ZED1_ARATH
ID ZED1_ARATH Reviewed; 334 AA.
AC Q8LGB6; Q9SVY9;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Non-functional pseudokinase ZED1 {ECO:0000305};
DE Short=AtZED1 {ECO:0000303|PubMed:28652264};
DE AltName: Full=Non-functional pseudokinase ZRK5 {ECO:0000303|PubMed:26355215};
DE AltName: Full=Protein CLUSTERED SILIQUE {ECO:0000303|PubMed:28499073};
DE AltName: Full=Protein HOPZ-ETI-DEFICIENT 1 {ECO:0000303|PubMed:24170858};
GN Name=ZED1 {ECO:0000303|PubMed:24170858};
GN Synonyms=CLS {ECO:0000303|PubMed:28499073},
GN ZRK5 {ECO:0000303|PubMed:26355215};
GN OrderedLocusNames=At3g57750 {ECO:0000312|Araport:AT3G57750};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH
RP RPP13L4/ZAR1, SUBCELLULAR LOCATION, ACETYLATION AT THR-125 AND THR-177, AND
RP MUTAGENESIS OF GLY-66; GLY-128; ASP-231 AND ALA-305.
RX PubMed=24170858; DOI=10.1073/pnas.1315520110;
RA Lewis J.D., Lee A.H., Hassan J.A., Wan J., Hurley B., Jhingree J.R.,
RA Wang P.W., Lo T., Youn J.Y., Guttman D.S., Desveaux D.;
RT "The Arabidopsis ZED1 pseudokinase is required for ZAR1-mediated immunity
RT induced by the Pseudomonas syringae type III effector HopZ1a.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:18722-18727(2013).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH RPP13L4/ZAR1, GENE FAMILY,
RP AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=26355215; DOI=10.1016/j.chom.2015.08.004;
RA Wang G., Roux B., Feng F., Guy E., Li L., Li N., Zhang X., Lautier M.,
RA Jardinaud M.-F., Chabannes M., Arlat M., Chen S., He C., Noel L.D.,
RA Zhou J.-M.;
RT "The decoy substrate of a pathogen effector and a pseudokinase specify
RT pathogen-induced modified-self recognition and immunity in plants.";
RL Cell Host Microbe 18:285-295(2015).
RN [7]
RP FUNCTION, MUTAGENESIS OF ASN-173, DISRUPTION PHENOTYPE, INTERACTION WITH
RP RPP13L4/ZAR1, INDUCTION BY ELEVATED TEMPERATURE, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=28499073; DOI=10.1111/nph.14585;
RA Wang Z., Cui D., Liu J., Zhao J., Liu C., Xin W., Li Y., Liu N., Ren D.,
RA Tang D., Hu Y.;
RT "Arabidopsis ZED1-related kinases mediate the temperature-sensitive
RT intersection of immune response and growth homeostasis.";
RL New Phytol. 215:711-724(2017).
RN [8]
RP FUNCTION, MUTAGENESIS OF GLY-66; GLY-128; ASP-231 AND ALA-305, INTERACTION
RP WITH RPP13L4/ZAR1, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=28652264; DOI=10.1104/pp.17.00441;
RA Baudin M., Hassan J.A., Schreiber K.J., Lewis J.D.;
RT "Analysis of the ZAR1 immune complex reveals determinants for immunity and
RT molecular interactions.";
RL Plant Physiol. 174:2038-2053(2017).
CC -!- FUNCTION: Together with RPP13L4/ZAR1, involved in the ambient
CC temperature (above 22 degrees Celsius)-sensitive aerial organ
CC development (PubMed:28499073). Together with RPP13L4/ZAR1, involved in
CC the regulation of the ambient temperature-sensitive intersection of
CC growth and immune response in the absence of pathogens, by repressing
CC the transcription of SNC1 (PubMed:28499073). Probable non-functional
CC kinase required for recognition of the Pseudomonas syringae type III
CC effector HopZ1a by RPP13L4/ZAR1 and to trigger subsequent defense
CC responses (PubMed:24170858, PubMed:26355215, PubMed:28652264). May.
