PCRK2_ARATH
ID PCRK2_ARATH Reviewed; 420 AA.
AC Q9LZF8;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Serine/threonine-protein kinase PCRK2 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305|PubMed:27208222};
DE AltName: Full=Protein PTI-COMPROMISED RECEPTOR-LIKE CYTOPLASMIC KINASE 2 {ECO:0000305};
GN Name=PCRK2 {ECO:0000303|PubMed:27208222};
GN OrderedLocusNames=At5g03320 {ECO:0000312|Araport:AT5G03320};
GN ORFNames=F12E4_50 {ECO:0000312|EMBL:CAB83288.1};
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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;
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 [5]
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 [6]
RP INDUCTION BY BACTERIAL INFECTION.
RX PubMed=25711411; DOI=10.1111/nph.13345;
RA Sreekanta S., Bethke G., Hatsugai N., Tsuda K., Thao A., Wang L.,
RA Katagiri F., Glazebrook J.;
RT "The receptor-like cytoplasmic kinase PCRK1 contributes to pattern-
RT triggered immunity against Pseudomonas syringae in Arabidopsis thaliana.";
RL New Phytol. 207:78-90(2015).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH FLS2, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF LYS-115.
RX PubMed=27208222; DOI=10.1104/pp.15.01954;
RA Kong Q., Sun T., Qu N., Ma J., Li M., Cheng Y.T., Zhang Q., Wu D.,
RA Zhang Z., Zhang Y.;
RT "Two redundant receptor-like cytoplasmic kinases function downstream of
RT pattern recognition receptors to regulate activation of SA biosynthesis.";
RL Plant Physiol. 171:1344-1354(2016).
CC -!- FUNCTION: Functions redundantly with PCRK1 in basal resistance against
CC bacterial pathogens and in regulation of plant immunity. Functions
CC together with PCRK1 downstream of the pathogen-associated molecular
CC pattern (PAMP) receptor FLS2. Contributes to the induction of SARD1 and
CC CBP60G, which are transcriptional activator of ICS1, an enzyme involved
CC in salicylate (SA) biosynthesis upon pathogen attack.
CC {ECO:0000269|PubMed:27208222}.
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|PubMed:27208222};
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|PubMed:27208222};
CC -!- SUBUNIT: Interacts with FLS2. {ECO:0000269|PubMed:27208222}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27208222};
CC Peripheral membrane protein {ECO:0000305|PubMed:27208222}.
CC -!- INDUCTION: Induced by infection with the bacterial pathogen Pseudomonas
CC syringae pv maculicola strain ES4326. {ECO:0000269|PubMed:25711411}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; AB005240; BAB08392.1; -; Genomic_DNA.
DR EMBL; AL162751; CAB83288.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90584.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68777.1; -; Genomic_DNA.
DR EMBL; BT028916; ABI49463.1; -; mRNA.
DR PIR; T48353; T48353.
DR RefSeq; NP_001330499.1; NM_001342698.1.
DR RefSeq; NP_195952.1; NM_120410.5.
DR AlphaFoldDB; Q9LZF8; -.
DR SMR; Q9LZF8; -.
DR STRING; 3702.AT5G03320.1; -.
DR iPTMnet; Q9LZF8; -.
DR PaxDb; Q9LZF8; -.
DR PRIDE; Q9LZF8; -.
DR ProteomicsDB; 236848; -.
DR EnsemblPlants; AT5G03320.1; AT5G03320.1; AT5G03320.
DR EnsemblPlants; AT5G03320.2; AT5G03320.2; AT5G03320.
DR GeneID; 831876; -.
DR Gramene; AT5G03320.1; AT5G03320.1; AT5G03320.
DR Gramene; AT5G03320.2; AT5G03320.2; AT5G03320.
DR KEGG; ath:AT5G03320; -.
DR Araport; AT5G03320; -.
DR TAIR; locus:2142639; AT5G03320.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_13_1; -.
DR InParanoid; Q9LZF8; -.
DR OMA; HCAEDNE; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9LZF8; -.
DR PRO; PR:Q9LZF8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZF8; baseline and differential.
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-EC.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0002221; P:pattern recognition receptor signaling pathway; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0080142; P:regulation of salicylic acid biosynthetic process; IMP:TAIR.
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 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.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Plant defense; Reference proteome; Transferase.
FT CHAIN 1..420
FT /note="Serine/threonine-protein kinase PCRK2"
FT /id="PRO_0000442931"
FT DOMAIN 81..366
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 87..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 70
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 164
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 250
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 255
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 263
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MUTAGEN 115
FT /note="K->E: Abolishes PCRK2 function in basal resistance
FT against bacterial pathogens."
FT /evidence="ECO:0000269|PubMed:27208222"
SQ SEQUENCE 420 AA; 47006 MW; 537221AADE43DD07 CRC64;
MKCFLFPLGD KKDEQRSPKP VSPTSNFSDV NKSGSDFSPR DVSGTSTVSS TGRNSNTSMS
ARENNLREFT IGDLKSATRN FSRSGMIGEG GFGCVFWGTI KNLEDPSKKI EVAVKQLGKR
GLQGHKEWVT EVNFLGVVEH SNLVKLLGHC AEDDERGIQR LLVYEYMPNQ SVEFHLSPRS
PTVLTWDLRL RIAQDAARGL TYLHEEMDFQ IIFRDFKSSN ILLDENWTAK LSDFGLARLG
PSPGSSHVST DVVGTMGYAA PEYIQTGRLT SKSDVWGYGV FIYELITGRR PLDRNKPKGE
QKLLEWVRPY LSDTRRFRLI VDPRLEGKYM IKSVQKLAVV ANLCLTRNAK ARPKMSEVLE
MVTKIVEASS PGNGGKKPQL VPLKSQETSR VEEGKNKKVL DGAEGGWLEK LWNPKNVRAC
