PBL36_ARATH
ID PBL36_ARATH Reviewed; 476 AA.
AC F4J0D2; A0A178VMS8; A0A1S5M0M9; B3LFC3;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Serine/threonine-protein kinase PBL36 {ECO:0000303|PubMed:29907700};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9LFP7};
DE AltName: Full=PBS1-like protein 36 {ECO:0000303|PubMed:29907700};
DE AltName: Full=Receptor-like cytoplasmic kinase PBL36 {ECO:0000303|PubMed:29907700};
GN Name=PBL36 {ECO:0000303|PubMed:29907700};
GN OrderedLocusNames=At3g28690 {ECO:0000312|EMBL:AEE77476.2};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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] OF 101-476.
RC STRAIN=cv. Columbia;
RA De Los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [5]
RP FUNCTION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=29907700; DOI=10.1104/pp.18.00486;
RA Rao S., Zhou Z., Miao P., Bi G., Hu M., Wu Y., Feng F., Zhang X.,
RA Zhou J.M.;
RT "Roles of receptor-like cytoplasmic kinase VII members in pattern-triggered
RT immune signaling.";
RL Plant Physiol. 177:1679-1690(2018).
RN [6]
RP FUNCTION, INTERACTION WITH SD129, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION.
RX PubMed=31922267; DOI=10.15252/embj.2019102856;
RA Luo X., Wu W., Liang Y., Xu N., Wang Z., Zou H., Liu J.;
RT "Tyrosine phosphorylation of the lectin receptor-like kinase LORE regulates
RT plant immunity.";
RL EMBO J. 39:e102856-e102856(2020).
CC -!- FUNCTION: Involved in chitin-triggered immune signaling and is required
CC for reactive oxygen species (ROS) production (PubMed:29907700). Acts
CC downstream of SD129 in defense signaling triggered by the pathogen-
CC associated molecular pattern (PAMP) 3-OH-C10:0, a medium-chain 3-
CC hydroxy fatty acid (PubMed:31922267). {ECO:0000269|PubMed:29907700,
CC ECO:0000269|PubMed:31922267}.
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:0000250|UniProtKB:Q9LFP7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000250|UniProtKB:Q9LFP7};
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:0000250|UniProtKB:Q9LFP7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000250|UniProtKB:Q9LFP7};
CC -!- SUBUNIT: Interacts with SD129. {ECO:0000269|PubMed:31922267}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31922267};
CC Lipid-anchor {ECO:0000250|UniProtKB:O48814}.
CC -!- PTM: Phosphorylated by SD129 in response to the pathogen-associated
CC molecular pattern (PAMP) 3-OH-C10:0, a medium-chain 3-hydroxy fatty
CC acid. {ECO:0000269|PubMed:31922267}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEE77475.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002686; AEE77475.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77476.2; -; Genomic_DNA.
DR EMBL; BT033112; ACF20467.1; -; mRNA.
DR RefSeq; NP_001030790.3; NM_001035713.4.
DR RefSeq; NP_189510.2; NM_113789.4.
DR AlphaFoldDB; F4J0D2; -.
DR SMR; F4J0D2; -.
DR STRING; 3702.AT3G28690.2; -.
DR PaxDb; F4J0D2; -.
DR PRIDE; F4J0D2; -.
DR ProteomicsDB; 187996; -.
DR ProteomicsDB; 196021; -.
DR EnsemblPlants; AT3G28690.1; AT3G28690.1; AT3G28690.
DR EnsemblPlants; AT3G28690.2; AT3G28690.2; AT3G28690.
DR GeneID; 822499; -.
DR Gramene; AT3G28690.1; AT3G28690.1; AT3G28690.
DR Gramene; AT3G28690.2; AT3G28690.2; AT3G28690.
DR KEGG; ath:AT3G28690; -.
DR Araport; AT3G28690; -.
DR TAIR; locus:2095517; AT3G28690.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_4_1; -.
DR InParanoid; F4J0D2; -.
DR OrthoDB; 684563at2759; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J0D2; 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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0002221; P:pattern recognition receptor signaling pathway; IDA: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; IPR017441; Protein_kinase_ATP_BS.
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; 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; Phosphoprotein; Plant defense; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..476
FT /note="Serine/threonine-protein kinase PBL36"
FT /id="PRO_0000452692"
FT DOMAIN 126..412
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 431..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 259
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 132..140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 209
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 294
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 299
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 307
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
SQ SEQUENCE 476 AA; 52878 MW; EE5CD49F38203490 CRC64;
MATKLESFKV VEKLGVEKGE KGKMMSKKKN VKKDGDESES GFWFRFKFIF SCISSRSKVD
SSMNATAVIA EPKKVIEKLE GHPAPTKDTG CAESGSSTPL MSGELKYSSK LRIFMFNDLK
LATRNFRPES LLGEGGFGCV FKGWIEENGT APVKPGTGLT VAVKTLNPDG LQGHKEWLAE
INFLGNLVHP SLVKLVGYCM EEDQRLLVYE FMPRGSLENH LFRRTLPLPW SVRMKIALGA
AKGLAFLHEE AEKPVIYRDF KTSNILLDGE YNAKLSDFGL AKDAPDEKKS HVSTRVMGTY
GYAAPEYVMT GHLTTKSDVY SFGVVLLEIL TGRRSVDKSR PNGEQNLVEW VRPHLLDKKR
FYRLLDPRLE GHYSIKGAQK ATQVAAQCLN RDSKARPKMS EVVEALKPLP NLKDFASSSS
SFQTMQPVAK NGVRTQGGGF VSRNGPPMRS LSSLNLPQAS PYRYARQSPK PKGKEP
