BIR2_ARATH
ID BIR2_ARATH Reviewed; 605 AA.
AC Q9LSI9;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Inactive LRR receptor-like serine/threonine-protein kinase BIR2 {ECO:0000305};
DE AltName: Full=Protein BAK1-INTERACTING RECEPTOR-LIKE KINASE 2 {ECO:0000303|PubMed:24388849};
DE Flags: Precursor;
GN Name=BIR2 {ECO:0000303|PubMed:24388849};
GN OrderedLocusNames=At3g28450 {ECO:0000312|Araport:AT3G28450};
GN ORFNames=MFJ20.14 {ECO:0000312|EMBL:BAB02861.1};
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=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].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17869214; DOI=10.1016/j.bbrc.2007.08.177;
RA Hem S., Rofidal V., Sommerer N., Rossignol M.;
RT "Novel subsets of the Arabidopsis plasmalemma phosphoproteome identify
RT phosphorylation sites in secondary active transporters.";
RL Biochem. Biophys. Res. Commun. 363:375-380(2007).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH
RP BAK1, INDUCTION BY PAMP, AND PHOSPHORYLATION BY BAK1.
RC STRAIN=cv. Columbia;
RX PubMed=24388849; DOI=10.1016/j.cub.2013.11.047;
RA Halter T., Imkampe J., Mazzotta S., Wierzba M., Postel S., Buecherl C.,
RA Kiefer C., Stahl M., Chinchilla D., Wang X., Nuernberger T., Zipfel C.,
RA Clouse S., Borst J.W., Boeren S., de Vries S.C., Tax F., Kemmerling B.;
RT "The leucine-rich repeat receptor kinase BIR2 is a negative regulator of
RT BAK1 in plant immunity.";
RL Curr. Biol. 24:134-143(2014).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 271-605, FUNCTION,
RP PHOSPHORYLATION AT SER-271; THR-283; SER-286; THR-304; SER-330; SER-389;
RP SER-448; SER-462; THR-466 AND THR-533, PHOSPHORYLATION BY BAK1, INTERACTION
RP WITH BAK1, AND DOMAIN.
RX PubMed=24556575; DOI=10.1016/j.jsb.2014.02.005;
RA Blaum B.S., Mazzotta S., Noeldeke E.R., Halter T., Madlung J.,
RA Kemmerling B., Stehle T.;
RT "Structure of the pseudokinase domain of BIR2, a regulator of BAK1-mediated
RT immune signaling in Arabidopsis.";
RL J. Struct. Biol. 186:112-121(2014).
CC -!- FUNCTION: Pseudokinases lacking protein kinase activity and unable to
CC bind ATP-analogs (PubMed:24556575). Negative regulator of pathogen-
CC associated molecular patterns- (PAMP-) triggered immunity by limiting
CC BAK1-receptor complex formation in the absence of ligands
CC (PubMed:24388849). {ECO:0000269|PubMed:24388849,
CC ECO:0000269|PubMed:24556575}.
CC -!- SUBUNIT: Interacts constitutively with BAK1, when phosphorylated,
CC thereby preventing interaction with the ligand-binding LRR-RLK FLS2.
CC Upon infection, pathogen-associated molecular patterns (PAMP)
CC perception leads to BIR2 release from the BAK1 complex and enables the
CC recruitment of BAK1 into the FLS2 complex.
CC {ECO:0000269|PubMed:24388849, ECO:0000269|PubMed:24556575}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24388849};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:24388849}.
CC -!- INDUCTION: Induced by nonpathogenic bacteria or pathogen-associated
CC molecular patterns (PAMP) treatments. {ECO:0000269|PubMed:24388849}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159,
CC ECO:0000269|PubMed:24556575}.
CC -!- PTM: Phosphorylated by BAK1, this interacts promotes interaction with
CC BAK1. {ECO:0000269|PubMed:24388849}.
