ID PBL1_ARATH Reviewed; 389 AA.
AC Q8H186; Q84WH8; Q9M2T4;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 143.
DE RecName: Full=Probable serine/threonine-protein kinase PBL1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=BIK1-like protein kinase {ECO:0000303|PubMed:20404519};
DE AltName: Full=PBS1-like protein 1 {ECO:0000303|PubMed:20413097};
DE AltName: Full=Protein CHANGED CALCIUM ELEVATION 5 {ECO:0000303|PubMed:25522736};
GN Name=PBL1 {ECO:0000303|PubMed:20413097};
GN Synonyms=BLK {ECO:0000303|PubMed:20404519},
GN CCE5 {ECO:0000303|PubMed:25522736};
GN OrderedLocusNames=At3g55450 {ECO:0000312|Araport:AT3G55450};
GN ORFNames=T22E16.110 {ECO:0000312|EMBL:CAB75903.1};
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 FUNCTION, INTERACTION WITH FLS2, PHOSPHORYLATION, INDUCTION BY FLAGELLIN,
RP GENE FAMILY, NOMENCLATURE, AND DISRUPTION PHENOTYPE.
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 [5]
RP PHOSPHORYLATION.
RX PubMed=20404519; DOI=10.4161/psb.11500;
RA Lu D., Wu S., He P., Shan L.;
RT "Phosphorylation of receptor-like cytoplasmic kinases by bacterial
RT flagellin.";
RL Plant Signal. Behav. 5:598-600(2010).
RN [6]
RP FUNCTION.
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 [7]
RP FUNCTION, AND INTERACTION WITH PEPR1.
RX PubMed=23431184; DOI=10.1073/pnas.1215543110;
RA Liu Z., Wu Y., Yang F., Zhang Y., Chen S., Xie Q., Tian X., Zhou J.M.;
RT "BIK1 interacts with PEPRs to mediate ethylene-induced immunity.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6205-6210(2013).
RN [8]
RP FUNCTION, MUTAGENESIS OF GLY-2; GLY-70; ALA-97 AND ARG-172, DISRUPTION
RP PHENOTYPE, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=25522736; DOI=10.1186/s12870-014-0374-4;
RA Ranf S., Eschen-Lippold L., Froehlich K., Westphal L., Scheel D., Lee J.;
RT "Microbe-associated molecular pattern-induced calcium signaling requires
RT the receptor-like cytoplasmic kinases, PBL1 and BIK1.";
RL BMC Plant Biol. 14:374-374(2014).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Contributes to pathogen-associated molecular pattern (PAMP)-
CC triggered immunity (PTI) signaling, including calcium signaling and
CC root growth inhibition, and defense responses downstream of FLS2
CC (PubMed:20413097, PubMed:25522736). Acts additively with BIK1 in PTI
CC defenses (PubMed:20413097, PubMed:25522736). Seems not required for
CC flg22-induced MAPK activation (Probable). Required for Pep1-induced
CC defenses (PubMed:25522736). Pep1 is an endogenous elicitor that
CC potentiates PAMP-inducible plant responses (PubMed:23431184,
CC PubMed:25522736). Required during SCOOP small peptides (e.g. SCOOP10
CC and SCOOP12) perception and signaling; receptor-like cytosolic kinases
CC (RLCK) activated by BAK1/SERK3 and SERK4 coreceptors when associated
CC with MIK2 upon the perception of SCOOP peptides (PubMed:34535661).
CC {ECO:0000269|PubMed:20413097, ECO:0000269|PubMed:23431184,
CC ECO:0000269|PubMed:25522736, ECO:0000269|PubMed:34535661,
CC ECO:0000305|PubMed:22504181}.
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 FLS2 (PubMed:20413097). Interacts with PEPR1
CC (PubMed:23431184). {ECO:0000269|PubMed:20413097,
CC ECO:0000269|PubMed:23431184}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25522736};
CC Lipid-anchor {ECO:0000269|PubMed:25522736}. Note=Myristoylation and
CC proper targeting to plasma membrane is essential for signaling function
CC in response to pathogen-associated molecular pattern (PAMP) such as
CC flg22. {ECO:0000269|PubMed:25522736}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8H186-1; Sequence=Displayed;
CC -!- INDUCTION: Induced by flagellin (flg22). {ECO:0000269|PubMed:20413097}.
CC -!- PTM: Phosphorylated upon flagellin (flg22) treatment.
CC {ECO:0000269|PubMed:20404519, ECO:0000269|PubMed:20413097,
CC ECO:0000269|PubMed:25522736}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:20413097). Abrogated kinase activity
CC (PubMed:25522736). In cce5-2 and cce5-4, reduced calcium levels after
CC elicitation with peptides representing bacteria-derived microbe- and
CC damage-associated molecular patterns (MAMPs, flg22 and elf18, and the
CC endogenous DAMP AtPep1), but normal response to chitin octamers.
CC Reduced root growth inhibition response to flg22 (PubMed:25522736).
