GenomeNet

Database: UniProt/SWISS-PROT
Entry: GYS1_HUMAN
LinkDB: GYS1_HUMAN
Original site: GYS1_HUMAN 
ID   GYS1_HUMAN              Reviewed;         737 AA.
AC   P13807; Q9BTT9;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   24-JAN-2024, entry version 217.
DE   RecName: Full=Glycogen [starch] synthase, muscle {ECO:0000305};
DE            EC=2.4.1.11 {ECO:0000250|UniProtKB:P13834, ECO:0000305|PubMed:35835870};
DE   AltName: Full=Glycogen synthase 1 {ECO:0000312|HGNC:HGNC:4706};
GN   Name=GYS1 {ECO:0000312|HGNC:HGNC:4706}; Synonyms=GYS;
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] (ISOFORM 1).
RC   TISSUE=Muscle;
RX   PubMed=2493642; DOI=10.1073/pnas.86.5.1443;
RA   Browner M.F., Nakano K., Bang A.G., Fletterick R.J.;
RT   "Human muscle glycogen synthase cDNA sequence: a negatively charged protein
RT   with an asymmetric charge distribution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:1443-1447(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT NIDDM SER-464.
RX   PubMed=7657035; DOI=10.2337/diab.44.9.1099;
RA   Orho M., Nikula-Ijas P., Schalin-Jantti C., Permutt M.A., Groop L.C.;
RT   "Isolation and characterization of the human muscle glycogen synthase
RT   gene.";
RL   Diabetes 44:1099-1105(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Endometrium;
RX   PubMed=9010351; DOI=10.1016/s0960-0760(96)00138-0;
RA   Su X., Schuler L., Shapiro S.S.;
RT   "Cloning and characterization of a glycogen synthase cDNA from human
RT   endometrium.";
RL   J. Steroid Biochem. Mol. Biol. 59:459-465(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Kidney, Lymph, and Skin;
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   [7]
RP   INTERACTION WITH GYG1.
RX   PubMed=17055998; DOI=10.1016/j.abb.2006.09.024;
RA   Skurat A.V., Dietrich A.D., Roach P.J.;
RT   "Interaction between glycogenin and glycogen synthase.";
RL   Arch. Biochem. Biophys. 456:93-97(2006).
RN   [8]
RP   INVOLVEMENT IN GSD0B.
RX   PubMed=17928598; DOI=10.1056/nejmoa066691;
RA   Kollberg G., Tulinius M., Gilljam T., Oestman-Smith I., Forsander G.,
RA   Jotorp P., Oldfors A., Holme E.;
RT   "Cardiomyopathy and exercise intolerance in muscle glycogen storage disease
RT   0.";
RL   N. Engl. J. Med. 357:1507-1514(2007).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641; SER-645 AND SER-649, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [13]
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   [14]
RP   DEPHOSPHORYLATION AT SER-641 AND SER-645 BY PP1.
RX   PubMed=21668450; DOI=10.1111/j.1471-4159.2011.07345.x;
RA   Kelsall I.R., Voss M., Munro S., Cuthbertson D.J., Cohen P.T.;
RT   "R3F, a novel membrane-associated glycogen targeting subunit of protein
RT   phosphatase 1 regulates glycogen synthase in astrocytoma cells in response
RT   to glucose and extracellular signals.";
RL   J. Neurochem. 118:596-610(2011).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412; SER-710 AND SER-727, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND THR-700, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [18] {ECO:0000312|PDB:7ZBN}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.62 ANGSTROMS) IN COMPLEX WITH GYG1,
RP   ACTIVITY REGULATION, SUBUNIT, AND PHOSPHORYLATION AT SER-8; SER-412;
RP   SER-641; SER-645; SER-652; SER-653; SER-657; SER-727 AND SER-731.
RX   PubMed=35690592; DOI=10.1038/s41467-022-31109-6;
RA   Marr L., Biswas D., Daly L.A., Browning C., Vial S.C.M., Maskell D.P.,
RA   Hudson C., Bertrand J.A., Pollard J., Ranson N.A., Khatter H., Eyers C.E.,
RA   Sakamoto K., Zeqiraj E.;
RT   "Mechanism of glycogen synthase inactivation and interaction with
RT   glycogenin.";
RL   Nat. Commun. 13:3372-3372(2022).
