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Glycogen [starch] synthase (EC 2.4.1.11) (Glycogen synthase)

 GYS_DROME               Reviewed;         709 AA.
Q9VFC8; A4V2X5;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
10-MAY-2004, sequence version 2.
25-OCT-2017, entry version 137.
RecName: Full=Glycogen [starch] synthase;
EC=2.4.1.11;
AltName: Full=Glycogen synthase;
Name=GlyS; ORFNames=CG6904;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-660, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17372656; DOI=10.1039/b617545g;
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,
Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
"An integrated chemical, mass spectrometric and computational strategy
for (quantitative) phosphoproteomics: application to Drosophila
melanogaster Kc167 cells.";
Mol. Biosyst. 3:275-286(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-30; SER-660;
SER-667; SER-671; SER-675; SER-679; THR-682; THR-683; SER-687; SER-691
AND SER-696, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[6]
FUNCTION, INTERACTION WITH ATG8A, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND MUTAGENESIS OF ARG-613; TRP-629 AND SER-671.
PubMed=24265594; DOI=10.1371/journal.pbio.1001708;
Zirin J., Nieuwenhuis J., Perrimon N.;
"Role of autophagy in glycogen breakdown and its relevance to
chloroquine myopathy.";
PLoS Biol. 11:E1001708-E1001708(2013).
-!- FUNCTION: Transfers the glycosyl residue from UDPG to the non-
reducing end of alpha-1,4-glucan. In larval skeletal muscle,
isoform B is required for the formation of autophagosomes during
starvation and during cloroquine-induced vacuolar myopathy.
{ECO:0000269|PubMed:24265594}.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose + ((1->4)-alpha-D-
glucosyl)(n) = UDP + ((1->4)-alpha-D-glucosyl)(n+1).
-!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
-!- SUBUNIT: Isoform B interacts with Atg8a upon starvation.
{ECO:0000269|PubMed:24265594}.
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome
{ECO:0000269|PubMed:24265594}. Note=Isoform B colocalizes with
Atg8a at autophagosomes upon starvation in larval skeletal muscle.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A;
IsoId=Q9VFC8-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=B; Synonyms=C;
IsoId=Q9VFC8-2; Sequence=VSP_010302;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: In third instar larvae, isoform B is highly
expressed in skeletal muscle but not detected in fat body.
{ECO:0000269|PubMed:24265594}.
-!- SIMILARITY: Belongs to the glycosyltransferase 3 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AE014297; AAF55132.2; -; Genomic_DNA.
EMBL; AE014297; AAN13623.1; -; Genomic_DNA.
EMBL; AE014297; AAN13624.1; -; Genomic_DNA.
EMBL; AY052005; AAK93429.1; -; mRNA.
RefSeq; NP_001262583.1; NM_001275654.1. [Q9VFC8-2]
RefSeq; NP_650422.1; NM_142165.3. [Q9VFC8-2]
RefSeq; NP_731967.2; NM_169610.2. [Q9VFC8-1]
RefSeq; NP_731968.1; NM_169611.2. [Q9VFC8-2]
UniGene; Dm.4414; -.
ProteinModelPortal; Q9VFC8; -.
SMR; Q9VFC8; -.
BioGrid; 66888; 17.
DIP; DIP-19447N; -.
IntAct; Q9VFC8; 6.
MINT; MINT-332090; -.
STRING; 7227.FBpp0082496; -.
CAZy; GT3; Glycosyltransferase Family 3.
iPTMnet; Q9VFC8; -.
PaxDb; Q9VFC8; -.
PRIDE; Q9VFC8; -.
EnsemblMetazoa; FBtr0083035; FBpp0082494; FBgn0266064. [Q9VFC8-2]
EnsemblMetazoa; FBtr0083036; FBpp0082495; FBgn0266064. [Q9VFC8-2]
EnsemblMetazoa; FBtr0083037; FBpp0082496; FBgn0266064. [Q9VFC8-1]
EnsemblMetazoa; FBtr0333276; FBpp0305474; FBgn0266064. [Q9VFC8-2]
GeneID; 41823; -.
KEGG; dme:Dmel_CG6904; -.
UCSC; CG6904-RC; d. melanogaster.
CTD; 41823; -.
FlyBase; FBgn0266064; GlyS.
eggNOG; KOG3742; Eukaryota.
eggNOG; COG0438; LUCA.
GeneTree; ENSGT00390000018612; -.
InParanoid; Q9VFC8; -.
KO; K00693; -.
OMA; KVYFGRW; -.
OrthoDB; EOG091G0304; -.
PhylomeDB; Q9VFC8; -.
Reactome; R-DME-3322077; Glycogen synthesis.
UniPathway; UPA00164; -.
GenomeRNAi; 41823; -.
PRO; PR:Q9VFC8; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0266064; -.
ExpressionAtlas; Q9VFC8; differential.
Genevisible; Q9VFC8; DM.
GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0004373; F:glycogen (starch) synthase activity; IDA:FlyBase.
GO; GO:0009267; P:cellular response to starvation; IMP:FlyBase.
GO; GO:0071329; P:cellular response to sucrose stimulus; IDA:FlyBase.
GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0005977; P:glycogen metabolic process; IMP:FlyBase.
GO; GO:0061723; P:glycophagy; IMP:FlyBase.
GO; GO:0045819; P:positive regulation of glycogen catabolic process; IMP:FlyBase.
GO; GO:0009744; P:response to sucrose; IMP:FlyBase.
CDD; cd03793; GT1_Glycogen_synthase_GSY2_lik; 1.
InterPro; IPR008631; Glycogen_synth.
PANTHER; PTHR10176; PTHR10176; 1.
Pfam; PF05693; Glycogen_syn; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasmic vesicle;
Glycogen biosynthesis; Glycosyltransferase; Phosphoprotein;
Reference proteome; Transferase.
CHAIN 1 709 Glycogen [starch] synthase.
/FTId=PRO_0000194771.
BINDING 61 61 UDP-glucose. {ECO:0000250}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 30 30 Phosphoserine.
{ECO:0000269|PubMed:17372656,
ECO:0000269|PubMed:18327897}.
MOD_RES 660 660 Phosphoserine.
{ECO:0000269|PubMed:17372656,
ECO:0000269|PubMed:18327897}.
MOD_RES 667 667 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 671 671 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 675 675 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 679 679 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 682 682 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 683 683 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 687 687 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 691 691 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 696 696 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
VAR_SEQ 1 20 Missing (in isoform B).
{ECO:0000303|PubMed:12537569}.
/FTId=VSP_010302.
MUTAGEN 613 613 R->A: Abolishes interaction with Atg8a.
{ECO:0000269|PubMed:24265594}.
MUTAGEN 629 629 W->A: Abolishes interaction with Atg8a.
{ECO:0000269|PubMed:24265594}.
MUTAGEN 671 671 S->A: Does not affect interaction with
Atg8a. {ECO:0000269|PubMed:24265594}.
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


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