PTI12_ARATH
ID PTI12_ARATH Reviewed; 366 AA.
AC O49339;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=PTI1-like tyrosine-protein kinase 2;
DE Short=PTI1-2;
DE EC=2.7.10.2;
GN Name=PTI12; OrderedLocusNames=At2g30740; ORFNames=T11J7.13;
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].
RC STRAIN=cv. Columbia;
RX PubMed=12442249;
RX DOI=10.1002/1615-9861(200211)2:11<1494::aid-prot1494>3.0.co;2-#;
RA Carpi A., Di Maira G., Vedovato M., Rossi V., Naccari T., Floriduz M.,
RA Terzi M., Filippini F.;
RT "Comparative proteome bioinformatics: identification of a whole complement
RT of putative protein tyrosine kinases in the model flowering plant
RT Arabidopsis thaliana.";
RL Proteomics 2:1494-1503(2002).
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;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, INTERACTION WITH OXI1, AUTOPHOSPHORYLATION, PHOSPHORYLATION BY
RP OXI1, MUTAGENESIS OF LYS-99 AND THR-238, AND ACTIVITY REGULATION.
RX PubMed=17040918; DOI=10.1074/jbc.m607341200;
RA Anthony R.G., Khan S., Costa J., Pais M.S., Boegre L.;
RT "The Arabidopsis protein kinase PTI1-2 is activated by convergent
RT phosphatidic acid and oxidative stress signaling pathways downstream of
RT PDK1 and OXI1.";
RL J. Biol. Chem. 281:37536-37546(2006).
CC -!- FUNCTION: Probable tyrosine-protein kinase involved in oxidative burst-
CC mediated signaling leading to specific genes expression.
CC {ECO:0000269|PubMed:17040918}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- ACTIVITY REGULATION: Strongly activated in response to phosphatidic
CC acid (PA) and xylanase in a OXI1- and PDK1-dependent manner, and, to a
CC lesser extent, by hydrogen peroxide and flagellin in a OXI1-dependent
CC manner. {ECO:0000269|PubMed:17040918}.
CC -!- SUBUNIT: Interacts with OXI1. {ECO:0000269|PubMed:17040918}.
CC -!- PTM: Autophosphorylated and phosphorylated by OXI1.
CC {ECO:0000269|PubMed:17040918}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- WEB RESOURCE: Name=Arabidopsis protein tyrosine kinases;
CC URL="http://www.bio.unipd.it/molbinfo/PTKtable.html";
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DR EMBL; AJ303007; CAC34450.1; -; mRNA.
DR EMBL; AC002340; AAC02745.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08434.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62808.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62809.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62810.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62811.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62812.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62813.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62814.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62815.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62816.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62817.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62818.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62819.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62820.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62821.1; -; Genomic_DNA.
DR EMBL; BT024893; ABD85164.1; -; mRNA.
DR EMBL; AK230305; BAF02106.1; -; mRNA.
DR PIR; B84712; B84712.
DR RefSeq; NP_001318322.1; NM_001336285.1.
DR RefSeq; NP_001324937.1; NM_001336289.1.
DR RefSeq; NP_001324938.1; NM_001336288.1.
DR RefSeq; NP_001324939.1; NM_001336287.1.
DR RefSeq; NP_001324940.1; NM_001336291.1.
DR RefSeq; NP_001324941.1; NM_001336286.1.
DR RefSeq; NP_001324942.1; NM_001336290.1.
DR RefSeq; NP_001324943.1; NM_001336297.1.
DR RefSeq; NP_001324944.1; NM_001336296.1.
DR RefSeq; NP_001324945.1; NM_001336295.1.
DR RefSeq; NP_001324946.1; NM_001336294.1.
DR RefSeq; NP_001324947.1; NM_001336293.1.
DR RefSeq; NP_001324948.1; NM_001336292.1.
DR RefSeq; NP_001324949.1; NM_001336299.1.
DR RefSeq; NP_001324950.1; NM_001336298.1.
DR AlphaFoldDB; O49339; -.
DR SMR; O49339; -.
DR BioGRID; 2974; 5.
DR STRING; 3702.AT2G30740.1; -.
DR iPTMnet; O49339; -.
DR SwissPalm; O49339; -.
DR PaxDb; O49339; -.
DR PRIDE; O49339; -.
DR ProteomicsDB; 226171; -.
DR EnsemblPlants; AT2G30740.1; AT2G30740.1; AT2G30740.
DR EnsemblPlants; AT2G30740.10; AT2G30740.10; AT2G30740.