CC -!- DISRUPTION PHENOTYPE: Increased cell death spreading after Alternaria
CC brassicicola infection, and enhanced salicylic acid (SA) responses and
CC resistance to the biotrophic bacterial pathogen Pseudomonas syringae
CC pv. tomato DC3000. Impact on several BAK1-regulated processes, such as
CC hyperresponsiveness to pathogen-associated molecular patterns (PAMP),
CC enhanced cell death, and resistance to bacterial pathogens, but normal
CC brassinosteroid-(BR-)regulated growth. {ECO:0000269|PubMed:24388849}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
CC -!- CAUTION: Nucleotide binding site is not accessible for binding to ATP-
CC analogs. {ECO:0000269|PubMed:24556575}.
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DR EMBL; AB026644; BAB02861.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77446.1; -; Genomic_DNA.
DR EMBL; AK117357; BAC42027.1; -; mRNA.
DR EMBL; FJ708730; ACN59325.1; -; mRNA.
DR RefSeq; NP_189486.1; NM_113765.3.
DR PDB; 4L68; X-ray; 2.00 A; A/B=271-605.
DR PDB; 6FG7; X-ray; 1.90 A; A/B=1-223.
DR PDBsum; 4L68; -.
DR PDBsum; 6FG7; -.
DR AlphaFoldDB; Q9LSI9; -.
DR SMR; Q9LSI9; -.
DR IntAct; Q9LSI9; 35.
DR STRING; 3702.AT3G28450.1; -.
DR iPTMnet; Q9LSI9; -.
DR PaxDb; Q9LSI9; -.
DR PRIDE; Q9LSI9; -.
DR ProteomicsDB; 240546; -.
DR EnsemblPlants; AT3G28450.1; AT3G28450.1; AT3G28450.
DR GeneID; 822474; -.
DR Gramene; AT3G28450.1; AT3G28450.1; AT3G28450.
DR KEGG; ath:AT3G28450; -.
DR Araport; AT3G28450; -.
DR TAIR; locus:2088937; AT3G28450.
DR eggNOG; ENOG502QRP1; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; Q9LSI9; -.
DR OMA; WVNMHSS; -.
DR OrthoDB; 681595at2759; -.
DR PhylomeDB; Q9LSI9; -.
DR PRO; PR:Q9LSI9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSI9; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:1900425; P:negative regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Glycoprotein;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Plant defense; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..605
FT /note="Inactive LRR receptor-like serine/threonine-protein
FT kinase BIR2"
FT /evidence="ECO:0000255"
FT /id="PRO_5005371271"
FT TOPO_DOM 29..229
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..605
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 101..125
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 127..150
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 152..173
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 174..197
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT DOMAIN 307..578
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 313..321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 271
FT /note="Phosphoserine; by BAK1"
FT /evidence="ECO:0000269|PubMed:24556575"
FT MOD_RES 283
FT /note="Phosphothreonine; by BAK1"
FT /evidence="ECO:0000269|PubMed:24556575"
FT MOD_RES 286
FT /note="Phosphoserine; by BAK1"
FT /evidence="ECO:0000269|PubMed:24556575"
FT MOD_RES 304
FT /note="Phosphothreonine; by BAK1"
FT /evidence="ECO:0000269|PubMed:24556575"
FT MOD_RES 330
FT /note="Phosphoserine; by BAK1"
FT /evidence="ECO:0000269|PubMed:24556575"
FT MOD_RES 389
FT /note="Phosphoserine; by BAK1"
FT /evidence="ECO:0000269|PubMed:24556575"
FT MOD_RES 402
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 448
FT /note="Phosphoserine; by BAK1"
FT /evidence="ECO:0000269|PubMed:24556575"
FT MOD_RES 462
FT /note="Phosphoserine; by BAK1"
FT /evidence="ECO:0000269|PubMed:24556575"
FT MOD_RES 466
FT /note="Phosphothreonine; by BAK1"
FT /evidence="ECO:0000269|PubMed:24556575"
FT MOD_RES 479
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 482
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 533
FT /note="Phosphothreonine; by BAK1"
