RIN4_ARATH
ID RIN4_ARATH Reviewed; 211 AA.
AC Q8GYN5; Q9LSG9;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=RPM1-interacting protein 4;
GN Name=RIN4; OrderedLocusNames=At3g25070; ORFNames=MJL12_1;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND
RP INTERACTION WITH RPM1; AVRRPM1 AND AVRB.
RC STRAIN=cv. Columbia;
RX PubMed=11955429; DOI=10.1016/s0092-8674(02)00661-x;
RA Mackey D., Holt B.F. III, Wiig A., Dangl J.L.;
RT "RIN4 interacts with Pseudomonas syringae type III effector molecules and
RT is required for RPM1-mediated resistance in Arabidopsis.";
RL Cell 108:743-754(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP PROTEIN SEQUENCE OF 11-26, INTERACTION WITH AVRRPT2, AND MUTAGENESIS OF
RP PHE-9 AND PHE-151.
RX PubMed=15746386; DOI=10.1126/science.1108633;
RA Coaker G., Falick A., Staskawicz B.J.;
RT "Activation of a phytopathogenic bacterial effector protein by a eukaryotic
RT cyclophilin.";
RL Science 308:548-550(2005).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AVRRPT2 AND RPS2.
RX PubMed=12581526; DOI=10.1016/s0092-8674(03)00036-9;
RA Axtell M.J., Staskawicz B.J.;
RT "Initiation of RPS2-specified disease resistance in Arabidopsis is coupled
RT to the AvrRpt2-directed elimination of RIN4.";
RL Cell 112:369-377(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH AVRRPT2.
RX PubMed=12581527; DOI=10.1016/s0092-8674(03)00040-0;
RA Mackey D., Belkhadir Y., Alonso J.M., Ecker J.R., Dangl J.L.;
RT "Arabidopsis RIN4 is a target of the type III virulence effector AvrRpt2
RT and modulates RPS2-mediated resistance.";
RL Cell 112:379-389(2003).
RN [8]
RP MUTAGENESIS OF 6-VAL--TRP-12; 148-VAL--TRP-154 AND 203-CYS--CYS-205.
RX PubMed=15845764; DOI=10.1073/pnas.0500792102;
RA Kim H.-S., Desveaux D., Singer A.U., Patel P., Sondek J., Dangl J.L.;
RT "The Pseudomonas syringae effector AvrRpt2 cleaves its C-terminally
RT acylated target, RIN4, from Arabidopsis membranes to block RPM1
RT activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:6496-6501(2005).
RN [9]
RP INTERACTION WITH NDR1.
RX PubMed=17012600; DOI=10.1105/tpc.106.044693;
RA Day B., Dahlbeck D., Staskawicz B.J.;
RT "NDR1 interaction with RIN4 mediates the differential activation of
RT multiple disease resistance pathways in Arabidopsis.";
RL Plant Cell 18:2782-2791(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 AND SER-141, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Seedling;
RX PubMed=17586839; DOI=10.1074/mcp.m700164-mcp200;
RA Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X.;
RT "Temporal analysis of sucrose-induced phosphorylation changes in plasma
RT membrane proteins of Arabidopsis.";
RL Mol. Cell. Proteomics 6:1711-1726(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-141, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [13]
RP INTERACTION WITH RIPK, PHOSPHORYLATION AT THR-21; SER-160 AND THR-166,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF THR-21; SER-160 AND
RP THR-166.
RX PubMed=21320696; DOI=10.1016/j.chom.2011.01.010;
RA Liu J., Elmore J.M., Lin Z.J., Coaker G.;
RT "A receptor-like cytoplasmic kinase phosphorylates the host target RIN4,
RT leading to the activation of a plant innate immune receptor.";
RL Cell Host Microbe 9:137-146(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 142-176 IN COMPLEX WITH AVRB.
RX PubMed=17397263; DOI=10.1371/journal.ppat.0030048;
RA Desveaux D., Singer A.U., Wu A.J., McNulty B.C., Musselwhite L.,
RA Nimchuk Z., Sondek J., Dangl J.L.;
RT "Type III effector activation via nucleotide binding, phosphorylation, and
RT host target interaction.";
RL PLoS Pathog. 3:E48-E48(2007).
