PBL27_ARATH
ID PBL27_ARATH Reviewed; 513 AA.
AC Q1PDV6; A0MFG6;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Serine/threonine-protein kinase PBL27 {ECO:0000303|PubMed:20413097};
DE EC=2.7.11.1 {ECO:0000269|PubMed:27679653};
DE AltName: Full=PBS1-like protein 27 {ECO:0000303|PubMed:20413097};
DE AltName: Full=Receptor-like cytoplasmic kinase PBL27 {ECO:0000303|PubMed:27679653};
GN Name=PBL27 {ECO:0000303|PubMed:20413097};
GN OrderedLocusNames=At5g18610 {ECO:0000312|Araport:AT5G18610};
GN ORFNames=T28N17.90 {ECO:0000312|EMBL:AC069328};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-112, PHOSPHORYLATION BY
RP CERK1, INTERACTION WITH CERK1, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=24750441; DOI=10.1111/tpj.12535;
RA Shinya T., Yamaguchi K., Desaki Y., Yamada K., Narisawa T., Kobayashi Y.,
RA Maeda K., Suzuki M., Tanimoto T., Takeda J., Nakashima M., Funama R.,
RA Narusaka M., Narusaka Y., Kaku H., Kawasaki T., Shibuya N.;
RT "Selective regulation of the chitin-induced defense response by the
RT Arabidopsis receptor-like cytoplasmic kinase PBL27.";
RL Plant J. 79:56-66(2014).
RN [9]
RP FUNCTION, MUTAGENESIS OF LYS-112; SER-244; THR-245 AND THR-250, INTERACTION
RP WITH CERK1; MAPKKK3 AND MAPKKK5, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP SER-244; THR-245 AND THR-250 BY CERK1, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=27679653; DOI=10.15252/embj.201694248;
RA Yamada K., Yamaguchi K., Shirakawa T., Nakagami H., Mine A., Ishikawa K.,
RA Fujiwara M., Narusaka M., Narusaka Y., Ichimura K., Kobayashi Y.,
RA Matsui H., Nomura Y., Nomoto M., Tada Y., Fukao Y., Fukamizo T., Tsuda K.,
RA Shirasu K., Shibuya N., Kawasaki T.;
RT "The Arabidopsis CERK1-associated kinase PBL27 connects chitin perception
RT to MAPK activation.";
RL EMBO J. 35:2468-2483(2016).
CC -!- FUNCTION: Receptor-like cytoplasmic kinase involved in the transduction
CC of signal between the host cell surface chitin receptor complex CERK1-
CC LYK5 and the intracellular MAPKKK5-dependent mitogen-activated protein
CC kinase (MAPK) cascade that leads to chitin-induced immunity
CC (PubMed:24750441, PubMed:27679653). Phosphorylates and activates
CC MAPKKK5 when phosphorylated by CERK1 after elicitation by chitin
CC (PubMed:27679653). {ECO:0000269|PubMed:24750441,
CC ECO:0000269|PubMed:27679653}.
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:0000269|PubMed:27679653};
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:0000269|PubMed:27679653};
CC -!- SUBUNIT: Interacts with CERK1 (preferentially unphosphorylated) at the
CC plasma membrane (PubMed:24750441, PubMed:27679653). Binds to MAPKKK5 at
CC the plasma membrane; disassociation is induced by chitin perception by
CC the CERK1 complex. Associates also with MAPKKK3 (PubMed:27679653).
CC {ECO:0000269|PubMed:24750441, ECO:0000269|PubMed:27679653}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24750441,
CC ECO:0000269|PubMed:27679653}; Lipid-anchor
CC {ECO:0000269|PubMed:24750441}.
CC -!- INDUCTION: Levels are regulated in a proteasome-dependent manner (at
CC proteome level). {ECO:0000269|PubMed:27679653}.
CC -!- PTM: Phosphorylated by CERK1 upon elicitation by chitin.
CC {ECO:0000269|PubMed:24750441, ECO:0000269|PubMed:27679653}.
CC -!- PTM: Palmitoylation at Cys-4 and Cys-7 are required for plasma membrane
CC location. {ECO:0000250|UniProtKB:Q9FE20}.
CC -!- DISRUPTION PHENOTYPE: Impaired chitin-induced defense responses such as
CC MAPK activation (e.g. MPK3/6) and callose deposition leading to reduced
CC disease resistance against fungal (e.g. A.brassicicola) and bacterial
CC (e.g. P.syringae pv. tomato DC3000 hrcC) infections.
CC {ECO:0000269|PubMed:24750441}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28701.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC051627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92585.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92586.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70412.1; -; Genomic_DNA.
DR EMBL; DQ446962; ABE66165.1; -; mRNA.
DR EMBL; DQ653292; ABK28701.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001190331.1; NM_001203402.1.
