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Glycogenin-1 (GN-1) (GN1) (EC 2.4.1.186)

 GLYG_RABIT              Reviewed;         333 AA.
P13280;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
31-JAN-2018, entry version 125.
RecName: Full=Glycogenin-1;
Short=GN-1;
Short=GN1;
EC=2.4.1.186;
Name=GYG1; Synonyms=GYG;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skeletal muscle;
PubMed=1281472;
Viskupic E., Cao Y., Zhang W., Cheng C., Depaoli-Roach A.A.,
Roach P.J.;
"Rabbit skeletal muscle glycogenin. Molecular cloning and production
of fully functional protein in Escherichia coli.";
J. Biol. Chem. 267:25759-25763(1992).
[2]
PROTEIN SEQUENCE OF 2-333.
STRAIN=New Zealand white; TISSUE=Skeletal muscle;
PubMed=2806254; DOI=10.1111/j.1432-1033.1989.tb15090.x;
Campbell D.G., Cohen P.;
"The amino acid sequence of rabbit skeletal muscle glycogenin.";
Eur. J. Biochem. 185:119-125(1989).
[3]
PROTEIN SEQUENCE OF 35-48; 182-202; 210-227 AND 308-325.
TISSUE=Liver;
PubMed=2526735; DOI=10.1111/j.1432-1033.1989.tb14914.x;
Smythe C., Villar-Palasi C., Cohen P.;
"Structural and functional studies on rabbit liver glycogenin.";
Eur. J. Biochem. 183:205-209(1989).
[4]
PROTEIN SEQUENCE OF 35-48, AND PHOSPHORYLATION AT SER-44.
PubMed=3151442;
Lomako J., Whelan W.J.;
"The occurrence of serine phosphate in glycogenin: a possible
regulatory site.";
BioFactors 1:261-264(1988).
[5]
CHARACTERIZATION.
PubMed=8143846; DOI=10.1016/0014-5793(94)80580-6;
Alonso M.D., Lomako J., Lomako W.M., Whelan W.J.;
"Tyrosine-194 of glycogenin undergoes autocatalytic glucosylation but
is not essential for catalytic function and activity.";
FEBS Lett. 342:38-42(1994).
[6]
CHARACTERIZATION.
PubMed=7771798; DOI=10.1006/abbi.1995.1295;
Cao Y., Steinrauf L.K., Roach P.J.;
"Mechanism of glycogenin self-glucosylation.";
Arch. Biochem. Biophys. 319:293-298(1995).
[7]
CHARACTERIZATION, ACTIVE SITE, AND MUTAGENESIS OF LYS-86.
PubMed=10049511; DOI=10.1006/abbi.1998.1073;
Lin A., Mu J., Yang J., Roach P.J.;
"Self-glucosylation of glycogenin, the initiator of glycogen
biosynthesis, involves an inter-subunit reaction.";
Arch. Biochem. Biophys. 363:163-170(1999).
[8]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), X-RAY CRYSTALLOGRAPHY (1.9
ANGSTROMS) IN COMPLEX WITH UDP-GLUCOSE AND MANGANESE IONS, AND
SUBUNIT.
PubMed=12051921; DOI=10.1016/S0022-2836(02)00305-4;
Gibbons B.J., Roach P.J., Hurley T.D.;
"Crystal structure of the autocatalytic initiator of glycogen
biosynthesis, glycogenin.";
J. Mol. Biol. 319:463-477(2002).
[9]
X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF
ASP-160 AND ASP-163.
PubMed=15849187; DOI=10.1074/jbc.M502344200;
Hurley T.D., Stout S., Miner E., Zhou J., Roach P.J.;
"Requirements for catalysis in mammalian glycogenin.";
J. Biol. Chem. 280:23892-23899(2005).
-!- FUNCTION: Self-glucosylates, via an inter-subunit mechanism, to
form an oligosaccharide primer that serves as substrate for
glycogen synthase.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose + glycogenin = UDP +
alpha-D-glucosylglycogenin.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:12051921};
Note=Divalent metal ions. Required for self-glucosylation.
Manganese is the most effective. {ECO:0000269|PubMed:12051921};
-!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
-!- SUBUNIT: Homodimer tightly complexed to the 86 kDa catalytic
subunit of glycogen synthase GYS1 (PubMed:12051921,
PubMed:15849187). Interacts (via C-terminus) with GYS2; required
for GYS2-mediated glycogen synthesis (By similarity).