RN   [19] {ECO:0000312|PDB:7Q0B, ECO:0000312|PDB:7Q0S, ECO:0000312|PDB:7Q12, ECO:0000312|PDB:7Q13}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH GYG1; UDP;
RP   ALPHA-D-GLUCOSE AND GLUCOSE-6-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY,
RP   ACTIVITY REGULATION, PATHWAY, AND SUBUNIT.
RX   PubMed=35835870; DOI=10.1038/s41594-022-00799-3;
RA   McCorvie T.J., Loria P.M., Tu M., Han S., Shrestha L., Froese D.S.,
RA   Ferreira I.M., Berg A.P., Yue W.W.;
RT   "Molecular basis for the regulation of human glycogen synthase by
RT   phosphorylation and glucose-6-phosphate.";
RL   Nat. Struct. Mol. Biol. 29:628-638(2022).
CC   -!- FUNCTION: Glycogen synthase participates in the glycogen biosynthetic
CC       process along with glycogenin and glycogen branching enzyme. Extends
CC       the primer composed of a few glucose units formed by glycogenin by
CC       adding new glucose units to it. In this context, glycogen synthase
CC       transfers the glycosyl residue from UDP-Glc to the non-reducing end of
CC       alpha-1,4-glucan. {ECO:0000269|PubMed:35835870}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-
CC         alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:18549, Rhea:RHEA-
CC         COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.11;
CC         Evidence={ECO:0000269|PubMed:35835870};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18550;
CC         Evidence={ECO:0000269|PubMed:35835870};
CC   -!- ACTIVITY REGULATION: Allosteric activation by glucose-6-phosphate
CC       (PubMed:35690592, PubMed:35835870). Phosphorylation reduces enzyme
CC       activity by constraining a tense conformation of the tetramer through
CC       inter-subunit interaction (PubMed:35690592, PubMed:35835870).
CC       Phosphorylation reduces the activity towards UDP-glucose (By
CC       similarity). When in the non-phosphorylated state, glycogen synthase
CC       does not require glucose-6-phosphate as an allosteric activator; when
CC       phosphorylated it does (By similarity). {ECO:0000250|UniProtKB:P13834,
CC       ECO:0000250|UniProtKB:P54840, ECO:0000269|PubMed:35690592,
CC       ECO:0000269|PubMed:35835870}.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000269|PubMed:35835870}.
CC   -!- SUBUNIT: Part of the GYS1-GYG1 complex, a heterooctamer composed of a
CC       tetramer of GYS1 and 2 dimers of GYG1, where each GYS1 protomer binds
CC       to one GYG1 subunit (via GYG1 C-terminus); the GYS1 tetramer may
CC       dissociate from GYG1 dimers to continue glycogen polymerization on its
CC       own. {ECO:0000269|PubMed:17055998, ECO:0000269|PubMed:35690592,
CC       ECO:0000269|PubMed:35835870}.
