ID   GYS1_PONAB              Reviewed;         737 AA.
AC   Q5R9H0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   RecName: Full=Glycogen [starch] synthase, muscle;
DE            EC=2.4.1.11 {ECO:0000250|UniProtKB:P13807};
DE   AltName: Full=Glycogen synthase 1 {ECO:0000250|UniProtKB:P13807};
GN   Name=GYS1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P13807}.
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:0000250|UniProtKB:P13807};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18550;
CC         Evidence={ECO:0000250|UniProtKB:P13807};
CC   -!- ACTIVITY REGULATION: Allosteric activation by glucose-6-phosphate.
CC       Phosphorylation reduces the activity towards UDP-glucose. When in the
CC       non-phosphorylated state, glycogen synthase does not require glucose-6-
CC       phosphate as an allosteric activator; when phosphorylated it does (By
CC       similarity). {ECO:0000250|UniProtKB:P13834,
CC       ECO:0000250|UniProtKB:P54840}.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000250|UniProtKB:P13807}.
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:0000250|UniProtKB:P13807}.
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.
CC       Phosphorylated at Ser-641 by PASK, leading to inactivation;
CC       phosphorylation by PASK is inhibited by glycogen. Phosphorylated at
CC       Ser-641 by DYRK2, leading to inactivation. Dephosphorylation at Ser-641
CC       and Ser-645 by PP1 activates the enzyme (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 3 family. {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; CR859418; CAH91590.1; -; mRNA.
DR   RefSeq; NP_001125937.1; NM_001132465.1.
DR   AlphaFoldDB; Q5R9H0; -.
DR   SMR; Q5R9H0; -.
DR   STRING; 9601.ENSPPYP00000011436; -.
DR   CAZy; GT3; Glycosyltransferase Family 3.
DR   GeneID; 100172871; -.
DR   KEGG; pon:100172871; -.
DR   CTD; 2997; -.
DR   eggNOG; KOG3742; Eukaryota.
DR   InParanoid; Q5R9H0; -.
DR   OrthoDB; 9432at2759; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; ISS:UniProtKB.
DR   GO; GO:0005978; P:glycogen biosynthetic process; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Allosteric enzyme; Glycogen biosynthesis; Glycosyltransferase;
KW   Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..737
FT                   /note="Glycogen [starch] synthase, muscle"
FT                   /id="PRO_0000366919"
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:0000250|UniProtKB:P13807"
FT   BINDING         205
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P13807"
FT   BINDING         211
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P13807"
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:0000250|UniProtKB:P13807"
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:0000250|UniProtKB:P13807"
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:0000250|UniProtKB:P13807"
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:0000250|UniProtKB:P13807"
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:0000250|UniProtKB:P13807"
FT   BINDING         331
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:P13807"
FT   BINDING         331
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P13807"
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:0000250|UniProtKB:P13807"
FT   BINDING         510
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P13807"
FT   BINDING         512
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P13807"
FT   BINDING         513
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P13807"
FT   BINDING         515
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:P13807"
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:0000250|UniProtKB:P13807"
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:0000250|UniProtKB:P13807"
FT   MOD_RES         8
FT                   /note="Phosphoserine; by AMPK and PKA"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1E4"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13834"
FT   MOD_RES         412
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13807"
FT   MOD_RES         641
FT                   /note="Phosphoserine; by DYRK2, GSK3-alpha, GSK3-beta and
FT                   PASK"
FT                   /evidence="ECO:0000250|UniProtKB:P13834"
FT   MOD_RES         645
FT                   /note="Phosphoserine; by GSK3-alpha and GSK3-beta"
FT                   /evidence="ECO:0000250|UniProtKB:P13834"
FT   MOD_RES         649
FT                   /note="Phosphoserine; by GSK3-alpha and GSK3-beta"
FT                   /evidence="ECO:0000250|UniProtKB:P13834"
FT   MOD_RES         652
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A2RRU1"
FT   MOD_RES         653
FT                   /note="Phosphoserine; by GSK3-alpha and GSK3-beta"
FT                   /evidence="ECO:0000250|UniProtKB:P13834"
FT   MOD_RES         657
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250|UniProtKB:P13834"
FT   MOD_RES         698
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13834"
FT   MOD_RES         700
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P13807"
FT   MOD_RES         710
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13807"
FT   MOD_RES         721
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1E4"
FT   MOD_RES         727
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13807"
FT   MOD_RES         731
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13807"
SQ   SEQUENCE   737 AA;  83798 MW;  21F7CF6CB0D40A35 CRC64;
     MPLNRTLSMS SLPGLEDWED EFDLENAVLF EVAWEVANKV GGIYTVLQTK AKVTGDEWGA
     NYFLVGPYTE QGVRTQVELL EAPTPALKRT LDSMNSKGCK VYFGRWLIEG GPLVVLLDVG
     ASAWALERWK GELWDTCNIG VPWYDREAND AVLFGFLTTW FLGEFLAQSE EKLHVVAHFH
     EWLAGIGLCL CRARRLPVAT IFTTHATLLG RYLCAGAVDF YNNLENFNVD KEAGERQIYH
     RYCMERAAAH CAHVFTTVSQ ITAIEAQYLL 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
//