CERK1_ARATH
ID CERK1_ARATH Reviewed; 617 AA.
AC A8R7E6; Q9LVE3;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Chitin elicitor receptor kinase 1;
DE Short=AtCERK1;
DE EC=2.7.11.1;
DE AltName: Full=LysM domain receptor-like kinase 1;
DE Short=LysM RLK1;
DE Short=LysM-containing receptor-like kinase 1;
DE Flags: Precursor;
GN Name=CERK1; Synonyms=LYK1, RLK1; OrderedLocusNames=At3g21630;
GN ORFNames=MIL23.20;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP PHENOTYPE, AUTOPHOSPHORYLATION, INDUCTION BY CHITIN, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=18042724; DOI=10.1073/pnas.0705147104;
RA Miya A., Albert P., Shinya T., Desaki Y., Ichimura K., Shirasu K.,
RA Narusaka Y., Kawakami N., Kaku H., Shibuya N.;
RT "CERK1, a LysM receptor kinase, is essential for chitin elicitor signaling
RT in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:19613-19618(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=18263776; DOI=10.1105/tpc.107.056754;
RA Wan J., Zhang X.-C., Neece D., Ramonell K.M., Clough S., Kim S.-Y.,
RA Stacey M.G., Stacey G.;
RT "A LysM receptor-like kinase plays a critical role in chitin signaling and
RT fungal resistance in Arabidopsis.";
RL Plant Cell 20:471-481(2008).
RN [5]
RP FUNCTION, UBIQUITINATION, AND INTERACTION WITH PSEUDOMONAS SYRINGAE
RP HOPAB2/AVRPTOB.
RC STRAIN=cv. Columbia, and cv. Wassilewskija-4;
RX PubMed=19249211; DOI=10.1016/j.cub.2009.01.054;
RA Gimenez-Ibanez S., Hann D.R., Ntoukakis V., Petutschnig E., Lipka V.,
RA Rathjen J.P.;
RT "AvrPtoB targets the LysM receptor kinase CERK1 to promote bacterial
RT virulence on plants.";
RL Curr. Biol. 19:423-429(2009).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND REVIEW.
RC STRAIN=cv. Columbia;
RX PubMed=19816132; DOI=10.4161/psb.4.6.8697;
RA Gimenez-Ibanez S., Ntoukakis V., Rathjen J.P.;
RT "The LysM receptor kinase CERK1 mediates bacterial perception in
RT Arabidopsis.";
RL Plant Signal. Behav. 4:539-541(2009).
RN [7]
RP INTERACTION WITH CHITIN, AND AUTOPHOSPHORYLATION.
RX PubMed=19951949; DOI=10.1074/jbc.m109.027540;
RA Iizasa E., Mitsutomi M., Nagano Y.;
RT "Direct binding of a plant LysM receptor-like kinase, LysM RLK1/CERK1, to
RT chitin in vitro.";
RL J. Biol. Chem. 285:2996-3004(2010).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CHITIN AND DERIVATIVES,
RP AUTOPHOSPHORYLATION, AND PHOSPHORYLATION AT SER-266; SER-268; SER-274 AND
RP THR-519.
RX PubMed=20610395; DOI=10.1074/jbc.m110.116657;
RA Petutschnig E.K., Jones A.M.E., Serazetdinova L., Lipka U., Lipka V.;
RT "The lysin motif receptor-like kinase (LysM-RLK) CERK1 is a major chitin-
RT binding protein in Arabidopsis thaliana and subject to chitin-induced
RT phosphorylation.";
RL J. Biol. Chem. 285:28902-28911(2010).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=22106285; DOI=10.1073/pnas.1112862108;
RA Willmann R., Lajunen H.M., Erbs G., Newman M.-A., Kolb D., Tsuda K.,
RA Katagiri F., Fliegmann J., Bono J.-J., Cullimore J.V., Jehle A.K.,
RA Goetz F., Kulik A., Molinaro A., Lipka V., Gust A.A., Nuernberger T.;
RT "Arabidopsis lysin-motif proteins LYM1 LYM3 CERK1 mediate bacterial
RT peptidoglycan sensing and immunity to bacterial infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:19824-19829(2011).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22461667; DOI=10.1093/mp/sss021;
RA Brotman Y., Landau U., Pnini S., Lisec J., Balazadeh S., Mueller-Roeber B.,
RA Zilberstein A., Willmitzer L., Chet I., Viterbo A.;
RT "The LysM receptor-like kinase LysM RLK1 is required to activate defense
RT and abiotic-stress responses induced by overexpression of fungal chitinases
RT in Arabidopsis plants.";
RL Mol. Plant 5:1113-1124(2012).
