ILK1_ARATH
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 03-AUG-2022, entry version 86.
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};
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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 AlphaFoldDB; F4IS56; -.
DR SMR; F4IS56; -.
DR IntAct; F4IS56; 5.
DR STRING; 3702.AT2G43850.1; -.
DR iPTMnet; F4IS56; -.
DR PaxDb; F4IS56; -.
DR PRIDE; 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 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 200..208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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
