LRKS2_ARATH
ID LRKS2_ARATH Reviewed; 851 AA.
AC O48837; O82658;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Receptor like protein kinase S.2;
DE Short=LecRK-S.2;
DE EC=2.7.11.1;
GN Name=LECRKS2; Synonyms=AP4.3A; OrderedLocusNames=At2g32800;
GN ORFNames=F24L7.6;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 [GENOMIC DNA] OF 1-509, AND INDUCTION BY PATHOGENS AND
RP ABIOTIC STRESSES.
RC STRAIN=cv. Columbia;
RX PubMed=9742960; DOI=10.1016/s0014-5793(98)01015-1;
RA Cordeiro M.C.R., Piqueras R., de Oliveira D.E., Castresana C.;
RT "Characterization of early induced genes in Arabidopsis thaliana responding
RT to bacterial inoculation: identification of centrin and of a novel protein
RT with two regions related to kinase domains.";
RL FEBS Lett. 434:387-393(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-851.
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 [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19773388; DOI=10.1093/jxb/erp277;
RA Bouwmeester K., Govers F.;
RT "Arabidopsis L-type lectin receptor kinases: phylogeny, classification, and
RT expression profiles.";
RL J. Exp. Bot. 60:4383-4396(2009).
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 -!- INDUCTION: Rapidly induced after both compatible and incompatible
CC pathogen inoculations (e.g. Xanthomonas campestris pv. campestris and
CC Pseudomonas syringae pv. tomato). Weakly and transiently induced in
CC response to wounding, salicylic acid (SA) and jasmonic acid (JA).
CC {ECO:0000269|PubMed:9742960}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC04483.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA08772.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC003974; AAC04483.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC08743.1; -; Genomic_DNA.
DR EMBL; AJ009671; CAA08772.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF370599; AAK43918.1; -; mRNA.
DR PIR; T00788; T00788.
DR RefSeq; NP_180839.2; NM_128840.3.
DR AlphaFoldDB; O48837; -.
DR SMR; O48837; -.
DR STRING; 3702.AT2G32800.1; -.
DR iPTMnet; O48837; -.
DR PaxDb; O48837; -.
DR PRIDE; O48837; -.
DR ProteomicsDB; 238431; -.
DR EnsemblPlants; AT2G32800.1; AT2G32800.1; AT2G32800.
DR GeneID; 817841; -.
DR Gramene; AT2G32800.1; AT2G32800.1; AT2G32800.
DR KEGG; ath:AT2G32800; -.
DR Araport; AT2G32800; -.
DR TAIR; locus:2046457; AT2G32800.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_016867_0_0_1; -.
DR InParanoid; O48837; -.
DR OMA; GMARWLE; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; O48837; -.
DR PRO; PR:O48837; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O48837; baseline and differential.
DR Genevisible; O48837; AT.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0071395; P:cellular response to jasmonic acid stimulus; IEP:UniProtKB.
DR GO; GO:0071446; P:cellular response to salicylic acid stimulus; IEP:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0002229; P:defense response to oomycetes; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP: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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 2.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..851
FT /note="Receptor like protein kinase S.2"
FT /id="PRO_0000403333"
FT DOMAIN 117..436
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 532..819
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 448..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 248
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 123..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 538..546
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 560
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 169..170
FT /note="QL -> HV (in Ref. 3; CAA08772)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="F -> Y (in Ref. 3; CAA08772)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 851 AA; 96086 MW; 9C6C11F441E0B36F CRC64;
MAPMAMDHLC FVLPTESGEL KPPVMVEETT EEEEEKKSRD CGRQVVSLIG DLFRRLHGSK
LVKSLNLCSI NESKDSISME INKSFTDMEG VQLSSKVGCE NPRIFGYSEL YIGTNGFSDE
LILGSGGFGR VYKALLPSDG TTVAVKCLAE KKGEQFEKTF AAELVAVAQL RHRNLVKLRG
WCLHEDELLL VYDYMPNRSL DRVLFRRPEV NSDFKPLDWD RRGKIVKGLA AALFYLHEQL
ETQIIHRDVK TSNVMLDSEF NAKLGDFGLA RWLEHKIDET EHDSSYDSVS SFRNHQFRVA
DSTRIGGTIG YLPPESFRKK TVATAKTDVF SFGVVVLEVV SGRRAVDLSF SEDKIILLDW
VRRLSDNRKL LDAGDSRLAK GSYDLSDMKR MIHLALLCSL NNPTHRPNMK WVIGALSGEF
SGNLPALPSF KSHPLYIPLS SLKSTSTSAT TTTTRTTMTT TTSTTSFNAS SESTPSSNYV
TALEDSIYQT AETGENPYFN YNSRRVMSSK SFVLDTPREI SYNDLVLATD NFSDARRVAE
VDFGTAYYGL LNGDQHIVVK RLGMTKCPAL VTRFSTELLN LGRLRHRNLV MLRGWCTEHG
EMLVVYDYSA NRKLSHLLFH NHIPGNSVLR WKSRYNVIKS LACAVRYLHE EWDEQVIHRN
ITSSTIFLDR DMNPRLCGFA LAEFLSRNDK AHQAAKKKGS AQGIFGYMAP EYMESGEATT
MADVYSFGVV VLEMVTGQPA VDYKRKKEDA LMVLRIREVV GNRKKLLEEI ADIHLDDEYE
NRELARLLRL GLVCTRTDPK LRPSISQVVS ILDGSERFFE EEGGKEGDVS RKQMYDSSML
MIRQMQALGI H
