ZRK3_ARATH
ID ZRK3_ARATH Reviewed; 355 AA.
AC Q8VZF4; A0A178V857; Q9SVY7;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Serine/threonine-protein kinase ZRK3 {ECO:0000303|PubMed:26355215};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
GN Name=ZRK3 {ECO:0000303|PubMed:26355215};
GN OrderedLocusNames=At3g57730 {ECO:0000312|Araport:AT3G57730};
GN ORFNames=F15B8.80 {ECO:0000312|EMBL:CAB41182.1};
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=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;
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 INTERACTION WITH RPP13L4/ZAR1, GENE FAMILY, 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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=28288096; DOI=10.1038/nplants.2017.27;
RA Seto D., Koulena N., Lo T., Menna A., Guttman D.S., Desveaux D.;
RT "Expanded type III effector recognition by the ZAR1 NLR protein using ZED1-
RT related kinases.";
RL Nat. Plants 3:17027-17027(2017).
CC -!- FUNCTION: Required for RPP13L4/ZAR1 recognition of the Pseudomonas
CC syringae type III effector (T3E) HopF2a. {ECO:0000269|PubMed:28288096}.
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:0000255|PROSITE-ProRule:PRU00159};
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:0000255|PROSITE-ProRule:PRU00159};
CC -!- SUBUNIT: Interacts with RPP13L4/ZAR1. {ECO:0000269|PubMed:26355215}.
CC -!- DISRUPTION PHENOTYPE: Reduced resistance to Pseudomonas syringae
CC expressing HopZ1a. {ECO:0000269|PubMed:28288096}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. ZRK subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41182.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL049660; CAB41182.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE79691.1; -; Genomic_DNA.
DR EMBL; AY064993; AAL57644.1; -; mRNA.
DR EMBL; AY124830; AAM70539.1; -; mRNA.
DR PIR; T06747; T06747.
DR RefSeq; NP_191332.2; NM_115633.4.
DR AlphaFoldDB; Q8VZF4; -.
DR SMR; Q8VZF4; -.
DR IntAct; Q8VZF4; 1.
DR STRING; 3702.AT3G57730.1; -.
DR PaxDb; Q8VZF4; -.
DR PRIDE; Q8VZF4; -.
DR ProteomicsDB; 183552; -.
DR EnsemblPlants; AT3G57730.1; AT3G57730.1; AT3G57730.
DR GeneID; 824942; -.
DR Gramene; AT3G57730.1; AT3G57730.1; AT3G57730.
DR KEGG; ath:AT3G57730; -.
DR Araport; AT3G57730; -.
DR TAIR; locus:2076671; AT3G57730.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_4_1; -.
DR InParanoid; Q8VZF4; -.
DR OMA; AYLHMAF; -.
DR OrthoDB; 778960at2759; -.
DR PhylomeDB; Q8VZF4; -.
DR PRO; PR:Q8VZF4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IEA:UniProtKB-EC.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..355
FT /note="Serine/threonine-protein kinase ZRK3"
FT /id="PRO_0000449491"
FT DOMAIN 67..353
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 196
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 73..81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 355 AA; 40855 MW; B4442247F6D029C4 CRC64;
MESMVKKLKQ NLRTGSWKKK EKSMKKERWF LENGSIFLKE LIVDCNGKSI PIRSFTSSQI
RKATKNFDLS CFVAEEGFYI WYKGVIEDRS YMIKRFSEYK VTDYRVSEVY KDIVLSARMS
NHNNFLKLLG CCLEFPFPVL VFEFAEHGVL NYRGGITVNG EESLLPLSLR LKIGKEIANA
LAYLHMAFPK IIIYRDVKPL HVFLDNNWTA KLSDLSFSIS LEEGKSQIEA EDVLGTYGYL
DPLYFATRIV TEYTDVYSFG VFLMVVITGI SVYFTGSDGY PVGILGYMKG LAENGKLNEI
VYPMIMKEMT SAQRLQVEAC VLLALRCCEE RVEDRPKMIQ VAKELKRIEH HVLRS
