ID   GYS_DROME               Reviewed;         709 AA.
AC   Q9VFC8; A4V2X5;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   24-JAN-2024, entry version 168.
DE   RecName: Full=Glycogen [starch] synthase;
DE            EC=2.4.1.11 {ECO:0000250|UniProtKB:Q9U2D9};
DE   AltName: Full=Glycogen synthase {ECO:0000303|PubMed:24265594};
GN   Name=Glys {ECO:0000303|PubMed:24265594,
GN   ECO:0000312|FlyBase:FBgn0266064};
GN   ORFNames=CG6904 {ECO:0000312|FlyBase:FBgn0266064};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-660, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17372656; DOI=10.1039/b617545g;
RA   Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA   Eng J.K., Aebersold R., Tao W.A.;
RT   "An integrated chemical, mass spectrometric and computational strategy for
RT   (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT   Kc167 cells.";
RL   Mol. Biosyst. 3:275-286(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-30; SER-660; SER-667;
RP   SER-671; SER-675; SER-679; THR-682; THR-683; SER-687; SER-691 AND SER-696,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
RN   [6]
RP   FUNCTION, INTERACTION WITH ATG8A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND MUTAGENESIS OF ARG-613; TRP-629 AND SER-671.
RX   PubMed=24265594; DOI=10.1371/journal.pbio.1001708;
RA   Zirin J., Nieuwenhuis J., Perrimon N.;
RT   "Role of autophagy in glycogen breakdown and its relevance to chloroquine
RT   myopathy.";
RL   PLoS Biol. 11:E1001708-E1001708(2013).
CC   -!- FUNCTION: Transfers the glycosyl residue from UDPG to the non-reducing
CC       end of alpha-1,4-glucan. In larval skeletal muscle, isoform B is
CC       required for the formation of autophagosomes during starvation and
CC       during cloroquine-induced vacuolar myopathy.
CC       {ECO:0000269|PubMed:24265594}.
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         Evidence={ECO:0000250|UniProtKB:Q9U2D9};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18550;
CC         Evidence={ECO:0000250|UniProtKB:Q9U2D9};
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000250|UniProtKB:Q9U2D9}.
CC   -!- SUBUNIT: Isoform B interacts with Atg8a upon starvation.
CC       {ECO:0000269|PubMed:24265594}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome
CC       {ECO:0000269|PubMed:24265594}. Note=Isoform B colocalizes with Atg8a at
CC       autophagosomes upon starvation in larval skeletal muscle.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=Q9VFC8-1; Sequence=Displayed;
CC       Name=B; Synonyms=C;
CC         IsoId=Q9VFC8-2; Sequence=VSP_010302;
CC   -!- TISSUE SPECIFICITY: In third instar larvae, isoform B is highly
CC       expressed in skeletal muscle but not detected in fat body.
CC       {ECO:0000269|PubMed:24265594}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 3 family. {ECO:0000305}.
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DR   EMBL; AE014297; AAF55132.2; -; Genomic_DNA.
DR   EMBL; AE014297; AAN13623.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAN13624.1; -; Genomic_DNA.
DR   EMBL; AY052005; AAK93429.1; -; mRNA.
DR   RefSeq; NP_001262583.1; NM_001275654.1. [Q9VFC8-2]
DR   RefSeq; NP_650422.1; NM_142165.3. [Q9VFC8-2]
DR   RefSeq; NP_731967.2; NM_169610.2. [Q9VFC8-1]
DR   RefSeq; NP_731968.1; NM_169611.2. [Q9VFC8-2]
DR   AlphaFoldDB; Q9VFC8; -.
DR   SMR; Q9VFC8; -.
DR   BioGRID; 66888; 19.
DR   DIP; DIP-19447N; -.
DR   IntAct; Q9VFC8; 7.
DR   STRING; 7227.FBpp0082496; -.
DR   CAZy; GT3; Glycosyltransferase Family 3.
DR   iPTMnet; Q9VFC8; -.
DR   PaxDb; 7227-FBpp0082496; -.
DR   DNASU; 41823; -.
DR   EnsemblMetazoa; FBtr0083035; FBpp0082494; FBgn0266064. [Q9VFC8-2]
DR   EnsemblMetazoa; FBtr0083036; FBpp0082495; FBgn0266064. [Q9VFC8-2]
DR   EnsemblMetazoa; FBtr0083037; FBpp0082496; FBgn0266064. [Q9VFC8-1]
DR   EnsemblMetazoa; FBtr0333276; FBpp0305474; FBgn0266064. [Q9VFC8-2]
DR   GeneID; 41823; -.
DR   KEGG; dme:Dmel_CG6904; -.
DR   UCSC; CG6904-RC; d. melanogaster.
DR   AGR; FB:FBgn0266064; -.
DR   CTD; 41823; -.
DR   FlyBase; FBgn0266064; Glys.
