ID   B2L109_HORSE            Unreviewed;       737 AA.
AC   B2L109;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   Name=GYS1 {ECO:0000313|EMBL:ACB14276.1};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|EMBL:ACB14276.1};
RN   [1] {ECO:0000313|EMBL:ACB14276.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18358695; DOI=10.1016/j.ygeno.2008.01.011;
RA   McCue M.E., Valberg S.J., Miller M.B., Wade C., DiMauro S., Akman H.O.,
RA   Mickelson J.R.;
RT   "Glycogen synthase (GYS1) mutation causes a novel skeletal muscle
RT   glycogenosis.";
RL   Genomics 91:458-466(2008).
RN   [2] {ECO:0000313|EMBL:BAI79302.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Skeletal muscle {ECO:0000313|EMBL:BAI79302.1};
RX   PubMed=20383748; DOI=10.1007/s11033-010-0129-8;
RA   Echigoya Y., Okabe H., Itou T., Endo H., Sakai T.;
RT   "Molecular characterization of glycogen synthase 1 and its tissue
RT   expression profile with type II hexokinase and muscle-type
RT   phosphofructokinase in horses.";
RL   Mol. Biol. Rep. 38:461-469(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; EU373801; ACB14276.1; -; mRNA.
DR   EMBL; AB522619; BAI79302.1; -; mRNA.
DR   RefSeq; NP_001119597.2; NM_001126125.2.
DR   AlphaFoldDB; B2L109; -.
DR   SMR; B2L109; -.
DR   CAZy; GT3; Glycosyltransferase Family 3.
DR   PeptideAtlas; B2L109; -.
DR   GeneID; 100054723; -.
DR   KEGG; ecb:100054723; -.
DR   CTD; 2997; -.
DR   HOGENOM; CLU_015910_1_0_1; -.
DR   OrthoDB; 9432at2759; -.
DR   TreeFam; TF300306; -.
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   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   2: Evidence at transcript level;
KW   Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056,
KW   ECO:0000256|RuleBase:RU363104};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU363104,
KW   ECO:0000313|EMBL:BAI79302.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT   REGION          630..737
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..677
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..692
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..730
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   737 AA;  83896 MW;  5F01E0C31E482363 CRC64;
     MPLNRTLSMS SLPGLDDWED EFDLENTVLF EVAWEVANKV GGIYTVLQTK AKVTGDEWGD
     NYYLVGPYTE QGVRTQVELL EPPTPALKRT LDSMNSKGCK VYFGRWLIEG GPLVVLLDVG
     ASAWALERWK GELWDTCNIG VPWYDREAND AVLFGFLTTW FLGEFLAQSE EKPHVVAHFH
     EWLAGIGLCL CRARRLPVAT IFTTHATLLG RYLCAGAVDF YNNLENFNVD KEAGERQIYH
     RYCMERAAAH CTHVFTTVSQ ITAIEAQHLL KRKPDIVTPN GLNVKKFSAM HEFQNLHAQS
     KARIQEFVRG HFYGHLDFNL DKTLYFFIAG RYEFSNKGAD VFLEALARLN YLLRVNGSEQ
     TVVAFFIMPA RTNNFNVETL KGQAVRKQLW DTANTVKEKF GRKLYESLLV GSLPDMNKML
     DKEDFTMMKR AIFATQRQSF PPVCTHNMLD DSSDPILTTI RRIGLFNSSA DRVKVIFHPE
     FLSSTSPLLP VDYEEFVRGC HLGVFPSYYE PWGYTPAECT VMGIPSISTN LSGFGCFMEE
     HIADPSAYGI YILDRRFRSL DDSCSQLTSF LYSFCQQSRR QRIIQRNRTE RLSDLLDWKY
     LGRYYMSARH MALAKAFPEH FTYEPREADA TQGYRYPRPA SVPPSPSLSR HSSPHQSEDE
     EEPRDVPPDE DSERYDEDEE AAKDRRNIRA PEWPRRASCT SSTSGSKRGS VDTGPSSSLS
     TPSEPLSPAS SLGEERN
//