GYS_CAEEL
ID GYS_CAEEL Reviewed; 672 AA.
AC Q9U2D9;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Glycogen [starch] synthase;
DE Short=GS {ECO:0000303|PubMed:24982189};
DE EC=2.4.1.11 {ECO:0000269|PubMed:24982189};
GN Name=gsy-1 {ECO:0000312|WormBase:Y46G5A.31};
GN ORFNames=Y46G5A.31 {ECO:0000312|WormBase:Y46G5A.31};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=26439621; DOI=10.1371/journal.pgen.1005520;
RA Possik E., Ajisebutu A., Manteghi S., Gingras M.C., Vijayaraghavan T.,
RA Flamand M., Coull B., Schmeisser K., Duchaine T., van Steensel M.,
RA Hall D.H., Pause A.;
RT "FLCN and AMPK Confer Resistance to Hyperosmotic Stress via Remodeling of
RT Glycogen Stores.";
RL PLoS Genet. 11:E1005520-E1005520(2015).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH GYG-1, PATHWAY,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF PHE-151; GLY-157; TYR-257 AND CYS-261.
RX PubMed=24982189; DOI=10.1073/pnas.1402926111;
RA Zeqiraj E., Tang X., Hunter R.W., Garcia-Rocha M., Judd A., Deak M.,
RA von Wilamowitz-Moellendorff A., Kurinov I., Guinovart J.J., Tyers M.,
RA Sakamoto K., Sicheri F.;
RT "Structural basis for the recruitment of glycogen synthase by glycogenin.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E2831-2840(2014).
CC -!- FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non-
CC reducing end of alpha-1,4-glucan. {ECO:0000269|PubMed:24982189}.
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:0000269|PubMed:24982189};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.9 mM for UDP-glucose (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:24982189};
CC Vmax=126 pmol/min/ug enzyme {ECO:0000269|PubMed:24982189};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000269|PubMed:24982189}.
CC -!- SUBUNIT: Forms a hetero-octamer with each protomer of the gsy-1
CC homotetramer bound to one molecule of gyg-1. The N-terminus is involved
CC in interprotomer contacts with gyg-1. The interaction with gyg-1 is
CC required for glycogen production but is not required for gsy-1
CC intrinsic activity. {ECO:0000269|PubMed:24982189}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in reduced
CC survival. {ECO:0000269|PubMed:26439621}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 3 family. {ECO:0000305}.
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DR EMBL; AL110485; CAB60373.1; -; Genomic_DNA.
DR RefSeq; NP_496736.1; NM_064335.5.
DR PDB; 4QLB; X-ray; 2.60 A; A/B/C/D=1-672.
DR PDBsum; 4QLB; -.
DR AlphaFoldDB; Q9U2D9; -.
DR SMR; Q9U2D9; -.
DR BioGRID; 40222; 23.
DR ComplexPortal; CPX-3523; Glycogen synthase-Glycogenin complex.
DR DIP; DIP-26557N; -.
DR IntAct; Q9U2D9; 15.
DR STRING; 6239.Y46G5A.31; -.
DR CAZy; GT3; Glycosyltransferase Family 3.
DR iPTMnet; Q9U2D9; -.
DR EPD; Q9U2D9; -.
DR PaxDb; Q9U2D9; -.
DR PeptideAtlas; Q9U2D9; -.
DR EnsemblMetazoa; Y46G5A.31.1; Y46G5A.31.1; WBGene00001793.
DR GeneID; 174924; -.
DR KEGG; cel:CELE_Y46G5A.31; -.
DR UCSC; Y46G5A.31; c. elegans.
DR CTD; 174924; -.
DR WormBase; Y46G5A.31; CE24302; WBGene00001793; gsy-1.
DR eggNOG; KOG3742; Eukaryota.
DR GeneTree; ENSGT00390000018612; -.
DR HOGENOM; CLU_015910_1_0_1; -.
DR InParanoid; Q9U2D9; -.
DR OMA; YFFTSGR; -.
DR OrthoDB; 264593at2759; -.
DR PhylomeDB; Q9U2D9; -.
DR Reactome; R-CEL-3322077; Glycogen synthesis.
DR SignaLink; Q9U2D9; -.
DR UniPathway; UPA00164; -.
DR PRO; PR:Q9U2D9; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001793; Expressed in larva and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0004373; F:glycogen (starch) synthase activity; IBA:GO_Central.
DR GO; GO:0005978; P:glycogen biosynthetic process; IDA:ComplexPortal.
DR InterPro; IPR008631; Glycogen_synth.
DR PANTHER; PTHR10176; PTHR10176; 1.
DR Pfam; PF05693; Glycogen_syn; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycogen biosynthesis; Glycosyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..672
FT /note="Glycogen [starch] synthase"
FT /id="PRO_0000194770"
FT REGION 645..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 56
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT MUTAGEN 151
FT /note="F->A: Partially inhibits the interaction with gyg-1.
FT Loss of function."
