RIPK_ARATH
ID RIPK_ARATH Reviewed; 462 AA.
AC Q9ZUF4;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Serine/threonine-protein kinase RIPK {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305|PubMed:21320696};
DE AltName: Full=ACIK1A/PBL14;
DE AltName: Full=ACRE protein ortholog 264A {ECO:0000305};
DE Short=AtACRE264a {ECO:0000303|PubMed:15181213};
DE AltName: Full=PBS1-like protein 14 {ECO:0000303|PubMed:20413097};
DE AltName: Full=RPM1-induced protein kinase {ECO:0000303|PubMed:21320696};
GN Name=RIPK {ECO:0000303|PubMed:21320696};
GN Synonyms=PBL14 {ECO:0000303|PubMed:20413097},
GN PIX8 {ECO:0000303|PubMed:23951354};
GN OrderedLocusNames=At2g05940 {ECO:0000312|Araport:AT2G05940};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP INDUCTION BY FLAGELLIN.
RX PubMed=15181213; DOI=10.1104/pp.103.036749;
RA Navarro L., Zipfel C., Rowland O., Keller I., Robatzek S., Boller T.,
RA Jones J.D.;
RT "The transcriptional innate immune response to flg22. Interplay and overlap
RT with Avr gene-dependent defense responses and bacterial pathogenesis.";
RL Plant Physiol. 135:1113-1128(2004).
RN [5]
RP INDUCTION BY 12-OXO-PHYTODIENOIC ACID.
RX PubMed=16258017; DOI=10.1104/pp.105.067058;
RA Taki N., Sasaki-Sekimoto Y., Obayashi T., Kikuta A., Kobayashi K.,
RA Ainai T., Yagi K., Sakurai N., Suzuki H., Masuda T., Takamiya K.,
RA Shibata D., Kobayashi Y., Ohta H.;
RT "12-oxo-phytodienoic acid triggers expression of a distinct set of genes
RT and plays a role in wound-induced gene expression in Arabidopsis.";
RL Plant Physiol. 139:1268-1283(2005).
RN [6]
RP INDUCTION.
RX PubMed=17587374; DOI=10.1111/j.1469-8137.2007.02092.x;
RA Hectors K., Prinsen E., De Coen W., Jansen M.A., Guisez Y.;
RT "Arabidopsis thaliana plants acclimated to low dose rates of ultraviolet B
RT radiation show specific changes in morphology and gene expression in the
RT absence of stress symptoms.";
RL New Phytol. 175:255-270(2007).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=20413097; DOI=10.1016/j.chom.2010.03.007;
RA Zhang J., Li W., Xiang T., Liu Z., Laluk K., Ding X., Zou Y., Gao M.,
RA Zhang X., Chen S., Mengiste T., Zhang Y., Zhou J.M.;
RT "Receptor-like cytoplasmic kinases integrate signaling from multiple plant
RT immune receptors and are targeted by a Pseudomonas syringae effector.";
RL Cell Host Microbe 7:290-301(2010).
RN [8]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RIN4 AND
RP PSEUDOMONAS SYRINGAE AVRB, SUBCELLULAR LOCATION, INDUCTION,
RP AUTOPHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH XANTHOMONAS
RP CAMPESTRIS XOPAC/AVRAC, AUTOPHOSPHORYLATION, AND URIDYLYLATION AT SER-251
RP AND THR-252.
RX PubMed=22504181; DOI=10.1038/nature10962;
RA Feng F., Yang F., Rong W., Wu X., Zhang J., Chen S., He C., Zhou J.M.;
RT "A Xanthomonas uridine 5'-monophosphate transferase inhibits plant immune
RT kinases.";
RL Nature 485:114-118(2012).
RN [10]
RP FUNCTION, AND INTERACTION WITH XANTHOMONAS CAMPESTRIS XOPAC/AVRAC.
RX PubMed=23951354; DOI=10.1371/journal.pone.0073469;
RA Guy E., Lautier M., Chabannes M., Roux B., Lauber E., Arlat M., Noel L.D.;
RT "xopAC-triggered immunity against Xanthomonas depends on Arabidopsis
RT receptor-like cytoplasmic kinase genes PBL2 and RIPK.";
RL PLoS ONE 8:E73469-E73469(2013).
RN [11]
RP FUNCTION.
RX PubMed=25625821; DOI=10.1094/mpmi-08-14-0248-r;
RA Russell A.R., Ashfield T., Innes R.W.;
RT "Pseudomonas syringae effector AvrPphB suppresses AvrB-induced activation
RT of RPM1 but not AvrRpm1-induced activation.";
RL Mol. Plant Microbe Interact. 28:727-735(2015).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in disease
CC resistance. During Pseudomonas syringae infection, and in response to
CC the bacterial effectors AvrB and AvrRpm1, RIPK phosphorylates the host
CC target RIN4, which subsequently activates RPM1-dependent effector-
CC triggered immunity (ETI) (PubMed:21320696, PubMed:25625821). Seems to
CC act as negative regulator of plant basal defense responses and may play
CC a role in pathogen-associated molecular pattern (PAMP)-triggered
CC immunity (PTI) (PubMed:21320696). Required for the bacterial
CC XopAC/AvrAC effector-triggered immunity against Xanthomonas campestris
CC (PubMed:23951354). {ECO:0000269|PubMed:21320696,
CC ECO:0000269|PubMed:23951354, ECO:0000269|PubMed:25625821}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000305|PubMed:21320696};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000305|PubMed:21320696};
CC -!- SUBUNIT: Interacts with the Pseudomonas syringae effector AvrB
CC (PubMed:21320696). Interacts with RIN4 (PubMed:21320696). Interacts
CC with the Xanthomonas campestris effector XopAC/AvrAC (PubMed:22504181,
CC PubMed:23951354). {ECO:0000269|PubMed:21320696,
CC ECO:0000269|PubMed:22504181, ECO:0000269|PubMed:23951354}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21320696}.
