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 20-DEC-2017, entry version 58. 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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., RA Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., RA Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis RT thaliana."; RL Nature 402:761-768(1999). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Portal (Araport); RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. 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., RA 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, ENZYME REGULATION, INTERACTION WITH CML9 RP AND POT5/HAK5, SUBCELLULAR LOCATION, INDUCTION, PHOSPHORYLATION AT RP SER-17 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 RT are 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, CC stress responses and potassium homeostasis. Promotes osmotic CC stress sensitivity, responses to the bacterial-derived pathogen- CC associated molecular pattern (PAMP) flg22, and resistance to CC bacterial pathogens. Promotes the accumulation of POT5/HAK5, a CC potassium transporter that mediates high-affinity uptake during CC potassium deficiency. {ECO:0000269|PubMed:27208244}. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC {ECO:0000269|PubMed:27208244}. CC -!- ENZYME REGULATION: Kinase activity is suppressed by interaction CC with 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}. CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:27208244}; CC Peripheral membrane 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 Note=No experimental confirmation available. {ECO:0000305}; CC -!- INDUCTION: Induced by mannitol and the pathogen-associated CC molecular 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 CC protein 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 UniGene; At.36834; -. DR UniGene; At.50136; -. DR SMR; F4IS56; -. DR IntAct; F4IS56; 2. 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 Araport; AT2G43850; -. DR TAIR; locus:2044034; AT2G43850. DR eggNOG; KOG0192; Eukaryota. DR eggNOG; COG0515; LUCA. DR InParanoid; 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:0004674; F:protein serine/threonine kinase activity; IDA:TAIR. DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; ISS:TAIR. DR GO; GO:0004871; F:signal transducer activity; IBA:GO_Central. DR GO; GO:0045087; P:innate immune response; IDA:TAIR. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR. DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR. DR CDD; cd00204; ANK; 1. DR Gene3D; 1.25.40.20; -; 1. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR020683; Ankyrin_rpt-contain_dom. 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; Pkinase_Tyr; 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 Complete proteome; Endoplasmic reticulum; Kinase; Membrane; KW Nucleotide-binding; Phosphoprotein; Plant defense; Reference proteome; KW Repeat; Serine/threonine-protein kinase; Stress response; Transferase. FT CHAIN 1 479 Integrin-linked protein kinase 1. FT /FTId=PRO_0000441780. FT REPEAT 77 106 ANK 1. {ECO:0000255}. FT REPEAT 110 139 ANK 2. {ECO:0000255}. FT DOMAIN 194 461 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT NP_BIND 200 208 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT ACT_SITE 319 319 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT BINDING 222 222 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT MOD_RES 17 17 Phosphoserine. FT {ECO:0000269|PubMed:27208244}. FT MOD_RES 26 26 Phosphoserine. FT {ECO:0000269|PubMed:27208244}. FT VAR_SEQ 207 208 GA -> AS (in isoform 2). FT /FTId=VSP_059111. FT MUTAGEN 222 222 K->A: Decreases kinase activity. FT {ECO:0000269|PubMed:27208244}. FT MUTAGEN 319 319 D->N: Increases kinase activity. FT {ECO:0000269|PubMed:27208244}. FT CONFLICT 307 307 L -> F (in Ref. 3; AAN03744). FT {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 //