /evidence="ECO:0007829|PDB:8ZEQ" FT TURN 754..756 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 767..778 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 780..783 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 787..789 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 793..795 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 802..805 FT /evidence="ECO:0007829|PDB:8ZEQ" FT TURN 812..814 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 816..827 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 830..839 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 846..851 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 854..856 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 857..868 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 893..897 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 901..904 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 913..917 FT /evidence="ECO:0007829|PDB:8ZEQ" FT TURN 926..928 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 936..946 FT /evidence="ECO:0007829|PDB:8ZEQ" FT TURN 947..950 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 955..962 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 965..974 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 980..995 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 1003..1024 FT /evidence="ECO:0007829|PDB:8ZEQ" FT TURN 1030..1032 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 1035..1047 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 1057..1060 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 1063..1065 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 1068..1070 FT /evidence="ECO:0007829|PDB:8ZEQ" FT TURN 1072..1074 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 1077..1079 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 1101..1113 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 1117..1130 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 1142..1144 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 1154..1167 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 1171..1173 FT /evidence="ECO:0007829|PDB:8ZEQ" FT TURN 1174..1176 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 1186..1188 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 1189..1192 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 1200..1213 FT /evidence="ECO:0007829|PDB:8ZEQ" FT TURN 1243..1246 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 1285..1302 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 1324..1338 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 1343..1345 FT /evidence="ECO:0007829|PDB:8ZEQ" FT TURN 1353..1355 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 1356..1358 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 1364..1369 FT /evidence="ECO:0007829|PDB:8ZEQ" FT TURN 1371..1374 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 1382..1387 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 1396..1404 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 1405..1407 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 1411..1413 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 1440..1442 FT /evidence="ECO:0007829|PDB:8ZEQ" FT TURN 1443..1446 FT /evidence="ECO:0007829|PDB:8ZEQ" FT STRAND 1452..1454 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 1457..1469 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 1471..1493 FT /evidence="ECO:0007829|PDB:8ZEQ" FT HELIX 1523..1531 FT /evidence="ECO:0007829|PDB:8ZEQ" 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 //