CC   -!- INTERACTION:
CC       P13807; Q13155: AIMP2; NbExp=3; IntAct=EBI-740553, EBI-745226;
CC       P13807; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-740553, EBI-10181188;
CC       P13807; Q53HL2: CDCA8; NbExp=3; IntAct=EBI-740553, EBI-979174;
CC       P13807; Q5SYC1: CLVS2; NbExp=3; IntAct=EBI-740553, EBI-12357161;
CC       P13807; O43186: CRX; NbExp=3; IntAct=EBI-740553, EBI-748171;
CC       P13807; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-740553, EBI-2349927;
CC       P13807; Q86W67: FAM228A; NbExp=3; IntAct=EBI-740553, EBI-12958227;
CC       P13807; P49841: GSK3B; NbExp=4; IntAct=EBI-740553, EBI-373586;
CC       P13807; P46976: GYG1; NbExp=7; IntAct=EBI-740553, EBI-740533;
CC       P13807; P46976-2: GYG1; NbExp=3; IntAct=EBI-740553, EBI-12017394;
CC       P13807; P17509: HOXB6; NbExp=3; IntAct=EBI-740553, EBI-741308;
CC       P13807; P31273: HOXC8; NbExp=3; IntAct=EBI-740553, EBI-1752118;
CC       P13807; Q8IYA8: IHO1; NbExp=6; IntAct=EBI-740553, EBI-8638439;
CC       P13807; Q0VD86: INCA1; NbExp=3; IntAct=EBI-740553, EBI-6509505;
CC       P13807; Q9H079: KATNBL1; NbExp=5; IntAct=EBI-740553, EBI-715394;
CC       P13807; Q13351: KLF1; NbExp=3; IntAct=EBI-740553, EBI-8284732;
CC       P13807; O43474: KLF4; NbExp=5; IntAct=EBI-740553, EBI-7232405;
CC       P13807; P50221: MEOX1; NbExp=3; IntAct=EBI-740553, EBI-2864512;
CC       P13807; P17568: NDUFB7; NbExp=3; IntAct=EBI-740553, EBI-1246238;
CC       P13807; P49585: PCYT1A; NbExp=3; IntAct=EBI-740553, EBI-2563309;
CC       P13807; Q96BK5: PINX1; NbExp=3; IntAct=EBI-740553, EBI-721782;
CC       P13807; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-740553, EBI-2876622;
CC       P13807; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-740553, EBI-10171633;
CC       P13807; Q9UQK1: PPP1R3C; NbExp=2; IntAct=EBI-740553, EBI-2506727;
CC       P13807; Q5RL73: RBM48; NbExp=3; IntAct=EBI-740553, EBI-473821;
CC       P13807; Q8TAD8: SNIP1; NbExp=3; IntAct=EBI-740553, EBI-749336;
CC       P13807; O60504: SORBS3; NbExp=3; IntAct=EBI-740553, EBI-741237;
CC       P13807; Q7Z6R9: TFAP2D; NbExp=3; IntAct=EBI-740553, EBI-11952651;
CC       P13807; Q08117-2: TLE5; NbExp=5; IntAct=EBI-740553, EBI-11741437;
CC       P13807; Q86T24: ZBTB33; NbExp=3; IntAct=EBI-740553, EBI-2515625;
CC       P13807; Q9UDV6: ZNF212; NbExp=3; IntAct=EBI-740553, EBI-1640204;
CC       P13807; Q5BKZ1: ZNF326; NbExp=3; IntAct=EBI-740553, EBI-2560158;
CC       P13807; Q6S9Z5: ZNF474; NbExp=3; IntAct=EBI-740553, EBI-17269964;
CC       P13807; Q9H707: ZNF552; NbExp=3; IntAct=EBI-740553, EBI-2555731;
CC       P13807; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-740553, EBI-4395669;
CC       P13807; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-740553, EBI-10251462;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P13807-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P13807-2; Sequence=VSP_042745;
CC   -!- TISSUE SPECIFICITY: Expressed in skeletal muscle and most other cell
CC       types where glycogen is present. {ECO:0000305|PubMed:2493642}.
CC   -!- PTM: Phosphorylation at Ser-8 by AMPK inactivates the enzyme activity.
CC       Primed phosphorylation at Ser-657 (site 5) by CSNK2A1 and CSNK2A2 is
CC       required for inhibitory phosphorylation at Ser-641 (site 3a), Ser-645
CC       (site 3b), Ser-649 (site 3c) and Ser-653 (site 4) by GSK3A an GSK3B (By
CC       similarity). Phosphorylated at Ser-641 by DYRK2, leading to
CC       inactivation (By similarity). Phosphorylated at Ser-641 by PASK,
CC       leading to inactivation; phosphorylation by PASK is inhibited by
CC       glycogen. Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the
CC       enzyme (PubMed:35835870). {ECO:0000250|UniProtKB:P13834,
CC       ECO:0000305|PubMed:35835870}.
CC   -!- DISEASE: Muscle glycogen storage disease 0 (GSD0b) [MIM:611556]:
CC       Metabolic disorder characterized by fasting hypoglycemia presenting in
CC       infancy or early childhood. The role of muscle glycogen is to provide
CC       critical energy during bursts of activity and sustained muscle work.
CC       {ECO:0000269|PubMed:17928598}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 3 family. {ECO:0000305}.
