Y3589_ARATH
ID Y3589_ARATH Reviewed; 361 AA.
AC Q9LSC2; Q8L9L7;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=PTI1-like tyrosine-protein kinase At3g15890;
DE EC=2.7.10.2;
GN OrderedLocusNames=At3g15890; ORFNames=MVC8.1;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 -!- 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";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB026653; BAB02873.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75743.1; -; Genomic_DNA.
DR EMBL; AY088361; AAM65900.1; -; mRNA.
DR RefSeq; NP_566530.1; NM_112459.1.
DR AlphaFoldDB; Q9LSC2; -.
DR SMR; Q9LSC2; -.
DR STRING; 3702.AT3G15890.1; -.
DR SwissPalm; Q9LSC2; -.
DR PaxDb; Q9LSC2; -.
DR PRIDE; Q9LSC2; -.
DR ProteomicsDB; 242865; -.
DR EnsemblPlants; AT3G15890.1; AT3G15890.1; AT3G15890.
DR GeneID; 820832; -.
DR Gramene; AT3G15890.1; AT3G15890.1; AT3G15890.
DR KEGG; ath:AT3G15890; -.
DR Araport; AT3G15890; -.
DR TAIR; locus:2093900; AT3G15890.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_4_1; -.
DR InParanoid; Q9LSC2; -.
DR OMA; WSNREEI; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9LSC2; -.
DR PRO; PR:Q9LSC2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSC2; baseline and differential.
DR Genevisible; Q9LSC2; AT.
DR GO; GO:0005886; C:plasma membrane; 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:0006468; P:protein phosphorylation; IBA:GO_Central.
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 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.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..361
FT /note="PTI1-like tyrosine-protein kinase At3g15890"
FT /id="PRO_0000403326"
FT DOMAIN 39..328
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 195..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 45..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 4
FT /note="L -> F (in Ref. 3; AAM65900)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="I -> M (in Ref. 3; AAM65900)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 40955 MW; 2211DC8959934CF2 CRC64;
MQLLNSCCGK GFDGKKKEKE EPSWRVFSLK ELHAATNSFN YDNKLGEGRF GSVYWGQLWD
GSQIAVKRLK EWSNREEIDF AVEVEILARI RHKNLLSVRG YCAEGQERLL VYEYMQNLSL
VSHLHGQHSA ECLLDWTKRM KIAISSAQAI AYLHDHATPH IVHGDVRASN VLLDSEFEAR
VTDFGYGKLM PDDDTGDGAT KAKSNNGYIS PECDASGKES ETSDVYSFGI LLMVLVSGKR
PLERLNPTTT RCITEWVLPL VYERNFGEIV DKRLSEEHVA EKLKKVVLVG LMCAQTDPDK
RPTMSEVVEM LVNESKEKIS ELEANPLFKN PYSSNENNRE HVAEESSDVI LEDKDHQQQQ
E
