ABLB1_PHYIT
ID ABLB1_PHYIT Reviewed; 152 AA.
AC D0P3S7;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=RxLR effector protein Avrblb1 {ECO:0000303|PubMed:19794118};
DE AltName: Full=Avirulence protein Avrblb1 {ECO:0000303|PubMed:19794118};
DE AltName: Full=In planta-induced protein O1 {ECO:0000303|PubMed:8125319};
DE Short=IPI-O1 {ECO:0000303|PubMed:8125319};
DE Flags: Precursor;
GN Name=Avrblb1 {ECO:0000303|PubMed:19794118};
GN Synonyms=IpiO1 {ECO:0000303|PubMed:8125319},
GN PexRD6 {ECO:0000303|PubMed:19794118}; ORFNames=PITG_21388;
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 IDENTIFICATION, AND INDUCTION.
RX PubMed=8125319; DOI=10.1016/0378-1119(94)90784-6;
RA Pieterse C.M., van West P., Verbakel H.M., Brasse P.W.,
RA van den Berg-Velthuis G.C., Govers F.;
RT "Structure and genomic organization of the ipiB and ipiO gene clusters of
RT Phytophthora infestans.";
RL Gene 138:67-77(1994).
RN [3]
RP DOMAIN, FUNCTION, MUTAGENESIS OF ASP-56, AND SUBCELLULAR LOCATION.
RX PubMed=14999409; DOI=10.1007/s00018-003-3394-z;
RA Senchou V., Weide R., Carrasco A., Bouyssou H., Pont-Lezica R., Govers F.,
RA Canut H.;
RT "High affinity recognition of a Phytophthora protein by Arabidopsis via an
RT RGD motif.";
RL Cell. Mol. Life Sci. 61:502-509(2004).
RN [4]
RP DOMAIN, AND INTERACTION WITH HOST LECRK19.
RX PubMed=16361528; DOI=10.1104/pp.105.066464;
RA Gouget A., Senchou V., Govers F., Sanson A., Barre A., Rouge P.,
RA Pont-Lezica R., Canut H.;
RT "Lectin receptor kinases participate in protein-protein interactions to
RT mediate plasma membrane-cell wall adhesions in Arabidopsis.";
RL Plant Physiol. 140:81-90(2006).
RN [5]
RP INDUCTION, AND DOMAIN.
RX PubMed=17914356; DOI=10.1038/nature06203;
RA Whisson S.C., Boevink P.C., Moleleki L., Avrova A.O., Morales J.G.,
RA Gilroy E.M., Armstrong M.R., Grouffaud S., van West P., Chapman S.,
RA Hein I., Toth I.K., Pritchard L., Birch P.R.;
RT "A translocation signal for delivery of oomycete effector proteins into
RT host plant cells.";
RL Nature 450:115-118(2007).
RN [6]
RP FUNCTION.
RX PubMed=18682852; DOI=10.1371/journal.pone.0002875;
RA Vleeshouwers V.G., Rietman H., Krenek P., Champouret N., Young C., Oh S.K.,
RA Wang M., Bouwmeester K., Vosman B., Visser R.G., Jacobsen E., Govers F.,
RA Kamoun S., Van der Vossen E.A.;
RT "Effector genomics accelerates discovery and functional profiling of potato
RT disease resistance and phytophthora infestans avirulence genes.";
RL PLoS ONE 3:E2875-E2875(2008).
RN [7]
RP DOMAIN, INTERACTION WITH HOST RGA2/RPI-BLB1, AND FUNCTION.
RX PubMed=19888819; DOI=10.1094/mpmi-22-12-1535;
RA Champouret N., Bouwmeester K., Rietman H., van der Lee T., Maliepaard C.,
RA Heupink A., van de Vondervoort P.J., Jacobsen E., Visser R.G.,
RA van der Vossen E.A., Govers F., Vleeshouwers V.G.;
RT "Phytophthora infestans isolates lacking class I ipiO variants are virulent
RT on Rpi-blb1 potato.";
RL Mol. Plant Microbe Interact. 22:1535-1545(2009).