RN [11]
RP FUNCTION, AND INTERACTION WITH CHITIN.
RC STRAIN=cv. Columbia;
RX PubMed=22891159; DOI=10.1093/pcp/pcs113;
RA Shinya T., Motoyama N., Ikeda A., Wada M., Kamiya K., Hayafune M., Kaku H.,
RA Shibuya N.;
RT "Functional characterization of CEBiP and CERK1 homologs in Arabidopsis and
RT rice reveals the presence of different chitin receptor systems in plants.";
RL Plant Cell Physiol. 53:1696-1706(2012).
RN [12]
RP INDUCTION BY CHITIN AND FLAGELLIN.
RX PubMed=22744984; DOI=10.1104/pp.112.201699;
RA Wan J., Tanaka K., Zhang X.-C., Son G.H., Brechenmacher L., Nguyen T.H.N.,
RA Stacey G.;
RT "LYK4, a lysin motif receptor-like kinase, is important for chitin
RT signaling and plant innate immunity in Arabidopsis.";
RL Plant Physiol. 160:396-406(2012).
RN [13]
RP INTERACTION WITH CHITIN, AND HOMODIMER.
RX PubMed=22740685; DOI=10.1126/scisignal.2003274;
RA Willmann R., Nuernberger T.;
RT "How plant lysin motif receptors get activated: lessons learned from
RT structural biology.";
RL Sci. Signal. 5:PE28-PE28(2012).
RN [14]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH PBL27, MUTAGENESIS OF
RP ASP-441, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=24750441; DOI=10.1111/tpj.12535;
RA Shinya T., Yamaguchi K., Desaki Y., Yamada K., Narisawa T., Kobayashi Y.,
RA Maeda K., Suzuki M., Tanimoto T., Takeda J., Nakashima M., Funama R.,
RA Narusaka M., Narusaka Y., Kaku H., Kawasaki T., Shibuya N.;
RT "Selective regulation of the chitin-induced defense response by the
RT Arabidopsis receptor-like cytoplasmic kinase PBL27.";
RL Plant J. 79:56-66(2014).
RN [15]
RP INTERACTION WITH PBL27, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=27679653; DOI=10.15252/embj.201694248;
RA Yamada K., Yamaguchi K., Shirakawa T., Nakagami H., Mine A., Ishikawa K.,
RA Fujiwara M., Narusaka M., Narusaka Y., Ichimura K., Kobayashi Y.,
RA Matsui H., Nomura Y., Nomoto M., Tada Y., Fukao Y., Fukamizo T., Tsuda K.,
RA Shirasu K., Shibuya N., Kawasaki T.;
RT "The Arabidopsis CERK1-associated kinase PBL27 connects chitin perception
RT to MAPK activation.";
RL EMBO J. 35:2468-2483(2016).
RN [16]
RP INTERACTION WITH IOS1.
RX PubMed=27317676; DOI=10.1105/tpc.16.00313;
RA Yeh Y.-H., Panzeri D., Kadota Y., Huang Y.-C., Huang P.-Y., Tao C.-N.,
RA Roux M., Chien H.-C., Chin T.-C., Chu P.-W., Zipfel C., Zimmerli L.;
RT "The Arabidopsis malectin-like/LRR-RLK IOS1 is critical for BAK1-dependent
RT and BAK1-independent pattern-triggered immunity.";
RL Plant Cell 28:1701-1721(2016).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 25-230 IN COMPLEX WITH CHITIN
RP OLIGOMERS, HOMODIMER, ACTIVITY REGULATION, MUTAGENESIS OF ALA-138,
RP PHOSPHORYLATION, GLYCOSYLATION AT ASN-40; ASN-52; ASN-102; ASN-123 AND
RP ASN-152, AND DISULFIDE BONDS.
RX PubMed=22654057; DOI=10.1126/science.1218867;
RA Liu T., Liu Z., Song C., Hu Y., Han Z., She J., Fan F., Wang J., Jin C.,
RA Chang J., Zhou J.-M., Chai J.;
RT "Chitin-induced dimerization activates a plant immune receptor.";
RL Science 336:1160-1164(2012).
CC -!- FUNCTION: Lysin motif (LysM) receptor kinase that functions as a cell
CC surface receptor in chitin elicitor (chitooligosaccharides) signaling
CC leading to innate immunity toward both biotic and abiotic stresses
CC (e.g. tolerance to salinity, heavy-metal stresses, and Botrytis cinerea
CC infection). Recognizes microbe-derived N-acetylglucosamine (NAG)-
CC containing ligands. Involved in the resistance to pathogenic fungi
CC Alternaria brassicicola and Erysiphe cichoracearum, probably by sensing
CC microbe-associated molecular patterns (MAMP) and pathogen-associated
CC molecular patterns (PAMP). Plays an essential role in detecting
CC peptidoglycans (e.g. PGNs) and restricting bacterial growth. Target of
CC the bacterial type III effector E3-ligase protein hopAB2/avrPtoB of
CC Pseudomonas syringae pv. tomato DC3000 that mediates ubiquitination and
CC subsequent proteolysis, thus blocking all defense responses by
CC suppressing PAMP-triggered immunity (PTI). Mediates chitin-induced
CC phosphorylation of PBL27 (PubMed:24750441).
