ID ILK1_ARATH Reviewed; 479 AA. AC F4IS56; F4IS57; Q8LL75; Q9SDB3; DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 1. DT 23-FEB-2022, entry version 84. DE RecName: Full=Integrin-linked protein kinase 1 {ECO:0000303|PubMed:27208244}; DE EC=2.7.11.1 {ECO:0000269|PubMed:27208244}; DE AltName: Full=Ankyrin protein kinase 1 {ECO:0000303|PubMed:12650621}; GN Name=ILK1 {ECO:0000303|PubMed:27208244}; GN Synonyms=APK1 {ECO:0000303|PubMed:12650621}; GN OrderedLocusNames=At2g43850 {ECO:0000312|Araport:AT2G43850}; GN ORFNames=F18O19.4 {ECO:0000312|EMBL:AEC10334.1}; 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=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 [MRNA] OF 218-479. RC STRAIN=cv. Columbia; RX PubMed=12650621; DOI=10.1023/a:1022337221225; RA Chinchilla D., Merchan F., Megias M., Kondorosi A., Sousa C., Crespi M.; RT "Ankyrin protein kinases: a novel type of plant kinase gene whose RT expression is induced by osmotic stress in alfalfa."; RL Plant Mol. Biol. 51:555-566(2003). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH CML9 RP AND POT5/HAK5, SUBCELLULAR LOCATION, INDUCTION, PHOSPHORYLATION AT SER-17 RP AND SER-26, AND MUTAGENESIS OF LYS-222 AND ASP-319. RX PubMed=27208244; DOI=10.1104/pp.16.00035; RA Brauer E.K., Ahsan N., Dale R., Kato N., Coluccio A.E., Pineros M.A., RA Kochian L.V., Thelen J.J., Popescu S.C.; RT "The Raf-like kinase ILK1 and the high affinity K+ transporter HAK5 are RT required for innate immunity and abiotic stress response."; RL Plant Physiol. 171:1470-1484(2016). CC -!- FUNCTION: Functions as a link between plant defense pathways, stress CC responses and potassium homeostasis. Promotes osmotic stress CC sensitivity, responses to the bacterial-derived pathogen-associated CC molecular pattern (PAMP) flg22, and resistance to bacterial pathogens. CC Promotes the accumulation of POT5/HAK5, a potassium transporter that CC mediates high-affinity uptake during potassium deficiency. CC {ECO:0000269|PubMed:27208244}. 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 Evidence={ECO:0000269|PubMed:27208244}; 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; Evidence={ECO:0000269|PubMed:27208244}; CC -!- ACTIVITY REGULATION: Kinase activity is suppressed by interaction with CC CML9. {ECO:0000269|PubMed:27208244}. CC -!- SUBUNIT: Interacts with CML9 and POT5/HAK5. CC {ECO:0000269|PubMed:27208244}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27208244}; CC Peripheral membrane protein {ECO:0000269|PubMed:27208244}. Endoplasmic CC reticulum membrane {ECO:0000269|PubMed:27208244}; Peripheral membrane CC protein {ECO:0000269|PubMed:27208244}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=F4IS56-1; Sequence=Displayed; CC Name=2; CC IsoId=F4IS56-2; Sequence=VSP_059111; CC -!- INDUCTION: Induced by mannitol and the pathogen-associated molecular CC pattern (PAMP) flg22. {ECO:0000269|PubMed:27208244}. CC -!- PTM: Autophosphorylated at Ser-17 and Ser-26. CC {ECO:0000269|PubMed:27208244}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF18591.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; 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; AC002333; AAF18591.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002685; AEC10334.1; -; Genomic_DNA. DR EMBL; CP002685; AEC10335.1; -; Genomic_DNA. DR EMBL; AF461113; AAN03744.1; -; mRNA. DR PIR; C84871; C84871. DR RefSeq; NP_181913.3; NM_129947.4. [F4IS56-1] DR RefSeq; NP_973683.1; NM_201954.1. [F4IS56-2] DR SMR; F4IS56; -. DR IntAct; F4IS56; 5. DR STRING; 3702.AT2G43850.1; -. DR iPTMnet; F4IS56; -. DR PaxDb; F4IS56; -. DR EnsemblPlants; AT2G43850.1; AT2G43850.1; AT2G43850. [F4IS56-1] DR EnsemblPlants; AT2G43850.2; AT2G43850.2; AT2G43850. [F4IS56-2] DR GeneID; 818989; -. DR Gramene; AT2G43850.1; AT2G43850.1; AT2G43850. [F4IS56-1] DR Gramene; AT2G43850.2; AT2G43850.2; AT2G43850. [F4IS56-2] DR KEGG; ath:AT2G43850; -. DR Araport; AT2G43850; -. DR TAIR; locus:2044034; AT2G43850. DR eggNOG; KOG0192; Eukaryota. DR HOGENOM; CLU_000288_7_35_1; -. DR InParanoid; F4IS56; -. DR PRO; PR:F4IS56; -. DR Proteomes; UP000006548; Chromosome 2. DR ExpressionAtlas; F4IS56; baseline and differential. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:TAIR. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004672; F:protein kinase activity; IMP:TAIR. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; HDA:TAIR. DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; ISS:TAIR. DR GO; GO:0045087; P:innate immune response; IDA:TAIR. DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR. DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR. DR Gene3D; 1.25.40.20; -; 1. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR Pfam; PF12796; Ank_2; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR SMART; SM00248; ANK; 3. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF48403; SSF48403; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW Alternative splicing; ANK repeat; ATP-binding; Cell membrane; KW Endoplasmic reticulum; Kinase; Membrane; Nucleotide-binding; KW Phosphoprotein; Plant defense; Reference proteome; Repeat; KW Serine/threonine-protein kinase; Stress response; Transferase. FT CHAIN 1..479 FT /note="Integrin-linked protein kinase 1" FT /id="PRO_0000441780" FT REPEAT 77..106 FT /note="ANK 1" FT /evidence="ECO:0000255" FT REPEAT 110..139 FT /note="ANK 2" FT /evidence="ECO:0000255" FT DOMAIN 194..461 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT NP_BIND 200..208 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 29..73 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 29..57 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 58..72 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 319 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 222 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 17 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:27208244" FT MOD_RES 26 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:27208244" FT VAR_SEQ 207..208 FT /note="GA -> AS (in isoform 2)" FT /id="VSP_059111" FT MUTAGEN 222 FT /note="K->A: Decreases kinase activity." FT /evidence="ECO:0000269|PubMed:27208244" FT MUTAGEN 319 FT /note="D->N: Increases kinase activity." FT /evidence="ECO:0000269|PubMed:27208244" FT CONFLICT 307 FT /note="L -> F (in Ref. 3; AAN03744)" FT /evidence="ECO:0000305" SQ SEQUENCE 479 AA; 54415 MW; 2D4220B043E1F657 CRC64; MENITAQLKR GISRQFSTGS IRRTLSRQFT RQSSLDPRRT NMRFSFGRQS SLDPIRRSPD SSKSDDEPHM SVPENLDSTM QLLFMASKGD VRGIEELLDE GIDVNSIDLD GRTALHIAAC EGHLGVVKAL LSRRANIDAR DRWGSTAAAD AKYYGNLDVY NLLKARGAKV PKTRKTPMTV SNPREVPEYE LNPLEVQVRK SDGISKGAYQ VAKWNGTRVS VKILDKDSYS DPERINAFRH ELTLLEKVRH PNVIQFVGAV TQNIPMMIVV EYNPKGDLSV YLQKKGRLSP SKALRFALDI ARGMNYLHEC KPDPIIHCDL KPKNILLDRG GQLKISGFGM IRLSKISQDK AKVANHKAHI DLSNYYIAPE VYKDEIFDLR VDAHSFGVIL YEITEGVPVF HPRPPEEVAR MMCLEGKRPV FKTKSRSYPP DIKELIEKCW HPEAGIRPTF SEIIIRLDKI VANCSKQGWW KDTFKFPWK //