ID   G5BAG4_HETGA            Unreviewed;       735 AA.
AC   G5BAG4;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   ORFNames=GW7_13622 {ECO:0000313|EMBL:EHB06275.1};
OS   Heterocephalus glaber (Naked mole rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Heterocephalus.
OX   NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB06275.1, ECO:0000313|Proteomes:UP000006813};
RN   [1] {ECO:0000313|EMBL:EHB06275.1, ECO:0000313|Proteomes:UP000006813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993625; DOI=10.1038/nature10533;
RA   Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA   Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA   Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA   Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA   Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA   Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT   "Genome sequencing reveals insights into physiology and longevity of the
RT   naked mole rat.";
RL   Nature 479:223-227(2011).
CC   -!- FUNCTION: Glycogen synthase participates in the glycogen biosynthetic
CC       process along with glycogenin and glycogen branching enzyme. Extends
CC       the primer composed of a few glucose units formed by glycogenin by
CC       adding new glucose units to it. In this context, glycogen synthase
CC       transfers the glycosyl residue from UDP-Glc to the non-reducing end of
CC       alpha-1,4-glucan. {ECO:0000256|ARBA:ARBA00043883}.
CC   -!- FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non-
CC       reducing end of alpha-1,4-glucan. {ECO:0000256|RuleBase:RU363104}.
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:0000256|ARBA:ARBA00043769};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18550;
CC         Evidence={ECO:0000256|ARBA:ARBA00043769};
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004964, ECO:0000256|RuleBase:RU363104}.
CC   -!- SUBUNIT: Part of the GYS1-GYG1 complex, a heterooctamer composed of a
CC       tetramer of GYS1 and 2 dimers of GYG1, where each GYS1 protomer binds
CC       to one GYG1 subunit (via GYG1 C-terminus); the GYS1 tetramer may
CC       dissociate from GYG1 dimers to continue glycogen polymerization on its
CC       own. {ECO:0000256|ARBA:ARBA00044021}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 3 family.
CC       {ECO:0000256|ARBA:ARBA00010686, ECO:0000256|RuleBase:RU363104}.
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DR   EMBL; JH169240; EHB06275.1; -; Genomic_DNA.
DR   RefSeq; XP_004867023.1; XM_004866966.2.
DR   AlphaFoldDB; G5BAG4; -.
DR   STRING; 10181.G5BAG4; -.
DR   Ensembl; ENSHGLT00100021808; ENSHGLP00100021582; ENSHGLG00100015886.
DR   GeneID; 101712358; -.
DR   KEGG; hgl:101712358; -.
DR   CTD; 2997; -.
DR   eggNOG; KOG3742; Eukaryota.
DR   InParanoid; G5BAG4; -.
DR   OMA; NDEEECY; -.
DR   OrthoDB; 9432at2759; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000006813; Unassembled WGS sequence.
DR   Bgee; ENSHGLG00000007154; Expressed in heart and 10 other cell types or tissues.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
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:SF2; GLYCOGEN [STARCH] SYNTHASE, MUSCLE; 1.
DR   PANTHER; PTHR10176; GLYCOGEN SYNTHASE; 1.
DR   Pfam; PF05693; Glycogen_syn; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 2.
PE   3: Inferred from homology;
KW   Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056,
KW   ECO:0000256|RuleBase:RU363104};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU363104};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT   REGION          632..735
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..670
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..691
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        693..728
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   735 AA;  83576 MW;  4A921B2E1223E95F CRC64;
     MPLSRTLSVS SLPGLEEWED EFDLENTVLF EVAWEVANKV GGIYTVLQTK AKVTGDEWGD
     NYYLVGPYTE QGVRTQVELL EPPTPAFKKT LDSMNSKGCK VYFGRWLIEG GPLVVLLDVG
     ASAWALERWK GELWDTCNIG VPWYDREAND AVLFGFLTTW FLGEFLAQSE EKPHVVAHFH
     EWLAGVGLCL CRARRLPVAT IFTTHATLLG RYLCAGAVDF YNNLENFNVD KEAGERQIYH
     RYCMERAAAH CAHVFTTVSQ ITAIEAQHLL KRKPDIVTPN GLNVKKFSAM HEFQNLHAQS
     KARIQEFVRG HFYGHLDFNL DKTLYFFIAG RYEFSNKGAD VFLEALARLN YLLRVNGSEQ
     TVVAFFIMPA RTNNFNVETL KGQAVRKQLW DTANAVKEKF GRKLYESLLV GSLPDMNKML
     DKEDFTMMKR AIFATQRQSF PPVCTHNMLD DSSDPILTTI RRIGLFNSSA DRVKVIFHPE
     FLSSTSPLLP VDYEEFVRGC HLGVFPSYYE PWGYTPAECT VMGIPSISTN LSGFGCFMEE
     HIADPSAYGI YILDRRFRSL DDSCSQLTSF LYSFCQQSRR QRIIQRNRTE RLSDLLDWKY
     LGRYYMSARH MALAKAFPDH FTYEPHEADA AQGYRYPRPA SVPPSPSLSR HSSPHQSEDE
     EEPREGPLED GERYDEDEEA AKDRRNIRAP EWPRRSSCTS STGKRSNSVD TAPSSSLSTP
     SEPLSPASSL GEERN
//