ID PYGM_HUMAN Reviewed; 842 AA. AC P11217; A0AVK1; A6NDY6; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 6. DT 27-MAR-2024, entry version 248. DE RecName: Full=Glycogen phosphorylase, muscle form {ECO:0000305|PubMed:3447177}; DE EC=2.4.1.1 {ECO:0000269|PubMed:1150650, ECO:0000269|PubMed:8316268}; DE AltName: Full=Myophosphorylase {ECO:0000303|PubMed:9633816}; GN Name=PYGM {ECO:0000312|HGNC:HGNC:9726}; 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 [GENOMIC DNA]. RX PubMed=3447177; DOI=10.1002/prot.340020303; RA Burke J., Hwang P.K., Anderson L., Lebo R., Gorin F., Fletterick R.J.; RT "Intron/exon structure of the human gene for the muscle isozyme of glycogen RT phosphorylase."; RL Proteins 2:177-187(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9633816; RX DOI=10.1002/(sici)1098-1004(1998)12:1<27::aid-humu4>3.0.co;2-#; RA Kubisch C., Wicklein E.M., Jentsch T.J.; RT "Molecular diagnosis of McArdle disease: revised genomic structure of the RT myophosphorylase gene and identification of a novel mutation."; RL Hum. Mutat. 12:27-32(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Muscle; RA Carty M.D., Clancy Y.C., Soeller W.C.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] 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 [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 676-842 (ISOFORM 1). RX PubMed=3840433; DOI=10.1111/j.1432-1033.1985.tb09193.x; RA Hwang P.K., See Y.P., Vincentini A.M., Powers M.A., Fletterick R.J., RA Crerar M.M.; RT "Comparative sequence analysis of rat, rabbit, and human muscle glycogen RT phosphorylase cDNAs."; RL Eur. J. Biochem. 152:267-274(1985). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 455-676 (ISOFORM 1). RX PubMed=3466902; DOI=10.1172/jci112794; RA Gautron S., Daegelen D., Mennecier F., Dubocq D., Kahn A., Dreyfus J.-C.; RT "Molecular mechanisms of McArdle's disease (muscle glycogen phosphorylase RT deficiency). RNA and DNA analysis."; RL J. Clin. Invest. 79:275-281(1987). RN [10] RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND PHOSPHORYLATION AT RP SER-15. RX PubMed=1150650; DOI=10.1016/s0021-9258(19)41265-9; RA Carty T.J., Tu J., Graves D.J.; RT "Regulation of glycogen phosphorylase. Role of the peptide region RT surrounding the phosphoserine residue in determining enzyme properties."; RL J. Biol. Chem. 250:4980-4985(1975). RN [11] {ECO:0007744|PDB:1Z8D} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH AMP AND GLUCOSE, AND RP SUBUNIT. RX PubMed=16523484; DOI=10.1002/prot.20939; RA Lukacs C.M., Oikonomakos N.G., Crowther R.L., Hong L.N., Kammlott R.U., RA Levin W., Li S., Liu C.M., Lucas-McGady D., Pietranico S., Reik L.; RT "The crystal structure of human muscle glycogen phosphorylase a with bound RT glucose and AMP: an intermediate conformation with T-state and R-state RT features."; RL Proteins 63:1123-1126(2006). RN [12] RP VARIANTS GSD5 50-ARG--ILE-842 DEL; SER-205 AND THR-543, FUNCTION, AND RP CATALYTIC ACTIVITY. RX PubMed=8316268; DOI=10.1056/nejm199307223290404; RA Tsujino S., Shanske S., Dimauro S.; RT "Molecular genetic heterogeneity of myophosphorylase deficiency (McArdle's RT disease)."; RL N. Engl. J. Med. 329:241-245(1993). RN [13] RP VARIANTS GSD5 PRO-397 AND LYS-655. RX PubMed=8535454; DOI=10.1002/humu.1380060318; RA Tsujino S., Shanske S., Martinuzzi A., Heiman-Patterson T., Dimauro S.; RT "Two novel missense mutations (E654K, L396P) in Caucasian patients with RT myophosphorylase deficiency (McArdle's disease)."; RL Hum. Mutat. 