DR RefSeq; NP_001318594.1; NM_001343556.1.
DR RefSeq; NP_197362.1; NM_121866.2.
DR AlphaFoldDB; Q1PDV6; -.
DR SMR; Q1PDV6; -.
DR STRING; 3702.AT5G18610.2; -.
DR iPTMnet; Q1PDV6; -.
DR SwissPalm; Q1PDV6; -.
DR PaxDb; Q1PDV6; -.
DR PRIDE; Q1PDV6; -.
DR ProteomicsDB; 236841; -.
DR EnsemblPlants; AT5G18610.1; AT5G18610.1; AT5G18610.
DR EnsemblPlants; AT5G18610.2; AT5G18610.2; AT5G18610.
DR EnsemblPlants; AT5G18610.3; AT5G18610.3; AT5G18610.
DR GeneID; 831979; -.
DR Gramene; AT5G18610.1; AT5G18610.1; AT5G18610.
DR Gramene; AT5G18610.2; AT5G18610.2; AT5G18610.
DR Gramene; AT5G18610.3; AT5G18610.3; AT5G18610.
DR KEGG; ath:AT5G18610; -.
DR Araport; AT5G18610; -.
DR TAIR; locus:2183018; AT5G18610.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_0_1; -.
DR InParanoid; Q1PDV6; -.
DR OMA; WSTRMTI; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q1PDV6; -.
DR PRO; PR:Q1PDV6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q1PDV6; baseline and differential.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:GO_Central.
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:0071323; P:cellular response to chitin; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IDA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IMP:TAIR.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
DR GO; GO:0045088; P:regulation of innate immune response; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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 ATP-binding; Cell membrane; Kinase; Lipoprotein; Membrane;
KW Nucleotide-binding; Palmitate; Phosphoprotein; Plant defense;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..513
FT /note="Serine/threonine-protein kinase PBL27"
FT /id="PRO_0000438618"
FT DOMAIN 83..360
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 210
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 89..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 244
FT /note="Phosphoserine; by CERK1"
FT /evidence="ECO:0000305|PubMed:27679653"
FT MOD_RES 245
FT /note="Phosphothreonine; by CERK1"
FT /evidence="ECO:0000305|PubMed:27679653"
FT MOD_RES 250
FT /note="Phosphothreonine; by CERK1"
FT /evidence="ECO:0000305|PubMed:27679653"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:14506206,
FT ECO:0007744|PubMed:15308754"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9FE20"
FT LIPID 7
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9FE20"
FT MUTAGEN 112
FT /note="K->E: No autophosphorylation activity. Directly
FT phosphorylated by CERK1 in vitro. Impaired CERK1-mediated
FT phosphorylation; when associated with A-244; A-245 and A-
FT 250."
FT /evidence="ECO:0000269|PubMed:24750441,
FT ECO:0000269|PubMed:27679653"
FT MUTAGEN 244
FT /note="S->A: Impaired CERK1-mediated phosphorylation; when
FT associated with E-112; A-245 and A-250."
FT /evidence="ECO:0000269|PubMed:27679653"
FT MUTAGEN 245
FT /note="T->A: Impaired CERK1-mediated phosphorylation; when
FT associated with E-112; A-244 and A-250."
FT /evidence="ECO:0000269|PubMed:27679653"
FT MUTAGEN 250
FT /note="T->A: Impaired CERK1-mediated phosphorylation; when
FT associated with E-112; A-244 and A-245."
FT /evidence="ECO:0000269|PubMed:27679653"
SQ SEQUENCE 513 AA; 55931 MW; 9FC534796025AB87 CRC64;
MSGCLPCFGS SAKDAASKDS VKKELSAKDG SVTQSHHISL DKSKSRRGPE QKKELTAPKE
GPTAHIAAQT FTFRELAAAT KNFRPECLLG EGGFGRVYKG RLETTGQIVA VKQLDRNGLQ
GNREFLVEVL MLSLLHHPNL VNLIGYCADG DQRLLVYEYM PLGSLEDHLH DLPPDKEPLD
WSTRMTIAAG AAKGLEYLHD KANPPVIYRD LKSSNILLGD GYHPKLSDFG LAKLGPVGDK
THVSTRVMGT YGYCAPEYAM TGQLTLKSDV YSFGVVFLEL ITGRKAIDNA RAPGEHNLVA
WARPLFKDRR KFPKMADPSL QGRYPMRGLY QALAVAAMCL QEQAATRPLI GDVVTALTYL
ASQTFDPNAP SGQNSRSGSG PPFIRTRDDR RSLGDGSSLD SPAETRSRLG SPATHKNSPD
YRRRDMVREV NAGSEGGSET GGGSGRKWGL SDLEGQESQR GSPASVGRSS RGTPRNRDLD
RERAVAEAKV WGENWRERKR ATNGPGSFDS TND
