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Entry version 44 (16 Oct 2019)
Sequence version 1 (10 May 2005)
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Protein

RxLR effector protein Avr3a

Gene

Avr3a

Organism
Phytophthora infestans (Potato late blight fungus) (Botrytis infestans)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Multifunctional effector that can suppress host BAK1/SERK3-mediated immunity through at least two different pathways (PubMed:19794118, PubMed:20457921, PubMed:21348873, PubMed:26348328). Manipulates plant immunity by targeting and stabilizing host E3 ligase CMPG1. Preventing the normal 26S proteasome-dependent degradation of potato CMPG1, and thus potentially of its protein substrates in the host cell, further abolishes host cell death during the biotrophic phase of infection (PubMed:19794118, PubMed:20457921, PubMed:21348873). Associates with and affects also the function of the dynamin-related protein 2 (DRP2), a plant GTPase involved in immune receptor-mediated endocytosis (PubMed:26348328). The Avr3a(EM) form evades recognition by R3a, thus does not trigger R3a-mediated hypersensitivity and does not suppress INF1-induced cell death (PubMed:15894622, PubMed:16965554, PubMed:19245321).7 Publications

Miscellaneous

The AVR3a protein of Phytophthora infestans is a polymorphic member of the RXLR class of cytoplasmic effectors with dual functions. AVR3a(KI) but not AVR3a(EM) activates innate immunity triggered by the potato resistance protein R3a and is a strong suppressor of the cell-death response induced by INF1 elicitin, a secreted P.infestans protein that has features of pathogen-associated molecular patterns. The 2 polymorphic residues between Avr3A(KI) and Avr3a(EM) are localized at positions 80 and 103, respectively.2 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processVirulence

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
RxLR effector protein Avr3a1 Publication
Alternative name(s):
Avirulence protein 3a1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Avr3a1 Publication
Synonyms:Avr3a(EM)1 Publication, Pex1471 Publication, PexRD71 Publication
ORF Names:PI35.0050, PI49.0530
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiPhytophthora infestans (Potato late blight fungus) (Botrytis infestans)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri4787 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaStramenopilesOomycetesPeronosporalesPeronosporaceaePhytophthora

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Host cytoplasm, Secreted

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 21Sequence analysisAdd BLAST21
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_501353196022 – 147RxLR effector protein Avr3aAdd BLAST126

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei48N6-acetyllysine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Proteolytically cleaved. The cleavage site directly after the RxLR sequence and the high conservation among other effector proteins suggest that the RxLR motif might play a crucial role in the intracellular processing before secretion.1 Publication
glycosylated.1 Publication
N-acetylated at Lys-48 after cleavage.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei47 – 48Cleavage1 Publication2

Keywords - PTMi

Acetylation, Glycoprotein

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q572D3

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression is induced during host plant infection.2 Publications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Forms homodimers via the RxLR-dEER motif (PubMed:22977236).

Interacts with host E3 ligase CMPG1 (PubMed:20457921).

Interacts with host DRP2 (PubMed:26348328).

3 Publications

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q572D3

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni77 – 147Effector domainBy similarityAdd BLAST71

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi44 – 59RxLR-dEER1 PublicationAdd BLAST16

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The RxLR-dEER motif is required for the delivery of the effector to the host cell cytoplasm but does not bind phosphatidylinositol monophosphates (PubMed:17914356, PubMed:22977236). The motif is cleaved after the RxLR sequence (PubMed:28522546). The RxLR motif (residues 44 to 47) plays a crucial role in the intracellular processing before secretion (PubMed:28522546). The Glu-rich part localized just after the cleavage site (residues 48 to 59) is required for homodimerization (PubMed:28522546).3 Publications
The conserved, positively charged effector domain (residues 77 to 147), rather than the RXLR domain, is required for binding to phosphatidylinositol monophosphates (PIPs). PIP binding is necessary for accumulation of CMPG1 and Avr3a in host plants.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the RxLR effector family.Curated