6:276-277(1995). RN [14] RP VARIANTS GSD5 SER-205; PRO-292; PRO-397; THR-543; LYS-655 AND PHE-709 DEL. RX PubMed=7603523; DOI=10.1002/mus.880181407; RA Tsujino S., Shanske S., Nonaka I., DiMauro S.; RT "The molecular genetic basis of myophosphorylase deficiency (McArdle's RT disease)."; RL Muscle Nerve 3:S23-S27(1995). RN [15] RP VARIANTS GSD5 GLU-666 AND ARG-686. RX PubMed=9506549; DOI=10.1002/ana.410430310; RA Vorgerd M., Kubisch C., Burwinkel B., Reichmann H., Mortier W., RA Tettenborn B., Pongratz D., Lindemuth R., Tegenthoff M., Malin J.P., RA Kilimann M.W.; RT "Mutation analysis in myophosphorylase deficiency (McArdle's disease)."; RL Ann. Neurol. 43:326-331(1998). RN [16] RP VARIANT GSD5 PRO-116. RX PubMed=10417800; RX DOI=10.1002/(sici)1097-4598(199908)22:8<1136::aid-mus21>3.0.co;2-2; RA Gamez J., Fernandez R., Bruno C., Andreu A.L., Cervera C., Navarro C., RA Schwartz S., Dimauro S.; RT "A new mutation in the regulatory domain of the myophosphorylase gene RT affecting protein dimer contact."; RL Muscle Nerve 22:1136-1138(1999). RN [17] RP VARIANTS GSD5 SER-205 AND TYR-685. RX PubMed=10382911; DOI=10.1016/s0960-8966(98)00125-4; RA Andreu A.L., Bruno C., Tamburino L., Gamez J., Shanske S., Cervera C., RA Navarro C., DiMauro S.; RT "A new mutation in the myophosphorylase gene (Asn684Tyr) in a Spanish RT patient with McArdle's disease."; RL Neuromuscul. Disord. 9:171-173(1999). RN [18] RP VARIANT GSD5 SER-205. RX PubMed=10382912; DOI=10.1016/s0960-8966(98)00127-8; RA Rubio J.C., Martin M.A., Garcia A., Campos Y., Cabello A., Culebras J.M., RA Arenas J.; RT "McArdle's disease associated with homozygosity for the missense mutation RT Gly204Ser of the myophosphorylase gene in a Spanish patient."; RL Neuromuscul. Disord. 9:174-175(1999). RN [19] RP VARIANT GSD5 ARG-798. RX PubMed=10681080; DOI=10.1001/archneur.57.2.217; RA Fernandez R., Navarro C., Andreu A.L., Bruno C., Shanske S., Gamez J., RA Teijeira S., Hernandez I., Teijeiro A., Fernandez J.M., Musumeci O., RA DiMauro S.; RT "A novel missense mutation (W797R) in the myophosphorylase gene in Spanish RT patients with McArdle disease."; RL Arch. Neurol. 57:217-219(2000). RN [20] RP VARIANT GSD5 ARG-798. RX PubMed=10590419; RX DOI=10.1002/(sici)1097-4598(200001)23:1<129::aid-mus20>3.0.co;2-f; RA Rubio J.C., Martin M.A., Campos Y., Auciello R., Cabello A., Arenas J.; RT "A missense mutation W797R in the myophosphorylase gene in a Spanish RT patient with McArdle's disease."; RL Muscle Nerve 23:129-131(2000). RN [21] RP VARIANT GSD5 ASN-488. RX PubMed=10714589; DOI=10.1016/s0960-8966(99)00082-6; RA Rubio J.C., Martin M.A., Campos Y., Cabello A., Arenas J.; RT "A missense mutation T487N in the myophosphorylase gene in a Spanish RT patient with McArdle's disease."; RL Neuromuscul. Disord. 10:138-140(2000). RN [22] RP VARIANT GSD5 ASP-660. RX PubMed=10899452; DOI=10.1016/s0960-8966(99)00124-8; RA Martin M.A., Rubio J.C., Campos Y., Ricoy J.R., Cabello A., Arenas J.; RT "A homozygous missense mutation (A659D) in the myophosphorylase gene in a RT Spanish patient with McArdle's disease."; RL Neuromuscul. Disord. 10:447-449(2000). RN [23] RP VARIANTS GSD5 PRO-116; TRP-194; SER-205; LYS-349; ASN-488; TRP-602; RP ASP-660; TYR-685; VAL-704 AND ARG-798. RX PubMed=11706962; DOI=10.1002/ana.1225.abs; RA Martin M.A., Rubio J.C., Buchbinder J., Fernandez-Hojas R., del Hoyo P., RA Teijeira S., Gamez J., Navarro C., Fernandez J.M., Cabello A., Campos Y., RA Cervera C., Culebras J.M., Andreu A.L., Fletterick R.J., Arenas J.; RT "Molecular heterogeneity of myophosphorylase deficiency (McArdle's RT disease): a genotype-phenotype correlation study."; RL Ann. Neurol. 50:574-581(2001). RN [24] RP VARIANT GSD5 PRO-687. RX PubMed=12031624; DOI=10.1016/s0960-8966(01)00320-0; RA Bruno C., Lanzillo R., Biedi C., Iadicicco L., Minetti C., Santoro L.; RT "Two new mutations in the myophosphorylase gene in Italian patients with RT McArdle's disease."; RL Neuromuscul. Disord. 