CC {ECO:0000269|PubMed:18042724, ECO:0000269|PubMed:18263776,
CC ECO:0000269|PubMed:19249211, ECO:0000269|PubMed:19816132,
CC ECO:0000269|PubMed:20610395, ECO:0000269|PubMed:22106285,
CC ECO:0000269|PubMed:22461667, ECO:0000269|PubMed:22891159,
CC ECO:0000269|PubMed:24750441}.
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:18042724, ECO:0000269|PubMed:20610395};
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:18042724,
CC ECO:0000269|PubMed:20610395};
CC -!- ACTIVITY REGULATION: Activated by chitin-mediated homodimerization.
CC {ECO:0000269|PubMed:22654057}.
CC -!- SUBUNIT: Forms homodimers and homooligomers. Homodimerization is
CC required to trigger plant defenses. Binds to chitin, chitosan and
CC chito-oligomer oligosaccharide elicitors. Interaction with chitin
CC octamer (NAG(8)) promotes homodimerization while shorter chitin
CC oligomers inhibit homodimerization. Interacts with Pseudomonas syringae
CC hopAB2/avrPtoB. Interacts (preferentially when unphosphorylated) with
CC PBL27 at the plasma membrane (PubMed:24750441, PubMed:27679653). Binds
CC to IOS1 (PubMed:27317676). {ECO:0000269|PubMed:19249211,
CC ECO:0000269|PubMed:19951949, ECO:0000269|PubMed:20610395,
CC ECO:0000269|PubMed:22654057, ECO:0000269|PubMed:22740685,
CC ECO:0000269|PubMed:22891159, ECO:0000269|PubMed:24750441,
CC ECO:0000269|PubMed:27317676, ECO:0000269|PubMed:27679653}.
CC -!- INTERACTION:
CC A8R7E6; A8R7E6: CERK1; NbExp=4; IntAct=EBI-15672582, EBI-15672582;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18042724,
CC ECO:0000269|PubMed:24750441, ECO:0000269|PubMed:27679653}; Single-pass
CC membrane protein {ECO:0000269|PubMed:18042724}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously, with lowest expression in
CC pollen. {ECO:0000269|PubMed:18263776}.
CC -!- INDUCTION: Induced upon treatment with chitin oligosaccharide elicitor
CC and flagellin (e.g. flg22). {ECO:0000269|PubMed:18042724,
CC ECO:0000269|PubMed:22744984}.
CC -!- PTM: Autophosphorylated. Autophosphorylation is induced by chitin and
CC derivatives. {ECO:0000269|PubMed:20610395,
CC ECO:0000269|PubMed:22654057}.
CC -!- PTM: Ubiquitinated and targeted to the proteasome by hopAB2/avrPtoB of
CC Pseudomonas syringae pv. tomato DC3000. {ECO:0000269|PubMed:19249211}.
CC -!- DISRUPTION PHENOTYPE: Complete loss of response to the chitin elicitor,
CC including loss of MAPK activation, generation of reactive oxygen
CC species, and transcriptional activation. Impaired chitin-mediated
CC resistance against biotic and abiotic stresses such as tolerance to
CC salinity, heavy-metal stresses, and Botrytis cinerea infection. Reduced
CC resistance to incompatible fungi such as Erysiphe cichoracearum and
CC Alternaria brassicicola. Enhanced susceptibility to Pseudomonas
CC syringae pv. tomato DC3000 associated with peptidoglycan insensitivity.
CC Impaired chitin-induced phosphorylation of PBL27 (PubMed:24750441).
CC {ECO:0000269|PubMed:18042724, ECO:0000269|PubMed:18263776,
CC ECO:0000269|PubMed:19816132, ECO:0000269|PubMed:22106285,
CC ECO:0000269|PubMed:22461667, ECO:0000269|PubMed:24750441}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02358.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB367524; BAF92788.1; -; mRNA.
DR EMBL; AB019232; BAB02358.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76532.1; -; Genomic_DNA.
DR RefSeq; NP_566689.2; NM_113058.4.
DR PDB; 4EBY; X-ray; 1.65 A; A=25-230.
