ID Q4VK67_PIG Unreviewed; 36 AA.
AC Q4VK67;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
DE Flags: Fragment;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|EMBL:AAX62157.1};
RN [1] {ECO:0000313|EMBL:AAX62157.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15932409; DOI=10.1111/j.1365-2052.2005.01286.x;
RA Zuo B., Xiong Y.Z., Deng C.Y., Su Y.H., Wang J., Lei M.G., Li F.E.,
RA Jiang S.W., Zheng R.;
RT "Polymorphism, linkage mapping and expression pattern of the porcine
RT skeletal muscle glycogen synthase (GYS1) gene.";
RL Anim. Genet. 36:254-257(2005).
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; AH014803; AAX62155.1; -; Genomic_DNA.
DR EMBL; AY870458; AAX62157.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4VK67; -.
DR HOGENOM; CLU_015910_1_0_1; -.
DR UniPathway; UPA00164; -.
DR GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
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.
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 NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAX62157.1"
FT NON_TER 36
FT /evidence="ECO:0000313|EMBL:AAX62157.1"
SQ SEQUENCE 36 AA; 4096 MW; D359F0355368226A CRC64;
YEFSNKGADV FLEALARLNY LLRVNGSEQT VVAFFI
//