12:498-500(2002). CC -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in CC glycogen catabolism, the phosphorolytic cleavage of glycogen to produce CC glucose-1-phosphate, and plays a central role in maintaining cellular CC and organismal glucose homeostasis. {ECO:0000269|PubMed:8316268}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D- CC glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732, CC Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1; CC Evidence={ECO:0000269|PubMed:1150650, ECO:0000269|PubMed:8316268}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41733; CC Evidence={ECO:0000269|PubMed:8316268}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250|UniProtKB:P00489}; CC -!- ACTIVITY REGULATION: Allosterically regulated through the non-covalent CC binding of metabolites, being activated by AMP and inhibited by ATP, CC ADP, and glucose-6-phosphate. The activity is also controlled by post- CC translational modifications including phosphorylation. CC {ECO:0000269|PubMed:1150650}. CC -!- SUBUNIT: Homodimer (PubMed:1150650, PubMed:16523484). Homotetramer; to CC form the enzymatically active phosphorylase A (PubMed:1150650). CC {ECO:0000269|PubMed:1150650, ECO:0000269|PubMed:16523484}. CC -!- INTERACTION: CC P11217; Q96HA8: NTAQ1; NbExp=4; IntAct=EBI-357469, EBI-741158; CC P11217; O43741: PRKAB2; NbExp=7; IntAct=EBI-357469, EBI-1053424; CC P11217; P11216: PYGB; NbExp=3; IntAct=EBI-357469, EBI-1047231; CC P11217; P06737: PYGL; NbExp=3; IntAct=EBI-357469, EBI-2511865; CC P11217; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-357469, EBI-25492395; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P11217-1; Sequence=Displayed; CC Name=2; CC IsoId=P11217-2; Sequence=VSP_043047; CC -!- PTM: Phosphorylation of Ser-15 converts phosphorylase B CC (unphosphorylated) to phosphorylase A. {ECO:0000269|PubMed:1150650}. CC -!- DISEASE: Glycogen storage disease 5 (GSD5) [MIM:232600]: A metabolic CC disorder resulting in myopathy characterized by exercise intolerance, CC cramps, muscle weakness and recurrent myoglobinuria. CC {ECO:0000269|PubMed:10382911, ECO:0000269|PubMed:10382912, CC ECO:0000269|PubMed:10417800, ECO:0000269|PubMed:10590419, CC ECO:0000269|PubMed:10681080, ECO:0000269|PubMed:10714589, CC ECO:0000269|PubMed:10899452, ECO:0000269|PubMed:11706962, CC ECO:0000269|PubMed:12031624, ECO:0000269|PubMed:7603523, CC ECO:0000269|PubMed:8316268, ECO:0000269|PubMed:8535454, CC ECO:0000269|PubMed:9506549}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family. CC {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; M32598; AAA60231.1; -; Genomic_DNA. DR EMBL; M32579; AAA60231.1; JOINED; Genomic_DNA. DR EMBL; M32580; AAA60231.1; JOINED; Genomic_DNA. DR EMBL; M32581; AAA60231.1; JOINED; Genomic_DNA. DR EMBL; M32582; AAA60231.1; JOINED; Genomic_DNA. DR EMBL; M32583; AAA60231.1; JOINED; Genomic_DNA. DR EMBL; M32584; AAA60231.1; JOINED; Genomic_DNA. DR EMBL; M32585; AAA60231.1; JOINED; Genomic_DNA. DR EMBL; M32586; AAA60231.1; JOINED; Genomic_DNA. DR EMBL; M32587; AAA60231.1; JOINED; Genomic_DNA. DR EMBL; M32588; AAA60231.1; JOINED; Genomic_DNA. DR EMBL; M32589; AAA60231.1; JOINED; Genomic_DNA. DR EMBL; M32590; AAA60231.1; JOINED; Genomic_DNA. DR EMBL; M32591; AAA60231.1; JOINED; Genomic_DNA. DR EMBL; M32592; AAA60231.1; JOINED; Genomic_DNA. DR EMBL; M32593; AAA60231.1; JOINED; Genomic_DNA. DR EMBL; M32594; AAA60231.1; JOINED; Genomic_DNA. DR EMBL; M32595; AAA60231.1; JOINED; Genomic_DNA. DR EMBL; M32596; AAA60231.1; JOINED; Genomic_DNA. DR EMBL; M32597; AAA60231.1; JOINED; Genomic_DNA. DR EMBL; U94777; AAC52081.1; -; Genomic_DNA. DR