ID A0A1S3AJQ4_ERIEU Unreviewed; 656 AA.
AC A0A1S3AJQ4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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|RefSeq:XP_007536037.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007536037.1};
RN [1] {ECO:0000313|RefSeq:XP_007536037.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_007536037.1; XM_007535975.2.
DR AlphaFoldDB; A0A1S3AJQ4; -.
DR CTD; 2997; -.
DR OrthoDB; 9432at2759; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000079721; Unplaced.
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; 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:UP000079721};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT REGION 553..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 656 AA; 74810 MW; 804AEA0FA4BA7815 CRC64;
MNSTWRIQCF SKWPGRWPTK VYFGRWLIEG GPLVVLLDVG ASAWALERWK GELWDTCNIG
VPWYDREAND AVLFGFLTTW FLGEFLAQSE EKPHVVAHFH EWLAGIGLCL CRARRLPVAT
IFTTHATLLG RYLCAGAVDF YNNLETFNVD KEAGERQIYH RYCMERAAAH CAHVFTTVSQ
ITAIEAQHLL KRKPDIVTPN GLNVKKFSAM HEFQNLHAQS KARIQEFVRG HFYGHLDFNL
DKTLYFFIAG RYEFSNKGAD VFLEALARLN YLLRVNSSEQ TVVAFFIMPA RTNNFNVETL
KGQAVRKQLW DTANAVKEKF GRKLYESLLV GALPDMNKML DKEDFTMMKR AIFATQRQSF
PPVCTHNMLD DSSDPILTTI RRIGLFNSSA DRVKVIFHPE FLSSTSPLLP VDYEEFVRGC
HLGVFPSYYE PWGYTPAECT VMGIPSISTN LSGFGCFMEE HIADPSAYGI YILDRRFRSL
DDSCSQLTSF LYSFCQQSRR QRIIQRNRTE RLSDLLDWKY LGRYYMSARH MALAKAFPEH
FTYEPHEADA AQGYRYPRPA SVPPSPSLSR HSSPHQSEDE EEPRDVPDAD GERYDEEAEA
AKDRRNIRAP EWPRRASCAS STGGSKRGSV DTAPSSTLST PSEPLSPASS LGDERN
//