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DR   EMBL; J04501; AAA88046.1; -; mRNA.
DR   EMBL; Z33622; CAA83916.1; -; Genomic_DNA.
DR   EMBL; Z33623; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; Z33609; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; Z33624; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; Z33625; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; Z33626; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; Z33610; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; Z33627; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; Z33628; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; Z33629; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; Z33630; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; Z33631; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; Z33633; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; U32573; AAB60385.1; -; mRNA.
DR   EMBL; AC008687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC026803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC098792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471177; EAW52424.1; -; Genomic_DNA.
DR   EMBL; BC002617; AAH02617.1; -; mRNA.
DR   EMBL; BC003182; AAH03182.1; -; mRNA.
DR   EMBL; BC007688; AAH07688.1; -; mRNA.
DR   CCDS; CCDS12747.1; -. [P13807-1]
DR   CCDS; CCDS54292.1; -. [P13807-2]
DR   PIR; A32156; A32156.
DR   RefSeq; NP_001155059.1; NM_001161587.1. [P13807-2]
DR   RefSeq; NP_002094.2; NM_002103.4. [P13807-1]
DR   PDB; 7Q0B; EM; 3.00 A; A/B/C/D=1-737.
DR   PDB; 7Q0S; EM; 4.00 A; A/B/C/D=1-737.
DR   PDB; 7Q12; EM; 3.70 A; A/B/C/D=1-737.
DR   PDB; 7Q13; EM; 3.00 A; A/B/C/D=1-737.
DR   PDB; 7ZBN; EM; 2.62 A; A/B/C/D=1-737.
DR   PDB; 8CVX; EM; 3.50 A; A/B/C/D=1-634.
DR   PDB; 8CVY; EM; 3.60 A; A/B/C/D=1-634.
DR   PDB; 8CVZ; EM; 3.52 A; A/B/C/D=1-634.
DR   PDBsum; 7Q0B; -.
DR   PDBsum; 7Q0S; -.
DR   PDBsum; 7Q12; -.
DR   PDBsum; 7Q13; -.
DR   PDBsum; 7ZBN; -.
DR   PDBsum; 8CVX; -.
DR   PDBsum; 8CVY; -.
DR   PDBsum; 8CVZ; -.
DR   AlphaFoldDB; P13807; -.
DR   EMDB; EMD-13743; -.
DR   EMDB; EMD-13751; -.
DR   EMDB; EMD-13752; -.
DR   EMDB; EMD-13753; -.
DR   EMDB; EMD-14587; -.
DR   EMDB; EMD-27020; -.
DR   EMDB; EMD-27021; -.
DR   EMDB; EMD-27022; -.
DR   SMR; P13807; -.
DR   BioGRID; 109252; 110.
DR   IntAct; P13807; 80.
DR   MINT; P13807; -.
DR   STRING; 9606.ENSP00000317904; -.
DR   BindingDB; P13807; -.
DR   ChEMBL; CHEMBL4000; -.
DR   CAZy; GT3; Glycosyltransferase Family 3.
DR   GlyGen; P13807; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P13807; -.
DR   PhosphoSitePlus; P13807; -.
DR   SwissPalm; P13807; -.
DR   BioMuta; GYS1; -.
DR   DMDM; 1351366; -.
DR   EPD; P13807; -.
DR   jPOST; P13807; -.
DR   MassIVE; P13807; -.
DR   MaxQB; P13807; -.
DR   PaxDb; 9606-ENSP00000317904; -.
DR   PeptideAtlas; P13807; -.
DR   ProteomicsDB; 52994; -. [P13807-1]
DR   ProteomicsDB; 52995; -. [P13807-2]
DR   Pumba; P13807; -.
DR   Antibodypedia; 3582; 497 antibodies from 39 providers.
DR   DNASU; 2997; -.
DR   Ensembl; ENST00000263276.6; ENSP00000263276.6; ENSG00000104812.15. [P13807-2]
DR   Ensembl; ENST00000323798.8; ENSP00000317904.3; ENSG00000104812.15. [P13807-1]
DR   GeneID; 2997; -.
DR   KEGG; hsa:2997; -.
DR   MANE-Select; ENST00000323798.8; ENSP00000317904.3; NM_002103.5; NP_002094.2.
