PCRK1_ARATH
ID PCRK1_ARATH Reviewed; 418 AA.
AC Q9SF86; B9DGR0;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Serine/threonine-protein kinase PCRK1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:25711411};
DE AltName: Full=Protein PTI-COMPROMISED RECEPTOR-LIKE CYTOPLASMIC KINASE 1 {ECO:0000303|PubMed:25711411};
GN Name=PCRK1 {ECO:0000303|PubMed:25711411};
GN OrderedLocusNames=At3g09830 {ECO:0000312|Araport:AT3G09830};
GN ORFNames=F8A24.12 {ECO:0000312|EMBL:AAF23252.1};
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].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION BY BACTERIAL INFECTION, MUTAGENESIS
RP OF LYS-118, AND DISRUPTION PHENOTYPE.
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 [6]
RP FUNCTION, PHOSPHORYLATION AT SER-373; SER-377 AND SER-385, AND MUTAGENESIS
RP OF SER-373; SER-377 AND SER-385.
RX PubMed=26237268; DOI=10.1080/15592324.2015.1063759;
RA Sreekanta S., Haruta M., Minkoff B.B., Glazebrook J.;
RT "Functional characterization of PCRK1, a putative protein kinase with a
RT role in immunity.";
RL Plant Signal. Behav. 10:E1063759-E1063759(2015).
RN [7]
RP FUNCTION, INTERACTION WITH FLS2, AND SUBCELLULAR LOCATION.
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: Involved in the activation of early immune responses. Plays a
CC role in pattern-triggered immunity (PTI) induced by pathogen-associated
CC molecular patterns (PAMPs) and damage-associated molecular patterns
CC (DAMPs) (PubMed:25711411). Contributes to PTI in response to the
CC bacterial pathogen Pseudomonas syringae pv maculicola strain ES4326
CC (PubMed:25711411, PubMed:26237268). Contributes to PTI in response to
CC the bacterial pathogen Pseudomonas syringae pv tomato strain DC3000
CC (PubMed:25711411). Functions redundantly with PCRK2 in basal resistance
CC against bacterial pathogens and in regulation of plant immunity.
CC Functions together with PCRK2 downstream of the PAMP receptor FLS2.
CC Contributes to the induction of SARD1 and CBP60G, which are
CC transcriptional activator of ICS1, an enzyme involved in salicylate
CC (SA) biosynthesis upon pathogen attack (PubMed:27208222).
CC {ECO:0000269|PubMed:25711411, ECO:0000269|PubMed:26237268,
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:0000269|PubMed:25711411};
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:0000269|PubMed:25711411};
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, but not by microbe-associated
CC molecular patterns (MAMPs) such as flg22.
CC {ECO:0000269|PubMed:25711411}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants exhibit increased susceptibility to
CC infection with the bacterial pathogens Pseudomonas syringae pv
CC maculicola strain ES4326 and pv tomato strain DC3000.
CC {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; AC015985; AAF23252.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74818.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74819.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63951.1; -; Genomic_DNA.
DR EMBL; AY091117; AAM14067.1; -; mRNA.
DR EMBL; AY122981; AAM67514.1; -; mRNA.
DR EMBL; AK317246; BAH19927.1; -; mRNA.
DR RefSeq; NP_001326011.1; NM_001337847.1.
DR RefSeq; NP_187594.1; NM_111818.4.
DR RefSeq; NP_974270.1; NM_202541.3.
DR AlphaFoldDB; Q9SF86; -.
DR SMR; Q9SF86; -.
DR STRING; 3702.AT3G09830.1; -.
DR iPTMnet; Q9SF86; -.
DR PaxDb; Q9SF86; -.
DR PRIDE; Q9SF86; -.
DR ProteomicsDB; 236372; -.
DR EnsemblPlants; AT3G09830.1; AT3G09830.1; AT3G09830.
DR EnsemblPlants; AT3G09830.2; AT3G09830.2; AT3G09830.