{ECO:0000250|UniProtKB:Q9R062, ECO:0000269|PubMed:12051921,
ECO:0000269|PubMed:15849187}.
-!- PTM: Self-glycosylated by the transfer of glucose residues from
UDP-glucose to itself, forming an alpha-1,4-glycan of around 10
residues attached to Tyr-195. {ECO:0000269|PubMed:8143846}.
-!- PTM: Phosphorylated. {ECO:0000269|PubMed:3151442}.
-!- SIMILARITY: Belongs to the glycosyltransferase 8 family.
Glycogenin subfamily. {ECO:0000305}.
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EMBL; L01791; AAA31404.1; -; mRNA.
PIR; A45094; A45094.
RefSeq; NP_001075710.1; NM_001082241.1.
UniGene; Ocu.1930; -.
PDB; 1LL0; X-ray; 3.43 A; A/B/C/D/E/F/G/H/I/J=1-333.
PDB; 1LL2; X-ray; 1.90 A; A=1-333.
PDB; 1LL3; X-ray; 1.90 A; A=1-333.
PDB; 1ZCT; X-ray; 2.60 A; A/B=1-270.
PDB; 1ZCU; X-ray; 2.00 A; A=1-333.
PDB; 1ZCV; X-ray; 1.98 A; A=1-333.
PDB; 1ZCY; X-ray; 1.99 A; A=1-333.
PDB; 1ZDF; X-ray; 2.45 A; A=1-333.
PDB; 1ZDG; X-ray; 2.30 A; A=1-333.
PDB; 3USQ; X-ray; 2.40 A; A=1-271.
PDB; 3USR; X-ray; 2.10 A; A=1-271.
PDB; 3V8Y; X-ray; 2.15 A; A=1-271.
PDB; 3V8Z; X-ray; 2.20 A; A=1-271.
PDB; 3V90; X-ray; 2.00 A; A=1-271.
PDB; 3V91; X-ray; 2.00 A; A=1-271.
PDBsum; 1LL0; -.
PDBsum; 1LL2; -.
PDBsum; 1LL3; -.
PDBsum; 1ZCT; -.
PDBsum; 1ZCU; -.
PDBsum; 1ZCV; -.
PDBsum; 1ZCY; -.
PDBsum; 1ZDF; -.
PDBsum; 1ZDG; -.
PDBsum; 3USQ; -.
PDBsum; 3USR; -.
PDBsum; 3V8Y; -.
PDBsum; 3V8Z; -.
PDBsum; 3V90; -.
PDBsum; 3V91; -.
ProteinModelPortal; P13280; -.
SMR; P13280; -.
CAZy; GT8; Glycosyltransferase Family 8.
iPTMnet; P13280; -.
PRIDE; P13280; -.
GeneID; 100009058; -.
KEGG; ocu:100009058; -.
CTD; 2992; -.
HOGENOM; HOG000008282; -.
HOVERGEN; HBG000681; -.
InParanoid; P13280; -.
KO; K00750; -.
BRENDA; 2.4.1.186; 1749.
UniPathway; UPA00164; -.
EvolutionaryTrace; P13280; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0008466; F:glycogenin glucosyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0102751; F:UDP-alpha-D-glucose:glucosyl-glycogenin alpha-D-glucosyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR002495; Glyco_trans_8.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
Pfam; PF01501; Glyco_transf_8; 1.
SUPFAM; SSF53448; SSF53448; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Glycogen biosynthesis; Glycoprotein;
Manganese; Metal-binding; Phosphoprotein; Reference proteome;
Transferase.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P46976,
ECO:0000269|PubMed:2806254}.
CHAIN 2 333 Glycogenin-1. {ECO:0000305}.
/FTId=PRO_0000215178.
REGION 284 316 Interaction with GYS1.
{ECO:0000250|UniProtKB:P46976}.
ACT_SITE 86 86 {ECO:0000269|PubMed:10049511}.
METAL 102 102 Manganese. {ECO:0000269|PubMed:12051921}.
METAL 104 104 Manganese. {ECO:0000269|PubMed:12051921}.
METAL 212 212 Manganese. {ECO:0000269|PubMed:12051921}.
SITE 160 160 Important for catalytic activity.
{ECO:0000269|PubMed:15849187}.
SITE 163 163 Important for catalytic activity.
{ECO:0000269|PubMed:15849187}.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000250|UniProtKB:P46976}.
MOD_RES 44 44 Phosphoserine; by PKA; in vitro.
{ECO:0000269|PubMed:3151442}.
CARBOHYD 195 195 O-linked (Glc...) tyrosine.