DR   UCSC; uc002plp.4; human. [P13807-1]
DR   AGR; HGNC:4706; -.
DR   CTD; 2997; -.
DR   DisGeNET; 2997; -.
DR   GeneCards; GYS1; -.
DR   HGNC; HGNC:4706; GYS1.
DR   HPA; ENSG00000104812; Group enriched (heart muscle, skeletal muscle, tongue).
DR   MalaCards; GYS1; -.
DR   MIM; 138570; gene.
DR   MIM; 611556; phenotype.
DR   neXtProt; NX_P13807; -.
DR   OpenTargets; ENSG00000104812; -.
DR   Orphanet; 137625; Glycogen storage disease due to muscle and heart glycogen synthase deficiency.
DR   PharmGKB; PA29084; -.
DR   VEuPathDB; HostDB:ENSG00000104812; -.
DR   eggNOG; KOG3742; Eukaryota.
DR   GeneTree; ENSGT00390000018612; -.
DR   HOGENOM; CLU_015910_1_0_1; -.
DR   InParanoid; P13807; -.
DR   OMA; RDVRNHI; -.
DR   OrthoDB; 9432at2759; -.
DR   PhylomeDB; P13807; -.
DR   TreeFam; TF300306; -.
DR   BioCyc; MetaCyc:HS02622-MONOMER; -.
DR   BRENDA; 2.4.1.11; 2681.
DR   PathwayCommons; P13807; -.
DR   Reactome; R-HSA-3322077; Glycogen synthesis.
DR   Reactome; R-HSA-3785653; Myoclonic epilepsy of Lafora.
DR   Reactome; R-HSA-3814836; Glycogen storage disease type XV (GYG1).
DR   Reactome; R-HSA-3828062; Glycogen storage disease type 0 (muscle GYS1).
DR   SignaLink; P13807; -.
DR   SIGNOR; P13807; -.
DR   UniPathway; UPA00164; -.
DR   BioGRID-ORCS; 2997; 106 hits in 1157 CRISPR screens.
DR   ChiTaRS; GYS1; human.
DR   GenomeRNAi; 2997; -.
DR   Pharos; P13807; Tchem.
DR   PRO; PR:P13807; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P13807; Protein.
DR   Bgee; ENSG00000104812; Expressed in hindlimb stylopod muscle and 167 other cell types or tissues.
DR   ExpressionAtlas; P13807; baseline and differential.
DR   Genevisible; P13807; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0016234; C:inclusion body; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005536; F:glucose binding; IEA:Ensembl.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; EXP:Reactome.
DR   GO; GO:0061547; F:glycogen synthase activity, transferring glucose-1-phosphate; EXP:Reactome.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IBA:GO_Central.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   CDD; cd03793; GT3_GSY2-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR008631; Glycogen_synth.
DR   PANTHER; PTHR10176:SF2; GLYCOGEN [STARCH] SYNTHASE, MUSCLE; 1.
DR   PANTHER; PTHR10176; GLYCOGEN SYNTHASE; 1.
