PTI13_ARATH
ID PTI13_ARATH Reviewed; 408 AA.
AC B9DFG5; B9DHY7; Q940H1; Q9LX36;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=PTI1-like tyrosine-protein kinase 3;
DE Short=PTI1-3;
DE EC=2.7.10.2;
GN Name=PTI13; OrderedLocusNames=At3g59350; ORFNames=F25L23.210;
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] (ISOFORM 2).
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] (ISOFORM 1).
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 INTERACTION WITH OXI1, AND PHOSPHORYLATION BY OXI1.
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).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17644812; DOI=10.1074/mcp.m700099-mcp200;
RA Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J.,
RA Barbier-Brygoo H., Ephritikhine G.;
RT "A high content in lipid-modified peripheral proteins and integral receptor
RT kinases features in the arabidopsis plasma membrane proteome.";
RL Mol. Cell. Proteomics 6:1980-1996(2007).
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 -!- SUBUNIT: Interacts with OXI1. {ECO:0000269|PubMed:17040918}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:17644812};
CC Peripheral membrane protein {ECO:0000305|PubMed:17644812}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B9DFG5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B9DFG5-2; Sequence=VSP_040369;
CC -!- PTM: Phosphorylated by OXI1. {ECO:0000269|PubMed:17040918}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB91605.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Arabidopsis protein tyrosine kinases;
CC URL="http://www.bio.unipd.it/molbinfo/PTKtable.html";
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DR EMBL; AL356014; CAB91605.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79908.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79909.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79910.1; -; Genomic_DNA.
DR EMBL; AY054639; AAK96830.1; -; mRNA.
DR EMBL; BT008449; AAP37808.1; -; mRNA.
DR EMBL; AK316761; BAH19482.1; -; mRNA.
DR EMBL; AK317695; BAH20354.1; -; mRNA.
DR PIR; T49003; T49003.
DR RefSeq; NP_001030893.1; NM_001035816.1. [B9DFG5-1]
DR RefSeq; NP_567082.2; NM_115797.6. [B9DFG5-1]
DR RefSeq; NP_850720.1; NM_180389.3. [B9DFG5-2]
DR AlphaFoldDB; B9DFG5; -.
DR SMR; B9DFG5; -.
DR BioGRID; 10419; 3.
DR IntAct; B9DFG5; 2.
DR STRING; 3702.AT3G59350.1; -.
DR iPTMnet; B9DFG5; -.
DR SwissPalm; B9DFG5; -.
DR PaxDb; B9DFG5; -.
DR PRIDE; B9DFG5; -.
DR EnsemblPlants; AT3G59350.1; AT3G59350.1; AT3G59350. [B9DFG5-1]
DR EnsemblPlants; AT3G59350.2; AT3G59350.2; AT3G59350. [B9DFG5-2]
DR EnsemblPlants; AT3G59350.3; AT3G59350.3; AT3G59350. [B9DFG5-1]
DR GeneID; 825104; -.
DR Gramene; AT3G59350.1; AT3G59350.1; AT3G59350. [B9DFG5-1]
DR Gramene; AT3G59350.2; AT3G59350.2; AT3G59350. [B9DFG5-2]
DR Gramene; AT3G59350.3; AT3G59350.3; AT3G59350. [B9DFG5-1]
DR KEGG; ath:AT3G59350; -.
DR Araport; AT3G59350; -.
DR TAIR; locus:2081277; AT3G59350.
DR eggNOG; KOG1187; Eukaryota.
DR InParanoid; B9DFG5; -.
DR PhylomeDB; B9DFG5; -.
DR PRO; PR:B9DFG5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; B9DFG5; baseline and differential.
DR Genevisible; B9DFG5; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IPI: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:0010375; P:stomatal complex patterning; IGI: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 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 Alternative splicing; ATP-binding; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..408
FT /note="PTI1-like tyrosine-protein kinase 3"
FT /id="PRO_0000403324"
FT DOMAIN 113..395
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 59..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 245
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 119..127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..42
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_040369"
SQ SEQUENCE 408 AA; 45658 MW; 57AF0E1D1E5B0F8C CRC64;
MYPMDSDYHR RGLVANDRSP AQFVRLDKPR AVDDLYIGKR EKMRRWLCCA CHVEEPYHSS
ENEHLRSPKH HNDFGHHTRK PQAAVKPDAL KEPPSIDVPA LSLDELKEKT DNFGSKSLIG
EGSYGRAYYA TLKDGKAVAV KKLDNAAEPE SNVEFLTQVS RVSKLKHDNF VELFGYCVEG
NFRILAYEFA TMGSLHDILH GRKGVQGAQP GPTLDWIQRV RIAVDAARGL EYLHEKVQPA
VIHRDIRSSN VLLFEDFKAK IADFNLSNQS PDMAARLHST RVLGTFGYHA PEYAMTGQLT
QKSDVYSFGV VLLELLTGRK PVDHTMPRGQ QSLVTWATPR LSEDKVKQCV DPKLKGEYPP
KAVAKLAAVA ALCVQYESEF RPNMSIVVKA LQPLLRSSTA AAVPVQEA
