PBL35_ARATH
ID PBL35_ARATH Reviewed; 490 AA.
AC Q9SRH7; Q8LBS0; Q93ZF1;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Serine/threonine-protein kinase PBL35 {ECO:0000303|PubMed:29907700};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9LFP7};
DE AltName: Full=PBS1-like protein 35 {ECO:0000303|PubMed:29907700};
DE AltName: Full=Receptor-like cytoplasmic kinase PBL35 {ECO:0000303|PubMed:29907700};
GN Name=PBL35 {ECO:0000303|PubMed:29907700};
GN OrderedLocusNames=At3g01300 {ECO:0000312|EMBL:AEE73634.1};
GN ORFNames=T22N4.7 {ECO:0000312|EMBL:AAF03496.1},
GN T4P13.2 {ECO:0000312|EMBL:AAF26145.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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=AAL14379.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAM64595.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC008261; AAF26145.1; -; Genomic_DNA.
DR EMBL; AC010676; AAF03496.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73634.1; -; Genomic_DNA.
DR EMBL; AY057584; AAL14379.1; ALT_FRAME; mRNA.
DR EMBL; AY087034; AAM64595.1; ALT_INIT; mRNA.
DR EMBL; BT028957; ABI54332.1; -; mRNA.
DR RefSeq; NP_186779.1; NM_110996.3.
DR AlphaFoldDB; Q9SRH7; -.
DR SMR; Q9SRH7; -.
DR BioGRID; 6322; 5.
DR IntAct; Q9SRH7; 5.
DR STRING; 3702.AT3G01300.1; -.
DR iPTMnet; Q9SRH7; -.
DR PaxDb; Q9SRH7; -.
DR PRIDE; Q9SRH7; -.
DR ProteomicsDB; 232362; -.
DR EnsemblPlants; AT3G01300.1; AT3G01300.1; AT3G01300.
DR GeneID; 820989; -.
DR Gramene; AT3G01300.1; AT3G01300.1; AT3G01300.
DR KEGG; ath:AT3G01300; -.
DR Araport; AT3G01300; -.
DR TAIR; locus:2100282; AT3G01300.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_1_1; -.
DR InParanoid; Q9SRH7; -.
DR OMA; MLCCVAS; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9SRH7; -.
DR PRO; PR:Q9SRH7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SRH7; baseline and differential.
DR Genevisible; Q9SRH7; 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: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; Coiled coil; Kinase; Lipoprotein; Membrane;
KW Nucleotide-binding; Phosphoprotein; Plant defense; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..490
FT /note="Serine/threonine-protein kinase PBL35"
FT /id="PRO_0000403351"
FT DOMAIN 136..422
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 14..39
FT /evidence="ECO:0000255"
FT COMPBIAS 449..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 142..150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 219
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 304
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 309
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 317
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
SQ SEQUENCE 490 AA; 54510 MW; B9E3D0D5CE06227B CRC64;
MGFDSVKVME NWQSKTSNEN EKKKKKRRRK KNNNVRNSEH YEEEANGCWV KFRYIVCCAS
STSDVETSLT LSTSTVGSQS AIVQSNDQPV GPVSSTTTTS NAESSLSTPI ISEELNIYSH
LKKFSFIDLK LATRNFRPES LLGEGGFGCV FKGWVEENGT APVKPGTGLT VAVKTLNPDG
LQGHKEWLAE INYLGNLLHP NLVKLVGYCI EDDQRLLVYE FMPRGSLENH LFRRSLPLPW
SIRMKIALGA AKGLSFLHEE ALKPVIYRDF KTSNILLDGE YNAKLSDFGL AKDAPDEGKT
HVSTRVMGTY GYAAPEYVMT GHLTSKSDVY SFGVVLLEML TGRRSMDKNR PNGEHNLVEW
ARPHLLDKRR FYRLLDPRLE GHFSVKGAQK VTQLAAQCLS RDSKIRPKMS EVVEVLKPLP
HLKDMASASY YFQTMQAERL KAGSGSGSGR GFGSRNGQPV FRTLSSPHGQ AGSSPYRHQI
PSPKPKGATT