{ECO:0000269|PubMed:8143846}.
MUTAGEN 86 86 K->Q: Loss of activity.
{ECO:0000269|PubMed:10049511}.
MUTAGEN 160 160 D->N,S: Reduced trans-glucosylation
activity by at least 260-fold and reduced
UDP-glucose hydrolytic activity by 4 to
14-fold. {ECO:0000269|PubMed:15849187}.
MUTAGEN 163 163 D->N: Loss of self-glucosylation activity
and ability to trans-glucosylate maltose.
Reduced UDP-glucose hydrolytic activity
by at least 190-fold.
{ECO:0000269|PubMed:15849187}.
MUTAGEN 163 163 D->S: Loss of self-glucosylation activity
and 18 to 30-fold reduction in its
ability to trans-glucosylate maltose.
Reduced UDP-glucose hydrolytic activity
by at least 190-fold.
{ECO:0000269|PubMed:15849187}.
CONFLICT 39 39 T -> L (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 89 89 C -> S (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 98 98 C -> L (in Ref. 2; AA sequence).
{ECO:0000305}.
STRAND 3 12 {ECO:0000244|PDB:1LL2}.
HELIX 13 28 {ECO:0000244|PDB:1LL2}.
STRAND 33 39 {ECO:0000244|PDB:1LL2}.
HELIX 45 54 {ECO:0000244|PDB:1LL2}.
STRAND 56 60 {ECO:0000244|PDB:1LL2}.
HELIX 71 76 {ECO:0000244|PDB:1LL2}.
HELIX 78 80 {ECO:0000244|PDB:1LL2}.
HELIX 81 86 {ECO:0000244|PDB:1LL2}.
HELIX 87 91 {ECO:0000244|PDB:1LL2}.
STRAND 96 101 {ECO:0000244|PDB:1LL2}.
STRAND 105 107 {ECO:0000244|PDB:1LL2}.
HELIX 112 116 {ECO:0000244|PDB:1LL2}.
STRAND 119 124 {ECO:0000244|PDB:1LL2}.
STRAND 126 128 {ECO:0000244|PDB:1LL2}.
STRAND 131 139 {ECO:0000244|PDB:1LL2}.
HELIX 143 155 {ECO:0000244|PDB:1LL2}.
STRAND 159 162 {ECO:0000244|PDB:1ZCY}.
HELIX 163 170 {ECO:0000244|PDB:1LL2}.
TURN 171 176 {ECO:0000244|PDB:1LL2}.
HELIX 179 181 {ECO:0000244|PDB:1LL2}.
HELIX 185 187 {ECO:0000244|PDB:1LL2}.
STRAND 188 190 {ECO:0000244|PDB:1LL2}.
HELIX 193 196 {ECO:0000244|PDB:1LL2}.
HELIX 198 204 {ECO:0000244|PDB:1LL2}.
HELIX 205 207 {ECO:0000244|PDB:1LL2}.
STRAND 209 212 {ECO:0000244|PDB:1LL2}.
STRAND 215 217 {ECO:0000244|PDB:1LL3}.
HELIX 219 221 {ECO:0000244|PDB:1LL2}.
STRAND 222 225 {ECO:0000244|PDB:3USR}.
TURN 226 229 {ECO:0000244|PDB:1LL2}.
STRAND 230 232 {ECO:0000244|PDB:3USR}.
HELIX 243 255 {ECO:0000244|PDB:1LL2}.
HELIX 257 261 {ECO:0000244|PDB:1LL2}.
HELIX 263 265 {ECO:0000244|PDB:1ZCV}.
SEQUENCE 333 AA; 37397 MW; 7C27F7B428F67571 CRC64;
MTDQAFVTLT TNDAYAKGAL VLGSSLKQHR TSRRLAVLTT PQVSDTMRKA LEIVFDEVIT
VDILDSGDSA HLTLMKRPEL GVTLTKLHCW SLTQYSKCVF MDADTLVLAN IDDLFEREEL
SAAPDPGWPD CFNSGVFVYQ PSVETYNQLL HVASEQGSFD GGDQGLLNTF FNSWATTDIR
KHLPFIYNLS SISIYSYLPA FKAFGANAKV VHFLGQTKPW NYTYDTKTKS VRSEGHDPTM
THPQFLNVWW DIFTTSVVPL LQQFGLVQDT CSYQHVEDVS GAVSHLSLGE TPATTQPFVS
SEERKERWEQ GQADYMGADS FDNIKKKLDT YLQ


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