PBL3_ARATH
ID PBL3_ARATH Reviewed; 426 AA.
AC O49840; Q8GYU1;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Probable serine/threonine-protein kinase PBL3 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=PBS1-like protein 3 {ECO:0000303|PubMed:20413097};
DE AltName: Full=Protein kinase 2B {ECO:0000305};
GN Name=PBL3 {ECO:0000303|PubMed:20413097};
GN Synonyms=APK2B {ECO:0000303|PubMed:9150601},
GN KIN2 {ECO:0000303|PubMed:21219905}, PIX14 {ECO:0000303|PubMed:23951354};
GN OrderedLocusNames=At2g02800; ORFNames=T20F6.6;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9150601; DOI=10.1093/oxfordjournals.pcp.a029160;
RA Ito T., Takahashi N., Shimura Y., Okada K.;
RT "A serine/threonine protein kinase gene isolated by an in vivo binding
RT procedure using the Arabidopsis floral homeotic gene product, AGAMOUS.";
RL Plant Cell Physiol. 38:248-258(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
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 [7]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-2, AND MYRISTOYLATION AT GLY-2.
RX PubMed=21219905; DOI=10.1016/j.febslet.2011.01.001;
RA Stael S., Bayer R.G., Mehlmer N., Teige M.;
RT "Protein N-acylation overrides differing targeting signals.";
RL FEBS Lett. 585:517-522(2011).
RN [8]
RP INTERACTION WITH XANTHOMONAS CAMPESTRIS XOPAC/AVRAC.
RX PubMed=23951354; DOI=10.1371/journal.pone.0073469;
RA Guy E., Lautier M., Chabannes M., Roux B., Lauber E., Arlat M., Noel L.D.;
RT "xopAC-triggered immunity against Xanthomonas depends on Arabidopsis
RT receptor-like cytoplasmic kinase genes PBL2 and RIPK.";
RL PLoS ONE 8:E73469-E73469(2013).
CC -!- FUNCTION: May be involved in plant defense signaling.
CC {ECO:0000250|UniProtKB:O48814}.
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 the Xanthomonas campestris effector
CC XopAC/AvrAC. {ECO:0000269|PubMed:23951354}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21219905};
CC Lipid-anchor {ECO:0000305|PubMed:21219905}. Nucleus
CC {ECO:0000269|PubMed:21219905}. Note=Predominantly localized at the
CC plasma membrane. {ECO:0000269|PubMed:21219905}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in leaves, moderately in
CC flowers, and barely in roots. {ECO:0000269|PubMed:9150601}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; D88207; BAA24695.1; -; mRNA.
DR EMBL; AC002521; AAC05342.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05625.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05626.1; -; Genomic_DNA.
DR EMBL; AK117389; BAC42058.1; -; mRNA.
DR EMBL; AF428432; AAL16201.1; -; mRNA.
DR EMBL; AY125559; AAM78069.1; -; mRNA.
DR PIR; T00848; T00848.
DR RefSeq; NP_178383.1; NM_126335.6.
DR RefSeq; NP_973403.1; NM_201674.2.
DR AlphaFoldDB; O49840; -.
DR SMR; O49840; -.
DR BioGRID; 212; 2.
DR IntAct; O49840; 2.
DR STRING; 3702.AT2G02800.1; -.
DR iPTMnet; O49840; -.
DR PaxDb; O49840; -.
DR PRIDE; O49840; -.
DR ProteomicsDB; 236280; -.
DR EnsemblPlants; AT2G02800.1; AT2G02800.1; AT2G02800.
DR EnsemblPlants; AT2G02800.2; AT2G02800.2; AT2G02800.
DR GeneID; 814810; -.
DR Gramene; AT2G02800.1; AT2G02800.1; AT2G02800.
DR Gramene; AT2G02800.2; AT2G02800.2; AT2G02800.
DR KEGG; ath:AT2G02800; -.
DR Araport; AT2G02800; -.
DR TAIR; locus:2058847; AT2G02800.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_1_1; -.
DR InParanoid; O49840; -.
DR OMA; SKYNMAS; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; O49840; -.
DR PRO; PR:O49840; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O49840; baseline and differential.
DR Genevisible; O49840; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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: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; Myristate;
KW Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein; Plant defense;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:21219905"
FT CHAIN 2..426
FT /note="Probable serine/threonine-protein kinase PBL3"
FT /id="PRO_0000389477"
FT DOMAIN 83..366
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 216
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 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 72
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 166
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 251
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 256
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 264
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000305|PubMed:21219905"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9FE20"
FT MUTAGEN 2
FT /note="G->A: Drastic reduction of plasma membrane
FT localization and strong increase of nuclear localization."
FT /evidence="ECO:0000269|PubMed:21219905"
FT CONFLICT 295
FT /note="K -> R (in Ref. 4; BAC42058)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 46289 MW; C73C695C98501EBA CRC64;
MGNCLDSSAK VDSSSHSPHA NSASLSSRVS SKTSRSTVPS SLSINSYSSV ESLPTPRTEG
EILSSPNLKA FTFNELKNAT RNFRPDSLLG EGGFGYVFKG WIDGTTLTAS KPGSGIVVAV
KKLKTEGYQG HKEWLTEVNY LGQLSHPNLV KLVGYCVEGE NRLLVYEFMP KGSLENHLFR
RGAQPLTWAI RMKVAIGAAK GLTFLHDAKS QVIYRDFKAA NILLDAEFNS KLSDFGLAKA
GPTGDKTHVS TQVMGTHGYA APEYVATGRL TAKSDVYSFG VVLLELLSGR RAVDKSKVGM
EQSLVDWATP YLGDKRKLFR IMDTRLGGQY PQKGAYTAAS LALQCLNPDA KLRPKMSEVL
AKLDQLESTK PGTGVGNRQA QIDSPRGSNG SIVQKSPRRY SYDRPLLHIT PGASPLPTHN
HSPRVR
