GYS1_BOVIN
ID GYS1_BOVIN Reviewed; 736 AA.
AC A7MB78;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Glycogen [starch] synthase, muscle;
DE EC=2.4.1.11;
GN Name=GYS1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) 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; BC151381; AAI51382.1; -; mRNA.
DR RefSeq; NP_001094769.1; NM_001101299.1.
DR AlphaFoldDB; A7MB78; -.
DR SMR; A7MB78; -.
DR STRING; 9913.ENSBTAP00000007423; -.
DR CAZy; GT3; Glycosyltransferase Family 3.
DR PaxDb; A7MB78; -.
DR PRIDE; A7MB78; -.
DR Ensembl; ENSBTAT00000007423; ENSBTAP00000007423; ENSBTAG00000039958.
DR GeneID; 786335; -.
DR KEGG; bta:786335; -.
DR CTD; 2997; -.
DR VEuPathDB; HostDB:ENSBTAG00000039958; -.
DR VGNC; VGNC:29730; GYS1.
DR eggNOG; KOG3742; Eukaryota.
DR GeneTree; ENSGT00390000018612; -.
DR HOGENOM; CLU_015910_1_0_1; -.
DR InParanoid; A7MB78; -.
DR OMA; YFFTSGR; -.
DR OrthoDB; 264593at2759; -.
DR TreeFam; TF300306; -.
DR Reactome; R-BTA-3322077; Glycogen synthesis.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000039958; Expressed in infraspinatus muscle and 104 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016234; C:inclusion body; IEA:Ensembl.
DR GO; GO:0004373; F:glycogen (starch) synthase activity; ISS:UniProtKB.
DR GO; GO:0061547; F:glycogen synthase activity, transferring glucose-1-phosphate; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0005978; P:glycogen biosynthetic process; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
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..736
FT /note="Glycogen [starch] synthase, muscle"
FT /id="PRO_0000358311"
FT REGION 631..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..678
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..729
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 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 709
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13807"
FT MOD_RES 720
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1E4"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13807"
SQ SEQUENCE 736 AA; 83814 MW; 22300D8723EF94BD CRC64;
MPLNRTLSMS SLPGLEDWED EFDLENTVLF EVAWEVANKV GGIYTVLQTK AKVTGDEWGD
NYYLVGPYTE QGVRTQVELL EPPTPALKRT 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 VMGIPSVSTN LSGFGCFMEE
HIADPSAYGI YILDRRFRSL DDSCSQLTSF LYSFCQQSRR QRIIQRNRTE RLSDLLDWKY
LGRYYMSARH MALAKAFPEY FTYEPHEADA TQGYRYPRPA SVPPSPSLSR HSSPHQSEDE
EEPRDLPPDE DDERYDEDEE AAKDRRNIRA PEWPRRASCT SSTGSKRGSV DTAPSSSVST
PSEPLSPASS LGEERN
