OXI1_ARATH
ID OXI1_ARATH Reviewed; 421 AA.
AC Q9LSF1; A1L4U5;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Serine/threonine-protein kinase OXI1;
DE EC=2.7.11.1;
DE AltName: Full=AGC serine/threonine-protein kinase subfamily 2 member 1 {ECO:0000303|PubMed:13678909};
DE AltName: Full=Protein OXIDATIVE SIGNAL-INDUCIBLE 1 {ECO:0000303|PubMed:14985766};
GN Name=OXI1 {ECO:0000303|PubMed:14985766};
GN Synonyms=AGC2-1 {ECO:0000303|PubMed:13678909}; OrderedLocusNames=At3g25250;
GN ORFNames=MJL12.21;
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=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].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, AND REVIEW.
RX PubMed=13678909; DOI=10.1016/s1360-1385(03)00188-2;
RA Boegre L., Okresz L., Henriques R., Anthony R.G.;
RT "Growth signalling pathways in Arabidopsis and the AGC protein kinases.";
RL Trends Plant Sci. 8:424-431(2003).
RN [5]
RP ACTIVITY REGULATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, INTERACTION
RP WITH PDK1 AND PDK2, AND MUTAGENESIS OF LYS-45; SER-235; PHE-418 AND
RP PHE-421.
RX PubMed=14749726; DOI=10.1038/sj.emboj.7600068;
RA Anthony R.G., Henriques R., Helfer A., Meszaros T., Rios G., Testerink C.,
RA Munnik T., Deak M., Koncz C., Boegre L.;
RT "A protein kinase target of a PDK1 signalling pathway is involved in root
RT hair growth in Arabidopsis.";
RL EMBO J. 23:572-581(2004).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=14985766; DOI=10.1038/nature02353;
RA Rentel M.C., Lecourieux D., Ouaked F., Usher S.L., Petersen L., Okamoto H.,
RA Knight H., Peck S.C., Grierson C.S., Hirt H., Knight M.R.;
RT "OXI1 kinase is necessary for oxidative burst-mediated signalling in
RT Arabidopsis.";
RL Nature 427:858-861(2004).
CC -!- FUNCTION: Involved in oxidative burst-mediated signaling. Required for
CC basal resistance to P.parasitica infection and root hair growth. Partly
CC required for the activation of MPK3 and MPK6 by hydrogen peroxide and
CC cellulase elicitor. {ECO:0000269|PubMed:14985766}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- ACTIVITY REGULATION: Activated in response to hydrogen peroxide and
CC cellulase elicitor. Activated by PDK1 in a phosphatidic acid dependent
CC manner. {ECO:0000269|PubMed:14749726, ECO:0000269|PubMed:14985766}.
CC -!- SUBUNIT: Interacts with PDK1 and PDK2. {ECO:0000269|PubMed:14749726}.
CC -!- INTERACTION:
CC Q9LSF1; O80719: At2g47060; NbExp=4; IntAct=EBI-8574783, EBI-4436376;
CC -!- TISSUE SPECIFICITY: Expressed in roots and root hair cells.
CC {ECO:0000269|PubMed:14749726, ECO:0000269|PubMed:14985766}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in fast-growing organs and
CC dividing cells.
CC -!- INDUCTION: By wounding, hydrogen peroxide and cellulase elicitor.
CC {ECO:0000269|PubMed:14985766}.
CC -!- DOMAIN: The activation loop within the kinase domain is the target of
CC phosphorylation. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Plants have enhanced susceptibility to virulent
CC P.parasitica pathogen and reduced root hair length.
CC {ECO:0000269|PubMed:14749726, ECO:0000269|PubMed:14985766}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AB026647; BAB02084.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77000.1; -; Genomic_DNA.
DR EMBL; BT029732; ABM06002.1; -; mRNA.
DR RefSeq; NP_189162.1; NM_113431.6.
DR AlphaFoldDB; Q9LSF1; -.
DR SMR; Q9LSF1; -.
DR BioGRID; 7450; 7.
DR ELM; Q9LSF1; -.
DR IntAct; Q9LSF1; 4.
DR MINT; Q9LSF1; -.
DR STRING; 3702.AT3G25250.1; -.
DR PaxDb; Q9LSF1; -.
DR PRIDE; Q9LSF1; -.
DR EnsemblPlants; AT3G25250.1; AT3G25250.1; AT3G25250.
DR GeneID; 822119; -.
DR Gramene; AT3G25250.1; AT3G25250.1; AT3G25250.
DR KEGG; ath:AT3G25250; -.
DR Araport; AT3G25250; -.
DR TAIR; locus:2090310; AT3G25250.
DR eggNOG; KOG0610; Eukaryota.
DR HOGENOM; CLU_000288_63_30_1; -.
DR InParanoid; Q9LSF1; -.
DR OMA; WELILLI; -.
DR OrthoDB; 910700at2759; -.
DR PhylomeDB; Q9LSF1; -.
DR PRO; PR:Q9LSF1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSF1; baseline and differential.
DR Genevisible; Q9LSF1; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; ISS:TAIR.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; Plant defense;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..421
FT /note="Serine/threonine-protein kinase OXI1"
FT /id="PRO_0000245827"
FT DOMAIN 17..329
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 330..421
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 167..246
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT MOTIF 418..421
FT /note="PIF"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 23..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 235
FT /note="Phosphoserine; by PDPK1"
FT /evidence="ECO:0000305"
FT MUTAGEN 45
FT /note="K->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:14749726"
FT MUTAGEN 235
FT /note="S->A: Strongly reduces catalytic activity."
FT /evidence="ECO:0000269|PubMed:14749726"
FT MUTAGEN 418
FT /note="F->A: Loss of interaction with PDPK1 and PDK2; when
FT associated with A-421."
FT /evidence="ECO:0000269|PubMed:14749726"
FT MUTAGEN 421
FT /note="F->A: Loss of interaction with PDPK1 and PDK2; when
FT associated with A-418."
FT /evidence="ECO:0000269|PubMed:14749726"
SQ SEQUENCE 421 AA; 47560 MW; 6855585F4DC14C4D CRC64;
MLEGDEKQSR ALDFNRLEVL SLLGRGAKGV VFLVRDDDAK LLALKVILKE AIEKKKKGRE
SEDDEYKRVS FEQGVLSRFD HPLFPSLHGV LATDKVIGYA IDYCPGQNLN SLRKMQSESM
FSDEIIRFYA AELVLALDYL HNQGIVYRDL KPDNVMIQEN GHLMLIDFDL STNLAPRTPQ
PSPSLSKPSP TMKRKKRLFR FTSFCNSGIS PQESISVHSS STLAVSDSSG EKSNSFVGTE
EYVAPEVISG DGHDFAVDWW SLGVVLYEML YGATPFRGSN RKETFYRILS KPPNLTGETT
SLRDLIRRLL EKDPSRRINV EEIKGHDFFR GVDWEKVILV SRPPYIPAPD DGGDKGTDVN
TKMDVENIVQ EIFAARQERE KQSGDNNKNA NMKIKDNTSG EWVKGLNNNH DLESDNNFLV
F
