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Database: UniProt/SWISS-PROT
Entry: GYS1_RABIT
LinkDB: GYS1_RABIT
Original site: GYS1_RABIT 
ID   GYS1_RABIT              Reviewed;         735 AA.
AC   P13834; O18817;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   30-AUG-2017, entry version 119.
DE   RecName: Full=Glycogen [starch] synthase, muscle;
DE            EC=2.4.1.11;
GN   Name=GYS1; Synonyms=GYS;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white; TISSUE=Skeletal muscle;
RX   PubMed=2509275;
RA   Zhang W.M., Browner M.F., Fletterick R.J., DePaoli-Roach A.A.,
RA   Roach P.J.;
RT   "Primary structure of rabbit skeletal muscle glycogen synthase deduced
RT   from cDNA clones.";
RL   FASEB J. 3:2532-2536(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-30 AND 612-735.
RX   PubMed=3087361; DOI=10.1016/0006-291X(86)91244-1;
RA   Cohen P., Holmes C.F.B.;
RT   "Identification of the C-terminus of rabbit skeletal muscle glycogen
RT   synthase.";
RL   Biochem. Biophys. Res. Commun. 137:542-545(1986).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-30, AND PHOSPHORYLATION AT SER-8; SER-641;
RP   SER-645 AND SER-649.
RX   PubMed=6772446;
RA   Rylatt D.B., Aitken A., Bilham T., Condon G.D., Embi N., Cohen P.;
RT   "Glycogen synthase from rabbit skeletal muscle. Amino acid sequence at
RT   the sites phosphorylated by glycogen synthase kinase-3, and extension
RT   of the N-terminal sequence containing the site phosphorylated by
RT   phosphorylase kinase.";
RL   Eur. J. Biochem. 107:529-537(1980).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-16.
RX   PubMed=107043; DOI=10.1016/0014-5793(79)80153-2;
RA   Huang T.S., Krebs E.G.;
RT   "Effect of proteases on the structure and activity of rabbit skeletal
RT   muscle glycogen synthetase.";
RL   FEBS Lett. 98:66-70(1979).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-15; 639-662 AND 694-735, AND PHOSPHORYLATION AT
RP   SER-8; SER-11; SER-641; SER-645; SER-649; SER-653; SER-657 AND
RP   SER-698.
RX   PubMed=2842154; DOI=10.1111/j.1432-1033.1988.tb14222.x;
RA   Poulter L., Ang S.G., Gibson B.W., Williams D.H., Holmes C.F.,
RA   Caudwell F.B., Pitcher J., Cohen P.;
RT   "Analysis of the in vivo phosphorylation state of rabbit skeletal
RT   muscle glycogen synthase by fast-atom-bombardment mass spectrometry.";
RL   Eur. J. Biochem. 175:497-510(1988).
RN   [6]
RP   PROTEIN SEQUENCE OF 6-21; 31-44 AND 286-300.
RX   PubMed=3134350;
RA   Mahrenholz A.M., Wang Y.H., Roach P.J.;
RT   "Catalytic site of rabbit glycogen synthase isozymes. Identification
RT   of an active site lysine close to the amino terminus of the subunit.";
RL   J. Biol. Chem. 263:10561-10567(1988).
RN   [7]
RP   PROTEIN SEQUENCE OF 665-683.
RX   PubMed=2117608;
RA   Flotow H., Graves P.R., Wang A.Q., Fiol C.J., Roeske R.W., Roach P.J.;
RT   "Phosphate groups as substrate determinants for casein kinase I
RT   action.";
RL   J. Biol. Chem. 265:14264-14269(1990).
RN   [8]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=3928373; DOI=10.1111/j.1432-1033.1985.tb09066.x;
RA   Kuret J., Woodgett J.R., Cohen P.;
RT   "Multisite phosphorylation of glycogen synthase from rabbit skeletal
RT   muscle. Identification of the sites phosphorylated by casein kinase-
RT   I.";
RL   Eur. J. Biochem. 151:39-48(1985).
RN   [9]
RP   PROTEIN SEQUENCE OF 665-683.
RX   PubMed=3137939; DOI=10.1016/S0006-291X(88)81048-9;
RA   Mahrenholz A.M., Votaw P., Roach P.J., Depaoli-Roach A.A.,
RA   Zioncheck T.F., Harrison M.L., Geahlen R.L.;
RT   "Phosphorylation of glycogen synthase by a bovine thymus protein-
RT   tyrosine kinase, p40.";
RL   Biochem. Biophys. Res. Commun. 155:52-58(1988).
