ID MIK2_ARATH Reviewed; 1045 AA.
AC Q8VZG8; B9DG82; Q8H7F4; Q9LCZ6;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 3.
DT 27-MAR-2024, entry version 150.
DE RecName: Full=MDIS1-interacting receptor like kinase 2 {ECO:0000303|PubMed:26863186};
DE Short=AtMIK2 {ECO:0000303|PubMed:26863186};
DE AltName: Full=Probable LRR receptor-like serine/threonine-protein kinase At4g08850;
DE EC=2.7.11.1 {ECO:0000305};
DE Flags: Precursor;
GN Name=MIK2 {ECO:0000303|PubMed:26863186};
GN OrderedLocusNames=At4g08850 {ECO:0000312|Araport:AT4G08850};
GN ORFNames=T32A17.160 {ECO:0000312|EMBL:CAB82121.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-159 (ISOFORMS 1 AND 2).
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17644812; DOI=10.1074/mcp.m700099-mcp200;
RA Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J.,
RA Barbier-Brygoo H., Ephritikhine G.;
RT "A high content in lipid-modified peripheral proteins and integral receptor
RT kinases features in the arabidopsis plasma membrane proteome.";
RL Mol. Cell. Proteomics 6:1980-1996(2007).
RN [9]
RP FUNCTION, INTERACTION WITH MDIS1 AND LURE1.2, AND TISSUE SPECIFICITY.
RX PubMed=26863186; DOI=10.1038/nature16975;
RA Wang T., Liang L., Xue Y., Jia P.F., Chen W., Zhang M.X., Wang Y.C.,
RA Li H.J., Yang W.C.;
RT "A receptor heteromer mediates the male perception of female attractants in
RT plants.";
RL Nature 531:241-244(2016).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH SCOOP12.
RC STRAIN=cv. Columbia, and cv. Wassilewskija-2;
RX PubMed=33514716; DOI=10.1038/s41467-021-20932-y;
RA Rhodes J., Yang H., Moussu S., Boutrot F., Santiago J., Zipfel C.;
RT "Perception of a divergent family of phytocytokines by the Arabidopsis
RT receptor kinase MIK2.";
RL Nat. Commun. 12:705-705(2021).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH SCOOP12, AND INDUCTION BY
RP FLG22 AND ELF18.
RC STRAIN=cv. Columbia;
RX PubMed=34535661; DOI=10.1038/s41467-021-25580-w;
RA Hou S., Liu D., Huang S., Luo D., Liu Z., Xiang Q., Wang P., Mu R., Han Z.,
RA Chen S., Chai J., Shan L., He P.;
RT "The Arabidopsis MIK2 receptor elicits immunity by sensing a conserved
RT signature from phytocytokines and microbes.";
RL Nat. Commun. 12:5494-5494(2021).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=35401621; DOI=10.3389/fpls.2022.852808;
RA Stahl E., Fernandez Martin A., Glauser G., Guillou M.-C., Aubourg S.,
RA Renou J.-P., Reymond P.;
RT "The MIK2/SCOOP signaling system contributes to Arabidopsis resistance
RT against herbivory by modulating jasmonate and indole glucosinolate
RT biosynthesis.";
RL Front. Plant Sci. 13:852808-852808(2022).
CC -!- FUNCTION: Acts as a receptor of SCOOP peptides from Brassicaceae plants
CC regulating multiple processing including plant growth, development and
CC stress responses (PubMed:34535661, PubMed:33514716). Perception of
CC SCOOP peptides induces the association of MIK2 with the coreceptors
CC BAK1/SERK3 and SERK4 and relays the signaling through the activation of
CC receptor-like cytosolic kinases (RLCKs) BIK1 and PBL1 (PubMed:34535661,
CC PubMed:33514716). Also able to detect SCOOP-like proteins (SCOOPL)
CC present in fungal Fusarium spp. and bacterial Comamonadaceae to elicit
CC various immune responses, including growth inhibition, ROS production,
CC calcium Ca(2+) influx, MAPK activation and MYB51 promoter activation in
CC roots, thus being required for resistance to several root pathogens
CC (PubMed:33514716, PubMed:34535661). Involved in the pollen tube
CC perception of the female signal (PubMed:26863186). Required to trigger
CC defense responses toward generalist herbivores such as Spodoptera
CC littoralis, probably via the activation of jasmonate and indole
CC glucosinolate biosynthesis (PubMed:35401621).
CC {ECO:0000269|PubMed:26863186, ECO:0000269|PubMed:33514716,
CC ECO:0000269|PubMed:34535661, ECO:0000269|PubMed:35401621}.
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};
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};
CC -!- SUBUNIT: Interacts with MDIS1 and LURE1.2 (PubMed:26863186). Binds to
CC SCOOP12; this interaction triggers the formation of complex between
CC MIK2 and the BAK1/SERK3 and SERK4 coreceptors (PubMed:33514716,
CC PubMed:34535661). {ECO:0000269|PubMed:26863186,
CC ECO:0000269|PubMed:33514716, ECO:0000269|PubMed:34535661}.
