GLYG_RAT
ID GLYG_RAT Reviewed; 333 AA.
AC O08730;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Glycogenin-1;
DE Short=GN-1;
DE Short=GN1;
DE EC=2.4.1.186 {ECO:0000250|UniProtKB:P46976};
GN Name=Gyg1; Synonyms=Gyg;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Heart;
RX PubMed=10391131; DOI=10.1023/a:1006924016809;
RA Pak B.J., Sangaralingham S.J., Pang S.C.;
RT "Molecular cloning and developmental expression of rat glycogenin in
RT cardiac tissue.";
RL Mol. Cell. Biochem. 194:117-123(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Self-glucosylates, via an inter-subunit mechanism, to form an
CC oligosaccharide primer that serves as substrate for glycogen synthase.
CC {ECO:0000250|UniProtKB:P46976}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = alpha-D-
CC glucosyl-L-tyrosyl-[glycogenin] + H(+) + UDP; Xref=Rhea:RHEA:23360,
CC Rhea:RHEA-COMP:14604, Rhea:RHEA-COMP:14605, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:140573; EC=2.4.1.186;
CC Evidence={ECO:0000250|UniProtKB:P46976};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[1,4-alpha-D-glucosyl](n)-L-tyrosyl-[glycogenin] + UDP-alpha-
CC D-glucose = [1,4-alpha-D-glucosyl](n+1)-L-tyrosyl-[glycogenin] + H(+)
CC + UDP; Xref=Rhea:RHEA:56560, Rhea:RHEA-COMP:14606, Rhea:RHEA-
CC COMP:14607, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:140574; EC=2.4.1.186;
CC Evidence={ECO:0000250|UniProtKB:P46976};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P13280};
CC Note=Divalent metal ions. Required for self-glucosylation. Manganese is
CC the most effective. {ECO:0000250|UniProtKB:P13280};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000250|UniProtKB:P46976}.
CC -!- SUBUNIT: Homodimer. Interacts (via C-terminus) with glycogen synthase
CC GYS1 (By similarity). Interacts (via C-terminus) with glycogen synthase
CC GYS2 (By similarity). This interaction is required for GYS2-mediated
CC glycogen synthesis (By similarity). {ECO:0000250|UniProtKB:P46976,
CC ECO:0000250|UniProtKB:Q9R062}.
CC -!- PTM: Self-glycosylated by the transfer of glucose residues from UDP-
CC glucose to itself, forming an alpha-1,4-glycan of around 10 residues
CC attached to Tyr-195. {ECO:0000250|UniProtKB:P13280}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:P13280}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. Glycogenin
CC subfamily. {ECO:0000305}.
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DR EMBL; AF021343; AAB81219.1; -; mRNA.
DR EMBL; U96130; AAB53334.1; -; mRNA.
DR EMBL; BC070944; AAH70944.1; -; mRNA.
DR RefSeq; NP_112305.1; NM_031043.2.
DR AlphaFoldDB; O08730; -.
DR SMR; O08730; -.
DR IntAct; O08730; 1.
DR STRING; 10116.ENSRNOP00000014837; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR GlyGen; O08730; 1 site.
DR iPTMnet; O08730; -.
DR PhosphoSitePlus; O08730; -.
DR jPOST; O08730; -.
DR PaxDb; O08730; -.
DR PRIDE; O08730; -.
DR GeneID; 81675; -.
DR KEGG; rno:81675; -.
DR UCSC; RGD:621785; rat.
DR CTD; 2992; -.
DR RGD; 621785; Gyg1.
DR eggNOG; KOG1950; Eukaryota.
DR InParanoid; O08730; -.
DR OrthoDB; 1424146at2759; -.
DR PhylomeDB; O08730; -.
DR Reactome; R-RNO-3322077; Glycogen synthesis.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-70221; Glycogen breakdown (glycogenolysis).
DR UniPathway; UPA00164; -.
DR PRO; PR:O08730; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005536; F:glucose binding; IDA:RGD.
DR GO; GO:0008466; F:glycogenin glucosyltransferase activity; IDA:RGD.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0102751; F:UDP-alpha-D-glucose:glucosyl-glycogenin alpha-D-glucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0005978; P:glycogen biosynthetic process; IDA:RGD.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR002495; Glyco_trans_8.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF01501; Glyco_transf_8; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Glycogen biosynthesis; Glycoprotein; Manganese; Metal-binding;
KW Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT CHAIN 2..333
FT /note="Glycogenin-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000215179"
FT REGION 284..316
FT /note="Interaction with GYS1"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT REGION 287..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 9..15
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 102..104
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 102
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT BINDING 104
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT BINDING 133..135
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 160..164
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 212..218
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 212
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT SITE 86
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT CARBOHYD 195
FT /note="O-linked (Glc...) tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P13280"
SQ SEQUENCE 333 AA; 37378 MW; E0B29DCDB4A82DD2 CRC64;
MTDQAFVTLT TNDAYAKGAL VLGSSLKQHR TTRRTVVLAS PQVSDSMRKV LETVFDEVIM
VDVLDSGDSA HLTLMKRPEL GITLTKLHCW SLTQYSKCVF MDADTLVLSN IDDLFEREEL
SAAPDPGWPD CFNSGVFVYQ PSIETYNQLL HLASEQGSFD GGDQGLLNTY FSGWATTDIT
KHLPFVYNLS SLSIYSYLPA FKAFGKNAKV VHFLGRTKPW NYTYNPQTKS VKCESQDPIV
SHPEFLNLWW DTFTTNVLPL LQHHGLVKDA GSYLMMEHVT GALSDLSFGE APPASQPSLS
SEERKERWEQ GQADYMGADS FDNIKRKLDT YLQ