DR EnsemblPlants; AT3G09830.3; AT3G09830.3; AT3G09830.
DR GeneID; 820141; -.
DR Gramene; AT3G09830.1; AT3G09830.1; AT3G09830.
DR Gramene; AT3G09830.2; AT3G09830.2; AT3G09830.
DR Gramene; AT3G09830.3; AT3G09830.3; AT3G09830.
DR KEGG; ath:AT3G09830; -.
DR Araport; AT3G09830; -.
DR TAIR; locus:2085069; AT3G09830.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_13_1; -.
DR InParanoid; Q9SF86; -.
DR OMA; IKSHEDS; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9SF86; -.
DR PRO; PR:Q9SF86; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SF86; baseline and differential.
DR GO; GO:0005829; C:cytosol; 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-EC.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
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 GO; GO:0009617; P:response to bacterium; IEP: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..418
FT /note="Serine/threonine-protein kinase PCRK1"
FT /id="PRO_0000442930"
FT DOMAIN 84..369
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 36..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 218
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 90..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26237268"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26237268"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26237268"
FT MUTAGEN 118
FT /note="K->E: Abolishes kinase activity. Abolishes PCRK1
FT function in pattern-triggered immunity (PTI)."
FT /evidence="ECO:0000269|PubMed:25711411"
FT MUTAGEN 373
FT /note="S->A: Abolishes PCRK1 function in pattern-triggered
FT immunity (PTI); when associated with A-377 and A-385."
FT /evidence="ECO:0000269|PubMed:26237268"
FT MUTAGEN 373
FT /note="S->D: No effect on PCRK1 function in pattern-
FT triggered immunity (PTI); when associated with D-377 and D-
FT 385."
FT /evidence="ECO:0000269|PubMed:26237268"
FT MUTAGEN 377
FT /note="S->A: Abolishes PCRK1 function in pattern-triggered
FT immunity (PTI); when associated with A-373 and A-385."
FT /evidence="ECO:0000269|PubMed:26237268"
FT MUTAGEN 377
FT /note="S->D: No effect on PCRK1 function in pattern-
FT triggered immunity (PTI); when associated with D-373 and D-
FT 385."
FT /evidence="ECO:0000269|PubMed:26237268"
FT MUTAGEN 385
FT /note="S->A: Abolishes PCRK1 function in pattern-triggered
FT immunity (PTI); when associated with A-373 and A-377."
FT /evidence="ECO:0000269|PubMed:26237268"
FT MUTAGEN 385
FT /note="S->D: No effect on PCRK1 function in pattern-
FT triggered immunity (PTI); when associated with D-373 and D-
FT 377."
FT /evidence="ECO:0000269|PubMed:26237268"
FT CONFLICT 395
FT /note="K -> E (in Ref. 4; BAH19927)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 46790 MW; 7AABB40D9644AEAB CRC64;
MKCFLFSGGD KRGEQKTPIS VSLTSIFSDR EINRSGSEFN SRDVSGTSTE SSMGRKNSYP
PVSTRASNLR EFSITDLKSA TKNFSRSVMI GEGGFGCVFR GTVRNLEDSS VKIEVAVKQL
GKRGLQGHKE WVTEVNFLGI VEHTNLVKLL GYCAEDDERG IQRLLVYEYM PNRSVEFHLS
PRSLTVLTWD LRLRIAQDAA RGLTYLHEEM EFQIIFRDFK SSNILLDEDW KAKLSDFGLA
RLGPSEGLTH VSTDVVGTMG YAAPEYIQTG RLTSKSDVWG YGVFLYELIT GRRPVDRNRP
KGEQKLLEWV RPYLSDTRKF KLILDPRLEG KYPIKSVQKL AVVANRCLVR NSKARPKMSE
VLEMVNKIVE ASSGNGSPQL VPLNSVKASR DARGKNNGGG GEGGWFGKLW NPKTIRAC