CC function as a decoy to trap HopZ1a in the ZAR1 complex for recognition
CC by the plant immune system (PubMed:24170858).
CC {ECO:0000269|PubMed:24170858, ECO:0000269|PubMed:26355215,
CC ECO:0000269|PubMed:28499073, ECO:0000269|PubMed:28652264}.
CC -!- SUBUNIT: Interacts with RPP13L4/ZAR1. {ECO:0000269|PubMed:24170858,
CC ECO:0000269|PubMed:26355215, ECO:0000269|PubMed:28499073,
CC ECO:0000269|PubMed:28652264}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:28499073}.
CC Nucleus {ECO:0000269|PubMed:28499073, ECO:0000269|PubMed:28652264}.
CC Cell membrane {ECO:0000269|PubMed:28652264}. Note=Associates with the
CC plasma membrane in the presence of the Xanthomonas campestris effector
CC XopAC/AvrAC. {ECO:0000269|PubMed:28652264}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, young leaves, floral
CC organs, shoot apical meristems (SAM) and inflorescence stems.
CC {ECO:0000269|PubMed:28499073}.
CC -!- INDUCTION: Induced by the elevation of ambient temperature both in the
CC nucleus and the cytosol. {ECO:0000269|PubMed:28499073}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- DISRUPTION PHENOTYPE: Reduced resistance to Pseudomonas syringae
CC expressing HopZ1a (PubMed:26355215). The double mutant zed1-6 zrk12-1
CC exhibits short inflorescence stem and autoimmunity symptoms when grown
CC at 25 degrees Celsius (PubMed:28499073). {ECO:0000269|PubMed:26355215,
CC ECO:0000269|PubMed:28499073}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. ZRK subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41180.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AL049660; CAB41180.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE79693.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79694.1; -; Genomic_DNA.
DR EMBL; AK175119; BAD42882.1; -; mRNA.
DR EMBL; AY084360; AAM60941.1; -; mRNA.
DR PIR; T06745; T06745.
DR RefSeq; NP_001030878.1; NM_001035801.1.
DR RefSeq; NP_567053.1; NM_115635.4.
DR AlphaFoldDB; Q8LGB6; -.
DR SMR; Q8LGB6; -.
DR STRING; 3702.AT3G57750.1; -.
DR iPTMnet; Q8LGB6; -.
DR PaxDb; Q8LGB6; -.
DR PRIDE; Q8LGB6; -.
DR ProteomicsDB; 242349; -.
DR DNASU; 824944; -.
DR EnsemblPlants; AT3G57750.1; AT3G57750.1; AT3G57750.
DR EnsemblPlants; AT3G57750.2; AT3G57750.2; AT3G57750.
DR GeneID; 824944; -.
DR Gramene; AT3G57750.1; AT3G57750.1; AT3G57750.
DR Gramene; AT3G57750.2; AT3G57750.2; AT3G57750.
DR KEGG; ath:AT3G57750; -.
DR Araport; AT3G57750; -.
DR TAIR; locus:2076646; AT3G57750.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_4_1; -.
DR InParanoid; Q8LGB6; -.
DR OMA; KLSDFWF; -.
DR OrthoDB; 778960at2759; -.
DR PRO; PR:Q8LGB6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8LGB6; baseline and differential.
DR Genevisible; Q8LGB6; AT.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0040008; P:regulation of growth; IMP:UniProtKB.
DR GO; GO:0050776; P:regulation of immune response; IMP:UniProtKB.
DR GO; GO:0009266; P:response to temperature stimulus; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR045274; WAK-like.
DR PANTHER; PTHR27005; PTHR27005; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell membrane; Cytoplasm; Membrane;
KW Nucleotide-binding; Nucleus; Plant defense; Reference proteome.