CC -!- INTERACTION:
CC Q8VZG8; Q4VP08: LURE1.2; NbExp=4; IntAct=EBI-2270407, EBI-16196186;
CC Q8VZG8; C0LGU7: MDIS1; NbExp=5; IntAct=EBI-2270407, EBI-16196163;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15308754,
CC ECO:0000305|PubMed:17644812}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:15308754, ECO:0000305|PubMed:17644812}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VZG8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VZG8-2; Sequence=VSP_038295;
CC -!- TISSUE SPECIFICITY: Expressed in pollen tubes (PubMed:26863186). Highly
CC expressed in shoots, roots and leaves (PubMed:34535661).
CC {ECO:0000269|PubMed:26863186, ECO:0000269|PubMed:34535661}.
CC -!- INDUCTION: Induced by pathogen elicitors flg22 and elf18.
CC {ECO:0000269|PubMed:34535661}.
CC -!- DISRUPTION PHENOTYPE: Defect in apoplastic reactive oxygen species
CC (ROS) production upon stimulation with some immune elicitors such as
CC flg22 and AtPep1, and in response to SCOOP10 and SCOOP12
CC (PubMed:33514716, PubMed:34535661). Disturbed SCOOP12-triggered BAK1
CC phosphorylation on Ser-612 (PubMed:33514716). Insensitivity to SCOOP
CC peptides including SCOOP4, SCOOP6, SCOOP8, SCOOP10, SCOOP12, SCOOP13,
CC SCOOP14, SCOOP15, SCOOP20 and SCOOP23 leading to the loss of modified
CC gene expression of several genes (PubMed:34535661). Altered activation
CC of MAPK (e.g. MPK3, MPK4 and MPK6) and root meristems distortion
CC triggered by SCOOP10 and SCOOP12 (PubMed:34535661). Reduced sensitivity
CC to proteinous elicitors containing SCOOP-like sequences (SCOOPL) with
CC SxS motifs isolated from several Fusarium spp, thus leading to reduced
CC SCOOPL-induced growth inhibition, ROS production, calcium Ca(2+)
CC influx, MAPK activation and MYB51 promoter activation in roots,
CC hallmarks of defense responses (PubMed:34535661). Decreased resistance
CC against the generalist herbivore Spodoptera littoralis, but not toward
CC the specialist herbivore Pieris brassicae, and associated with reduced
CC accumulation of jasmonic acid (JA), jasmonate-isoleucine and indolic
CC glucosinolates due to a lower expression of several genes (e.g.
CC CYP79B2, CYP79B3, CYP83B1 and GSTF9) (PubMed:35401621).
CC {ECO:0000269|PubMed:33514716, ECO:0000269|PubMed:34535661,
CC ECO:0000269|PubMed:35401621}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN60259.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB78010.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB82121.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL161513; CAB78010.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161813; CAB82121.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82682.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82683.1; -; Genomic_DNA.
DR EMBL; AY064972; AAL57627.1; -; mRNA.
DR EMBL; AK317056; BAH19749.1; -; mRNA.
DR EMBL; FJ708744; ACN59338.1; -; mRNA.
DR EMBL; AF083700; AAN60259.1; ALT_INIT; mRNA.
DR PIR; B85089; B85089.
DR RefSeq; NP_192625.4; NM_116955.5. [Q8VZG8-2]
DR RefSeq; NP_849538.2; NM_179207.3. [Q8VZG8-1]
DR AlphaFoldDB; Q8VZG8; -.
DR SMR; Q8VZG8; -.
DR BioGRID; 11755; 15.
DR DIP; DIP-53470N; -.
DR IntAct; Q8VZG8; 12.
DR STRING; 3702.Q8VZG8; -.
DR GlyCosmos; Q8VZG8; 18 sites, No reported glycans.
DR iPTMnet; Q8VZG8; -.
DR SwissPalm; Q8VZG8; -.
DR PaxDb; 3702-AT4G08850-1; -.
DR ProteomicsDB; 238339; -. [Q8VZG8-1]
DR EnsemblPlants; AT4G08850.1; AT4G08850.1; AT4G08850. [Q8VZG8-1]
DR EnsemblPlants; AT4G08850.2; AT4G08850.2; AT4G08850. [Q8VZG8-2]
DR GeneID; 826456; -.
DR Gramene; AT4G08850.1; AT4G08850.1; AT4G08850. [Q8VZG8-1]
DR Gramene; AT4G08850.2; AT4G08850.2; AT4G08850. [Q8VZG8-2]
DR KEGG; ath:AT4G08850; -.
DR Araport; AT4G08850; -.
DR TAIR; AT4G08850; MIK2.
DR eggNOG; ENOG502QQYD; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q8VZG8; -.
DR OMA; MMEADEQ; -.
DR OrthoDB; 1125039at2759; -.
DR PhylomeDB; Q8VZG8; -.
DR PRO; PR:Q8VZG8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8VZG8; baseline and differential.
DR Genevisible; Q8VZG8; AT.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0090406; C:pollen tube; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042277; F:peptide binding; IDA:UniProtKB.
DR GO; GO:0001653; F:peptide receptor activity; IMP:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:1901653; P:cellular response to peptide; IMP:UniProtKB.