RN [8]
RP INDUCTION, FUNCTION, AND DOMAIN.
RX PubMed=19794118; DOI=10.1105/tpc.109.068247;
RA Oh S.K., Young C., Lee M., Oliva R., Bozkurt T.O., Cano L.M., Win J.,
RA Bos J.I., Liu H.Y., van Damme M., Morgan W., Choi D., Van der Vossen E.A.,
RA Vleeshouwers V.G., Kamoun S.;
RT "In planta expression screens of Phytophthora infestans RXLR effectors
RT reveal diverse phenotypes, including activation of the Solanum
RT bulbocastanum disease resistance protein Rpi-blb2.";
RL Plant Cell 21:2928-2947(2009).
RN [9]
RP FUNCTION.
RX PubMed=20479869; DOI=10.1371/journal.pone.0010536;
RA Halterman D.A., Chen Y., Sopee J., Berduo-Sandoval J., Sanchez-Perez A.;
RT "Competition between Phytophthora infestans effectors leads to increased
RT aggressiveness on plants containing broad-spectrum late blight
RT resistance.";
RL PLoS ONE 5:E10536-E10536(2010).
RN [10]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF ASP-56.
RX PubMed=21483488; DOI=10.1371/journal.ppat.1001327;
RA Bouwmeester K., de Sain M., Weide R., Gouget A., Klamer S., Canut H.,
RA Govers F.;
RT "The lectin receptor kinase LecRK-I.9 is a novel Phytophthora resistance
RT component and a potential host target for a RXLR effector.";
RL PLoS Pathog. 7:E1001327-E1001327(2011).
RN [11]
RP INTERACTION WITH HOST RPI-BLB1, AND MUTAGENESIS OF LEU-129.
RX PubMed=22438813; DOI=10.1371/journal.ppat.1002595;
RA Chen Y., Liu Z., Halterman D.A.;
RT "Molecular determinants of resistance activation and suppression by
RT Phytophthora infestans effector IPI-O.";
RL PLoS Pathog. 8:E1002595-E1002595(2012).
RN [12]
RP INDUCTION.
RX PubMed=28228125; DOI=10.1186/s12864-017-3585-x;
RA Ah-Fong A.M., Kim K.S., Judelson H.S.;
RT "RNA-seq of life stages of the oomycete Phytophthora infestans reveals
RT dynamic changes in metabolic, signal transduction, and pathogenesis genes
RT and a major role for calcium signaling in development.";
RL BMC Genomics 18:198-198(2017).
RN [13]
RP INDUCTION, FUNCTION, AND DOMAIN.
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 [14]
RP FUNCTION.
RX PubMed=28350531; DOI=10.1094/phyto-06-16-0240-r;
RA Chen Y., Halterman D.A.;
RT "Phytophthora infestans Effectors IPI-O1 and IPI-O4 Each Contribute to
RT Pathogen Virulence.";
RL Phytopathology 107:600-606(2017).
RN [15]
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 RGA2/Rpi-
CC blb1 (PubMed:18682852, PubMed:19888819, PubMed:19794118,
CC PubMed:20479869, PubMed:21483488). Enhances P.infestans colonization of
CC plant hosts Nicotiana benthamiana and potato Solanum bulbocastanum
CC leaves (PubMed:28350531, PubMed:30329083). Associates with host legume-
CC type lectin receptor kinases and disrupts attachments between the host
CC plasma membrane and cell wall (PubMed:14999409, PubMed:21483488).
CC {ECO:0000269|PubMed:14999409, ECO:0000269|PubMed:18682852,
CC ECO:0000269|PubMed:19794118, ECO:0000269|PubMed:19888819,
CC ECO:0000269|PubMed:20479869, ECO:0000269|PubMed:21483488,
CC ECO:0000269|PubMed:28350531, ECO:0000269|PubMed:30329083}.
