PYGM_HUMAN
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 03-AUG-2022, entry version 239.
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}.
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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; 92.
DR IntAct; P11217; 29.
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 BioMuta; PYGM; -.
DR DMDM; 3041717; -.
DR EPD; P11217; -.
DR jPOST; P11217; -.
DR MassIVE; P11217; -.
DR MaxQB; P11217; -.
DR PaxDb; P11217; -.
DR PeptideAtlas; P11217; -.
DR PRIDE; P11217; -.
DR ProteomicsDB; 52721; -. [P11217-1]
DR ProteomicsDB; 52722; -. [P11217-2]
DR Antibodypedia; 29416; 325 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 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; IYDINWR; -.
DR OrthoDB; 240595at2759; -.
DR PhylomeDB; P11217; -.
DR TreeFam; TF300309; -.
DR BioCyc; MetaCyc:HS00949-MON; -.
DR PathwayCommons; P11217; -.
DR Reactome; R-HSA-70221; Glycogen breakdown (glycogenolysis).
DR SignaLink; P11217; -.
DR SIGNOR; P11217; -.
DR BioGRID-ORCS; 5837; 32 hits in 1072 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 143 other tissues.
DR Genevisible; P11217; HS.
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 InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR PANTHER; PTHR11468; PTHR11468; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR TIGRFAMs; TIGR02093; P_ylase; 1.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
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
