GYS2_RAT
ID GYS2_RAT Reviewed; 704 AA.
AC P17625; Q99MF8;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Glycogen [starch] synthase, liver;
DE EC=2.4.1.11;
GN Name=Gys2;
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 [MRNA].
RC TISSUE=Liver;
RX PubMed=2110561; DOI=10.1016/s0021-9258(19)39007-6;
RA Bai G., Zhang Z., Werner R., Nuttall F.Q., Tan A.W.H., Lee E.Y.C.;
RT "The primary structure of rat liver glycogen synthase deduced by cDNA
RT cloning. Absence of phosphorylation sites 1a and 1b.";
RL J. Biol. Chem. 265:7843-7848(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Liver;
RA Ferrer J.C., Baque S., Guinovart J.J.;
RT "Glucose-regulated localization of liver glycogen synthase at the
RT hepatocyte periphery.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-11 AND SER-627, AND
RP IDENTIFICATION BY MASS 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.
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 (via C-terminus); required for GYS2-
CC mediated glycogen synthesis. {ECO:0000250|UniProtKB:Q8VCB3}.
CC -!- PTM: Primed phosphorylation at Ser-657 (site 5) by CSNK2A1 and CSNK2A2
CC is required for inhibitory phosphorylation at Ser-641 (site 3a), Ser-
CC 645 (site 3b), Ser-649 (site 3c) and Ser-653 (site 4) by GSK3A an
CC GSK3B. Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the
CC enzyme (By similarity). Phosphorylation at Ser-8 is not required for
CC interaction with GYG1 (By similarity). Interaction with GYG1 does not
CC regulate the phosphorylation at Ser-8 and Ser-641 (By similarity).
CC {ECO:0000250|UniProtKB:P13807, ECO:0000250|UniProtKB:P13834,
CC ECO:0000250|UniProtKB:Q8VCB3}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 3 family. {ECO:0000305}.
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DR EMBL; J05446; AAA41255.1; -; mRNA.
DR EMBL; AF346902; AAK16592.1; -; mRNA.
DR PIR; A35362; A35362.
DR AlphaFoldDB; P17625; -.
DR SMR; P17625; -.
DR IntAct; P17625; 1.
DR STRING; 10116.ENSRNOP00000059573; -.
DR CAZy; GT3; Glycosyltransferase Family 3.
DR iPTMnet; P17625; -.
DR PhosphoSitePlus; P17625; -.
DR PaxDb; P17625; -.
DR PRIDE; P17625; -.
DR UCSC; RGD:2773; rat.
DR RGD; 2773; Gys2.
DR eggNOG; KOG3742; Eukaryota.
DR InParanoid; P17625; -.
DR PhylomeDB; P17625; -.
DR UniPathway; UPA00164; -.
DR PRO; PR:P17625; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0043265; C:ectoplasm; IDA:UniProtKB.
DR GO; GO:0005536; F:glucose binding; IDA:RGD.
DR GO; GO:0004373; F:glycogen (starch) synthase activity; IDA:UniProtKB.
DR GO; GO:0005978; P:glycogen biosynthetic process; IDA:UniProtKB.
DR GO; GO:0005977; P:glycogen metabolic process; IDA:RGD.
DR GO; GO:0009749; P:response to glucose; IDA:UniProtKB.
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..704
FT /note="Glycogen [starch] synthase, liver"
FT /id="PRO_0000194769"
FT REGION 620..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..673
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..704
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 641
FT /note="Phosphoserine; by GSK3-alpha and GSK3-beta"
FT /evidence="ECO:0000250"
FT MOD_RES 645
FT /note="Phosphoserine; by GSK3-alpha and GSK3-beta"
FT /evidence="ECO:0000250"
FT MOD_RES 649
FT /note="Phosphoserine; by GSK3-alpha and GSK3-beta"
FT /evidence="ECO:0000250"
FT MOD_RES 653
FT /note="Phosphoserine; by GSK3-alpha and GSK3-beta"
FT /evidence="ECO:0000250"
FT MOD_RES 657
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54840"
FT CONFLICT 82
FT /note="E -> R (in Ref. 1; AAA41255)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="H -> D (in Ref. 1; AAA41255)"
FT /evidence="ECO:0000305"
FT CONFLICT 555..557
FT /note="RRF -> SV (in Ref. 1; AAA41255)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="H -> Y (in Ref. 1; AAA41255)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 704 AA; 80734 MW; 926BD3057470A1D4 CRC64;
MLRGRSLSVT SLGGLPAWEA ERLPVEDLLL FEVSWEVTNK VGGICTVIQS KAKTTANEWG
ENYFLIGPYF EHNVKTQVEP CEPANDAVRK AVDAMNKHGC QVHFGRWLIE GSPYVVLFDI
SSSVWNLDRW KGDFWEACGV GIPHDDREAN DMLIFGSLTA WFLKEVTDHA DGKHVIAQFH
EWQAGTGLIL SRARKLPIAT IFTTHATLLG RYLCAANIDF YNQLDKFNID KEAGERQIYH
RYCMERASVH CAHVFTTVSE ITAIEADHML KRKPDVVTPN GLNVKKFSAV HEFQNLHATY
KARIQDFVRG HFYGHLDFDL EKTLFLFIAG RYEFSNKGAD IFLESLSRLN FLLRMHKSNV
TVVVFFIMPA KTNNFNVETL KGQAVRKQLW DTVHCMKEKF GKKLYDGLLR GEIPDMNSIL
DRDDLTIMKR AIFSTQRHSL PPVTTHNMID DSTDPILSTI RRIGLFNNRT DRVKVILHPE
FLSSTSPLLP MDYEEFVRGC HLGVFPSYYE PWGYTPAECT VMGIPSVTTN LSGFGCFMQE
HVADPTAYGI YIVDRRFRSP DDSCNQLTQF LYGFCKQSRR QRIIQRNRTE RLSDLLDWRY
LGRYYQHARH LTLSRAFPDK FHLEPTSPPT TDGFKYPRPS SVPPSPSGSQ TSSPQSSDVE
NEGDEDERYD EEEEAERDRL NIKSPFSLNH IPKGKKKLHG EYKN