CC Compromised SCOOP10- and SCOOP12-induced root growth inhibition and
CC reactive oxygen species (ROS) production in the double mutant bik1 pbl1
CC (PubMed:34535661). {ECO:0000269|PubMed:20413097,
CC ECO:0000269|PubMed:25522736, ECO:0000269|PubMed:34535661}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB75903.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL132975; CAB75903.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79385.1; -; Genomic_DNA.
DR EMBL; BT000431; AAN17408.1; -; mRNA.
DR EMBL; BT003347; AAO29965.1; -; mRNA.
DR PIR; T47684; T47684.
DR RefSeq; NP_191105.2; NM_115403.4. [Q8H186-1]
DR AlphaFoldDB; Q8H186; -.
DR SMR; Q8H186; -.
DR STRING; 3702.Q8H186; -.
DR iPTMnet; Q8H186; -.
DR SwissPalm; Q8H186; -.
DR PaxDb; 3702-AT3G55450-2; -.
DR ProteomicsDB; 236793; -. [Q8H186-1]
DR EnsemblPlants; AT3G55450.1; AT3G55450.1; AT3G55450. [Q8H186-1]
DR GeneID; 824711; -.
DR Gramene; AT3G55450.1; AT3G55450.1; AT3G55450. [Q8H186-1]
DR KEGG; ath:AT3G55450; -.
DR Araport; AT3G55450; -.
DR TAIR; AT3G55450; PBL1.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_1_1; -.
DR InParanoid; Q8H186; -.
DR OMA; VQCKPLS; -.
DR PhylomeDB; Q8H186; -.
DR PRO; PR:Q8H186; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8H186; baseline and differential.
DR Genevisible; Q8H186; AT.
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; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:1900424; P:regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IMP:UniProtKB.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR45621; OS01G0588500 PROTEIN-RELATED; 1.
DR PANTHER; PTHR45621:SF184; SERINE_THREONINE-PROTEIN KINASE PBL1-RELATED; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Kinase; Lipoprotein;
KW Membrane; Myristate; Nucleotide-binding; Palmitate; Phosphoprotein;
KW Plant defense; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..389
FT /note="Probable serine/threonine-protein kinase PBL1"
FT /id="PRO_0000389473"
FT DOMAIN 61..352
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 67..75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 144
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 232
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 237
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 245
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9FE20"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9FE20"
FT MUTAGEN 2
FT /note="G->A: Mis-localization and impaired phosphorylation
FT upon flagellin (flg22) treatment, but conserved kinase
FT activity and autophosphorylation."
FT /evidence="ECO:0000269|PubMed:25522736"
FT MUTAGEN 70
FT /note="G->D: In cce5-1; reduced calcium levels after
FT elicitation with peptides representing bacteria-derived
FT microbe- and damage-associated molecular patterns (MAMPs,
FT flg22 and elf18, and the endogenous DAMP AtPep1), but
FT normal response to chitin octamers. Impaired
FT phosphorylation upon flagellin (flg22) treatment, and lost
FT kinase activity and autophosphorylation."
FT /evidence="ECO:0000269|PubMed:25522736"
FT MUTAGEN 97
FT /note="A->V: In cce5-3; reduced calcium levels after
FT elicitation with peptides representing bacteria-derived
FT microbe- and damage-associated molecular patterns (MAMPs,
FT flg22 and elf18, and the endogenous DAMP AtPep1), but
FT normal response to chitin octamers. Impaired
FT phosphorylation upon flagellin (flg22) treatment, and lost
FT kinase activity and autophosphorylation."
FT /evidence="ECO:0000269|PubMed:25522736"
FT MUTAGEN 172
FT /note="R->Q: In cce5-5; reduced calcium levels after
FT elicitation with peptides representing bacteria-derived
FT microbe- and damage-associated molecular patterns (MAMPs,
FT flg22 and elf18, and the endogenous DAMP AtPep1), but
FT normal response to chitin octamers. Impaired
FT phosphorylation upon flagellin (flg22) treatment, and lost
FT kinase activity and autophosphorylation."
FT /evidence="ECO:0000269|PubMed:25522736"
FT CONFLICT 6
FT /note="S -> T (in Ref. 3; AAO29965)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 389 AA; 43087 MW; 61F5F218D3AC5862 CRC64;
MGSCLSSRVL NKSSSGLDDL HLSSCKSSSS ATAHKTEGEI LSSTTVKSFS FNELKLATRN
FRSDSVVGEG GFGCVFRGWL DETTLTPTKS SSGLVIAVKR LNPDGFQGHR EWLTEINYLG
QLSHPNLVKL IGYCLEDEQR LLVYEFMHKG SLENHLFANG NKDFKPLSWI LRIKVALDAA
KGLAFLHSDP VKVIYRDIKA SNILLDSDFN AKLSDFGLAR DGPMGEQSYV STRVMGTFGY
AAPEYVSTGH LNARSDVYSF GVVLLELLCG RQALDHNRPA KEQNLVDWAR PYLTSRRKVL
LIVDTRLNSQ YKPEGAVRLA SIAVQCLSFE PKSRPTMDQV VRALVQLQDS VVKPANVDPL
KVKDTKKLVG LKTEDKYQRN GLNKKTVGL
//
