ID A0A218UGG2_9PASE Unreviewed; 704 AA.
AC A0A218UGG2;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN Name=GYS2 {ECO:0000313|EMBL:OWK52829.1};
GN ORFNames=RLOC_00014308 {ECO:0000313|EMBL:OWK52829.1};
OS Lonchura striata domestica (Bengalese finch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Lonchura.
OX NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK52829.1, ECO:0000313|Proteomes:UP000197619};
RN [1] {ECO:0000313|EMBL:OWK52829.1, ECO:0000313|Proteomes:UP000197619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=White83orange57 {ECO:0000313|EMBL:OWK52829.1};
RA Colquitt B.M., Brainard M.S.;
RT "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWK52829.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MUZQ01000319; OWK52829.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218UGG2; -.
DR STRING; 299123.ENSLSDP00000020595; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000197619; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000197619};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT REGION 621..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 81011 MW; 6C932A16A37C7320 CRC64;
MPLARSLSMT SLNGLLQCED EDLPVEDLLL FEISWEVTNK VGGIYTVIQT KAKTTADEWG
ENYFLIGPYF EQNVKTQVEF SEPPNSAVKK AMDTMKSQGC QVFFGRWLIE GSPYVLLFDI
GSAAWNLDKW KGGFWEVSNI GIPFHDREAN DAVIFGSLTA WFLKELSCQF DDKPNIIAHF
HEWQAGVGLI LSRSQKLPVA TIFTTHATLL GRYLCAASID FYNNLDQFDI DKEAGERQIY
HRYCMERASV HCAHVFTTVS QITATEAEHM LKKCPDVVTP NGLNIKKFSA MHEFQNLHSM
YKARIQEFIR GHFYGHLDFD LDKTLFFFIA GRYEFSNKGA DMFLEALSRL NFLLRVHKTD
ITVIVFFIMP AKTNNFNVET LKGQAVRKQL WDTAQSVKEK FGRKLYNALL KGEIPDLNKI
LDRDDISIMK RAIFSTQRHS LPPVTTHNMI DDSNDPILNT IRRIGLFNNR TDRVKVILHP
EFLSSTSPLL PLDYEEFVRG CHLGVFPSYY EPWGYTPAEC TVMGIPSVTT NLSGFGCFMQ
EHVADPEAYG IYIVDRRFRS PDESCNQLTQ FLYGFCQQNR RQRIIQRNRT ERLSDLLDWK
YLGRYYMHAR HLALSRTFPD KFEMEPSAPP KTEGFRFPRP SSVPPSPSAS QHSSPHHSEA
EDDDEDERYD EDEEAERDRQ NIKSPFSLGA LPQGKKKQHG EYRN
//