RN   [10]
RP   PHOSPHORYLATION AT SER-641; SER-645; SER-649; SER-653 AND SER-657.
RX   PubMed=2820993;
RA   Fiol C.J., Mahrenholz A.M., Wang Y., Roeske R.W., Roach P.J.;
RT   "Formation of protein kinase recognition sites by covalent
RT   modification of the substrate. Molecular mechanism for the synergistic
RT   action of casein kinase II and glycogen synthase kinase 3.";
RL   J. Biol. Chem. 262:14042-14048(1987).
RN   [11]
RP   FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT SER-641, ENZYME
RP   REGULATION, AND MUTAGENESIS OF SER-641.
RX   PubMed=14593110; DOI=10.1074/jbc.M301769200;
RA   Skurat A.V., Dietrich A.D.;
RT   "Phosphorylation of Ser640 in muscle glycogen synthase by DYRK family
RT   protein kinases.";
RL   J. Biol. Chem. 279:2490-2498(2004).
CC   -!- FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non-
CC       reducing end of alpha-1,4-glucan. {ECO:0000269|PubMed:14593110}.
CC   -!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose + ((1->4)-alpha-D-
CC       glucosyl)(n) = UDP + ((1->4)-alpha-D-glucosyl)(n+1).
CC       {ECO:0000269|PubMed:14593110}.
CC   -!- ENZYME REGULATION: Allosteric activation by glucose-6-phosphate.
CC       Phosphorylation reduces the activity towards UDP-glucose. When in
CC       the non-phosphorylated state, glycogen synthase does not require
CC       glucose-6-phosphate as an allosteric activator; when
CC       phosphorylated it does. {ECO:0000269|PubMed:14593110}.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC   -!- SUBUNIT: Interacts with GYG1. {ECO:0000250}.
CC   -!- PTM: Phosphorylation at Ser-8 is required for modification of Ser-
CC       11 by casein kinase I. {ECO:0000269|PubMed:2842154,
CC       ECO:0000269|PubMed:6772446}.
CC   -!- PTM: Phosphorylated at Ser-641 by PASK, leading to inactivation;
CC       phosphorylation by PASK is inhibited by glycogen.
CC       Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the
CC       enzyme (By similarity). Phosphorylation at Ser-8 by AMPK
CC       inactivates the enzyme activity (By similarity). Phosphorylated at
CC       Ser-641 by DYRK2, leading to inactivation. Primed phosphorylation
CC       at Ser-657 (site 5) by CSNK2A1 and CSNK2A2 is required for
CC       inhibitory phosphorylation at Ser-641 (site 3a), Ser-645 (site
CC       3b), Ser-649 (site 3c) and Ser-653 (site 4) by GSK3A and GSK3B.
CC       {ECO:0000250, ECO:0000269|PubMed:14593110,
CC       ECO:0000269|PubMed:2820993, ECO:0000269|PubMed:2842154,
CC       ECO:0000269|PubMed:6772446}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 3 family.
CC       {ECO:0000305}.
DR   EMBL; AF017114; AAB69872.1; -; mRNA.
DR   PIR; A33369; A33369.
DR   RefSeq; NP_001075492.1; NM_001082023.1.
DR   RefSeq; XP_017195288.1; XM_017339799.1.
DR   UniGene; Ocu.2171; -.
DR   ProteinModelPortal; P13834; -.
DR   SMR; P13834; -.
DR   IntAct; P13834; 4.
DR   MINT; MINT-8146730; -.
DR   STRING; 9986.ENSOCUP00000000015; -.
DR   CAZy; GT3; Glycosyltransferase Family 3.
DR   iPTMnet; P13834; -.
DR   GeneID; 100008660; -.
DR   KEGG; ocu:100008660; -.
DR   CTD; 2997; -.
DR   eggNOG; KOG3742; Eukaryota.
DR   eggNOG; COG0438; LUCA.
DR   HOGENOM; HOG000160890; -.
DR   HOVERGEN; HBG001960; -.
DR   InParanoid; P13834; -.
DR   KO; K00693; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0098723; C:skeletal muscle myofibril; IDA:CAFA.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; ISS:UniProtKB.
DR   GO; GO:0005978; P:glycogen biosynthetic process; ISS:UniProtKB.
DR   CDD; cd03793; GT1_Glycogen_synthase_GSY2_lik; 1.
