W2PDG1 · XLP1_PHYN3

Function

function

Non-functional secreted XEG1-like protein that binds to host Nicotiana benthamiana apoplastic glucanase inhibitor protein GIP2 more tightly than does XEG1, thus it outcompetes XEG1 for GIP2 binding and frees functional XEG1 to support P.parasitica infection (PubMed:28082413).
With XEG1, is required to elevate apoplastic sugar during P.parasitica infection (PubMed:28082413).

Caution

In contrast to its ortholog from P.sojae, still has the conserved Glu residue in position 222 essential activity, but, as for P.sojae XLP1, does not show xyloglucanase activity.

Features

Showing features for active site.

123820406080100120140160180200220
TypeIDPosition(s)Description
Active site133
Active site219

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular region
Molecular Functioncellulase activity
Biological Processpolysaccharide catabolic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Inactive glycoside hydrolase XLP1
  • Alternative names
    • Glycoside hydrolase family 12 protein XLP1
      (GH12 protein XLP1
      )
    • XEG1-like protein 1

Gene names

    • Name
      XLP1
    • ORF names
      PPTG_19378

Organism names

Accessions

  • Primary accession
    W2PDG1

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis25Affects the binding to host GIP2 and relieves GIP2 inhibition of XEG1-induced sugar elevation; when associated with A-39, A-41, A-42, A-43, A-44, A-77 and A-78.
Mutagenesis38Affects the binding to host GIP2 and relieves GIP2 inhibition of XEG1-induced sugar elevation; when associated with A-26, A-41, A-42, A-43, A-44, A-77 and A-78.
Mutagenesis40Affects the binding to host GIP2 and relieves GIP2 inhibition of XEG1-induced sugar elevation; when associated with A-26, A-39, A42, A-43, A-44, A-77 and A-78.
Mutagenesis41Affects the binding to host GIP2 and relieves GIP2 inhibition of XEG1-induced sugar elevation; when associated with A-26, A-39, A-41, A-43, A-44, A-77 and A-78.
Mutagenesis42Affects the binding to host GIP2 and relieves GIP2 inhibition of XEG1-induced sugar elevation; when associated with A-26, A-39, A-41, A-42, A-44, A-77 and A-78.
Mutagenesis43Affects the binding to host GIP2 and relieves GIP2 inhibition of XEG1-induced sugar elevation; when associated with A-26, A-39, A-41, A-42, A-43, A-77 and A-78.
Mutagenesis75Affects the binding to host GIP2 and relieves GIP2 inhibition of XEG1-induced sugar elevation; when associated with A-26, A-39, A-41, A-42, A-43, A-44 and A-78.
Mutagenesis76Affects the binding to host GIP2 and relieves GIP2 inhibition of XEG1-induced sugar elevation; when associated with A-26, A-39, A-41, A-42, A-43, A-44 and A-77.

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-19
ChainPRO_500482194220-238Inactive glycoside hydrolase XLP1
Glycosylation171N-linked (GlcNAc...) asparagine
Glycosylation187N-linked (GlcNAc...) asparagine

Keywords

PTM databases

Interaction

Subunit

Interacts with host apoplastic glucanase inhibitor GIP2.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    238
  • Mass (Da)
    25,545
  • Last updated
    2014-03-19 v1
  • Checksum
    65F8BA5CC9C5A2D8
MKSFLIAIVIAVLLPVSAADFCAQWRLSKAGKYIIYNNLWNQNTATSGSQCTGVDKVSGSTVAWHTSYSWAGAPTQVKSYSNAALVFTKKQIKNIKTIPTTMKYSYSYSGTLIADVAYDLFTSSTASGSNEYEIMIWLAAYGGAGPISSTGKAIATVTINSNSFKLYKGPNGSTTVYSFVATKTITNFSADLLDFFTYLVKTQAFPSSQYLTTLEAGTEPFTGSNAKMTVSSYSAAVN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KI669674
EMBL· GenBank· DDBJ
ETM98685.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp