ID   GYS1_MACMU              Reviewed;         737 AA.
AC   Q8MJ26;
DT   27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Glycogen [starch] synthase, muscle;
DE            EC=2.4.1.11;
GN   Name=GYS1; Synonyms=GYS;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skeletal muscle;
RA   Ortmeyer H.K., Marciani K.R., Hansen B.C.;
RT   "Monkey skeletal muscle glycogen synthase sequence.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non-
CC       reducing end of alpha-1,4-glucan. {ECO:0000250}.
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   -!- 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}.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC   -!- SUBUNIT: Interacts with GYG1. {ECO:0000250}.
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}.
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DR   EMBL; AF529178; AAM93267.1; -; mRNA.
DR   RefSeq; NP_001028058.1; NM_001032886.1.
DR   AlphaFoldDB; Q8MJ26; -.
DR   SMR; Q8MJ26; -.
DR   STRING; 9544.ENSMMUP00000005219; -.
DR   CAZy; GT3; Glycosyltransferase Family 3.
DR   GeneID; 574233; -.
DR   KEGG; mcc:574233; -.
DR   CTD; 2997; -.
DR   eggNOG; KOG3742; Eukaryota.
DR   InParanoid; Q8MJ26; -.
DR   OrthoDB; 264593at2759; -.
DR   BRENDA; 2.4.1.11; 3126.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; ISS:UniProtKB.
DR   GO; GO:0005978; P:glycogen biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR008631; Glycogen_synth.
DR   PANTHER; PTHR10176; PTHR10176; 1.
DR   Pfam; PF05693; Glycogen_syn; 1.
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_0000194764"
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-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
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         672
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1E4"
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"
SQ   SEQUENCE   737 AA;  83787 MW;  B8B0B3114C58F56C CRC64;
     MPLNRTLSMS SLPGLEDWED EFDLENTVLF EVAWEVANKV GGIYTVLQTK AKVTGDEWGD
     NYYLVGPYTE QGVRTQVELL EAPTPALKKT LDSMNSKGCK VYFGRWLIEG GPLVVLLDVG
     ASAWALERWK GELWDTCNIG VPWYDREAND AVLFGFLTTW FLGEFLAQSE EKPHVVAHFH
     EWLAGIGLCL CRARRLPVAT IFTTHATLLG RYLCAGAVDF YNNLENFNVD KEAGERQIYH
     RYCMERAAAH CAHVFTTVSQ ITAIEAQHLL KRKPDIVTPN GLNVKKFSAM HEFQNLHAQS
     KARIQEFVRG HFYGHLDFNL DKTLYFFIAG RYEFSNKGAD VFLEALARLN YLLRVNGSEQ
     TVVALFIMPA 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 FTYEPSEADA AQGYRYPRPA SVPPSPSLSR HSSPHQSEDE
     EDPRNGPLEE DSERYDEDEE AAKDRRNIRA PEWPRRASCT SSTSGSKRNS VDTATSSSLS
     TPSEPLSPTS SLGEERN