EMBL; U94774; AAC52081.1; JOINED; Genomic_DNA. DR EMBL; U94775; AAC52081.1; JOINED; Genomic_DNA. DR EMBL; U94776; AAC52081.1; JOINED; Genomic_DNA. DR EMBL; AF066859; AAC17451.1; -; mRNA. DR EMBL; AK056607; BAG51762.1; -; mRNA. DR EMBL; AP001462; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471076; EAW74284.1; -; Genomic_DNA. DR EMBL; BC126392; AAI26393.1; -; mRNA. DR EMBL; BC130514; AAI30515.1; -; mRNA. DR EMBL; X03031; CAA26834.1; -; mRNA. DR EMBL; M16013; AAA36216.1; -; mRNA. DR CCDS; CCDS53659.1; -. [P11217-2] DR CCDS; CCDS8079.1; -. [P11217-1] DR PIR; A27335; A27335. DR RefSeq; NP_001158188.1; NM_001164716.1. [P11217-2] DR RefSeq; NP_005600.1; NM_005609.3. [P11217-1] DR PDB; 1Z8D; X-ray; 2.30 A; A=1-842. DR PDBsum; 1Z8D; -. DR AlphaFoldDB; P11217; -. DR SMR; P11217; -. DR BioGRID; 111795; 97. DR IntAct; P11217; 30. DR MINT; P11217; -. DR STRING; 9606.ENSP00000164139; -. DR BindingDB; P11217; -. DR ChEMBL; CHEMBL3526; -. DR DrugBank; DB07793; (2S)-N-[(3S)-1-(2-AMINO-2-OXOETHYL)-2-OXO-1,2,3,4-TETRAHYDROQUINOLIN-3-YL]-2-CHLORO-2H-THIENO[2,3-B]PYRROLE-5-CARBOXAMIDE. DR DrugBank; DB03392; (3,4,5-Trihydroxy-6-Hydroxymethyl-Tetrahydro-Pyran-2-Yl)-Phosphoramidic Acid Dimethyl Ester. DR DrugBank; DB07807; (3R,4R,5R)-5-(HYDROXYMETHYL)-1-(3-PHENYLPROPYL)PIPERIDINE-3,4-DIOL. DR DrugBank; DB08500; (3S,5R,7R,8S,9S,10R)-7-(hydroxymethyl)-3-(2-naphthyl)-1,6-dioxa-2-azaspiro[4.5]decane-8,9,10-triol. DR DrugBank; DB08503; (3S,5R,7R,8S,9S,10R)-7-(hydroxymethyl)-3-(4-methylphenyl)-1,6-dioxa-2-azaspiro[4.5]decane-8,9,10-triol. DR DrugBank; DB08151; (5R,7R,8S,9S,10R)-7-(hydroxymethyl)-3-phenyl-1,6-dioxa-2-azaspiro[4.5]dec-2-ene-8,9,10-triol. DR DrugBank; DB01843; (5S,7R,8S,9S,10R)-3-Amino-8,9,10-trihydroxy-7-(hydroxymethyl)-6-oxa-1,3-diazaspiro[4.5]decane-2,4-dione. DR DrugBank; DB07792; (S)-2-CHLORO-N-(1-(2-(2-HYDROXYETHYLAMINO)-2-OXOETHYL)-2-OXO-1,2,3,4-TETRAHYDROQUINOLIN-3-YL)-6H-THIENO[2,3-B]PYRROLE-5-CARBOXAMIDE. DR DrugBank; DB07949; ({[(3E)-2'-Oxo-2',7'-dihydro-2,3'-biindol-3(7H)-ylidene]amino}oxy)acetic acid. DR DrugBank; DB04544; 1-Deoxy-1-acetylamino-beta-D-gluco-2-heptulopyranosonamide. DR DrugBank; DB04013; 1-Deoxy-1-methoxycarbamido-beta-D-gluco-2-heptulopyranosonamide. DR DrugBank; DB03657; 1-deoxy-1-methoxycarbamido-beta-D-glucopyranose. DR DrugBank; DB04055; 2,3-Dicarboxy-4-(2-Chloro-Phenyl)-1-Ethyl-5-Isopropoxycarbonyl-6-Methyl-Pyridinium. DR DrugBank; DB03133; 2-(Beta-D-Glucopyranosyl)-5-Methyl-1,2,3-Benzimidazole. DR DrugBank; DB03250; 2-(Beta-D-Glucopyranosyl)-5-Methyl-1,3,4-Benzothiazole. DR DrugBank; DB03354; 2-(Beta-D-Glucopyranosyl)-5-Methyl-1,3,4-Oxadiazole. DR DrugBank; DB06986; 2-CHLORO-N-[(1R,2R)-1-HYDROXY-2,3-DIHYDRO-1H-INDEN-2-YL]-6H-THIENO[2,3-B]PYRROLE-5-CARBOXAMIDE. DR DrugBank; DB07066; 2-CHLORO-N-[(3R)-2-OXO-1,2,3,4-TETRAHYDROQUINOLIN-3-YL]-6H-THIENO[2,3-B]PYRROLE-5-CARBOXAMIDE. DR DrugBank; DB08322; 2-DEOXY-3,4-BIS-O-[3-(4-HYDROXYPHENYL)PROPANOYL]-L-THREO-PENTARIC ACID. DR DrugBank; DB02604; 2-Deoxy-Glucose-6-Phosphate. DR DrugBank; DB02447; 3,8,9,10-tetrahydroxy-7-hydroxymethyl-6-oxa-1,3-diaza-spiro[4.5]decane-2,4-dione. DR DrugBank; DB03067; 4-{2,4-Bis[(3-Nitrobenzoyl)Amino]Phenoxy}Phthalic Acid. DR DrugBank; DB04044; 4-{2-[(3-Nitrobenzoyl)Amino]Phenoxy}Phthalic Acid. DR DrugBank; DB04643; 4-{3-CHLORO-4-[3-(2,4-DICHLORO-BENZOYL)-UREIDO]-PHENOXY}-BUTYRIC ACID. DR DrugBank; DB04644; 4-{4-[3-(2,4-DICHLORO-BENZOYL)-UREIDO]-2,3-DIMETHYL-PHENOXY}-BUTYRIC ACID. DR DrugBank; DB04645; 5-{3-[3-(2,4-DICHLORO-BENZOYL)-UREIDO]-2-METHYL-PHENOXY}-PENTANOIC ACID. DR DrugBank; DB04642; 7-{2,6-DICHLORO-4-[3-(2-CHLORO-BENZOYL)-UREIDO]-PHENOXY}-HEPTANOIC ACID. DR DrugBank; DB02964; 8,9,10-Trihydroxy-7-hydroxymethyl-2-thioxo-6-oxa-1,3-diaza-spiro[4.5]decan-4-one. DR