FT /evidence="ECO:0000269|PubMed:24556575"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:6FG7"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:6FG7"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:6FG7"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:6FG7"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:6FG7"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:6FG7"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:6FG7"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:6FG7"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:6FG7"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:6FG7"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:6FG7"
FT HELIX 145..149
FT /evidence="ECO:0007829|PDB:6FG7"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:6FG7"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:6FG7"
FT HELIX 169..173
FT /evidence="ECO:0007829|PDB:6FG7"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6FG7"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:6FG7"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:6FG7"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:6FG7"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:6FG7"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:6FG7"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:4L68"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:4L68"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:4L68"
FT HELIX 297..303
FT /evidence="ECO:0007829|PDB:4L68"
FT TURN 304..307
FT /evidence="ECO:0007829|PDB:4L68"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:4L68"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:4L68"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:4L68"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:4L68"
FT HELIX 344..355
FT /evidence="ECO:0007829|PDB:4L68"
FT STRAND 365..371
FT /evidence="ECO:0007829|PDB:4L68"
FT STRAND 374..380
FT /evidence="ECO:0007829|PDB:4L68"
FT HELIX 387..393
FT /evidence="ECO:0007829|PDB:4L68"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:4L68"
FT HELIX 400..419
FT /evidence="ECO:0007829|PDB:4L68"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:4L68"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:4L68"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:4L68"
FT TURN 448..450
FT /evidence="ECO:0007829|PDB:4L68"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:4L68"
FT HELIX 479..482
FT /evidence="ECO:0007829|PDB:4L68"
FT HELIX 487..503
FT /evidence="ECO:0007829|PDB:4L68"
FT HELIX 517..526
FT /evidence="ECO:0007829|PDB:4L68"
FT HELIX 530..533
FT /evidence="ECO:0007829|PDB:4L68"
FT TURN 536..540
FT /evidence="ECO:0007829|PDB:4L68"
FT HELIX 544..557
FT /evidence="ECO:0007829|PDB:4L68"
FT TURN 562..564
FT /evidence="ECO:0007829|PDB:4L68"
FT HELIX 568..580
FT /evidence="ECO:0007829|PDB:4L68"
FT TURN 581..583
FT /evidence="ECO:0007829|PDB:4L68"
FT HELIX 587..590
FT /evidence="ECO:0007829|PDB:4L68"
SQ SEQUENCE 605 AA; 66945 MW; B5FAF8D3BCB2B55F CRC64;
MKEIGSKPRK LLPLCFIIFL CFCSSVMAAD EDDIRCLRGL KASLTDPQNA LKSWNFDNTT
LGFLCNFVGV SCWNNQENRV INLELRDMGL SGKIPDSLQY CASLQKLDLS SNRLSGNIPT
ELCNWLPFLV SLDLSNNELN GEIPPDLAKC SFVNSLVLSD NRLSGQIPVQ FSALGRLGRF
SVANNDLSGR IPVFFSSPSY SSDDFSGNKG LCGRPLSSSC GGLSKKNLGI IIAAGVFGAA
ASMLLAFGIW WYYHLKWTRR RRSGLTEVGV SGLAQRLRSH KLTQVSLFQK PLVKVKLGDL
MAATNNFNSE NIIVSTRTGT TYKALLPDGS ALAVKHLSTC KLGEREFRYE MNQLWELRHS
NLAPLLGFCV VEEEKFLVYK YMSNGTLHSL LDSNRGELDW STRFRIGLGA ARGLAWLHHG
CRPPILHQNI CSSVILIDED FDARIIDSGL ARLMVPSDNN ESSFMTGDLG EFGYVAPEYS
TTMLASLKGD VYGLGVVLLE LATGLKAVGG EGFKGSLVDW VKQLESSGRI AETFDENIRG
KGHDEEISKF VEIALNCVSS RPKERWSMFQ AYQSLKAIAE KQGYSFSEQD DDFPLIFDTQ
ENEKV
