ID B2L109_HORSE Unreviewed; 737 AA.
AC B2L109;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 24-JAN-2024, entry version 83.
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: Transfers the glycosyl residue from UDP-Glc to the non-
CC reducing end of alpha-1,4-glucan. {ECO:0000256|ARBA:ARBA00003605,
CC 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:ARBA00000075,
CC ECO:0000256|RuleBase:RU363104};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004964, ECO:0000256|RuleBase:RU363104}.
CC -!- SUBUNIT: Interacts with GYG1. {ECO:0000256|ARBA:ARBA00038520}.
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|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU363104};
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
//