FT CHAIN 1..334
FT /note="Non-functional pseudokinase ZED1"
FT /id="PRO_0000433373"
FT DOMAIN 49..334
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 55..63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 231
FT /note="Required for Pseudomonas syringae type III effector
FT HopZ1a recognition and interaction with ZAR1"
FT /evidence="ECO:0000269|PubMed:28652264"
FT MOD_RES 125
FT /note="O-acetylthreonine"
FT /evidence="ECO:0000269|PubMed:24170858"
FT MOD_RES 177
FT /note="O-acetylthreonine"
FT /evidence="ECO:0000269|PubMed:24170858"
FT MUTAGEN 66
FT /note="G->S: In zed1-1; loss of function and reduced
FT interaction with RPP13L4/ZAR1 and Pseudomonas syringae type
FT III effector HopZ1a."
FT /evidence="ECO:0000269|PubMed:24170858,
FT ECO:0000269|PubMed:28652264"
FT MUTAGEN 128
FT /note="G->E: In zed1-3; loss of function and reduced
FT interaction with RPP13L4/ZAR1 and Pseudomonas syringae type
FT III effector HopZ1a."
FT /evidence="ECO:0000269|PubMed:24170858,
FT ECO:0000269|PubMed:28652264"
FT MUTAGEN 173
FT /note="N->S: In zed1-D; normal growth of plants grown below
FT 22 degrees Celsius, but high temperature (above 22 degrees
FT Celsius)-dependent RPP13L4/ZAR1-influenced autoimmunity and
FT growth retardation. Plants cultivated above 23 degrees
FT Celsius are dwarf with crinkled lamina, shortened petiole,
FT reduced pedicel length and silique numbers, increased
FT branches, severely shortened inflorescence stem and
FT clustered siliques. These phenotypes are associated with
FT inhibited cell elongation and/or expansion and disturbed
FT differentiation of trichomes and stomata, disorganized
FT interfascicular fibers and fewer pith tissues in
FT inflorescence stems as well as increased lignin deposition
FT in the vasculatures. Elevated reactive oxygen species (ROS)
FT content and extensive cell death as well as reduced
FT expression of pathogenesis related genes (e.g. PR1 and PR2)
FT but accumulation of SNC1 when grown at 25 degrees Celsius.
FT The high temperature-induced autoimmune phenotype is
FT blocked in the double mutant zed1-D zar1-3. Stronger
FT binding activity with RPP13L4/ZAR1. Confined to the
FT cytosol. Fully rescued by the over-expression of RKS1/ZRK1
FT and ZRK12, and partially by the over-expression of ZRK4,
FT ZRK10, ZRK13 and ZRK14. The double mutants zed1-D snc1-11
FT and zed1-D nahG have restored normal growth phenotypes and
FT rescued autoimmunity defects."
FT /evidence="ECO:0000269|PubMed:28499073"
FT MUTAGEN 231
FT /note="D->N: In zed1-4; loss of function, impaired
FT interaction with RPP13L4/ZAR1 and Pseudomonas syringae type
FT III effector HopZ1a, and completely abrogated
FT hypersensitive response (HR)."
FT /evidence="ECO:0000269|PubMed:24170858,
FT ECO:0000269|PubMed:28652264"
FT MUTAGEN 305
FT /note="A->T: In zed1-5; loss of function and reduced
FT interaction with RPP13L4/ZAR1 and Pseudomonas syringae type
FT III effector HopZ1a."
FT /evidence="ECO:0000269|PubMed:24170858,
FT ECO:0000269|PubMed:28652264"
SQ SEQUENCE 334 AA; 37957 MW; F52E5D92DFEE0A3E CRC64;
MSKNNKKKRR WDLKNGGILL EELIASFDGK TNPIRCFSSD QILKATDNFS ESRIISSWGY
FIWYKGVIEE RQVSIKKWSS QNLSSFTEAY RDISVSSQMS GHKNALKLIG CCLEFDLPAL
VCEYTEHGPL NRDGGLSSGV VLPWKVRLKI AKEIASSVTY LHTAFPETIV HRNINPTNIF
IDENWTAKLS DFWFCVAIPE GELYVEDDVK GVIGFVDPDY YWTMKVTEKV DIYSFGVVML
VLLSGRAAVF NGPDEAPMSL NDHVSEVMEK GEFDEIVDKE IWNDLGGDDD LVLRRSQVKA
FLRLALRCVR YKKEDPVSGM LEVAKELKLI EKLS