DrugBank; DB03479; 8,9,10-trihydroxy-7-hydroxymethyl-3-methyl-6-oxa-1,3-diaza-spiro[4.5]decane-2,4-dione. DR DrugBank; DB02720; alpha-D-glucopyranosyl-2-carboxylic acid amide. DR DrugBank; DB02007; alpha-D-glucose 6-phosphate. DR DrugBank; DB02843; alpha-D-glucose-1-phosphate. DR DrugBank; DB03496; Alvocidib. DR DrugBank; DB01823; Beta-D-Glucopyranose Spirohydantoin. DR DrugBank; DB02379; Beta-D-Glucose. DR DrugBank; DB03286; C-(1-Azido-Alpha-D-Glucopyranosyl) Formamide. DR DrugBank; DB02719; C-(1-hydrogyl-beta-D-glucopyranosyl) formamide. DR DrugBank; DB03383; CP-320626. DR DrugBank; DB04522; Dexfosfoserine. DR DrugBank; DB04195; Heptulose-2-Phosphate. DR DrugBank; DB02519; Indirubin-5-sulphonate. DR DrugBank; DB04566; Inosinic Acid. DR DrugBank; DB02348; Monofluorophosphate ion. DR DrugBank; DB04083; N(6)-(pyridoxal phosphate)-L-lysine. DR DrugBank; DB04295; N-(Benzoylcarbamoyl)-beta-D-glucopyranosylamine. DR DrugBank; DB03835; N-[(5S,7R,8S,9S,10R)-8,9,10-Trihydroxy-7-(hydroxymethyl)-2,4-dioxo-6-oxa-1,3-diazaspiro[4.5]dec-3-yl]acetamide. DR DrugBank; DB03218; N-acetyl-N'-beta-D-glucopyranosyl urea. DR DrugBank; DB02320; N-beta-D-glucopyranosylacetamide. DR DrugBank; DB02471; Nojirimycine Tetrazole. DR DrugBank; DB00114; Pyridoxal phosphate. DR CAZy; GT35; Glycosyltransferase Family 35. DR GlyGen; P11217; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P11217; -. DR PhosphoSitePlus; P11217; -. DR SwissPalm; P11217; -. DR BioMuta; PYGM; -. DR DMDM; 3041717; -. DR EPD; P11217; -. DR jPOST; P11217; -. DR MassIVE; P11217; -. DR MaxQB; P11217; -. DR PaxDb; 9606-ENSP00000164139; -. DR PeptideAtlas; P11217; -. DR ProteomicsDB; 52721; -. [P11217-1] DR ProteomicsDB; 52722; -. [P11217-2] DR Pumba; P11217; -. DR Antibodypedia; 29416; 362 antibodies from 30 providers. DR DNASU; 5837; -. DR Ensembl; ENST00000164139.4; ENSP00000164139.3; ENSG00000068976.14. [P11217-1] DR Ensembl; ENST00000377432.7; ENSP00000366650.3; ENSG00000068976.14. [P11217-2] DR GeneID; 5837; -. DR KEGG; hsa:5837; -. DR MANE-Select; ENST00000164139.4; ENSP00000164139.3; NM_005609.4; NP_005600.1. DR UCSC; uc001oax.5; human. [P11217-1] DR AGR; HGNC:9726; -. DR CTD; 5837; -. DR DisGeNET; 5837; -. DR GeneCards; PYGM; -. DR GeneReviews; PYGM; -. DR HGNC; HGNC:9726; PYGM. DR HPA; ENSG00000068976; Group enriched (skeletal muscle, tongue). DR MalaCards; PYGM; -. DR MIM; 232600; phenotype. DR MIM; 608455; gene. DR neXtProt; NX_P11217; -. DR OpenTargets; ENSG00000068976; -. DR Orphanet; 368; Glycogen storage disease due to muscle glycogen phosphorylase deficiency. DR PharmGKB; PA34069; -. DR VEuPathDB; HostDB:ENSG00000068976; -. DR eggNOG; KOG2099; Eukaryota. DR GeneTree; ENSGT00950000183148; -. DR HOGENOM; CLU_010198_1_1_1; -. DR InParanoid; P11217; -. DR OMA; HGIKYEY; -. DR OrthoDB; 5473321at2759; -. DR PhylomeDB; P11217; -. DR TreeFam; TF300309; -. DR BioCyc; MetaCyc:HS00949-MONOMER; -. DR PathwayCommons; P11217; -. DR Reactome; R-HSA-70221; Glycogen breakdown (glycogenolysis). DR SignaLink; P11217; -. DR SIGNOR; P11217; -. DR BioGRID-ORCS; 5837; 32 hits in 1152 CRISPR screens. DR EvolutionaryTrace; P11217; -. DR GenomeRNAi; 5837; -. DR Pharos; P11217; Tchem. DR PRO; PR:P11217; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P11217; Protein. DR Bgee; ENSG00000068976; Expressed in skeletal muscle tissue of biceps brachii and 145 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0008184; F:glycogen phosphorylase activity; IDA:UniProtKB. DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0005980; P:glycogen catabolic process; IDA:UniProtKB. DR GO; GO:0005977; P:glycogen metabolic process; TAS:ProtInc. DR CDD; cd04300; GT35_Glycogen_Phosphorylase; 1. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2. DR InterPro; IPR011833; Glycg_phsphrylas. DR InterPro; IPR000811; Glyco_trans_35. DR InterPro; IPR035090; Pyridoxal_P_attach_site. DR NCBIfam; TIGR02093; P_ylase; 1. DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1. DR PANTHER; PTHR11468:SF13; GLYCOGEN PHOSPHORYLASE, MUSCLE FORM; 1. DR Pfam; PF00343; Phosphorylase; 1. DR PIRSF; PIRSF000460; Pprylas_GlgP; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. DR PROSITE; PS00102; PHOSPHORYLASE; 1. DR Genevisible; P11217; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Allosteric enzyme; Alternative splicing; KW Carbohydrate metabolism; Disease variant; Glycogen metabolism; KW Glycogen storage disease; Glycosyltransferase; Nucleotide-binding; KW Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P00489" FT CHAIN 2..842 FT /note="Glycogen phosphorylase, muscle form" FT /id="PRO_0000188529" FT BINDING 43 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000269|PubMed:16523484, FT ECO:0007744|PDB:1Z8D" FT BINDING 76 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000269|PubMed:16523484, FT ECO:0007744|PDB:1Z8D" FT BINDING 310..319 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000269|PubMed:16523484, FT ECO:0007744|PDB:1Z8D" FT SITE 109 FT /note="Involved in the association of subunits" FT /evidence="ECO:0000250|UniProtKB:P00489" FT SITE 143 FT /note="Involved in the association of subunits" FT /evidence="ECO:0000250|UniProtKB:P00489" FT SITE 156 FT /note="May be involved in allosteric control" FT /evidence="ECO:0000250|UniProtKB:P00489" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:P00489" FT MOD_RES 15 FT /note="Phosphoserine; by PHK; in form phosphorylase A" FT /evidence="ECO:0000269|PubMed:1150650" FT MOD_RES 204 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P09812" FT MOD_RES 227 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P09812" FT MOD_RES 430 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9WUB3" FT MOD_RES 473 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9WUB3" FT MOD_RES 514 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P09812" FT MOD_RES 681 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000250|UniProtKB:P00489" FT MOD_RES 747 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P09812" FT MOD_RES 748 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P09812" FT VAR_SEQ 82..169 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043047" FT VARIANT 50..842 FT /note="Missing (in GSD5)" FT /evidence="ECO:0000269|PubMed:8316268" FT /id="VAR_085195" FT VARIANT 116 FT /note="L -> P (in GSD5; dbSNP:rs776680924)" FT /evidence="ECO:0000269|PubMed:10417800, FT ECO:0000269|PubMed:11706962" FT /id="VAR_014002" FT VARIANT 194 FT /note="R -> W (in GSD5; dbSNP:rs376581557)" FT /evidence="ECO:0000269|PubMed:11706962" FT /id="VAR_014003" FT VARIANT 205 FT /note="G -> S (in GSD5; dbSNP:rs119103251)" FT /evidence="ECO:0000269|PubMed:10382911, FT ECO:0000269|PubMed:10382912, ECO:0000269|PubMed:11706962, FT ECO:0000269|PubMed:7603523, ECO:0000269|PubMed:8316268" FT /id="VAR_003431" FT VARIANT 292 FT /note="L -> P (in GSD5; rare mutation; dbSNP:rs780375860)" FT /evidence="ECO:0000269|PubMed:7603523" FT /id="VAR_014004" FT VARIANT 349 FT /note="E -> K (in GSD5)" FT /evidence="ECO:0000269|PubMed:11706962" FT /id="VAR_014005" FT VARIANT 397 FT /note="L -> P (in GSD5; dbSNP:rs1005687078)" FT /evidence="ECO:0000269|PubMed:7603523, FT ECO:0000269|PubMed:8535454" FT /id="VAR_003432" FT VARIANT 414 FT /note="R -> G (in dbSNP:rs11231866)" FT /id="VAR_061198" FT VARIANT 488 FT /note="T -> N (in GSD5; dbSNP:rs1555134900)" FT /evidence="ECO:0000269|PubMed:10714589, FT ECO:0000269|PubMed:11706962" FT /id="VAR_014006" FT VARIANT 543 FT /note="K -> T (in GSD5; dbSNP:rs119103252)" FT /evidence="ECO:0000269|PubMed:7603523, FT ECO:0000269|PubMed:8316268" FT /id="VAR_003433" FT VARIANT 602 FT /note="R -> W (in GSD5; dbSNP:rs750195683)" FT /evidence="ECO:0000269|PubMed:11706962" FT /id="VAR_014007" FT VARIANT 655 FT /note="E -> K (in GSD5; dbSNP:rs119103253)" FT /evidence="ECO:0000269|PubMed:7603523, FT ECO:0000269|PubMed:8535454" FT /id="VAR_003434" FT VARIANT 660 FT /note="A -> D (in GSD5)" FT /evidence="ECO:0000269|PubMed:10899452, FT ECO:0000269|PubMed:11706962" FT /id="VAR_014008" FT VARIANT 666 FT /note="Q -> E (in GSD5; dbSNP:rs119103256)" FT /evidence="ECO:0000269|PubMed:9506549" FT /id="VAR_014009" FT VARIANT 685 FT /note="N -> Y (in GSD5)" FT /evidence="ECO:0000269|PubMed:10382911, FT ECO:0000269|PubMed:11706962" FT /id="VAR_014010" FT VARIANT 686 FT /note="G -> R (in GSD5; dbSNP:rs144081869)" FT /evidence="ECO:0000269|PubMed:9506549" FT /id="VAR_014011" FT VARIANT 687 FT /note="A -> P (in GSD5)" FT /evidence="ECO:0000269|PubMed:12031624" FT /id="VAR_014012" FT VARIANT 704 FT /note="A -> V (in GSD5; dbSNP:rs1483102315)" FT /evidence="ECO:0000269|PubMed:11706962" FT /id="VAR_014013" FT VARIANT 709 FT /note="Missing (in GSD5; common in Japanese patients)" FT /evidence="ECO:0000269|PubMed:7603523" FT /id="VAR_014014" FT VARIANT 798 FT /note="W -> R (in GSD5; dbSNP:rs119103258)" FT /evidence="ECO:0000269|PubMed:10590419, FT ECO:0000269|PubMed:10681080, ECO:0000269|PubMed:11706962" FT /id="VAR_014015" FT CONFLICT 791 FT /note="L -> W (in Ref. 1; AAA60231)" FT /evidence="ECO:0000305" FT HELIX 7..10 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 11..13 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 25..38 FT /evidence="ECO:0007829|PDB:1Z8D" FT TURN 44..46 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 49..78 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 82..86 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 96..102 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 106..114 FT /evidence="ECO:0007829|PDB:1Z8D" FT TURN 115..117 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 120..126 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 136..150 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 155..160 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 168..172 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 175..179 FT /evidence="ECO:0007829|PDB:1Z8D" FT TURN 183..186 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 195..197 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 199..204 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 206..210 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 213..218 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 220..232 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 234..236 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 239..248 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 263..270 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 271..277 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 291..313 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 330..333 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 334..341 FT /evidence="ECO:0007829|PDB:1Z8D" FT TURN 342..345 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 346..356 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 362..372 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 373..376 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 382..384 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 387..389 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 390..396 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 