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Database: UniProt/SWISS-PROT
Entry: GYS1_RAT
LinkDB: GYS1_RAT
Original site: 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   12-SEP-2018, entry version 87.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   project: 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
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat 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: UDP-alpha-D-glucose + ((1->4)-alpha-D-
CC       glucosyl)(n) = UDP + ((1->4)-alpha-D-glucosyl)(n+1).
CC   -!- ACTIVITY 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 (By 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
CC       activity. Primed phosphorylation at Ser-657 (site 5) by CSNK2A1
CC       and CSNK2A2 is required for inhibitory phosphorylation at Ser-641
CC       (site 3a), Ser-645 (site 3b), Ser-649 (site 3c) and Ser-653 (site
CC       4) by GSK3A an GSK3B. Phosphorylated at Ser-641 by PASK, leading
CC       to inactivation; phosphorylation by PASK is inhibited by glycogen.
CC       Phosphorylated at Ser-641 by DYRK2, leading to inactivation.
CC       Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the
CC       enzyme (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 3 family.
CC       {ECO:0000305}.
DR   EMBL; BC131849; AAI31850.1; -; mRNA.
DR   RefSeq; NP_001103085.1; NM_001109615.1.
DR   UniGene; Rn.95278; -.
DR   ProteinModelPortal; A2RRU1; -.
DR   SMR; A2RRU1; -.
DR   BioGrid; 605796; 2.
DR   STRING; 10116.ENSRNOP00000028271; -.
DR   CAZy; GT3; Glycosyltransferase Family 3.
DR   iPTMnet; A2RRU1; -.
DR   PhosphoSitePlus; 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   eggNOG; COG0438; LUCA.
DR   GeneTree; ENSGT00390000018612; -.
DR   HOGENOM; HOG000160890; -.
DR   HOVERGEN; HBG001960; -.
DR   InParanoid; A2RRU1; -.
DR   KO; K00693; -.
DR   OMA; KVYFGRW; -.
DR   OrthoDB; EOG091G0304; -.
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 10 organ(s), highest expression level in skeletal muscle tissue.
DR   Genevisible; A2RRU1; RN.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0016234; C:inclusion body; IEA:Ensembl.
DR   GO; GO:0005536; F:glucose binding; IDA:RGD.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IDA:RGD.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
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; IEA:Ensembl.
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; Glycogen biosynthesis;
KW   Glycosyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN         1    738       Glycogen [starch] synthase, muscle.
FT                                /FTId=PRO_0000366920.
FT   BINDING      39     39       UDP-glucose. {ECO:0000250}.
FT   MOD_RES       8      8       Phosphoserine; by AMPK and PKA.
FT                                {ECO:0000250|UniProtKB:Q9Z1E4}.
FT   MOD_RES      11     11       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P13834}.
FT   MOD_RES     412    412       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     641    641       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     645    645       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     649    649       Phosphoserine; by GSK3-alpha and GSK3-
FT                                beta. {ECO:0000250|UniProtKB:P13834}.
FT   MOD_RES     652    652       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     653    653       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     657    657       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     672    672       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     698    698       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P13834}.
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     722    722       Phosphothreonine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     728    728       Phosphoserine.
FT                                {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
//
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