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Serine/threonine-protein kinase RIPK (EC 2.7.11.1) (ACIK1A/PBL14) (ACRE protein ortholog 264A) (AtACRE264a) (PBS1-like protein 14) (RPM1-induced protein kinase)

 RIPK_ARATH              Reviewed;         462 AA.
Q9ZUF4;
30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
18-JUL-2018, entry version 144.
RecName: Full=Serine/threonine-protein kinase RIPK {ECO:0000305};
EC=2.7.11.1 {ECO:0000305|PubMed:21320696};
AltName: Full=ACIK1A/PBL14;
AltName: Full=ACRE protein ortholog 264A {ECO:0000305};
Short=AtACRE264a {ECO:0000303|PubMed:15181213};
AltName: Full=PBS1-like protein 14 {ECO:0000303|PubMed:20413097};
AltName: Full=RPM1-induced protein kinase {ECO:0000303|PubMed:21320696};
Name=RIPK {ECO:0000303|PubMed:21320696};
Synonyms=PBL14 {ECO:0000303|PubMed:20413097},
PIX8 {ECO:0000303|PubMed:23951354};
OrderedLocusNames=At2g05940 {ECO:0000312|Araport:AT2G05940};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
INDUCTION BY FLAGELLIN.
PubMed=15181213; DOI=10.1104/pp.103.036749;
Navarro L., Zipfel C., Rowland O., Keller I., Robatzek S., Boller T.,
Jones J.D.;
"The transcriptional innate immune response to flg22. Interplay and
overlap with Avr gene-dependent defense responses and bacterial
pathogenesis.";
Plant Physiol. 135:1113-1128(2004).
[5]
INDUCTION BY 12-OXO-PHYTODIENOIC ACID.
PubMed=16258017; DOI=10.1104/pp.105.067058;
Taki N., Sasaki-Sekimoto Y., Obayashi T., Kikuta A., Kobayashi K.,
Ainai T., Yagi K., Sakurai N., Suzuki H., Masuda T., Takamiya K.,
Shibata D., Kobayashi Y., Ohta H.;
"12-oxo-phytodienoic acid triggers expression of a distinct set of
genes and plays a role in wound-induced gene expression in
Arabidopsis.";
Plant Physiol. 139:1268-1283(2005).
[6]
INDUCTION.
PubMed=17587374; DOI=10.1111/j.1469-8137.2007.02092.x;
Hectors K., Prinsen E., De Coen W., Jansen M.A., Guisez Y.;
"Arabidopsis thaliana plants acclimated to low dose rates of
ultraviolet B radiation show specific changes in morphology and gene
expression in the absence of stress symptoms.";
New Phytol. 175:255-270(2007).
[7]
GENE FAMILY, AND NOMENCLATURE.
PubMed=20413097; DOI=10.1016/j.chom.2010.03.007;
Zhang J., Li W., Xiang T., Liu Z., Laluk K., Ding X., Zou Y., Gao M.,
Zhang X., Chen S., Mengiste T., Zhang Y., Zhou J.M.;
"Receptor-like cytoplasmic kinases integrate signaling from multiple
plant immune receptors and are targeted by a Pseudomonas syringae
effector.";
Cell Host Microbe 7:290-301(2010).
[8]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RIN4
AND PSEUDOMONAS SYRINGAE AVRB, SUBCELLULAR LOCATION, INDUCTION,
AUTOPHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
PubMed=21320696; DOI=10.1016/j.chom.2011.01.010;
Liu J., Elmore J.M., Lin Z.J., Coaker G.;
"A receptor-like cytoplasmic kinase phosphorylates the host target
RIN4, leading to the activation of a plant innate immune receptor.";
Cell Host Microbe 9:137-146(2011).
[9]
IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH XANTHOMONAS
CAMPESTRIS XOPAC/AVRAC, AUTOPHOSPHORYLATION, AND URIDYLYLATION AT
SER-251 AND THR-252.
PubMed=22504181; DOI=10.1038/nature10962;
Feng F., Yang F., Rong W., Wu X., Zhang J., Chen S., He C., Zhou J.M.;
"A Xanthomonas uridine 5'-monophosphate transferase inhibits plant
immune kinases.";
Nature 485:114-118(2012).
[10]
FUNCTION, AND INTERACTION WITH XANTHOMONAS CAMPESTRIS XOPAC/AVRAC.
PubMed=23951354; DOI=10.1371/journal.pone.0073469;
Guy E., Lautier M., Chabannes M., Roux B., Lauber E., Arlat M.,
Noel L.D.;
"xopAC-triggered immunity against Xanthomonas depends on Arabidopsis
receptor-like cytoplasmic kinase genes PBL2 and RIPK.";
PLoS ONE 8:E73469-E73469(2013).
[11]
FUNCTION.
PubMed=25625821; DOI=10.1094/MPMI-08-14-0248-R;
Russell A.R., Ashfield T., Innes R.W.;
"Pseudomonas syringae effector AvrPphB suppresses AvrB-induced
activation of RPM1 but not AvrRpm1-induced activation.";
Mol. Plant Microbe Interact. 28:727-735(2015).