DR GO; GO:0002213; P:defense response to insect; IMP:UniProtKB.
DR GO; GO:0009759; P:indole glucosinolate biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009695; P:jasmonic acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010183; P:pollen tube guidance; IGI:TAIR.
DR GO; GO:0031349; P:positive regulation of defense response; IMP:UniProtKB.
DR GO; GO:0080027; P:response to herbivore; IMP:UniProtKB.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IEP:UniProtKB.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR48053; LEUCINE RICH REPEAT FAMILY PROTEIN, EXPRESSED; 1.
DR PANTHER; PTHR48053:SF112; MDIS1-INTERACTING RECEPTOR LIKE KINASE 2; 1.
DR Pfam; PF00560; LRR_1; 6.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00365; LRR_SD22; 7.
DR SMART; SM00369; LRR_TYP; 9.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS51450; LRR; 16.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Glycoprotein;
KW Jasmonic acid signaling pathway; Kinase; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Plant defense; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..43
FT /evidence="ECO:0000255"
FT CHAIN 44..1045
FT /note="MDIS1-interacting receptor like kinase 2"
FT /id="PRO_0000387559"
FT TOPO_DOM 44..709
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..730
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 731..1045
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 92..116
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 117..140
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 141..165
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 166..189
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 191..212
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 213..237
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 238..260
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 262..285
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 286..309
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 311..333
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 334..356
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 357..381
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 383..405
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 406..429
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 431..452
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 453..476
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 477..501
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 502..525
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 527..549
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 550..573
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 575..597
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 598..620
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 621..644
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 646..670
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT DOMAIN 775..1045
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 905
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 781..789
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 802
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 772
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 853
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 892
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 938
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 946
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 953
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 633
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 687
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 950..1045
FT /note="ELAYAMKVTEKCDVYSFGVLTLEVIKGEHPGDLVSTLSSSPPDATLSLKSIS
FT DHRLPEPTPEIKEEVLEILKVALLCLHSDPQARPTMLSISTAFS -> GTLFDPLDKLV
FT VDLTRLWSGRVEIMVRFGLFGLNFNQIKTKMFCFGLKFFLTMGWIWFSF (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640, ECO:0000303|Ref.6"
FT /id="VSP_038295"
FT CONFLICT 10
FT /note="I -> S (in Ref. 6; AAN60259)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="D -> N (in Ref. 6; AAN60259)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="L -> V (in Ref. 1; CAB78010/CAB82121)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1045 AA; 115423 MW; 7C9E44DE99DAE8BF CRC64;
MNKTNPERKI SLTSFKERMA CKEKPRDLQV LLIISIVLSC SFAVSATVEE ANALLKWKST
FTNQTSSSKL SSWVNPNTSS FCTSWYGVAC SLGSIIRLNL TNTGIEGTFE DFPFSSLPNL
TFVDLSMNRF SGTISPLWGR FSKLEYFDLS INQLVGEIPP ELGDLSNLDT LHLVENKLNG
SIPSEIGRLT KVTEIAIYDN LLTGPIPSSF GNLTKLVNLY LFINSLSGSI PSEIGNLPNL
RELCLDRNNL TGKIPSSFGN LKNVTLLNMF ENQLSGEIPP EIGNMTALDT LSLHTNKLTG
PIPSTLGNIK TLAVLHLYLN QLNGSIPPEL GEMESMIDLE ISENKLTGPV PDSFGKLTAL
EWLFLRDNQL SGPIPPGIAN STELTVLQLD TNNFTGFLPD TICRGGKLEN LTLDDNHFEG
PVPKSLRDCK SLIRVRFKGN SFSGDISEAF GVYPTLNFID LSNNNFHGQL SANWEQSQKL
VAFILSNNSI TGAIPPEIWN MTQLSQLDLS SNRITGELPE SISNINRISK LQLNGNRLSG
KIPSGIRLLT NLEYLDLSSN RFSSEIPPTL NNLPRLYYMN LSRNDLDQTI PEGLTKLSQL
QMLDLSYNQL DGEISSQFRS LQNLERLDLS HNNLSGQIPP SFKDMLALTH VDVSHNNLQG
PIPDNAAFRN APPDAFEGNK DLCGSVNTTQ GLKPCSITSS KKSHKDRNLI IYILVPIIGA
IIILSVCAGI FICFRKRTKQ IEEHTDSESG GETLSIFSFD GKVRYQEIIK ATGEFDPKYL
IGTGGHGKVY KAKLPNAIMA VKKLNETTDS SISNPSTKQE FLNEIRALTE IRHRNVVKLF
GFCSHRRNTF LVYEYMERGS LRKVLENDDE AKKLDWGKRI NVVKGVAHAL SYMHHDRSPA
IVHRDISSGN ILLGEDYEAK ISDFGTAKLL KPDSSNWSAV AGTYGYVAPE LAYAMKVTEK
CDVYSFGVLT LEVIKGEHPG DLVSTLSSSP PDATLSLKSI SDHRLPEPTP EIKEEVLEIL
KVALLCLHSD PQARPTMLSI STAFS
//