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; Complete proteome; Direct protein sequencing;
KW   Glycogen biosynthesis; Glycosyltransferase; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:107043,
FT                                ECO:0000269|PubMed:2842154,
FT                                ECO:0000269|PubMed:3087361,
FT                                ECO:0000269|PubMed:6772446}.
FT   CHAIN         2    735       Glycogen [starch] synthase, muscle.
FT                                /FTId=PRO_0000194767.
FT   BINDING      39     39       UDP-glucose. {ECO:0000250}.
FT   MOD_RES       8      8       Phosphoserine; by AMPK and PKA.
FT                                {ECO:0000269|PubMed:2842154,
FT                                ECO:0000269|PubMed:6772446}.
FT   MOD_RES      11     11       Phosphoserine.
FT                                {ECO:0000269|PubMed:2842154,
FT                                ECO:0000269|PubMed:3928373}.
FT   MOD_RES     412    412       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P13807}.
FT   MOD_RES     641    641       Phosphoserine; by DYRK2, GSK3-alpha,
FT                                GSK3-beta and PASK.
FT                                {ECO:0000269|PubMed:14593110,
FT                                ECO:0000269|PubMed:2820993,
FT                                ECO:0000269|PubMed:2842154,
FT                                ECO:0000269|PubMed:6772446}.
FT   MOD_RES     645    645       Phosphoserine; by GSK3-alpha and GSK3-
FT                                beta. {ECO:0000269|PubMed:2820993,
FT                                ECO:0000269|PubMed:2842154,
FT                                ECO:0000269|PubMed:6772446}.
FT   MOD_RES     649    649       Phosphoserine; by GSK3-alpha and GSK3-
FT                                beta. {ECO:0000269|PubMed:2820993,
FT                                ECO:0000269|PubMed:2842154,
FT                                ECO:0000269|PubMed:6772446}.
FT   MOD_RES     652    652       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:A2RRU1}.
FT   MOD_RES     653    653       Phosphoserine; by GSK3-alpha and GSK3-
FT                                beta. {ECO:0000269|PubMed:2820993,
FT                                ECO:0000269|PubMed:2842154}.
FT   MOD_RES     657    657       Phosphoserine; by CK2.
FT                                {ECO:0000269|PubMed:2820993,
FT                                ECO:0000269|PubMed:2842154}.
FT   MOD_RES     698    698       Phosphoserine.
FT                                {ECO:0000269|PubMed:2842154,
FT                                ECO:0000269|PubMed:3928373}.
FT   MOD_RES     700    700       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P13807}.
FT   MOD_RES     709    709       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Z1E4}.
FT   MOD_RES     711    711       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P13807}.
FT   MOD_RES     719    719       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9Z1E4}.
FT   MOD_RES     725    725       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P13807}.
FT   MUTAGEN     641    641       S->A: Loss of an inhibitory
FT                                phosphorylation site. Abolishes
FT                                phosphorylation by DYRK2.
FT                                {ECO:0000269|PubMed:14593110}.
FT   CONFLICT    692    692       E -> Q (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    726    726       P -> S (in Ref. 2; AA sequence and 5; AA
FT                                sequence). {ECO:0000305}.
FT   CONFLICT    728    728       S -> P (in Ref. 2; AA sequence and 5; AA
FT                                sequence). {ECO:0000305}.
SQ   SEQUENCE   735 AA;  83601 MW;  53ABE9DBE769ADBC CRC64;
     MPLSRTLSVS SLPGLEDWED EFDLENSVLF EVAWEVANKV GGIYTVLQTK AKVTGDEWGD
     NYFLVGPYTE QGVRTQVELL EPPTPALKRT LDSMNSKGCK VYFGRWLIEG GPLVVLLDVG
     ASAWALERWK GELWDTCNIG VPWYDREAND AVLFGFLTTW FLGEFLAQNE EKPHVVAHFH
     EWLAGIGLCL 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 VMGIPSISTN LSGFGCFMEE
     HIADPSAYGI YILDRRFRSL DDSCSQLTSF LYSFCQQSRR QRIIQRNRTE RLSDLLDWKY
     LGRYYMSARH MALAKAFPDH FTYEPHEADA TQGYRYPRPA SVPPSPSLSR HSSPHQSEDE
     EEPRDGLPEE DGERYDEDEE AAKDRRNIRA PEWPRRASCT SSSGGSKRSN SVDTSSLSTP
     SEPLSPASSL GEERN
//
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