GYS_DROME
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 03-AUG-2022, entry version 161.
DE RecName: Full=Glycogen [starch] synthase;
DE EC=2.4.1.11;
DE AltName: Full=Glycogen synthase;
GN Name=GlyS; ORFNames=CG6904;
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 -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
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; 17.
DR DIP; DIP-19447N; -.
DR IntAct; Q9VFC8; 7.
DR STRING; 7227.FBpp0082496; -.
DR CAZy; GT3; Glycosyltransferase Family 3.
DR iPTMnet; Q9VFC8; -.
DR PaxDb; Q9VFC8; -.
DR PRIDE; Q9VFC8; -.
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 CTD; 41823; -.
DR FlyBase; FBgn0266064; GlyS.
DR VEuPathDB; VectorBase:FBgn0266064; -.
DR eggNOG; KOG3742; Eukaryota.
DR GeneTree; ENSGT00390000018612; -.
DR InParanoid; Q9VFC8; -.
DR OMA; YFFTSGR; -.
DR PhylomeDB; Q9VFC8; -.
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 tissues.
DR ExpressionAtlas; Q9VFC8; baseline and differential.
DR Genevisible; Q9VFC8; DM.
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 InterPro; IPR008631; Glycogen_synth.
DR PANTHER; PTHR10176; PTHR10176; 1.
DR Pfam; PF05693; Glycogen_syn; 1.
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