CC -!- INDUCTION: Induced by the microbe-associated molecular pattern (MAMP)
CC flagellin (flg22) (PubMed:15181213). Induced by the Pseudomonas
CC syringae effectors AvrB and AvrRpm1 (PubMed:21320696). Induced by 12-
CC oxo-phytodienoic acid (OPDA) (PubMed:16258017). Down-regulated by UV-B
CC (PubMed:17587374). {ECO:0000269|PubMed:15181213,
CC ECO:0000269|PubMed:16258017, ECO:0000269|PubMed:17587374,
CC ECO:0000269|PubMed:21320696}.
CC -!- PTM: Autophosphorylated (PubMed:21320696, PubMed:22504181).
CC Autophosphorylation is reduced in presence of the Xanthomonas
CC campestris effector XopAC/AvrAC (PubMed:22504181).
CC {ECO:0000269|PubMed:21320696, ECO:0000269|PubMed:22504181}.
CC -!- PTM: Uridylylated at Ser-251 and Thr-252 by the Xanthomonas campestris
CC effector XopAC/AvrAC. This conceals conserved phosphorylation sites in
CC the activation loop, reducing RIPK kinase activity and consequently
CC inhibiting downstream signaling. {ECO:0000269|PubMed:22504181}.
CC -!- DISRUPTION PHENOTYPE: Reduced leaf width. Enhanced disease resistance
CC to the bacterial pathogen Pseudomonas syringae pv. tomato.
CC {ECO:0000269|PubMed:21320696}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC005970; AAC95171.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05986.1; -; Genomic_DNA.
DR EMBL; AY056245; AAL07094.1; -; mRNA.
DR EMBL; AY113963; AAM45011.1; -; mRNA.
DR PIR; C84473; C84473.
DR RefSeq; NP_178651.1; NM_126607.3.
DR AlphaFoldDB; Q9ZUF4; -.
DR SMR; Q9ZUF4; -.
DR IntAct; Q9ZUF4; 1.
DR STRING; 3702.AT2G05940.1; -.
DR iPTMnet; Q9ZUF4; -.
DR PaxDb; Q9ZUF4; -.
DR PRIDE; Q9ZUF4; -.
DR ProteomicsDB; 236195; -.
DR EnsemblPlants; AT2G05940.1; AT2G05940.1; AT2G05940.
DR GeneID; 815147; -.
DR Gramene; AT2G05940.1; AT2G05940.1; AT2G05940.
DR KEGG; ath:AT2G05940; -.
DR Araport; AT2G05940; -.
DR TAIR; locus:2064712; AT2G05940.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_2_1; -.
DR InParanoid; Q9ZUF4; -.
DR OMA; CHHHENH; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9ZUF4; -.
DR PRO; PR:Q9ZUF4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZUF4; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Plant defense; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..462
FT /note="Serine/threonine-protein kinase RIPK"
FT /id="PRO_0000438603"
FT DOMAIN 87..367
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 378..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 93..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 76
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 167
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 251
FT /note="O-UMP-serine; by the Xanthomonas campestris effector
FT XopAC/AvrAC; alternate"
FT /evidence="ECO:0000269|PubMed:22504181"
FT MOD_RES 251
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 252
FT /note="O-UMP-threonine; by the Xanthomonas campestris
FT effector XopAC/AvrAC; alternate"
FT /evidence="ECO:0000269|PubMed:22504181"
FT MOD_RES 252
FT /note="Phosphothreonine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 257
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 265
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
SQ SEQUENCE 462 AA; 51701 MW; F7C353AFF3F121B6 CRC64;
MAVKKKVSWR SLIVGCLGDP ETLMASSKKP KRKNDVIKKQ SSFQRLSILD MSNPSSNTLS
EDLSISLAGS DLHVFTLAEL KVITQSFSST NFLGEGGFGP VHKGFIDDKL RPGLKAQPVA
VKLLDLEGLQ GHREWLTEVM FLGQLKHKNL VKLIGYCCEE EHRTLVYEFM PRGSLENQLF
RRYSASLPWS TRMKIAHGAA TGLQFLHEAE NPVIYRDFKA SNILLDSDYT AKLSDFGLAK
DGPEGDDTHV STRVMGTQGY AAPEYIMTGH LTARSDVYSF GVVLLELLTG RRSVDKKRSS
REQNLVDWAR PMLNDPRKLS RIMDPRLEGQ YSETGARKAA TLAYQCLSHR PKNRPCMSAV
VSILNDLKDY NDIPMGTFTY TVPNTPDNKE DDGRVGNKPR KSSHHHHHQQ QQSNHPRSSP
SPTTKSPSPT AKSPRNSTEN HRRTLRNGVN SPLRSEAGGE RY
