AVR1_PHYIT
ID AVR1_PHYIT Reviewed; 208 AA.
AC D0NVB5;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=RxLR effector protein Avr1 {ECO:0000303|PubMed:25760731};
DE AltName: Full=Avirulence protein 1 {ECO:0000303|PubMed:12000683};
DE Flags: Precursor;
GN Name=Avr1 {ECO:0000303|PubMed:12000683}; ORFNames=PITG_16663;
OS Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=403677;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND INDUCTION.
RC STRAIN=T30-4;
RX PubMed=19741609; DOI=10.1038/nature08358;
RG The Broad Institute Genome Sequencing Platform;
RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA Nusbaum C.;
RT "Genome sequence and analysis of the Irish potato famine pathogen
RT Phytophthora infestans.";
RL Nature 461:393-398(2009).
RN [2]
RP FUNCTION.
RX PubMed=12000683; DOI=10.1046/j.1365-313x.2001.01292.x;
RA Ballvora A., Ercolano M.R., Weiss J., Meksem K., Bormann C.A.,
RA Oberhagemann P., Salamini F., Gebhardt C.;
RT "The R1 gene for potato resistance to late blight (Phytophthora infestans)
RT belongs to the leucine zipper/NBS/LRR class of plant resistance genes.";
RL Plant J. 30:361-371(2002).
RN [3]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=25760731; DOI=10.1111/nph.13355;
RA Du Y., Berg J., Govers F., Bouwmeester K.;
RT "Immune activation mediated by the late blight resistance protein R1
RT requires nuclear localization of R1 and the effector AVR1.";
RL New Phytol. 207:735-747(2015).
RN [4]
RP FUNCTION, DOMAIN, INTERACTION WITH HOST SEC5, AND MUTAGENESIS OF
RP 171-LEU--PHE-208.
RX PubMed=26336092; DOI=10.1104/pp.15.01169;
RA Du Y., Mpina M.H., Birch P.R., Bouwmeester K., Govers F.;
RT "Phytophthora infestans RXLR effector AVR1 interacts with exocyst component
RT Sec5 to manipulate plant immunity.";
RL Plant Physiol. 169:1975-1990(2015).
RN [5]
RP INDUCTION.
RX PubMed=29312401; DOI=10.3389/fpls.2017.02155;
RA Yin J., Gu B., Huang G., Tian Y., Quan J., Lindqvist-Kreuze H., Shan W.;
RT "Conserved RXLR effector genes of Phytophthora infestans expressed at the
RT early stage of potato infection are suppressive to host defense.";
RL Front. Plant Sci. 8:2155-2155(2017).
RN [6]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF 70-LYS--ARG-92; 111-LYS--PHE-136;
RP 137-ASP--LYS-157 AND 158-LYS--LEU-170.
RX PubMed=29910515; DOI=10.1016/j.simyco.2018.01.003;
RA Du Y., Weide R., Zhao Z., Msimuko P., Govers F., Bouwmeester K.;
RT "RXLR effector diversity in Phytophthora infestans isolates determines
RT recognition by potato resistance proteins; the case study AVR1 and R1.";
RL Stud. Mycol. 89:85-93(2018).
RN [7]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=30329083; DOI=10.1093/jxb/ery360;
RA Wang S., McLellan H., Bukharova T., He Q., Murphy F., Shi J., Sun S.,
RA van Weymers P., Ren Y., Thilliez G., Wang H., Chen X., Engelhardt S.,
RA Vleeshouwers V., Gilroy E.M., Whisson S.C., Hein I., Wang X., Tian Z.,
RA Birch P.R.J., Boevink P.C.;
RT "Phytophthora infestans RXLR effectors act in concert at diverse
RT subcellular locations to enhance host colonization.";
RL J. Exp. Bot. 70:343-356(2019).
CC -!- FUNCTION: Secreted effector that acts as an elicitor of hypersensitive
CC response (HR) specifically on plants carrying defense protein R1,
CC through its interaction with this protein (PubMed:12000683,
CC PubMed:25760731, PubMed:29910515). Acts also as a virulence factor that
CC promotes colonization and suppresses cell death induced by CRN2 as well
CC as callose deposition, a hallmark of basal defense (PubMed:26336092,
CC PubMed:30329083). Interacts with host exocyst component Sec5 and
CC thereby disturbs vesicle trafficking, a cellular process that is
CC important for basal defense. By targeting and stabilizing Sec5 in the
CC cytoplasm, the exocyst complex is thus out of balance and not able to
CC mediate the focal secretion of PR-1 and callose (PubMed:26336092).
CC {ECO:0000269|PubMed:12000683, ECO:0000269|PubMed:25760731,
CC ECO:0000269|PubMed:26336092, ECO:0000269|PubMed:29910515,
CC ECO:0000269|PubMed:30329083}.
CC -!- SUBUNIT: Interacts with host exocyst component Sec5.
