Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P80607 (UPTG_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

EC=2.4.1.-
Alternative name(s):
Amylogenin
Golgi-associated protein se-wap41
Reversibly glycosylated polypeptide
Short name=RGP
UDP-glucose:protein transglucosylase
Short name=UPTG
Gene names
Name:UPTG
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Possible role in the synthesis of cell wall polysaccharides By similarity.

Catalytic activity

UDP-glucose + protein = UDP + alpha-D-glucosyl-protein. Ref.4

Enzyme regulation

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

Subunit structure

Homopentamer or homohexamer By similarity.

Subcellular location

Secretedcell wall. Cell junctionplasmodesma. Golgi apparatus. Note: Cell wall-associated, with highest concentrations on plasmodesmata. Also located in the Golgi apparatus. Ref.5

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.2

Sequence similarities

Belongs to the RGP family.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
Cellulose biosynthesis
   Cellular componentCell junction
Cell wall
Golgi apparatus
Secreted
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processUDP-L-arabinose metabolic process

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

cellulose biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

plant-type cell wall organization or biogenesis

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

pollen development

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

response to cadmium ion

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

response to salt stress

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Cellular_componentGolgi trans cisterna

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

cell wall

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosolic ribosome

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

plasmodesma

Inferred from electronic annotation. Source: UniProtKB-SubCell

vacuolar membrane

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Molecular_functionintramolecular transferase activity

Inferred from electronic annotation. Source: InterPro

transferase activity, transferring glycosyl groups

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 364364Alpha-1,4-glucan-protein synthase [UDP-forming]
PRO_0000221193

Regions

Motif110 – 1123DXD motif

Sites

Site1581Required for activity By similarity
Site1651Required for activity By similarity

Amino acid modifications

Glycosylation1581N-linked (Glc...)

Experimental info

Sequence conflict401A → P AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P80607 [UniParc].

Last modified September 9, 2003. Version 2.
Checksum: 00CEC4FD30378D0C

FASTA36441,204
        10         20         30         40         50         60 
MAGTVTVPGS STPSTPLLKD ELDIVIPTIR NLDFLEMWRA FFQPYHLIIV QDGDPTKTIK 

        70         80         90        100        110        120 
VPEGFDYELY NRNDINRILG PKASCISFKD SACRCFGYMV SKKKYIYTID DDCFVAKDPS 

       130        140        150        160        170        180 
GKDINALEQH IKNLLSPSTP FFFNTLYDPY REGADFVRGY PFSLREGAHT AVSHGLWLNI 

       190        200        210        220        230        240 
PDYDAPTQLV KPKERNERYV DAVMTIPKGT LFPMCGMNLA FDRDLIGPAM YFGLMGDGQP 

       250        260        270        280        290        300 
IGRYDDMWAG WCVKVICDHL SLGVKTGLPY IWHSKASNPF VNLKKEYKGI FWQEDIIPFF 

       310        320        330        340        350        360 
QNVTIPKDCD TVQKCYIYLS GQVKEKLGTI DPYFVKLGDA MVTWIEAWDE LNPSTPAAAN 


GKAK 

« Hide

References

[1]"Isolation of a maize 41 kDa Golgi associated protein."
Katz A., Van Lent J.W.M., Kotlizky G., Yahalom A., Epel B.L.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Jubile.
[2]"Beta-glucosylarginine: a new glucose-protein bond in a self-glucosylating protein from sweet corn."
Singh D.G., Lomako J., Lomako W.M., Whelan W.J., Meyer H.E., Serwe M., Metzger J.W.
FEBS Lett. 376:61-64(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 31-57; 133-193; 199-208; 244-254; 289-307 AND 337-359, GLYCOSYLATION.
[3]"The maize two dimensional gel protein database: towards an integrated genome analysis program."
Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., Pernollet J.-C., Zivy M., de Vienne D.
Theor. Appl. Genet. 93:997-1005(1996) [AGRICOLA] [Europe PMC]
Cited for: PROTEIN SEQUENCE OF 61-75.
Tissue: Coleoptile.
[4]"UDP-glucose:protein transglucosylase in developing maize endosperm."
Rothschild A., Tandecarz J.S.
Plant Sci. 97:119-127(1994)
Cited for: ENZYME ACTIVITY.
[5]"A 41kDa protein isolated from maize mesocotyl cell walls immunolocalizes to plasmodesmata."
Epel B.L., Van Lent J.W.M., Cohen L., Kotlizky G., Katz A., Yahalom A.
Protoplasma 191:70-78(1996)
Cited for: SUBCELLULAR LOCATION.
[6]"Inhibition of UDP-glucose: protein transglucosylase by a maize endosperm protein factor."
Rothschild A., Wald F.A., Bocca S.N., Tandecarz J.S.
Cell. Mol. Biol. 42:645-651(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INHIBITION BY IP.
[7]"Identification of a UPTG inhibitor protein from maize endosperm: high homology with sucrose synthase protein."
Wald F.A., Rothschild A., Moreno S., Tandecarz J.S.
Cell. Mol. Biol. 44:397-406(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INHIBITION BY IP.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U89897 mRNA. Translation: AAB49896.1.
PIRT04331.
RefSeqNP_001105598.1. NM_001112128.1.
UniGeneZm.752.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGT75. Glycosyltransferase Family 75.

Proteomic databases

PRIDEP80607.
ProMEXP80607.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID542592.
KEGGzma:542592.

Organism-specific databases

GrameneP80607.
MaizeGDB123920.
131466.

Phylogenomic databases

HOGENOMHOG000234443.
KOK13379.

Family and domain databases

InterProIPR029044. Nucleotide-diphossugar_trans.
IPR004901. RGP_fam.
[Graphical view]
PfamPF03214. RGP. 1 hit.
[Graphical view]
PIRSFPIRSF016429. UPTG. 1 hit.
SUPFAMSSF53448. SSF53448. 2 hits.
ProtoNetSearch...

Entry information

Entry nameUPTG_MAIZE
AccessionPrimary (citable) accession number: P80607
Secondary accession number(s): Q9SAQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 9, 2003
Last modified: July 9, 2014
This is version 77 of the entry and version 2 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