PTI11_ARATH
ID PTI11_ARATH Reviewed; 361 AA.
AC Q8H1G6; Q94K67; Q9M9X8; Q9SHK8;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=PTI1-like tyrosine-protein kinase 1;
DE Short=PTI1-1;
DE EC=2.7.10.2;
GN Name=PTI11; OrderedLocusNames=At1g06700; ORFNames=F12K11.1, F4H5.21;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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; TISSUE=Root;
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, AUTOPHOSPHORYLATION, 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 -!- 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 -!- SEQUENCE CAUTION:
CC Sequence=AAF24808.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF63147.1; 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; AC007592; AAF24808.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC011001; AAF63147.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28025.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28026.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60512.1; -; Genomic_DNA.
DR EMBL; AF370260; AAK44075.1; -; mRNA.
DR EMBL; AY150374; AAN12919.1; -; mRNA.
DR EMBL; AK317491; BAH20156.1; -; mRNA.
DR PIR; F86201; F86201.
DR RefSeq; NP_001030981.1; NM_001035904.2.
DR RefSeq; NP_001322793.1; NM_001331644.1.
DR RefSeq; NP_172155.1; NM_100547.3.
DR AlphaFoldDB; Q8H1G6; -.
DR SMR; Q8H1G6; -.
DR BioGRID; 22421; 5.
DR IntAct; Q8H1G6; 1.
DR MINT; Q8H1G6; -.
DR STRING; 3702.AT1G06700.2; -.
DR PaxDb; Q8H1G6; -.
DR PRIDE; Q8H1G6; -.
DR ProteomicsDB; 224828; -.
DR EnsemblPlants; AT1G06700.1; AT1G06700.1; AT1G06700.
DR EnsemblPlants; AT1G06700.2; AT1G06700.2; AT1G06700.
DR EnsemblPlants; AT1G06700.3; AT1G06700.3; AT1G06700.
DR GeneID; 837180; -.
DR Gramene; AT1G06700.1; AT1G06700.1; AT1G06700.
DR Gramene; AT1G06700.2; AT1G06700.2; AT1G06700.
DR Gramene; AT1G06700.3; AT1G06700.3; AT1G06700.
DR KEGG; ath:AT1G06700; -.
DR Araport; AT1G06700; -.
DR TAIR; locus:2009115; AT1G06700.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_4_1; -.
DR InParanoid; Q8H1G6; -.
DR OMA; TCQIEDS; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q8H1G6; -.
DR PRO; PR:Q8H1G6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8H1G6; baseline and differential.
DR Genevisible; Q8H1G6; AT.
DR GO; GO:0005886; C:plasma membrane; 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 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; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..361
FT /note="PTI1-like tyrosine-protein kinase 1"
FT /id="PRO_0000403322"
FT DOMAIN 68..350
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 16..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 74..82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 343
FT /note="V -> A (in Ref. 3; AAK44075)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 39820 MW; 49CD8A555DEF458B CRC64;
MRKWICCTCQ IEDSNEEQQL KSSQQQSDAN HKNSKPAPVA KHEVKKEALP IEVPPLSLDE
VKEKTENFGS KALIGEGSYG RVYYATLNDG VAVALKKLDV APEAETDTEF LSQVSMVSRL
KHENLIQLLG FCVDGNLRVL AYEFATMGSL HDILHGRKGV QGAQPGPTLD WITRVKIAVE
AARGLEYLHE KSQPPVIHRD IRSSNVLLFE DYKAKIADFN LSNQAPDNAA RLHSTRVLGT
FGYHAPEYAM TGQLTQKSDV YSFGVVLLEL LTGRKPVDHT MPRGQQSLVT WATPRLSEDK
VKQCIDPKLK ADYPPKAVAK LAAVAALCVQ YEAEFRPNMS IVVKALQPLL KPPAAAPAPE
S
