P13280 (GLYG_RABIT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glycogenin-1
Short name=GN-1
Short name=GN1
EC=2.4.1.186

Gene names

Name:	GYG1
Synonyms:	GYG

Organism

Oryctolagus cuniculus (Rabbit) [Complete proteome]

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	333 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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	Divalent metal ions. Required for self-glucosylation. Manganese is the most effective.
Pathway	Glycan biosynthesis; glycogen biosynthesis.
Subunit structure	Homodimer tightly complexed to the 86 kDa catalytic subunit of glycogen synthase GYS1 By similarity. Ref.8 Ref.9
Post-translational modification	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. Phosphorylated. Ref.4
Sequence similarities	Belongs to the glycogenin family.

Ontologies

Keywords
Biological process	Glycogen biosynthesis
Ligand	Manganese Metal-binding
Molecular function	Transferase
PTM	Acetylation Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	glycogen biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	glycogenin glucosyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 333

332

Glycogenin-1

PRO_0000215178

Regions

Region

284 – 316

33

Interaction with GYS1 By similarity

Sites

Active site

86

1

Metal binding

102

1

Manganese

Metal binding

104

1

Manganese

Metal binding

212

1

Manganese

Site

160

1

Important for catalytic activity

Site

163

1

Important for catalytic activity

Amino acid modifications

Modified residue

2

1

N-acetylthreonine

Modified residue

44

1

Phosphoserine; by PKA; in vitro

Glycosylation

195

1

O-linked (Glc...)

Experimental info

Mutagenesis

86

1

K → Q: Loss of activity. Ref.7

Mutagenesis

160

1

D → N or S: Reduced trans-glucosylation activity by at least 260-fold and reduced UDP-glucose hydrolytic activity by 4 to 14-fold. Ref.9

Mutagenesis

163

1

D → N: Loss of self-glucosylation activity and ability to trans-glucosylate maltose. Reduced UDP-glucose hydrolytic activity by at least 190-fold. Ref.9

Mutagenesis

163

1

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. Ref.9

Sequence conflict

39

1

T → L AA sequence Ref.4

Sequence conflict

89

1

C → S AA sequence Ref.2

Sequence conflict

98

1

C → L AA sequence Ref.2

Secondary structure

1

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333

Helix Strand Turn

Details...

Beta strand

3 – 12

10

Helix

13 – 28

16

Beta strand

33 – 39

7

Helix

45 – 54

10

Beta strand

56 – 60

5

Helix

71 – 76

6

Helix

78 – 80

3

Helix

81 – 86

6

Helix

87 – 91

5

Beta strand

96 – 101

6

Beta strand

105 – 107

3

Helix

112 – 116

5

Beta strand

119 – 124

6

Beta strand

126 – 128

3

Beta strand

131 – 139

9

Helix

143 – 155

13

Helix

163 – 170

8

Turn

171 – 176

6

Helix

179 – 181

3

Helix

185 – 187

3

Beta strand

188 – 190

3

Helix

193 – 196

4

Helix

198 – 204

7

Helix

205 – 207

3

Beta strand

209 – 212

4

Helix

219 – 221

3

Turn

226 – 229

4

Helix

243 – 255

13

Helix

257 – 261

5

Sequences

	Sequence		Length	Mass (Da)
	P13280 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 7C27F7B428F67571	FASTA	333	37,397
	10 20 30 40 50 60 MTDQAFVTLT TNDAYAKGAL VLGSSLKQHR TSRRLAVLTT PQVSDTMRKA LEIVFDEVIT 70 80 90 100 110 120 VDILDSGDSA HLTLMKRPEL GVTLTKLHCW SLTQYSKCVF MDADTLVLAN IDDLFEREEL 130 140 150 160 170 180 SAAPDPGWPD CFNSGVFVYQ PSVETYNQLL HVASEQGSFD GGDQGLLNTF FNSWATTDIR 190 200 210 220 230 240 KHLPFIYNLS SISIYSYLPA FKAFGANAKV VHFLGQTKPW NYTYDTKTKS VRSEGHDPTM 250 260 270 280 290 300 THPQFLNVWW DIFTTSVVPL LQQFGLVQDT CSYQHVEDVS GAVSHLSLGE TPATTQPFVS 310 320 330 SEERKERWEQ GQADYMGADS FDNIKKKLDT YLQ

