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Database: UniProt
Entry: G7N6H9_MACMU
LinkDB: G7N6H9_MACMU
Original site: G7N6H9_MACMU 
ID   G7N6H9_MACMU            Unreviewed;       701 AA.
AC   G7N6H9;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   ORFNames=EGK_03453 {ECO:0000313|EMBL:EHH20575.1};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|EMBL:EHH20575.1};
RN   [1] {ECO:0000313|EMBL:EHH20575.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CR-5 {ECO:0000313|EMBL:EHH20575.1};
RX   PubMed=22002653; DOI=10.1038/nbt.1992;
RA   Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA   Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA   Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA   Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA   Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA   Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT   "Genome sequencing and comparison of two nonhuman primate animal models,
RT   the cynomolgus and Chinese rhesus macaques.";
RL   Nat. Biotechnol. 29:1019-1023(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   -!- SIMILARITY: Belongs to the glycosyltransferase 3 family.
CC       {ECO:0000256|ARBA:ARBA00010686, ECO:0000256|RuleBase:RU363104}.
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DR   EMBL; CM001263; EHH20575.1; -; Genomic_DNA.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000013456; Chromosome 11.
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:SF1; GLYCOGEN [STARCH] SYNTHASE, LIVER; 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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT   REGION          626..701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..701
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   701 AA;  80869 MW;  4195E700CDBB61F5 CRC64;
     MLRGRSLSVT SLSGLPRWEV EELPVEELLL FEVAWEVTNK VGGIYTVIQT KAKTTADEWG
     DNYFLIGPYF EHNMKTQVEQ CEPVNDAVRR AVDAMNKHGC QVHFGRWLIE GSPYVVLFDI
     GFSAWNLDRW KGDLWEACSV GIPYHDREAN DMLIFGSLTA WFLKEVTDHA DDKHVVAQFH
     EWQAGIGLIL SRARKLPIAT IFTTHATLLG RYLCAANIDF YNHLDKFNID KEAGERQIYH
     RYCMERASVH CAHVFTTVSE ITAIEAEHML KRKPDVVTLL NVKKFSAVHE FQNLHAMYKA
     RIQDFVRGHF YGHLDFDLEK TLFLFIAGRY EFSNKGADIF LESLSRLNFL LRMHKSDVTV
     VVFFIMPAKT NNFNVETLKG QAVRKQLWDI AHSVKEKFGK KLYDALLRGE IPDMNNILDL
     DDLTIMKRAI XXLQRQSLPP VTTHNMIDDS TDPILSTIRR IGLFNNRTDR VKVILHPEFL
     SSTSPLLPMD YEEFVRGCHL GVFPSYYEPW GYTPAECTVM GIPSVTTNLS GFGCFMQEHV
     ADPTAYGIYI VDRRFRSPDD SCNQLTQFLY GFCKQSRRQR IIQRNRTERL SDLLDWRYLG
     RYYQHARHLT LSRAFPDKFH VELTSPPMTE GFKYPRPSSV PPSPSGSQAS SPQSSDVEDE
     VEDERYDEEK EAERDRLNIK SPFALSHVPR GKKKLHGEYK N
//
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