398..418 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 423..429 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 431..433 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 435..437 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 439..441 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 442..448 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 451..457 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 458..466 FT /evidence="ECO:0007829|PDB:1Z8D" FT TURN 467..469 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 470..475 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 477..479 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 480..482 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 490..495 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 498..508 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 511..514 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 516..525 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 529..553 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 562..569 FT /evidence="ECO:0007829|PDB:1Z8D" FT TURN 573..576 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 577..593 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 602..607 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 615..631 FT /evidence="ECO:0007829|PDB:1Z8D" FT TURN 635..637 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 638..640 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 641..646 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 651..657 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 658..660 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 662..666 FT /evidence="ECO:0007829|PDB:1Z8D" FT TURN 670..672 FT /evidence="ECO:0007829|PDB:1Z8D" FT TURN 683..686 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 688..691 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 697..704 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 706..708 FT /evidence="ECO:0007829|PDB:1Z8D" FT STRAND 709..711 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 716..725 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 730..733 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 737..748 FT /evidence="ECO:0007829|PDB:1Z8D" FT TURN 749..751 FT /evidence="ECO:0007829|PDB:1Z8D" FT TURN 756..759 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 760..768 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 774..792 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 795..806 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 810..812 FT /evidence="ECO:0007829|PDB:1Z8D" FT HELIX 814..824 FT /evidence="ECO:0007829|PDB:1Z8D" SQ SEQUENCE 842 AA; 97092 MW; EBDB7D80D740B68F CRC64; MSRPLSDQEK RKQISVRGLA GVENVTELKK NFNRHLHFTL VKDRNVATPR DYYFALAHTV RDHLVGRWIR TQQHYYEKDP KRIYYLSLEF YMGRTLQNTM VNLALENACD EATYQLGLDM EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK ISGGWQMEEA DDWLRYGNPW EKARPEFTLP VHFYGHVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN TMRLWSAKAP NDFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV VAATLQDIIR RFKSSKFGCR DPVRTNFDAF PDKVAIQLND THPSLAIPEL MRILVDLERM DWDKAWDVTV RTCAYTNHTV LPEALERWPV HLLETLLPRH LQIIYEINQR FLNRVAAAFP GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS HAVNGVARIH SEILKKTIFK DFYELEPHKF QNKTNGITPR RWLVLCNPGL AEVIAERIGE DFISDLDQLR KLLSFVDDEA FIRDVAKVKQ ENKLKFAAYL EREYKVHINP NSLFDIQVKR IHEYKRQLLN CLHVITLYNR IKREPNKFFV PRTVMIGGKA APGYHMAKMI IRLVTAIGDV VNHDPAVGDR LRVIFLENYR VSLAEKVIPA ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENFF IFGMRVEDVD KLDQRGYNAQ EYYDRIPELR QVIEQLSSGF FSPKQPDLFK DIVNMLMHHD RFKVFADYED YIKCQEKVSA LYKNPREWTR MVIRNIATSG KFSSDRTIAQ YAREIWGVEP SRQRLPAPDE AI //