DR   Pfam; PF05693; Glycogen_syn; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Allosteric enzyme; Alternative splicing; Diabetes mellitus;
KW   Disease variant; Glycogen biosynthesis; Glycosyltransferase;
KW   Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..737
FT                   /note="Glycogen [starch] synthase, muscle"
FT                   /id="PRO_0000194763"
FT   REGION          634..737
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..671
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..692
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..737
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000269|PubMed:35835870,
FT                   ECO:0007744|PDB:7Q13"
FT   BINDING         205
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000305|PubMed:35835870,
FT                   ECO:0007744|PDB:7Q13"
FT   BINDING         211
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000305|PubMed:35835870,
FT                   ECO:0007744|PDB:7Q13"
FT   BINDING         291
FT                   /ligand="alpha-D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58225"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   two neighboring subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000269|PubMed:35835870,
FT                   ECO:0007744|PDB:7Q13"
FT   BINDING         292
FT                   /ligand="alpha-D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58225"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   two neighboring subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000269|PubMed:35835870,
FT                   ECO:0007744|PDB:7Q13"
FT   BINDING         294
FT                   /ligand="alpha-D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58225"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   two neighboring subunits"
FT                   /evidence="ECO:0000269|PubMed:35835870,
FT                   ECO:0007744|PDB:7Q12, ECO:0007744|PDB:7Q13"
FT   BINDING         297
FT                   /ligand="alpha-D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58225"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   two neighboring subunits"
FT                   /evidence="ECO:0000269|PubMed:35835870,
FT                   ECO:0007744|PDB:7Q13"
FT   BINDING         301
FT                   /ligand="alpha-D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58225"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   two neighboring subunits"
FT                   /evidence="ECO:0000269|PubMed:35835870,
FT                   ECO:0007744|PDB:7Q13"
FT   BINDING         331
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000269|PubMed:35835870,
FT                   ECO:0007744|PDB:7Q13"
FT   BINDING         331
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000305|PubMed:35835870,
FT                   ECO:0007744|PDB:7Q13"
FT   BINDING         501
FT                   /ligand="alpha-D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58225"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   two neighboring subunits"
FT                   /evidence="ECO:0000269|PubMed:35835870,
FT                   ECO:0007744|PDB:7Q12, ECO:0007744|PDB:7Q13"
FT   BINDING         510
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000305|PubMed:35835870,
FT                   ECO:0007744|PDB:7Q13"
FT   BINDING         512
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000305|PubMed:35835870,
FT                   ECO:0007744|PDB:7Q13"
FT   BINDING         513
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000305|PubMed:35835870,
FT                   ECO:0007744|PDB:7Q13"
FT   BINDING         515
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000269|PubMed:35835870,
FT                   ECO:0007744|PDB:7Q13"
FT   BINDING         582
FT                   /ligand="alpha-D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58225"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   two neighboring subunits"
FT                   /evidence="ECO:0000269|PubMed:35835870,
FT                   ECO:0007744|PDB:7Q12, ECO:0007744|PDB:7Q13"
FT   BINDING         586
FT                   /ligand="alpha-D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58225"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   two neighboring subunits"
FT                   /evidence="ECO:0000269|PubMed:35835870,
FT                   ECO:0007744|PDB:7Q12, ECO:0007744|PDB:7Q13"
FT   MOD_RES         8
FT                   /note="Phosphoserine; by AMPK and PKA"
FT                   /evidence="ECO:0000269|PubMed:35690592"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13834"
FT   MOD_RES         412
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:35690592,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         641
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:35690592,
FT                   ECO:0007744|PubMed:18669648"
FT   MOD_RES         645
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:35690592,
FT                   ECO:0007744|PubMed:18669648"
FT   MOD_RES         649
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         652
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:35690592"
FT   MOD_RES         653
FT                   /note="Phosphoserine; by GSK3-alpha and GSK3-beta"
FT                   /evidence="ECO:0000269|PubMed:35690592"
FT   MOD_RES         657
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000269|PubMed:35690592"
FT   MOD_RES         698
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13834"
FT   MOD_RES         700
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         710
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         721
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1E4"
FT   MOD_RES         727
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:35690592,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT   MOD_RES         731
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:35690592"
FT   VAR_SEQ         101..164
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_042745"
FT   VARIANT         108
FT                   /note="I -> M (in dbSNP:rs5455)"
FT                   /id="VAR_037958"
FT   VARIANT         130
FT                   /note="K -> E (in dbSNP:rs5456)"
FT                   /id="VAR_014727"
FT   VARIANT         283
FT                   /note="N -> S (in dbSNP:rs5461)"
FT                   /id="VAR_014728"
FT   VARIANT         359
FT                   /note="E -> G (in dbSNP:rs5465)"
FT                   /id="VAR_014729"
FT   VARIANT         416
