Reviewed, UniProtKB/Swiss-Prot Q8RU27 (UPTG2_SOLTU)

Names and origin

Protein names

Recommended name:
    Alpha-1,4-glucan-protein synthase [UDP-forming] 2
    EC=2.4.1.-
Alternative name(s):
    UDP-glucose:protein transglucosylase 2
      Short name=UPTG 2

Gene names

Name:

UPTG2

Organism

Solanum tuberosum (Potato)

Taxonomic identifier

4113 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum

Protein attributes

Sequence length	366 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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	Secreted › cell wall By similarity. Cell junction › plasmodesma 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
Post-translational modification	Reversibly glycosylated by UDP-glucose, UDP-xylose and UDP-galactose, but not UDP-mannose. Ref.4 Ref.1 Ref.3 UniProtKB O04300
Sequence similarities	Belongs to the RGP family.
biophysicochemical properties	Kinetic parameters: KM=0.7 µM for UDP-glucose

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation Cellulose biosynthesis
Cellular component	Cell junction Cell wall Golgi apparatus Secreted
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW cellulose biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell plant-type cell wall Inferred from electronic annotation. Source: InterPro plasmodesma Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	transferase activity, transferring hexosyl groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 366	366	Alpha-1,4-glucan-protein synthase [UDP-forming] 2		PRO_0000221196
Amino acid modifications
	Glycosylation	152	1	N-linked (Glc...) By similarity UniProtKB Q9SAQ2

Sequences

	Sequence		Length	Mass (Da)
	Q8RU27-1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 65816F41ACD6F581	FASTA	366	41,603
	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

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
EMBLGenBankDDBJ	AJ310910 mRNA. Translation: CAC84517.1.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GT75. Glycosyltransferase Family 75.
Enzyme and pathway databases
BRENDA	2.4.1.112. 296.
Family and domain databases
InterPro	IPR004901. UPTG_synth. [Graphical view]
Pfam	PF03214. RGP. 1 hit. [Graphical view]
PIRSF	PIRSF016429. UPTG. 1 hit.
ProtoNet	Search...

Entry information

Entry name

UPTG2_SOLTU

Accession

Primary (citable) accession number: Q8RU27

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 9, 2003
Last sequence update:	June 1, 2002
Last modified:	June 16, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)