GYG1_CAEEL
ID GYG1_CAEEL Reviewed; 429 AA.
AC H2KYQ5; H2KYQ6; Q95Q50;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Glycogenin-1 {ECO:0000312|WormBase:F56B6.4a};
DE Short=GN {ECO:0000303|PubMed:24982189};
DE EC=2.4.1.186 {ECO:0000250|UniProtKB:P13280};
GN Name=gyg-1 {ECO:0000312|WormBase:F56B6.4a};
GN ORFNames=F56B6.4 {ECO:0000312|WormBase:F56B6.4a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000312|PDB:4QLB}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 394-429 IN COMPLEX WITH GYS-1,
RP PATHWAY, SUBUNIT, DOMAIN, GLYCOSYLATION, AND MUTAGENESIS OF TYR-194;
RP ARG-400; TRP-403; TYR-410; PHE-416; ILE-419; LEU-423 AND LEU-427.
RX PubMed=24982189; DOI=10.1073/pnas.1402926111;
RA Zeqiraj E., Tang X., Hunter R.W., Garcia-Rocha M., Judd A., Deak M.,
RA von Wilamowitz-Moellendorff A., Kurinov I., Guinovart J.J., Tyers M.,
RA Sakamoto K., Sicheri F.;
RT "Structural basis for the recruitment of glycogen synthase by glycogenin.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E2831-2840(2014).
CC -!- FUNCTION: Self-glucosylates, via an inter-subunit mechanism, to form an
CC oligosaccharide primer that serves as substrate for gsy-1.
CC {ECO:0000269|PubMed:24982189}.
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:0000269|PubMed:24982189};
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:0000269|PubMed:24982189};
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:0000269|PubMed:24982189}.
CC -!- SUBUNIT: Forms a heterooctamer with one molecule of gyg-1 bound to each
CC protomer of the gys-1 homotetramer. The N-terminus of gys-1 is involved
CC in interprotomer contacts with gyg-1. The interaction with gys-1 is
CC required for glycogen production but is not required for gys-1
CC intrinsic activity. {ECO:0000269|PubMed:24982189}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:F56B6.4a};
CC IsoId=H2KYQ5-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F56B6.4b};
CC IsoId=H2KYQ5-2; Sequence=VSP_057309;
CC Name=c {ECO:0000312|WormBase:F56B6.4c};
CC IsoId=H2KYQ5-3; Sequence=VSP_057310;
CC -!- DOMAIN: The length of the linker region between residues 387-394 which
CC separates two alpha-helices regulates the size of the glycogen
CC particles synthesized but plays no role in the interaction with gsy-1.
CC {ECO:0000269|PubMed:24982189}.
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-194. {ECO:0000250|UniProtKB:P13280}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. Glycogenin
CC subfamily. {ECO:0000305}.
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DR EMBL; FO080515; CCD64318.1; -; Genomic_DNA.
DR EMBL; FO080515; CCD64319.1; -; Genomic_DNA.
DR EMBL; FO080515; CCD64320.1; -; Genomic_DNA.
DR RefSeq; NP_508608.1; NM_076207.5. [H2KYQ5-1]
DR RefSeq; NP_508609.1; NM_076208.6. [H2KYQ5-2]
DR RefSeq; NP_741749.1; NM_171944.4. [H2KYQ5-3]
DR PDB; 4QLB; X-ray; 2.60 A; E/F/G/H=394-429.
DR PDBsum; 4QLB; -.
DR AlphaFoldDB; H2KYQ5; -.
DR SMR; H2KYQ5; -.
DR ComplexPortal; CPX-3523; Glycogen synthase-Glycogenin complex.
DR IntAct; H2KYQ5; 1.
DR STRING; 6239.F56B6.4a; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR EPD; H2KYQ5; -.
DR PaxDb; H2KYQ5; -.
DR EnsemblMetazoa; F56B6.4a.1; F56B6.4a.1; WBGene00006863. [H2KYQ5-1]
DR EnsemblMetazoa; F56B6.4b.1; F56B6.4b.1; WBGene00006863. [H2KYQ5-2]
DR EnsemblMetazoa; F56B6.4c.1; F56B6.4c.1; WBGene00006863. [H2KYQ5-3]
DR GeneID; 180644; -.
DR KEGG; cel:CELE_F56B6.4; -.
DR UCSC; F56B6.4c; c. elegans.
DR CTD; 180644; -.
DR WormBase; F56B6.4a; CE04664; WBGene00006863; gyg-1. [H2KYQ5-1]
DR WormBase; F56B6.4b; CE29405; WBGene00006863; gyg-1. [H2KYQ5-2]
DR WormBase; F56B6.4c; CE31185; WBGene00006863; gyg-1. [H2KYQ5-3]
DR eggNOG; KOG1950; Eukaryota.
DR GeneTree; ENSGT00940000175485; -.
DR HOGENOM; CLU_017171_3_1_1; -.
DR InParanoid; H2KYQ5; -.
DR OMA; FVHIQEA; -.
DR OrthoDB; 1424146at2759; -.
DR PhylomeDB; H2KYQ5; -.
DR Reactome; R-CEL-3322077; Glycogen synthesis.
DR Reactome; R-CEL-70221; Glycogen breakdown (glycogenolysis).
DR UniPathway; UPA00164; -.
DR PRO; PR:H2KYQ5; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006863; Expressed in larva and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0055120; C:striated muscle dense body; HDA:WormBase.
DR GO; GO:0008466; F:glycogenin glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0102751; F:UDP-alpha-D-glucose:glucosyl-glycogenin alpha-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005978; P:glycogen biosynthetic process; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Glycogen biosynthesis; Glycoprotein;
KW Manganese; Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..429
FT /note="Glycogenin-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000431509"
FT REGION 254..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 8..14
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 101..103
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT BINDING 101
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT BINDING 103
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT BINDING 132..134
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT BINDING 159..163
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT BINDING 211..217
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT BINDING 211
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT SITE 85
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT CARBOHYD 194
FT /note="O-linked (Glc...) tyrosine"
FT /evidence="ECO:0000305|PubMed:24982189"
FT VAR_SEQ 246..390
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057309"
FT VAR_SEQ 246..371
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_057310"
FT MUTAGEN 194
FT /note="Y->P: Loss of auto-glucosylation. No effect on
FT interaction with gsy-1 but loss of gsy-1 function."
FT /evidence="ECO:0000269|PubMed:24982189"
FT MUTAGEN 400
FT /note="R->A: Loss of interaction with gsy-1. Partial loss
FT of gsy-1 function."
FT /evidence="ECO:0000269|PubMed:24982189"
FT MUTAGEN 403
FT /note="W->A: Loss of interaction with gsy-1. Partial loss
FT of gsy-1 function."
FT /evidence="ECO:0000269|PubMed:24982189"
FT MUTAGEN 410
FT /note="Y->A: Loss of interaction with gsy-1. Partial loss
FT of gsy-1 function."
FT /evidence="ECO:0000269|PubMed:24982189"
FT MUTAGEN 416
FT /note="F->A: Loss of interaction with gsy-1. Complete loss
FT of gsy-1 function."
FT /evidence="ECO:0000269|PubMed:24982189"
FT MUTAGEN 419
FT /note="I->A: Loss of interaction with gsy-1. Complete loss
FT of gsy-1 function."
FT /evidence="ECO:0000269|PubMed:24982189"
FT MUTAGEN 423
FT /note="L->A: Loss of interaction with gsy-1. Complete loss
FT of gsy-1 function."
FT /evidence="ECO:0000269|PubMed:24982189"
FT MUTAGEN 427
FT /note="L->A: Loss of interaction with gsy-1. Partial loss
FT of gsy-1 function."
FT /evidence="ECO:0000269|PubMed:24982189"
FT HELIX 396..404
FT /evidence="ECO:0007829|PDB:4QLB"
FT TURN 410..414
FT /evidence="ECO:0007829|PDB:4QLB"
FT HELIX 416..426
FT /evidence="ECO:0007829|PDB:4QLB"
SQ SEQUENCE 429 AA; 49007 MW; AD3856F797662654 CRC64;
MSEAWITLAT NDNYAQGALV LVHSLRTAGT TRKIHCLISN EVSAPVRKQL EEHFDDVSIV
DVFNSNDSDN LRLIERPDLG VTFTKLHCWR LTQYTKCVFL DADTLVLRNA DELFTRPDFS
AASDIGWPDS FNSGVFVYVP NNETYRQLVD FAVTHGSYDG GDQGLLNDFF SNWRDLPSEH
RLPFIYNMTA GAFYTYAAAY KRYGANTKIV HFIGSVKPWH GSAAVHTGEH FQQWQKIYHA
HVNHTSRTNE HAAVFPSHHH TPEHRSHSAD HPKIERKDSI VREIGNFVMH VVQSVNILPS
YDTDANTSDS HRNNEPHKHD QQREEHHELP HNKFQTPHEE SQDIVGSTDC FGSQMPKYNA
DSETDREVEQ ITNNTPCPAF VPFERREEYQ AASPSTEERR AAWEAGQPDY LGRDAFVHIQ
EALNRALNE