CC {ECO:0000269|PubMed:26336092}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25760731,
CC ECO:0000269|PubMed:30329083}. Host cytoplasm
CC {ECO:0000269|PubMed:25760731, ECO:0000269|PubMed:30329083}. Host
CC nucleus {ECO:0000269|PubMed:25760731, ECO:0000269|PubMed:30329083}.
CC Host peroxisome {ECO:0000269|PubMed:30329083}. Note=Nuclear-localized
CC Avr1 triggers the R1-mediated HR, whereas cytoplasmic localization is
CC required for suppression of CRN2-induced cell death (PubMed:25760731).
CC Also localized at Sec5-associated subcellular bodies (PubMed:30329083).
CC {ECO:0000269|PubMed:25760731, ECO:0000269|PubMed:30329083}.
CC -!- INDUCTION: Expression is induced during host plant infection.
CC {ECO:0000269|PubMed:19741609, ECO:0000269|PubMed:29312401}.
CC -!- DOMAIN: The RxLR-dEER motif acts to carry the protein into the host
CC cell cytoplasm through binding to cell surface phosphatidylinositol-3-
CC phosphate. {ECO:0000305|PubMed:29312401}.
CC -!- DOMAIN: The C-terminal domain of Avr1 comprises three motifs (W1, W2,
CC and Y), two linker regions (ln1 and ln2), and at the very end the T-
CC region. The T-region of AVR1 is important but not sufficient to trigger
CC R1-mediated HR and W1, W2 and Y are equally important for recognition
CC by R1. {ECO:0000269|PubMed:26336092, ECO:0000269|PubMed:29910515}.
CC -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR EMBL; DS028168; EEY66592.1; -; Genomic_DNA.
DR RefSeq; XP_002896893.1; XM_002896847.1.
DR AlphaFoldDB; D0NVB5; -.
DR SMR; D0NVB5; -.
DR EnsemblProtists; PITG_16663T0; PITG_16663T0; PITG_16663.
DR GeneID; 9465293; -.
DR KEGG; pif:PITG_16663; -.
DR VEuPathDB; FungiDB:PITG_16663; -.
DR eggNOG; ENOG502RGGT; Eukaryota.
DR HOGENOM; CLU_1323178_0_0_1; -.
DR InParanoid; D0NVB5; -.
DR OMA; IGNMVGL; -.
DR OrthoDB; 1530934at2759; -.
DR PHI-base; PHI:5113; -.
DR Proteomes; UP000006643; Partially assembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Host cytoplasm; Host nucleus; Reference proteome; Repeat; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..208
FT /note="RxLR effector protein Avr1"
FT /id="PRO_5003013687"
FT REGION 70..92
FT /note="W1-motif"
FT /evidence="ECO:0000305|PubMed:26336092"
FT REGION 93..110
FT /note="Linker region ln1"
FT /evidence="ECO:0000305|PubMed:26336092"
FT REGION 111..136
FT /note="W2-motif"
FT /evidence="ECO:0000305|PubMed:26336092"
FT REGION 137..157
FT /note="Y-motif"
FT /evidence="ECO:0000305|PubMed:26336092"
FT REGION 158..170
FT /note="Linker region ln2"
FT /evidence="ECO:0000305|PubMed:26336092"
FT REGION 170..208
FT /note="T-region"
FT /evidence="ECO:0000305|PubMed:26336092"
FT MOTIF 41..54
FT /note="RxLR-dEER"
FT /evidence="ECO:0000305|PubMed:29312401"
FT MUTAGEN 70..92
FT /note="Missing: Does not abolish the recognition of Avr1 by
FT host R1."
FT /evidence="ECO:0000269|PubMed:29910515"
FT MUTAGEN 111..136
FT /note="Missing: Abolishes the recognition of Avr1 by host
FT R1."
FT /evidence="ECO:0000269|PubMed:29910515"
FT MUTAGEN 137..157
FT /note="Missing: Abolishes the recognition of Avr1 by host
FT R1."
FT /evidence="ECO:0000269|PubMed:29910515"
FT MUTAGEN 158..170
FT /note="Missing: Abolishes the recognition of Avr1 by host
FT R1."
FT /evidence="ECO:0000269|PubMed:29910515"
FT MUTAGEN 170..208
FT /note="Missing: Loses the virulence function, but also the
FT ability to suppress CRN2-induced cell death and to interact
FT with Sec5."
FT /evidence="ECO:0000269|PubMed:26336092"
SQ SEQUENCE 208 AA; 23420 MW; 995A5BEC2D3E718C CRC64;
MGLMHRVLLL ATFALLCMHA KAAGFDHDKV PRTVERGGGA RQLRTATMSD DEARVSKLPS
FIESFVKNRK IESWIQNKVT DDFVLSELKL VRLPGTSLAD DPNFKLFQKF KIGGWLEEKA
TTTKAWENLG LDSLPFDQVS KIDEFKTYTQ YVTVLNKKAS KLDIDQWHGL LSGGSPEELM
AKAMILRTLG RDVLERRVML GGHVVVPF
