SIRK_ARATH
ID SIRK_ARATH Reviewed; 876 AA.
AC O64483;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Senescence-induced receptor-like serine/threonine-protein kinase;
DE AltName: Full=FLG22-induced receptor-like kinase 1;
DE Flags: Precursor;
GN Name=SIRK; Synonyms=FRK1; OrderedLocusNames=At2g19190; ORFNames=T20K24.21;
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.
RC STRAIN=cv. Columbia;
RX PubMed=12000796; DOI=10.1101/gad.222702;
RA Robatzek S., Somssich I.E.;
RT "Targets of AtWRKY6 regulation during plant senescence and pathogen
RT defense.";
RL Genes Dev. 16:1139-1149(2002).
RN [2]
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 [3]
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 [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=11875555; DOI=10.1038/415977a;
RA Asai T., Tena G., Plotnikova J., Willmann M.R., Chiu W.-L., Gomez-Gomez L.,
RA Boller T., Ausubel F.M., Sheen J.;
RT "MAP kinase signalling cascade in Arabidopsis innate immunity.";
RL Nature 415:977-983(2002).
CC -!- FUNCTION: Involved in innate immune response of plants.
CC {ECO:0000269|PubMed:11875555}.
CC -!- INTERACTION:
CC O64483; C0LGE4: At1g12460; NbExp=2; IntAct=EBI-16905038, EBI-17126713;
CC O64483; Q9LRT1: At3g28040; NbExp=2; IntAct=EBI-16905038, EBI-16956175;
CC O64483; Q9FRI1: LRR-RLK; NbExp=2; IntAct=EBI-16905038, EBI-17071528;
CC O64483; Q9LZV7: PXC2; NbExp=2; IntAct=EBI-16905038, EBI-1238200;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- INDUCTION: Highly induced by WRKY22 or WRKY29 and by WRKY6 in senescent
CC leaves. Also induced 30 minutes after flagellin treatment.
CC {ECO:0000269|PubMed:11875555}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AF486619; AAL92103.1; -; mRNA.
DR EMBL; AC002392; AAD12037.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06856.1; -; Genomic_DNA.
DR PIR; T00540; T00540.
DR RefSeq; NP_179509.1; NM_127476.2.
DR AlphaFoldDB; O64483; -.
DR SMR; O64483; -.
DR BioGRID; 1793; 43.
DR IntAct; O64483; 42.
DR STRING; 3702.AT2G19190.1; -.
DR iPTMnet; O64483; -.
DR PaxDb; O64483; -.
DR PRIDE; O64483; -.
DR ProteomicsDB; 232537; -.
DR EnsemblPlants; AT2G19190.1; AT2G19190.1; AT2G19190.
DR GeneID; 816436; -.
DR Gramene; AT2G19190.1; AT2G19190.1; AT2G19190.
DR KEGG; ath:AT2G19190; -.
DR Araport; AT2G19190; -.
DR TAIR; locus:2059093; AT2G19190.
DR eggNOG; ENOG502QQCZ; Eukaryota.
DR HOGENOM; CLU_000288_41_1_1; -.
DR InParanoid; O64483; -.
DR OMA; ALALFWH; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; O64483; -.
DR PRO; PR:O64483; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64483; baseline and differential.
DR Genevisible; O64483; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR024788; Malectin-like_Carb-bd_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF12819; Malectin_like; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 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; Leucine-rich repeat; Membrane; Nucleotide-binding;
KW Phosphoprotein; Plant defense; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..876
FT /note="Senescence-induced receptor-like serine/threonine-
FT protein kinase"
FT /id="PRO_0000024384"
FT TOPO_DOM 25..517
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 539..876
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 415..438
FT /note="LRR 1"
FT REPEAT 439..462
FT /note="LRR 2"
FT REPEAT 463..483
FT /note="LRR 3"
FT DOMAIN 574..847
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 697
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 580..588
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 601
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 646
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 731
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 732
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 745
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
SQ SEQUENCE 876 AA; 98712 MW; EEE1C13E335BC7B6 CRC64;
MAMLKSLSSI LFTSFALLFF LVHAQDQSGF ISIDCGIPDD SSYNDETTGI KYVSDSAFVD
SGTTKRIAAQ FQSSGFDRHL LNVRSFPQSK RSCYDVPTPR GKGFKYLIRT RFMYGNYDDL
GRVPEFDLYL GVNFWDSVKL DDATTILNKE IITIPLLDNV QVCVVDKNAG TPFLSVLEIR
LLLNTTYETP YDALTLLRRL DYSKTGKLPS RYKDDIYDRI WTPRIVSSEY KILNTSLTVD
QFLNNGYQPA STVMSTAETA RNESLYLTLS FRPPDPNAKF YVYMHFAEIE VLKSNQTREF
SIWLNEDVIS PSFKLRYLLT DTFVTPDPVS GITINFSLLQ PPGEFVLPPI INALEVYQVN
EFLQIPTHPQ DVDAMRKIKA TYRVKKNWQG DPCVPVDYSW EGIDCIQSDN TTNPRVVSLN
ISFSELRGQI DPAFSNLTSI RKLDLSGNTL TGEIPAFLAN LPNLTELNVE GNKLTGIVPQ
RLHERSKNGS LSLRFGRNPD LCLSDSCSNT KKKNKNGYII PLVVVGIIVV LLTALALFRR
FKKKQQRGTL GERNGPLKTA KRYFKYSEVV NITNNFERVI GKGGFGKVYH GVINGEQVAV
KVLSEESAQG YKEFRAEVDL LMRVHHTNLT SLVGYCNEIN HMVLIYEYMA NENLGDYLAG
KRSFILSWEE RLKISLDAAQ GLEYLHNGCK PPIVHRDVKP TNILLNEKLQ AKMADFGLSR
SFSVEGSGQI STVVAGSIGY LDPEYYSTRQ MNEKSDVYSL GVVLLEVITG QPAIASSKTE
KVHISDHVRS ILANGDIRGI VDQRLRERYD VGSAWKMSEI ALACTEHTSA QRPTMSQVVM
ELKQIVYGIV TDQENYDDST KMLTVNLDTE MVPRAR