DR   VEuPathDB; VectorBase:FBgn0266064; -.
DR   eggNOG; KOG3742; Eukaryota.
DR   GeneTree; ENSGT00390000018612; -.
DR   InParanoid; Q9VFC8; -.
DR   OMA; RDVRNHI; -.
DR   OrthoDB; 9432at2759; -.
DR   PhylomeDB; Q9VFC8; -.
DR   Reactome; R-DME-3322077; Glycogen synthesis.
DR   UniPathway; UPA00164; -.
DR   BioGRID-ORCS; 41823; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 41823; -.
DR   PRO; PR:Q9VFC8; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0266064; Expressed in capitellum (Drosophila) and 49 other cell types or tissues.
DR   ExpressionAtlas; Q9VFC8; baseline and differential.
DR   GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IDA:FlyBase.
DR   GO; GO:0009267; P:cellular response to starvation; IMP:FlyBase.
DR   GO; GO:0071329; P:cellular response to sucrose stimulus; IDA:FlyBase.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IMP:FlyBase.
DR   GO; GO:0005977; P:glycogen metabolic process; IMP:FlyBase.
DR   GO; GO:0061723; P:glycophagy; IMP:FlyBase.
DR   GO; GO:0045819; P:positive regulation of glycogen catabolic process; IMP:FlyBase.
DR   GO; GO:0009744; P:response to sucrose; IMP:FlyBase.
DR   CDD; cd03793; GT3_GSY2-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR008631; Glycogen_synth.
DR   PANTHER; PTHR10176:SF3; GLYCOGEN [STARCH] SYNTHASE; 1.
DR   PANTHER; PTHR10176; GLYCOGEN SYNTHASE; 1.
DR   Pfam; PF05693; Glycogen_syn; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 2.
DR   Genevisible; Q9VFC8; DM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasmic vesicle; Glycogen biosynthesis;
KW   Glycosyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..709
FT                   /note="Glycogen [starch] synthase"
FT                   /id="PRO_0000194771"
FT   REGION          666..709
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        666..686
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         61
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         26
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17372656,
FT                   ECO:0000269|PubMed:18327897"
FT   MOD_RES         660
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17372656,
FT                   ECO:0000269|PubMed:18327897"
FT   MOD_RES         667
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         671
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         675
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         679
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         682
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         683
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         687
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         691
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         696
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   VAR_SEQ         1..20
FT                   /note="Missing (in isoform B)"
FT                   /evidence="ECO:0000303|PubMed:12537569"
FT                   /id="VSP_010302"
FT   MUTAGEN         613
FT                   /note="R->A: Abolishes interaction with Atg8a."
FT                   /evidence="ECO:0000269|PubMed:24265594"
FT   MUTAGEN         629
FT                   /note="W->A: Abolishes interaction with Atg8a."
FT                   /evidence="ECO:0000269|PubMed:24265594"
FT   MUTAGEN         671
FT                   /note="S->A: Does not affect interaction with Atg8a."
FT                   /evidence="ECO:0000269|PubMed:24265594"
SQ   SEQUENCE   709 AA;  81754 MW;  23E6381BC900CE54 CRC64;
     MRRQQSYRFE DNESTSYALR MNRRFSRVES GADLKDYFDR GDIASRENRW NFEVAWEVAN
     KVGGIYTVIR SKAYVSTEEM GEQLCMMGPY KEHCARTEME EMEFPRGNPL LDAVNSLRSR
     GYKIHTGRWL VDGNPQLILF DIGSAAWKLD QFKSEMWEKC HIGIPHLDIE TNDAIILGFM
     IAEFLEEFRN FAVTYSQNNE LSAPRIVAHF HEWQAGVGLI VLRTRLVEIA TVFTTHATLL
     GRYLCAGNTD FYNNLDKFAV DEEAGKRQIY HRYCLERGAT HLAHVFTTVS EITGYEAEHL
     LKRKPDIITP NGLNVKKFSA IHEFQNLHAV AKEKINEFVR GHFYGHIDFD LDKTLYFFIA
     GRYEFGNKGA DIFIEALARL NAMLKHEKPD TTVVAFLIFP TKTNNFNVDS LRGHAVIKQL
     RDTINNVQQA VGKRMFDTCL QGNIPNADDL LQKDDLVKIK RCMFAMQRDS MPPVTTHNVA
     DDWNDPVLSS IRRCHLFNSR HDRVKMVFHP EFLTSTNPLF GIDYEEFVRG CHLGVFPSYY
     EPWGYTPAEC TVMGIPSVTT NLSGFGCFME EHISDPKSYG IYIVDRRYIG LENSVQQLSS
     FMMEFSRLNR RQRIIQRNRT ERLSDLLDWR TLGIYYRQAR VKALQAVYPD YVDELSLYGS
     KNNLIFSRPH SEPPSPTSSR HTTPAPSVHG SDDEDSVDEE TELKELGIK
//