CC -!- FUNCTION: Essential regulator of plant defense, which plays a central
CC role in resistance in case of infection by a pathogen. It is a common
CC target for both type III avirulence proteins from P.syringae (AvrB,
CC AvrRpm1 and AvrRpt2) and for the plant Resistance (R) proteins RPM1 and
CC RPS2. In strains carrying the appropriate R gene for avirulence
CC proteins of the pathogen, its association with avirulence proteins
CC triggers a defense system including the hypersensitive response, which
CC limits the spread of disease. In contrast, in plants lacking
CC appropriate R genes, its association with avirulence proteins of the
CC pathogen impairs the defense system and leads to the pathogen
CC multiplication. {ECO:0000269|PubMed:11955429,
CC ECO:0000269|PubMed:12581526, ECO:0000269|PubMed:12581527}.
CC -!- SUBUNIT: Interacts with the unrelated avirulence proteins AvrB, AvrRpm1
CC and AvrRpt2 from P.syringae. Interacts with the N-terminal domain of
CC PRM1. Interacts indirectly with RPS2. Its association with AvrB and
CC AvrRpm1 results in its phosphorylation, which is in turn recognized by
CC the resistance RPM1 protein, leading to the activation of RPM1-
CC dependent disease resistance responses. On the other hand, its
CC association with AvrRpt2 results in its destruction, which activates
CC RPS2-dependent disease resistance responses. Interacts (via C-terminus)
CC with NDR1. Interaction with NDR1 is required for association with RPS2
CC and RPS2-mediated resistance (PubMed:11955429, PubMed:12581526,
CC PubMed:12581527, PubMed:15746386, PubMed:17012600, PubMed:17397263).
CC Interacts with RIPK (PubMed:21320696). {ECO:0000269|PubMed:11955429,
CC ECO:0000269|PubMed:12581526, ECO:0000269|PubMed:12581527,
CC ECO:0000269|PubMed:15746386, ECO:0000269|PubMed:17012600,
CC ECO:0000269|PubMed:17397263, ECO:0000269|PubMed:21320696}.
CC -!- INTERACTION:
CC Q8GYN5; O48915: NDR1; NbExp=3; IntAct=EBI-2270391, EBI-2314492;
CC Q8GYN5; Q88A90: hopF2; Xeno; NbExp=3; IntAct=EBI-2270391, EBI-2619325;
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:11955429,
CC ECO:0000269|PubMed:12581526}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11955429, ECO:0000269|PubMed:12581526}.
CC -!- PTM: Phosphorylated following the interaction with the Pseudomonas
CC syringae effectors AvrB or AvrRpm1 (PubMed:11955429). Phosphorylated at
CC Thr-21, Ser-160 and Thr-166 by RIPK following interaction with the
CC effectors AvrB or AvrRpm1 (PubMed:21320696).
CC {ECO:0000269|PubMed:11955429, ECO:0000269|PubMed:21320696}.
CC -!- PTM: Palmitoylation is required for membrane localization. It is
CC uncertain whether Cys-203, Cys-204 or Cys-205 is palmitoylated.
CC -!- MISCELLANEOUS: Cleavage after Gly-152 by AvrRpt2 is critical for the
CC release of RIN4 from the membrane and its subsequent proteasome-
CC dependent elimination.
CC -!- SIMILARITY: Belongs to the RIN4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02065.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB026647; BAB02065.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76974.1; -; Genomic_DNA.
DR EMBL; AK117488; BAC42151.1; -; mRNA.
DR RefSeq; NP_189143.2; NM_113411.3.
DR PDB; 2NUD; X-ray; 2.30 A; C/D=142-176.
DR PDBsum; 2NUD; -.
DR AlphaFoldDB; Q8GYN5; -.
DR SMR; Q8GYN5; -.
DR BioGRID; 7429; 15.
DR DIP; DIP-53466N; -.
DR IntAct; Q8GYN5; 4.
DR STRING; 3702.AT3G25070.1; -.
DR iPTMnet; Q8GYN5; -.
DR SwissPalm; Q8GYN5; -.
DR PaxDb; Q8GYN5; -.
DR PRIDE; Q8GYN5; -.
DR ProteomicsDB; 237003; -.
DR EnsemblPlants; AT3G25070.1; AT3G25070.1; AT3G25070.
DR GeneID; 822098; -.
DR Gramene; AT3G25070.1; AT3G25070.1; AT3G25070.
DR KEGG; ath:AT3G25070; -.