FT /evidence="ECO:0000269|PubMed:24982189"
FT MUTAGEN 151
FT /note="F->R: Partially inhibits the interaction with gyg-1.
FT Loss of function."
FT /evidence="ECO:0000269|PubMed:24982189"
FT MUTAGEN 157
FT /note="G->R: Partially inhibits the interaction with gyg-1.
FT Loss of function."
FT /evidence="ECO:0000269|PubMed:24982189"
FT MUTAGEN 257
FT /note="Y->A: Complete inhibition of the interaction with
FT gyg-1. Loss of function."
FT /evidence="ECO:0000269|PubMed:24982189"
FT MUTAGEN 261
FT /note="C->A: Slight reduction in the interaction with gyg-
FT 1. Partial loss of function in absence of glycogen
FT branching enzyme."
FT /evidence="ECO:0000269|PubMed:24982189"
FT MUTAGEN 261
FT /note="C->R: Complete inhibition of the interaction with
FT gyg-1. Loss of function."
FT /evidence="ECO:0000269|PubMed:24982189"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 13..21
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:4QLB"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:4QLB"
FT TURN 51..54
FT /evidence="ECO:0007829|PDB:4QLB"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 60..75
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:4QLB"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:4QLB"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:4QLB"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:4QLB"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 143..153
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 163..184
FT /evidence="ECO:0007829|PDB:4QLB"
FT STRAND 192..199
FT /evidence="ECO:0007829|PDB:4QLB"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:4QLB"
FT STRAND 215..224
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 226..233
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 257..269
FT /evidence="ECO:0007829|PDB:4QLB"
FT STRAND 270..277
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 278..287
FT /evidence="ECO:0007829|PDB:4QLB"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:4QLB"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 311..329
FT /evidence="ECO:0007829|PDB:4QLB"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:4QLB"
FT STRAND 341..350
FT /evidence="ECO:0007829|PDB:4QLB"
FT TURN 352..356
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 357..373
FT /evidence="ECO:0007829|PDB:4QLB"
FT TURN 377..381
FT /evidence="ECO:0007829|PDB:4QLB"
FT STRAND 383..389
FT /evidence="ECO:0007829|PDB:4QLB"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 399..430
FT /evidence="ECO:0007829|PDB:4QLB"
FT TURN 431..433
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 444..455
FT /evidence="ECO:0007829|PDB:4QLB"
FT STRAND 465..471
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 476..483
FT /evidence="ECO:0007829|PDB:4QLB"
FT STRAND 493..498
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 514..520
FT /evidence="ECO:0007829|PDB:4QLB"
FT STRAND 522..525
FT /evidence="ECO:0007829|PDB:4QLB"
FT STRAND 529..533
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 535..542
FT /evidence="ECO:0007829|PDB:4QLB"
FT STRAND 547..550
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 554..562
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 566..569
FT /evidence="ECO:0007829|PDB:4QLB"
FT STRAND 571..574
FT /evidence="ECO:0007829|PDB:4QLB"
FT STRAND 577..579
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 581..596
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 600..613
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 614..617
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 619..622
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 624..637
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 641..647
FT /evidence="ECO:0007829|PDB:4QLB"
FT TURN 649..651
FT /evidence="ECO:0007829|PDB:4QLB"
SQ SEQUENCE 672 AA; 76459 MW; 3B3C3E9044CAC8A0 CRC64;
MPDHARMPRN LSSNKIAKTI AGEDLDEEEV LEMDAGQSAR EEGRFVFECA WEVANKVGGI
YTVLRSKAQI STEELGDQYC MFGPMKDGKW RLEVDPIEPE NRTIRAAMKR FQADGFRCMY
GRWLIEGYPK VILFDLGSGA VKMNEWKHEL FEQCKIGIPH EDIESNDAVI LGFMVALFLK
HFRESVTSYT PLVVAHFHEW QAGVGLLMTR LWKLDIATVY TTHATLLGRH LCAGGADLYN
NLDSFDLDAE AGKRKIYHQY CLERAACQTA HIFTTVSEIT GLEAEHFLCR KPDVLTPNGL
NVVKFAALHE FQNLHAQNKE KINQFIRGHF HGHLDFDLDK TLYFFTAGRY EFSNKGGDMF
IESLARLNHY LKTTSDPRHM GVTVVAFLIY PAPANSFNVE SLKGQAVTKQ LKEAVDRIKE
KVGQRIFDIC LQGHLPEPEE LMSPADNILL KRCIMSLHNS SLPPICTHNM IRADDPVLES
LRRTSLFNKP EDRVKVVFHP EFLSSVSPLI GLDYEDFVRG CHLGVFPSYY EPWGYTPAEC
TVMGIPSVST NLSGFGCFMQ EHVEDHEQKG IYVIDRRHKA AEESVQELAQ VMYDFCGQSR
RQRIILRNSN EGLSALLDWQ NLGVFYRDCR RLALERLHPD VDKIMRDNEG KVPSAATSRR
PSIHSSDGED DE