References

[1]	"Rabbit skeletal muscle glycogenin. Molecular cloning and production of fully functional protein in Escherichia coli." Viskupic E., Cao Y., Zhang W., Cheng C., Depaoli-Roach A.A., Roach P.J. J. Biol. Chem. 267:25759-25763(1992) [PubMed: 1281472] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Skeletal muscle.
[2]	"The amino acid sequence of rabbit skeletal muscle glycogenin." Campbell D.G., Cohen P. Eur. J. Biochem. 185:119-125(1989) [PubMed: 2806254] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-333. Strain: New Zealand white. Tissue: Skeletal muscle.
[3]	"Structural and functional studies on rabbit liver glycogenin." Smythe C., Villar-Palasi C., Cohen P. Eur. J. Biochem. 183:205-209(1989) [PubMed: 2526735] [Abstract] Cited for: PROTEIN SEQUENCE OF 35-48; 182-202; 210-227 AND 308-325. Tissue: Liver.
[4]	"The occurrence of serine phosphate in glycogenin: a possible regulatory site." Lomako J., Whelan W.J. BioFactors 1:261-264(1988) [PubMed: 3151442] [Abstract] Cited for: PROTEIN SEQUENCE OF 35-48, PHOSPHORYLATION.
[5]	"Tyrosine-194 of glycogenin undergoes autocatalytic glucosylation but is not essential for catalytic function and activity." Alonso M.D., Lomako J., Lomako W.M., Whelan W.J. FEBS Lett. 342:38-42(1994) [PubMed: 8143846] [Abstract] Cited for: CHARACTERIZATION.
[6]	"Mechanism of glycogenin self-glucosylation." Cao Y., Steinrauf L.K., Roach P.J. Arch. Biochem. Biophys. 319:293-298(1995) [PubMed: 7771798] [Abstract] Cited for: CHARACTERIZATION.
[7]	"Self-glucosylation of glycogenin, the initiator of glycogen biosynthesis, involves an inter-subunit reaction." Lin A., Mu J., Yang J., Roach P.J. Arch. Biochem. Biophys. 363:163-170(1999) [PubMed: 10049511] [Abstract] Cited for: CHARACTERIZATION, MUTAGENESIS OF LYS-86.
[8]	"Crystal structure of the autocatalytic initiator of glycogen biosynthesis, glycogenin." Gibbons B.J., Roach P.J., Hurley T.D. J. Mol. Biol. 319:463-477(2002) [PubMed: 12051921] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH UDP-GLUCOSE AND MANGANESE IONS, SUBUNIT.
[9]	"Requirements for catalysis in mammalian glycogenin." Hurley T.D., Stout S., Miner E., Zhou J., Roach P.J. J. Biol. Chem. 280:23892-23899(2005) [PubMed: 15849187] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS), SUBUNIT, MUTAGENESIS OF ASP-160 AND ASP-163.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L01791 mRNA. Translation: AAA31404.1.

PIR

A45094.

RefSeq

NP_001075710.1. NM_001082241.1.

UniGene

Ocu.1930.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LL0	X-ray	3.43	A/B/C/D/E/F/G/H/I/J	1-333	[»]
1LL2	X-ray	1.90	A	1-333	[»]
1LL3	X-ray	1.90	A	1-333	[»]
1ZCT	X-ray	2.60	A/B	1-270	[»]
1ZCU	X-ray	2.00	A	1-333	[»]
1ZCV	X-ray	1.98	A	1-333	[»]
1ZCY	X-ray	1.99	A	1-333	[»]
1ZDF	X-ray	2.45	A	1-333	[»]
1ZDG	X-ray	2.30	A	1-333	[»]

ProteinModelPortal

P13280.

SMR

P13280. Positions 1-267.

ModBase

Search...

Protein-protein interaction databases

STRING

P13280.

Protein family/group databases

CAZy

GT8. Glycosyltransferase Family 8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

100009058.

Organism-specific databases

CTD

2992.

Phylogenomic databases

eggNOG

maNOG14836.

GeneTree

ENSGT00390000004721.

HOVERGEN

HBG000681.

Enzyme and pathway databases

BRENDA

2.4.1.186. 1749.

Family and domain databases

InterPro

IPR002495. Glyco_trans_8.
[Graphical view]

Pfam

PF01501. Glyco_transf_8. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GLYG_RABIT

Accession

Primary (citable) accession number: P13280

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 96 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program