CC -!- SUBUNIT: Interacts with host defense protein RGA2/Rpi-blb1
CC (PubMed:19888819, PubMed:22438813). Interacts with host legume-type
CC lectin receptor kinase LECRK19 (PubMed:16361528).
CC {ECO:0000269|PubMed:16361528, ECO:0000269|PubMed:19888819,
CC ECO:0000269|PubMed:22438813}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30329083}. Host
CC nucleus, host nucleolus {ECO:0000269|PubMed:30329083}. Host nucleus
CC {ECO:0000269|PubMed:30329083}. Host cell membrane
CC {ECO:0000269|PubMed:14999409}.
CC -!- INDUCTION: Expression is induced during host plant infection.
CC {ECO:0000269|PubMed:17914356, ECO:0000269|PubMed:19741609,
CC ECO:0000269|PubMed:19794118, ECO:0000269|PubMed:28228125,
CC ECO:0000269|PubMed:29312401, ECO:0000269|PubMed:8125319}.
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:17914356}.
CC -!- DOMAIN: The RGD RLK-binding motif is required for binding to host
CC legume-type lectin receptor kinases and disruption of the attachments
CC between the host plasma membrane and cell wall.
CC {ECO:0000269|PubMed:14999409, ECO:0000269|PubMed:16361528,
CC ECO:0000269|PubMed:21483488}.
CC -!- DOMAIN: The conserved W motif is found in already well characterized
CC effectors and is essential for triggering RGA2/Rpi-blb1-mediated cell
CC death. {ECO:0000269|PubMed:19888819}.
CC -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS028419; EEY61733.1; -; Genomic_DNA.
DR RefSeq; XP_002895051.1; XM_002895005.1.
DR AlphaFoldDB; D0P3S7; -.
DR EnsemblProtists; PITG_21388T0; PITG_21388T0; PITG_21388.
DR GeneID; 9466643; -.
DR KEGG; pif:PITG_21388; -.
DR VEuPathDB; FungiDB:PITG_21388; -.
DR eggNOG; ENOG502RGT9; Eukaryota.
DR HOGENOM; CLU_135914_0_0_1; -.
DR OMA; YKSGETP; -.
DR OrthoDB; 1617918at2759; -.
DR Proteomes; UP000006643; Partially assembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Glycoprotein; Host cell membrane; Host membrane; Host nucleus; Membrane;
KW Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..152
FT /note="RxLR effector protein Avrblb1"
FT /id="PRO_5003013206"
FT REGION 99..152
FT /note="W motif"
FT /evidence="ECO:0000305|PubMed:19888819"
FT MOTIF 51..72
FT /note="RxLR-dEER"
FT /evidence="ECO:0000305|PubMed:17914356"
FT MOTIF 54..56
FT /note="RGD RLK-binding motif"
FT /evidence="ECO:0000305|PubMed:16361528"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 56
FT /note="D->A,E: Impairs the ability to disrupt attachments
FT between the host plasma membrane and cell wall."
FT /evidence="ECO:0000269|PubMed:14999409,
FT ECO:0000269|PubMed:21483488"
FT MUTAGEN 129
FT /note="L->P: Fails to elicit the RGA2/Rpi-blb1-mediated
FT hypersensitive response in host."
FT /evidence="ECO:0000269|PubMed:22438813"
SQ SEQUENCE 152 AA; 17242 MW; 41757249C50CF8BE CRC64;
MRSLLLTVLL NLVVLLATTG AVSSNLNTAV NYASTSKIRF LSTEYNADEK RSLRGDYNNE
VTKEPNTSDE ERAFSISKSA EYVKMVLYGF KLGFSPRTQS KTVLRYEDKL FTALYKSGET
PRSLRTKHLD KASASVFFNR FKKWYDKNVG PS
