GYS1_RAT
ID GYS1_RAT Reviewed; 738 AA.
AC A2RRU1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Glycogen [starch] synthase, muscle;
DE EC=2.4.1.11;
GN Name=Gys1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412; SER-641; SER-645;
RP SER-652; SER-653; SER-657; SER-672 AND THR-722, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; BC131849; AAI31850.1; -; mRNA.
DR RefSeq; NP_001103085.1; NM_001109615.1.
DR AlphaFoldDB; A2RRU1; -.
DR SMR; A2RRU1; -.
DR BioGRID; 605796; 3.
DR IntAct; A2RRU1; 2.
DR STRING; 10116.ENSRNOP00000028271; -.
DR ChEMBL; CHEMBL4523104; -.
DR CAZy; GT3; Glycosyltransferase Family 3.
DR iPTMnet; A2RRU1; -.
DR PhosphoSitePlus; A2RRU1; -.
DR jPOST; A2RRU1; -.
DR PaxDb; A2RRU1; -.
DR PeptideAtlas; A2RRU1; -.
DR PRIDE; A2RRU1; -.
DR Ensembl; ENSRNOT00000028271; ENSRNOP00000028271; ENSRNOG00000020812.
DR GeneID; 690987; -.
DR KEGG; rno:690987; -.
DR UCSC; RGD:1589798; rat.
DR CTD; 2997; -.
DR RGD; 1589798; Gys1.
DR eggNOG; KOG3742; Eukaryota.
DR GeneTree; ENSGT00390000018612; -.
DR HOGENOM; CLU_015910_1_0_1; -.
DR InParanoid; A2RRU1; -.
DR OMA; YFFTSGR; -.
DR OrthoDB; 264593at2759; -.
DR PhylomeDB; A2RRU1; -.
DR TreeFam; TF300306; -.
DR Reactome; R-RNO-3322077; Glycogen synthesis.
DR UniPathway; UPA00164; -.
DR PRO; PR:A2RRU1; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020812; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; A2RRU1; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016234; C:inclusion body; ISO:RGD.
DR GO; GO:0005536; F:glucose binding; IDA:RGD.
DR GO; GO:0004373; F:glycogen (starch) synthase activity; IDA:RGD.
DR GO; GO:0061547; F:glycogen synthase activity, transferring glucose-1-phosphate; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0005978; P:glycogen biosynthetic process; IDA:RGD.
DR GO; GO:0005977; P:glycogen metabolic process; IDA:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR InterPro; IPR008631; Glycogen_synth.
DR PANTHER; PTHR10176; PTHR10176; 1.
DR Pfam; PF05693; Glycogen_syn; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Glycogen biosynthesis; Glycosyltransferase;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..738
FT /note="Glycogen [starch] synthase, muscle"
FT /id="PRO_0000366920"
FT REGION 632..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..738
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:0007744|PubMed:22673903"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13834"
FT MOD_RES 709
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1E4"
FT MOD_RES 711
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13807"
FT MOD_RES 722
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13807"
SQ SEQUENCE 738 AA; 84072 MW; 912823E398F5263C CRC64;
MPLSRSLSMS SLPGLEDWED EFDPENAVLF EVAWEVANKV GGIYTVLQTK AKVTGDEWGD
NYYLVGPYTE QGVRTQVELL EPPTPELKRT LDSMNSKGCK VYFGRWLIEG GPLVVLLDVG
ASAWALERWK GELWDTCNIG VPWYDREAND AVLFGFLTTW FLGEFLAQNE EKPYVVAHFH
EWLAGVGLCL CRARRLPVAT IFTTHATLLG RYLCAGAVDF YNNLENFNVD KEAGERQIYH
RYCMERAAAH CAHVFTTVSQ ITAIEAQHLL KRKPDIVTPN GLNVKKFSAM HEFQNLHAQS
KARIQEFVRG HFYGHLDFNL DKTLYFFIAG RYEFSNKGAD IFLEALARLN 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 MALAKAFPDH FTYEPHEVDA TQGYRYPRPA SVPPSPSLSR HSSPHQSEDE
EEPRDGPLRE DSERYDEEEE AAKDRRNIRA PEWPRRASCS SSTGGSKRSN SVDTGPSSSL
STPTEPLSPT SSLGEERN