Keywords - Domaini

Signal

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR031825 RXLR

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16810 RXLR, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q572D3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRLAIMLSAT AVAINFATSS AIDQTKVLVY GTPAHYIHDS AGRRLLRKNE
60 70 80 90 100
ENEETSEERA PNFNLANLNE EMFNVAALTE RADAKKLAKQ LMGNDKLADA
110 120 130 140
AYMWWQHNRV TLDQIDTFLK LASRKTQGAK YNQIYNSYMM HLGLTGY
Length:147
Mass (Da):16,661
Last modified:May 10, 2005 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i24CD19EADC7B8B39
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
GU258052 Genomic DNA Translation: ADC96691.1
HQ639930 Genomic DNA Translation: AEH27535.1
JN849402 Genomic DNA Translation: AFQ32411.1
JN849403 Genomic DNA Translation: AFQ32412.1
JN849404 Genomic DNA Translation: AFQ32413.1
JN849405 Genomic DNA Translation: AFQ32414.1
JN849406 Genomic DNA Translation: AFQ32415.1
JN849407 Genomic DNA Translation: AFQ32416.1
KF154421 Genomic DNA Translation: AGV54925.1
KF154423 Genomic DNA Translation: AGV54927.1
KF154424 Genomic DNA Translation: AGV54928.1
KF154429 Genomic DNA Translation: AGV54933.1
KF154430 Genomic DNA Translation: AGV54934.1
KP317569 Genomic DNA Translation: AKH40250.1
KP317575 Genomic DNA Translation: AKH40255.1
KP317576 Genomic DNA Translation: AKH40256.1
KP317585 Genomic DNA Translation: AKH40263.1
MH043151 Genomic DNA Translation: AXU25232.1
MH043159 Genomic DNA Translation: AXU25240.1
MH043178 Genomic DNA Translation: AXU25259.1
MH043185 Genomic DNA Translation: AXU25266.1
MG976602 Genomic DNA Translation: AYP64705.1
MG976603 Genomic DNA Translation: AYP64706.1
MG976604 Genomic DNA Translation: AYP64707.1
AJ893356 Genomic DNA Translation: CAI72254.1
AJ893357 Genomic DNA Translation: CAI72345.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GU258052 Genomic DNA Translation: ADC96691.1
HQ639930 Genomic DNA Translation: AEH27535.1
JN849402 Genomic DNA Translation: AFQ32411.1
JN849403 Genomic DNA Translation: AFQ32412.1
JN849404 Genomic DNA Translation: AFQ32413.1
JN849405 Genomic DNA Translation: AFQ32414.1
JN849406 Genomic DNA Translation: AFQ32415.1
JN849407 Genomic DNA Translation: AFQ32416.1
KF154421 Genomic DNA Translation: AGV54925.1
KF154423 Genomic DNA Translation: AGV54927.1
KF154424 Genomic DNA Translation: AGV54928.1
KF154429 Genomic DNA Translation: AGV54933.1
KF154430 Genomic DNA Translation: AGV54934.1
KP317569 Genomic DNA Translation: AKH40250.1
KP317575 Genomic DNA Translation: AKH40255.1
KP317576 Genomic DNA Translation: AKH40256.1
KP317585 Genomic DNA Translation: AKH40263.1
MH043151 Genomic DNA Translation: AXU25232.1
MH043159 Genomic DNA Translation: AXU25240.1
MH043178 Genomic DNA Translation: AXU25259.1
MH043185 Genomic DNA Translation: AXU25266.1
MG976602 Genomic DNA Translation: AYP64705.1
MG976603 Genomic DNA Translation: AYP64706.1
MG976604 Genomic DNA Translation: AYP64707.1
AJ893356 Genomic DNA Translation: CAI72254.1
AJ893357 Genomic DNA Translation: CAI72345.1

3D structure databases

SMRiQ572D3
ModBaseiSearch...

PTM databases

iPTMnetiQ572D3

Family and domain databases

InterProiView protein in InterPro
IPR031825 RXLR
PfamiView protein in Pfam
PF16810 RXLR, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiA3AEM_PHYIN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q572D3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 8, 2019
Last sequence update: May 10, 2005
Last modified: October 16, 2019
This is version 44 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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