DR EnsemblPlants; AT2G30740.11; AT2G30740.11; AT2G30740.
DR EnsemblPlants; AT2G30740.12; AT2G30740.12; AT2G30740.
DR EnsemblPlants; AT2G30740.13; AT2G30740.13; AT2G30740.
DR EnsemblPlants; AT2G30740.14; AT2G30740.14; AT2G30740.
DR EnsemblPlants; AT2G30740.15; AT2G30740.15; AT2G30740.
DR EnsemblPlants; AT2G30740.2; AT2G30740.2; AT2G30740.
DR EnsemblPlants; AT2G30740.3; AT2G30740.3; AT2G30740.
DR EnsemblPlants; AT2G30740.4; AT2G30740.4; AT2G30740.
DR EnsemblPlants; AT2G30740.5; AT2G30740.5; AT2G30740.
DR EnsemblPlants; AT2G30740.6; AT2G30740.6; AT2G30740.
DR EnsemblPlants; AT2G30740.7; AT2G30740.7; AT2G30740.
DR EnsemblPlants; AT2G30740.8; AT2G30740.8; AT2G30740.
DR EnsemblPlants; AT2G30740.9; AT2G30740.9; AT2G30740.
DR GeneID; 817625; -.
DR Gramene; AT2G30740.1; AT2G30740.1; AT2G30740.
DR Gramene; AT2G30740.10; AT2G30740.10; AT2G30740.
DR Gramene; AT2G30740.11; AT2G30740.11; AT2G30740.
DR Gramene; AT2G30740.12; AT2G30740.12; AT2G30740.
DR Gramene; AT2G30740.13; AT2G30740.13; AT2G30740.
DR Gramene; AT2G30740.14; AT2G30740.14; AT2G30740.
DR Gramene; AT2G30740.15; AT2G30740.15; AT2G30740.
DR Gramene; AT2G30740.2; AT2G30740.2; AT2G30740.
DR Gramene; AT2G30740.3; AT2G30740.3; AT2G30740.
DR Gramene; AT2G30740.4; AT2G30740.4; AT2G30740.
DR Gramene; AT2G30740.5; AT2G30740.5; AT2G30740.
DR Gramene; AT2G30740.6; AT2G30740.6; AT2G30740.
DR Gramene; AT2G30740.7; AT2G30740.7; AT2G30740.
DR Gramene; AT2G30740.8; AT2G30740.8; AT2G30740.
DR Gramene; AT2G30740.9; AT2G30740.9; AT2G30740.
DR KEGG; ath:AT2G30740; -.
DR Araport; AT2G30740; -.
DR TAIR; locus:2054502; AT2G30740.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_4_1; -.
DR InParanoid; O49339; -.
DR OMA; HLKSPWQ; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; O49339; -.
DR PRO; PR:O49339; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O49339; baseline and differential.
DR Genevisible; O49339; AT.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; Plant defense;
KW Reference proteome; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..366
FT /note="PTI1-like tyrosine-protein kinase 2"
FT /id="PRO_0000403323"
FT DOMAIN 71..353
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 8..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 203
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 77..85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MUTAGEN 99
FT /note="K->N: Reduced phosphorylation and impaired kinase
FT activity. No phosphorylation; when associated with A-238."
FT /evidence="ECO:0000269|PubMed:17040918"
FT MUTAGEN 238
FT /note="T->A: No phosphorylation; when associated with N-
FT 99."
FT /evidence="ECO:0000269|PubMed:17040918"
SQ SEQUENCE 366 AA; 40500 MW; E9A0450069D35C72 CRC64;
MRRWICCGDK KGDSDLSNEE VHLKSPWQNS EANQKNQKPQ AVVKPEAQKE ALPIEVPPLS
VDEVKEKTDN FGSKSLIGEG SYGRVYYATL NDGKAVALKK LDVAPEAETN TEFLNQVSMV
SRLKHENLIQ LVGYCVDENL RVLAYEFATM GSLHDILHGR KGVQGAQPGP TLDWLTRVKI
AVEAARGLEY LHEKVQPPVI HRDIRSSNVL LFEDYQAKVA DFNLSNQAPD NAARLHSTRV
LGTFGYHAPE YAMTGQLTQK SDVYSFGVVL LELLTGRKPV DHTMPRGQQS LVTWATPRLS
EDKVKQCVDP KLKGEYPPKS VAKLAAVAAL CVQYESEFRP NMSIVVKALQ PLLKPPAPAP
APVPES
