PBL13_ARATH
ID PBL13_ARATH Reviewed; 494 AA.
AC F4JZW1; Q56YK6; Q9FH10;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Serine/threonine-protein kinase PBL13 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:26432875};
DE AltName: Full=PBS1-like protein 13 {ECO:0000303|PubMed:20413097};
DE AltName: Full=Ser/Thr protein kinase ACIK1b {ECO:0000312|EMBL:AED93983.1};
GN Name=PBL13 {ECO:0000303|PubMed:20413097};
GN OrderedLocusNames=At5g35580 {ECO:0000312|Araport:AT5G35580};
GN ORFNames=K2K18.3 {ECO:0000312|EMBL:BAB09992.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INDUCTION.
RX PubMed=16673935; DOI=10.1094/mpmi-19-0480;
RA Siemens J., Keller I., Sarx J., Kunz S., Schuller A., Nagel W.,
RA Schmuelling T., Parniske M., Ludwig-Mueller J.;
RT "Transcriptome analysis of Arabidopsis clubroots indicate a key role for
RT cytokinins in disease development.";
RL Mol. Plant Microbe Interact. 19:480-494(2006).
RN [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH RBOHD, SUBCELLULAR LOCATION,
RP IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-240; SER-321;
RP THR-323; THR-383; SER-384; THR-395; THR-398; THR-406; THR-413; THR-421;
RP THR-428; SER-429; THR-443; SER-444; SER-455; THR-456 AND TYR-481,
RP MUTAGENESIS OF LYS-111, AND DISRUPTION PHENOTYPE.
RX PubMed=26432875; DOI=10.1104/pp.15.01391;
RA Lin Z.J., Liebrand T.W., Yadeta K.A., Coaker G.;
RT "PBL13 is a serine/threonine protein kinase that negatively regulates
RT Arabidopsis immune responses.";
RL Plant Physiol. 169:2950-2962(2015).
CC -!- FUNCTION: Involved in defense responses. Acts as negative regulator of
CC plant immune responses. {ECO:0000269|PubMed:26432875}.
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:26432875};
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:26432875};
CC -!- SUBUNIT: Interacts with RBHOD. Interaction is disrupted by flagellin-
CC induced immune signaling. {ECO:0000269|PubMed:26432875}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26432875}.
CC -!- INDUCTION: Down-regulated during infection by Plasmodiophora brassicae.
CC {ECO:0000269|PubMed:16673935}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. Mutant plants exhibit enhanced disease resistance after
CC inoculation with virulent Pseudomonas syringae, elevated basal-level
CC expression of the PR1 defense marker gene, enhanced reactive oxygen
CC species (ROS) burst in response to perception of bacterial microbial
CC patterns, and accelerated flagellin-induced activation of MAP kinases.
CC {ECO:0000269|PubMed:26432875}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09992.1; Type=Erroneous gene model prediction; 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; AB023031; BAB09992.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93983.1; -; Genomic_DNA.
DR EMBL; AK221316; BAD94092.1; -; mRNA.
DR RefSeq; NP_198408.2; NM_122949.3.
DR AlphaFoldDB; F4JZW1; -.
DR SMR; F4JZW1; -.
DR STRING; 3702.AT5G35580.1; -.
DR iPTMnet; F4JZW1; -.
DR PaxDb; F4JZW1; -.
DR PRIDE; F4JZW1; -.
DR ProteomicsDB; 236441; -.
DR EnsemblPlants; AT5G35580.1; AT5G35580.1; AT5G35580.
DR GeneID; 833523; -.
DR Gramene; AT5G35580.1; AT5G35580.1; AT5G35580.
DR KEGG; ath:AT5G35580; -.
DR Araport; AT5G35580; -.
DR TAIR; locus:2157101; AT5G35580.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_2_1; -.
DR InParanoid; F4JZW1; -.
DR OMA; FHHHENH; -.
DR PRO; PR:F4JZW1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4JZW1; baseline and differential.
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; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0050777; P:negative regulation of immune response; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 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..494
FT /note="Serine/threonine-protein kinase PBL13"
FT /id="PRO_0000438608"
FT DOMAIN 76..356
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 434..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 206
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 82..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 65
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 156
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 240
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26432875"
FT MOD_RES 241
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 246
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 254
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 321
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26432875"
FT MOD_RES 323
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26432875"
FT MOD_RES 383
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26432875"
FT MOD_RES 384
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26432875"
FT MOD_RES 395
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26432875"
FT MOD_RES 398
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26432875"
FT MOD_RES 406
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26432875"
FT MOD_RES 413
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26432875"
FT MOD_RES 421
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26432875"
FT MOD_RES 428
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26432875"
FT MOD_RES 429
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26432875"
FT MOD_RES 443
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26432875"
FT MOD_RES 444
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26432875"
FT MOD_RES 455
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26432875"
FT MOD_RES 456
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26432875"
FT MOD_RES 481
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26432875"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9FE20"
FT MUTAGEN 111
FT /note="K->A: Abolishes kinase activity."
FT /evidence="ECO:0000269|PubMed:26432875"
FT CONFLICT 89
FT /note="P -> L (in Ref. 3; BAD94092)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="D -> G (in Ref. 3; BAD94092)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 56172 MW; 0C9D1B2C898052F5 CRC64;
MVLCFQDPDN IYSPKKTKKD DGERVITKQK SFLGLSILDI SNPSSTTLSE DLSISLAGSD
LHVFTQAELR VITQSFSSSN FLGEGGFGPV HKGFIDDKLR PGLKAQPVAV KLLDLDGLQG
HREFMTEVMC LGKLKHPNLV KLIGYCCEEA HRLLVYEFMP RGSLESQLFR RCSLPLPWTT
RLNIAYEAAK GLQFLHEAEK PIIYRDFKAS NILLDSDYTA KLSDFGLAKD GPQGDDTHVS
TRVMGTQGYA APEYIMTGHL TAKSDVYSFG VVLLELLTGR KSVDIARSSR KETLVEWARP
MLNDARKLGR IMDPRLEDQY SETGARKAAT LAYQCLRYRP KTRPDISTVV SVLQDIKDYK
DDIPIGIFTY TVPTKPRREV KETSLQNFDK PRRETKVTSL QNFDKTRREV KDTSLQNFDK
TRREVKETSL QNFDKTRREV KETSLQNFDK PRNVSTTDNH QKFRSPAHTA RNHRITLRNG
YNSPMRNEAG GERY
