O49339 (PTI12_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
PTI1-like tyrosine-protein kinase 2
Short name=PTI1-2
EC=2.7.10.2

Gene names

Name:	PTI12
Ordered Locus Names:	At2g30740
ORF Names:	T11J7.13

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	366 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable tyrosine-protein kinase involved in oxidative burst-mediated signaling leading to specific genes expression. Ref.6
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Enzyme regulation	Strongly activated in response to phosphatidic acid (PA) and xylanase in a OXI1- and PDK1-dependent manner, and, to a lesser extent, by hydrogen peroxide and flagellin in a OXI1-dependent manner. Ref.6
Subunit structure	Interacts with OXI1. Ref.6
Subcellular location	Cell membrane; Peripheral membrane protein Ref.7.
Post-translational modification	Autophosphorylated and phosphorylated by OXI1. Ref.6
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Plant defense
Cellular component	Cell membrane Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	defense response Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	plasma membrane Inferred from direct assay Ref.7. Source: TAIR plasmodesma Inferred from direct assay PubMed 21533090. Source: TAIR
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 366	366	PTI1-like tyrosine-protein kinase 2		PRO_0000403323
Regions
	Domain	71 – 353	283	Protein kinase
	Nucleotide binding	77 – 85	9	ATP By similarity
Sites
	Active site	203	1	Proton acceptor By similarity
	Binding site	99	1	ATP Probable
Experimental info
	Mutagenesis	99	1	K → N: Reduced phosphorylation and impaired kinase activity. No phosphorylation; when associated with A-238. Ref.6
	Mutagenesis	238	1	T → A: No phosphorylation; when associated with N-99. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	O49339 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: E9A0450069D35C72	FASTA	366	40,500
	10 20 30 40 50 60 MRRWICCGDK KGDSDLSNEE VHLKSPWQNS EANQKNQKPQ AVVKPEAQKE ALPIEVPPLS 70 80 90 100 110 120 VDEVKEKTDN FGSKSLIGEG SYGRVYYATL NDGKAVALKK LDVAPEAETN TEFLNQVSMV 130 140 150 160 170 180 SRLKHENLIQ LVGYCVDENL RVLAYEFATM GSLHDILHGR KGVQGAQPGP TLDWLTRVKI 190 200 210 220 230 240 AVEAARGLEY LHEKVQPPVI HRDIRSSNVL LFEDYQAKVA DFNLSNQAPD NAARLHSTRV 250 260 270 280 290 300 LGTFGYHAPE YAMTGQLTQK SDVYSFGVVL LELLTGRKPV DHTMPRGQQS LVTWATPRLS 310 320 330 340 350 360 EDKVKQCVDP KLKGEYPPKS VAKLAAVAAL CVQYESEFRP NMSIVVKALQ PLLKPPAPAP APVPES

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Comparative proteome bioinformatics: identification of a whole complement of putative protein tyrosine kinases in the model flowering plant Arabidopsis thaliana." Carpi A., Di Maira G., Vedovato M., Rossi V., Naccari T., Floriduz M., Terzi M., Filippini F. Proteomics 2:1494-1503(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Arabidopsis ORF clones." Shinn P., Chen H., Kim C.J., Ecker J.R. Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"The Arabidopsis protein kinase PTI1-2 is activated by convergent phosphatidic acid and oxidative stress signaling pathways downstream of PDK1 and OXI1." Anthony R.G., Khan S., Costa J., Pais M.S., Boegre L. J. Biol. Chem. 281:37536-37546(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH OXI1, AUTOPHOSPHORYLATION, PHOSPHORYLATION BY OXI1, MUTAGENESIS OF LYS-99 AND THR-238, ENZYME REGULATION.
[7]	"Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis." Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M., Menke F.L.H. Mol. Cell. Proteomics 6:1198-1214(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Web resources

PlantP kinase Classification PPC

Arabidopsis protein tyrosine kinases

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ303007 mRNA. Translation: CAC34450.1. AC002340 Genomic DNA. Translation: AAC02745.1. CP002685 Genomic DNA. Translation: AEC08434.1. BT024893 mRNA. Translation: ABD85164.1. AK230305 mRNA. Translation: BAF02106.1.
IPI	IPI00531607.
PIR	B84712.
RefSeq	NP_180632.1. NM_128627.2.
UniGene	At.20728.
3D structure databases
HSSP	HSSP built from PDB template 2PTK based on UniProtKB P00523.
ProteinModelPortal	O49339.
SMR	O49339. Positions 43-352.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT2G30740.1-P.
Proteomic databases
PaxDb	O49339.
PRIDE	O49339.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G30740.1; AT2G30740.1; AT2G30740.
GeneID	817625.
KEGG	ath:AT2G30740.
Organism-specific databases
GeneFarm	1792. 139.
TAIR	At2g30740.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000116550.
InParanoid	O49339.
OMA	PYLENEN.
PhylomeDB	O49339.
ProtClustDB	CLSN2682494.
Gene expression databases
Genevestigator	O49339.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001245. Ser-Thr/Tyr_kinase_cat_dom. IPR008266. Tyr_kinase_AS. [Graphical view]
Pfam	PF07714. Pkinase_Tyr. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PTI12_ARATH

Accession

Primary (citable) accession number: O49339

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2011
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program