FT                   /note="M -> V (in dbSNP:rs5447)"
FT                   /id="VAR_014730"
FT   VARIANT         464
FT                   /note="G -> S (in NIDDM; dbSNP:rs200862074)"
FT                   /evidence="ECO:0000269|PubMed:7657035"
FT                   /id="VAR_007859"
FT   VARIANT         619
FT                   /note="E -> Q (in dbSNP:rs5450)"
FT                   /id="VAR_014731"
FT   VARIANT         691
FT                   /note="P -> A (in dbSNP:rs5453)"
FT                   /id="VAR_014732"
FT   CONFLICT        136
FT                   /note="T -> I (in Ref. 1; AAA88046 and 3; AAB60385)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        462
FT                   /note="Missing (in Ref. 3; AAB60385)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        608
FT                   /note="A -> D (in Ref. 3; AAB60385)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        706
FT                   /note="S -> R (in Ref. 1; AAA88046 and 3; AAB60385)"
FT                   /evidence="ECO:0000305"
FT   TURN            16..21
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   STRAND          28..32
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   TURN            34..37
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   STRAND          40..42
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           43..58
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   STRAND          61..67
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           70..75
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   STRAND          77..79
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           85..96
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   STRAND          100..106
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   STRAND          108..110
FT                   /evidence="ECO:0007829|PDB:7Q0B"
FT   STRAND          113..118
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           120..125
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           126..137
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           146..167
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   TURN            169..171
FT                   /evidence="ECO:0007829|PDB:7Q13"
FT   STRAND          175..179
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           182..194
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   STRAND          197..206
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           208..216
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   TURN            218..226
FT                   /evidence="ECO:0007829|PDB:8CVX"
FT   HELIX           229..235
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           239..250
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   STRAND          253..259
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           260..269
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   STRAND          275..277
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           284..286
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           294..311
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   TURN            312..314
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   STRAND          323..331
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   TURN            334..338
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           339..355
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   STRAND          361..367
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   STRAND          372..375
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           377..409
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           416..419
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           422..435
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   STRAND          443..448
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   TURN            449..453
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           455..463
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   STRAND          472..477
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   STRAND          483..485
FT                   /evidence="ECO:0007829|PDB:8CVX"
FT   STRAND          487..490
FT                   /evidence="ECO:0007829|PDB:8CVX"
FT   HELIX           493..498
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   STRAND          501..504
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   STRAND          508..512
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           514..521
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   STRAND          526..529
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           533..541
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   STRAND          542..544
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           545..548
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   STRAND          550..553
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   STRAND          556..558
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           560..576
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           579..591
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           592..596
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   HELIX           598..616
FT                   /evidence="ECO:0007829|PDB:7ZBN"
FT   TURN            618..620
FT                   /evidence="ECO:0007829|PDB:7ZBN"
SQ   SEQUENCE   737 AA;  83786 MW;  0E321BBFDEB0BD7F CRC64;
     MPLNRTLSMS SLPGLEDWED EFDLENAVLF EVAWEVANKV GGIYTVLQTK AKVTGDEWGD
     NYFLVGPYTE QGVRTQVELL EAPTPALKRT LDSMNSKGCK VYFGRWLIEG GPLVVLLDVG
     ASAWALERWK GELWDTCNIG VPWYDREAND AVLFGFLTTW FLGEFLAQSE EKPHVVAHFH
     EWLAGVGLCL CRARRLPVAT IFTTHATLLG RYLCAGAVDF YNNLENFNVD KEAGERQIYH
     RYCMERAAAH CAHVFTTVSQ ITAIEAQHLL KRKPDIVTPN GLNVKKFSAM HEFQNLHAQS
     KARIQEFVRG HFYGHLDFNL DKTLYFFIAG RYEFSNKGAD VFLEALARLN YLLRVNGSEQ
     TVVAFFIMPA RTNNFNVETL KGQAVRKQLW DTANTVKEKF GRKLYESLLV GSLPDMNKML
     DKEDFTMMKR AIFATQRQSF PPVCTHNMLD DSSDPILTTI RRIGLFNSSA DRVKVIFHPE
     FLSSTSPLLP VDYEEFVRGC HLGVFPSYYE PWGYTPAECT VMGIPSISTN LSGFGCFMEE
     HIADPSAYGI YILDRRFRSL DDSCSQLTSF LYSFCQQSRR QRIIQRNRTE RLSDLLDWKY
     LGRYYMSARH MALSKAFPEH FTYEPNEADA AQGYRYPRPA SVPPSPSLSR HSSPHQSEDE
     EDPRNGPLEE DGERYDEDEE AAKDRRNIRA PEWPRRASCT SSTSGSKRNS VDTATSSSLS
     TPSEPLSPTS SLGEERN
//
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