DR Araport; AT3G25070; -.
DR TAIR; locus:2090250; AT3G25070.
DR eggNOG; ENOG502QQ5R; Eukaryota.
DR HOGENOM; CLU_057946_1_1_1; -.
DR InParanoid; Q8GYN5; -.
DR PhylomeDB; Q8GYN5; -.
DR EvolutionaryTrace; Q8GYN5; -.
DR PRO; PR:Q8GYN5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8GYN5; baseline and differential.
DR Genevisible; Q8GYN5; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:TAIR.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0034051; P:negative regulation of plant-type hypersensitive response; IMP:CACAO.
DR GO; GO:0009626; P:plant-type hypersensitive response; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IMP:TAIR.
DR DisProt; DP01776; -.
DR InterPro; IPR040387; RIN4/NOI4.
DR InterPro; IPR008700; TypeIII_avirulence_cleave.
DR PANTHER; PTHR33159; PTHR33159; 1.
DR Pfam; PF05627; AvrRpt-cleavage; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hypersensitive response; Immunity;
KW Innate immunity; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Plant defense; Reference proteome.
FT CHAIN 1..211
FT /note="RPM1-interacting protein 4"
FT /id="PRO_0000221387"
FT REGION 1..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 10..11
FT /note="Cleavage; by AvrRpt2"
FT SITE 152..153
FT /note="Cleavage; by AvrRpt2"
FT MOD_RES 21
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:21320696"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17586839"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17586839,
FT ECO:0007744|PubMed:19245862, ECO:0007744|PubMed:19376835"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21320696"
FT MOD_RES 166
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:21320696"
FT LIPID 203
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 204
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 205
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT MUTAGEN 6..12
FT /note="VPKFGNW->APKAANA: No alteration of membrane
FT localization."
FT /evidence="ECO:0000269|PubMed:15845764"
FT MUTAGEN 9
FT /note="F->A: No cleavage at position 9-10 by AvrRpt2."
FT /evidence="ECO:0000269|PubMed:15746386"
FT MUTAGEN 21
FT /note="T->A: Loss of phosphorylation by RIPK; when
FT associated with A-160 and A-166."
FT /evidence="ECO:0000269|PubMed:21320696"
FT MUTAGEN 21
FT /note="T->D: Induction of RPM1 activation; when associated
FT with D-160 and D-166."
FT /evidence="ECO:0000269|PubMed:21320696"
FT MUTAGEN 148..154
FT /note="VPKFGDW->APKAANA: Loss of RIN4 degradation, but no
FT alteration of membrane localization."
FT /evidence="ECO:0000269|PubMed:15845764"
FT MUTAGEN 151
FT /note="F->A: No cleavage at position 152-153 by AvrRpt2."
FT /evidence="ECO:0000269|PubMed:15746386"
FT MUTAGEN 160
FT /note="S->A: Loss of phosphorylation by RIPK; when
FT associated with A-21 and A-166."
FT /evidence="ECO:0000269|PubMed:21320696"
FT MUTAGEN 160
FT /note="S->D: Induction of RPM1 activation; when associated
FT with D-21 and D-166."
FT /evidence="ECO:0000269|PubMed:21320696"
FT MUTAGEN 166
FT /note="T->A: Loss of phosphorylation by RIPK; when
FT associated with A-21 and A-166."
FT /evidence="ECO:0000269|PubMed:21320696"
FT MUTAGEN 166
FT /note="T->D: Induction of RPM1 activation; when associated
FT with D-21 and D-166."
FT /evidence="ECO:0000269|PubMed:21320696"
FT MUTAGEN 203..205
FT /note="CCC->AAA: Loss of membrane association."
FT /evidence="ECO:0000269|PubMed:15845764"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:2NUD"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:2NUD"
SQ SEQUENCE 211 AA; 23371 MW; AB391ECF840AEA09 CRC64;
MARSNVPKFG NWEAEENVPY TAYFDKARKT RAPGSKIMNP NDPEYNSDSQ SQAPPHPPSS
RTKPEQVDTV RRSREHMRSR EESELKQFGD AGGSSNEAAN KRQGRASQNN SYDNKSPLHK
NSYDGTGKSR PKPTNLRADE SPEKVTVVPK FGDWDENNPS SADGYTHIFN KVREERSSGA
NVSGSSRTPT HQSSRNPNNT SSCCCFGFGG K