-!- FUNCTION: Serine/threonine-protein kinase involved in disease
resistance. During Pseudomonas syringae infection, and in response
to the bacterial effectors AvrB and AvrRpm1, RIPK phosphorylates
the host target RIN4, which subsequently activates RPM1-depedent
effector-triggered immunity (ETI) (PubMed:21320696,
PubMed:25625821). Seems to act as negative regulator of plant
basal defense responses and may play a role in pathogen-associated
molecular pattern (PAMP)-triggered immunity (PTI)
(PubMed:21320696). Required for the bacterial XopAC/AvrAC
effector-triggered immunity against Xanthomonas campestris
(PubMed:23951354). {ECO:0000269|PubMed:21320696,
ECO:0000269|PubMed:23951354, ECO:0000269|PubMed:25625821}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000305|PubMed:21320696}.
-!- SUBUNIT: Interacts with the Pseudomonas syringae effector AvrB
(PubMed:21320696). Interacts with RIN4 (PubMed:21320696).
Interacts with the Xanthomonas campestris effector XopAC/AvrAC
(PubMed:22504181, PubMed:23951354). {ECO:0000269|PubMed:21320696,
ECO:0000269|PubMed:22504181, ECO:0000269|PubMed:23951354}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21320696}.
-!- INDUCTION: Induced by the microbe-associated molecular pattern
(MAMP) flagellin (flg22) (PubMed:15181213). Induced by the
Pseudomonas syringae effectors AvrB and AvrRpm1 (PubMed:21320696).
Induced by 12-oxo-phytodienoic acid (OPDA) (PubMed:16258017).
Down-regulated by UV-B (PubMed:17587374).
{ECO:0000269|PubMed:15181213, ECO:0000269|PubMed:16258017,
ECO:0000269|PubMed:17587374, ECO:0000269|PubMed:21320696}.
-!- PTM: Autophosphorylated (PubMed:21320696, PubMed:22504181).
Autophosphorylation is reduced in presence of the Xanthomonas
campestris effector XopAC/AvrAC (PubMed:22504181).
{ECO:0000269|PubMed:21320696, ECO:0000269|PubMed:22504181}.
-!- PTM: Uridylylated at Ser-251 and Thr-252 by the Xanthomonas
campestris effector XopAC/AvrAC. This conceals conserved
phosphorylation sites in the activation loop, reducing RIPK kinase
activity and consequently inhibiting downstream signaling.
{ECO:0000269|PubMed:22504181}.
-!- DISRUPTION PHENOTYPE: Reduced leaf width. Enhanced disease
resistance to the bacterial pathogen Pseudomonas syringae pv.
tomato. {ECO:0000269|PubMed:21320696}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
URL="http://plantsp.genomics.purdue.edu/family/class.html";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AC005970; AAC95171.1; -; Genomic_DNA.
EMBL; CP002685; AEC05986.1; -; Genomic_DNA.
EMBL; AY056245; AAL07094.1; -; mRNA.
EMBL; AY113963; AAM45011.1; -; mRNA.
PIR; C84473; C84473.
RefSeq; NP_178651.1; NM_126607.3.
UniGene; At.23011; -.
ProteinModelPortal; Q9ZUF4; -.
SMR; Q9ZUF4; -.
IntAct; Q9ZUF4; 1.
STRING; 3702.AT2G05940.1; -.
iPTMnet; Q9ZUF4; -.
PaxDb; Q9ZUF4; -.
PRIDE; Q9ZUF4; -.
EnsemblPlants; AT2G05940.1; AT2G05940.1; AT2G05940.
GeneID; 815147; -.
Gramene; AT2G05940.1; AT2G05940.1; AT2G05940.
KEGG; ath:AT2G05940; -.
Araport; AT2G05940; -.
TAIR; locus:2064712; AT2G05940.
eggNOG; KOG1187; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000116550; -.
OMA; PCMSAVV; -.
OrthoDB; EOG09360855; -.
PhylomeDB; Q9ZUF4; -.
PRO; PR:Q9ZUF4; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q9ZUF4; baseline and differential.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF07714; Pkinase_Tyr; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Kinase; Membrane;
Nucleotide-binding; Phosphoprotein; Plant defense; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 462 Serine/threonine-protein kinase RIPK.
/FTId=PRO_0000438603.
DOMAIN 87 367 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 93 101 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 404 415 His-rich. {ECO:0000255|PROSITE-
ProRule:PRU00009}.
ACT_SITE 217 217 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 122 122 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 76 76 Phosphothreonine.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 167 167 Phosphotyrosine.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 221 221 Phosphoserine.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 251 251 O-UMP-serine; by the Xanthomonas
campestris effector XopAC/AvrAC;
alternate. {ECO:0000269|PubMed:22504181}.
MOD_RES 251 251 Phosphoserine; alternate.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 252 252 O-UMP-threonine; by the Xanthomonas
campestris effector XopAC/AvrAC;
alternate. {ECO:0000269|PubMed:22504181}.
MOD_RES 252 252 Phosphothreonine; alternate.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 257 257 Phosphothreonine.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 265 265 Phosphotyrosine.
{ECO:0000250|UniProtKB:O48814}.
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


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