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Q8RU27 (UPTG2_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 27, 2011. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alpha-1,4-glucan-protein synthase [UDP-forming] 2

EC=2.4.1.-
Alternative name(s):
Reversibly glycosylated polypeptide 2
Short name=RGP2
UDP-glucose:protein transglucosylase 2
Short name=UPTG 2
Gene names
Name:UPTG2
OrganismSolanum tuberosum (Potato)
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

Protein attributes

Sequence length366 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Possible role in the synthesis of cell wall polysaccharides. Ref.1

Catalytic activity

UDP-glucose + protein = UDP + alpha-D-glucosyl-protein. Ref.2

Cofactor

Divalent cations. Manganese or magnesium are the most effective while cobalt only has a slight effect. Manganese enhances glycosylation by UDP-glucose and UDP-xylose but inhibits glycosylation by UDP-galactose.

Enzyme regulation

Inhibited by inhibitor protein (IP) which may be a form of sucrose synthase By similarity.

Subunit structure

Homopentamer or homohexamer. Ref.4

Subcellular location

Secretedcell wall By similarity. Cell junctionplasmodesma By similarity. Golgi apparatus By similarity. Note: Cell wall-associated, with highest concentrations on plasmodesmata. Also located in the Golgi apparatus By similarity.

Tissue specificity

Expressed in all tissues tested, including root, tuber, leaf, petiole, shoot, stolon and stem. Ref.1

Domain

The conserved DXD motif is involved in enzyme activity By similarity.

Post-translational modification

Reversibly glycosylated by UDP-glucose, UDP-xylose and UDP-galactose, but not UDP-mannose. Ref.1 Ref.3 Ref.4 UniProtKB O04300

Sequence similarities

Belongs to the RGP family.

Biophysicochemical properties

Kinetic parameters:

KM=0.7 µM for UDP-glucose

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 366366Alpha-1,4-glucan-protein synthase [UDP-forming] 2
PRO_0000221196

Regions

Motif104 – 1063DXD motif

Sites

Site1521Required for activity By similarity
Site1591Required for activity By similarity

Amino acid modifications

Glycosylation1521N-linked (Glc...) By similarity UniProtKB Q9SAQ2

Sequences

Sequence LengthMass (Da)Tools
Q8RU27 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 65816F41ACD6F581

FASTA36641,603
        10         20         30         40         50         60 
MAGSSVTPTP LLKDELDIVI PTIRNLDFLE MWRPFFQPYH LIIVQDGDPS KIINVPEGFD 

        70         80         90        100        110        120 
YELYNRNDIN RILGPKASCI SFKDSACRCF GYMVSKKKYI YTIDDDCFVA KDPSGKDINA 

       130        140        150        160        170        180 
LEQHIKNLLC PSTPHFFNTL YDPYREGADF VRGYPFSMRE GAATAVSHGL WLNIPDYDAP 

       190        200        210        220        230        240 
TQLVKPRERN TRYVDAVMTI PKGTLFPMCG MNLAFDRELI GPAMYFGLMG DGQPIGRYDD 

       250        260        270        280        290        300 
MWAGWCIKVI CDHLGLGVKT GLPYIWHSKA SNPFVNLKKE YKGIYWQEEI IPFSQSATLP 

       310        320        330        340        350        360 
KDCTSVQQCY LELSKQVKEK LSTIDPYFTK LADAMVTWIE AWDELNPTGE GLAKLPSRTA 


PESRLH 

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References

[1]"Molecular cloning and characterization of the enzyme UDP-glucose:protein transglucosylase from potato."
Bocca S.N., Kissen R., Rojas-Beltran J.A., Noel F., Gebhardt C., Moreno S., du Jardin P., Tandecarz J.S.
Plant Physiol. Biochem. 37:809-819(1999) [PubMed: 10580281] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 99-113, GLYCOSYLATION, TISSUE SPECIFICITY.
Tissue: Stolon tip.
[2]"Alpha-glucan synthesis on a protein primer, uridine diphosphoglucose: protein transglucosylase I. Separation from starch synthetase and phosphorylase and a study of its properties."
Moreno S., Cardini C.E., Tandecarz J.S.
Eur. J. Biochem. 157:539-545(1986) [PubMed: 2941300] [Abstract]
Cited for: ENZYME ACTIVITY.
[3]"Potato tuber UDP-glucose:protein transglucosylase catalyzes its own glucosylation."
Ardila F.J., Tandecarz J.S.
Plant Physiol. 99:1342-1347(1992) [PubMed: 16669042] [Abstract]
Cited for: GLYCOSYLATION.
[4]"Initiation of starch biosynthesis: purification and characterization of UDP-glucose:protein transglucosylase from potato tubers."
Bocca S.N., Rothschild A., Tandecarz J.S.
Plant Physiol. Biochem. 35:205-212(1997)
Cited for: GLYCOSYLATION, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ310910 mRNA. Translation: CAC84517.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGT75. Glycosyltransferase Family 75.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.4.1.112. 5757.

Family and domain databases

InterProIPR004901. UPTG_synth.
[Graphical view]
PfamPF03214. RGP. 1 hit.
[Graphical view]
PIRSFPIRSF016429. UPTG. 1 hit.
ProtoNetSearch...

Entry information

Entry nameUPTG2_SOLTU
AccessionPrimary (citable) accession number: Q8RU27
Entry history
Integrated into UniProtKB/Swiss-Prot: September 9, 2003
Last sequence update: June 1, 2002
Last modified: July 27, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families