DR PDB; 4EBZ; X-ray; 1.79 A; A=25-230.
DR PDBsum; 4EBY; -.
DR PDBsum; 4EBZ; -.
DR AlphaFoldDB; A8R7E6; -.
DR SMR; A8R7E6; -.
DR BioGRID; 7049; 70.
DR IntAct; A8R7E6; 8.
DR STRING; 3702.AT3G21630.1; -.
DR iPTMnet; A8R7E6; -.
DR PaxDb; A8R7E6; -.
DR PRIDE; A8R7E6; -.
DR ProteomicsDB; 220385; -.
DR EnsemblPlants; AT3G21630.1; AT3G21630.1; AT3G21630.
DR GeneID; 821717; -.
DR Gramene; AT3G21630.1; AT3G21630.1; AT3G21630.
DR KEGG; ath:AT3G21630; -.
DR Araport; AT3G21630; -.
DR TAIR; locus:2089860; AT3G21630.
DR eggNOG; ENOG502QPX8; Eukaryota.
DR HOGENOM; CLU_000288_99_3_1; -.
DR InParanoid; A8R7E6; -.
DR OMA; VCRYARY; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; A8R7E6; -.
DR PRO; PR:A8R7E6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; A8R7E6; baseline and differential.
DR Genevisible; A8R7E6; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; IDA:UniProtKB.
DR GO; GO:2001080; F:chitosan binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016301; F:kinase activity; IDA:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IMP:GO_Central.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0019199; F:transmembrane receptor protein kinase activity; IDA:TAIR.
DR GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0071323; P:cellular response to chitin; IMP:UniProtKB.
DR GO; GO:0071219; P:cellular response to molecule of bacterial origin; IEP:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0032491; P:detection of molecule of fungal origin; IMP:TAIR.
DR GO; GO:0032499; P:detection of peptidoglycan; IMP:TAIR.
DR GO; GO:0045087; P:innate immune response; IMP:TAIR.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:0010200; P:response to chitin; IMP:TAIR.
DR CDD; cd00118; LysM; 1.
DR InterPro; IPR044812; CERK1/LYK3-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018392; LysM_dom.
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 PANTHER; PTHR46204; PTHR46204; 1.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51782; LYSM; 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 3D-structure; ATP-binding; Cell membrane; Chitin-binding; Disulfide bond;
KW Glycoprotein; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Plant defense; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..617
FT /note="Chitin elicitor receptor kinase 1"
FT /id="PRO_0000420826"
FT TOPO_DOM 24..232
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..617
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 46..74
FT /note="LysM 1; degenerate"
FT DOMAIN 108..140
FT /note="LysM 2; degenerate"
FT DOMAIN 168..211
FT /note="LysM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 322..594
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 441
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 109..115
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT BINDING 137..143
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT BINDING 328..336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20610395"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20610395"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20610395"
FT MOD_RES 390
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 479
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 519
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:20610395"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22654057,
FT ECO:0007744|PDB:4EBY"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22654057,
FT ECO:0007744|PDB:4EBY"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22654057,
FT ECO:0007744|PDB:4EBY"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22654057,
FT ECO:0007744|PDB:4EBY"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22654057,
FT ECO:0007744|PDB:4EBY"
FT DISULFID 25..93
FT /evidence="ECO:0000269|PubMed:22654057,
FT ECO:0007744|PDB:4EBY"
FT DISULFID 29..155
FT /evidence="ECO:0000269|PubMed:22654057,
FT ECO:0007744|PDB:4EBY"
FT DISULFID 91..153
FT /evidence="ECO:0000269|PubMed:22654057,
FT ECO:0007744|PDB:4EBY"
FT MUTAGEN 138
FT /note="A->H: Slower chitin-mediated phosphorylation."
FT /evidence="ECO:0000269|PubMed:22654057"
FT MUTAGEN 441
FT /note="D->V: Increased affinity for PBL27."
FT /evidence="ECO:0000269|PubMed:24750441"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:4EBY"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:4EBY"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:4EBY"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:4EBY"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:4EBY"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:4EBY"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:4EBY"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:4EBY"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:4EBY"
FT TURN 119..123
FT /evidence="ECO:0007829|PDB:4EBY"
FT HELIX 127..133
FT /evidence="ECO:0007829|PDB:4EBY"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:4EBZ"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:4EBY"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:4EBY"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:4EBY"
FT HELIX 178..185
FT /evidence="ECO:0007829|PDB:4EBY"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:4EBY"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:4EBY"
SQ SEQUENCE 617 AA; 67315 MW; CF5019DB428CFE1E CRC64;
MKLKISLIAP ILLLFSFFFA VESKCRTSCP LALASYYLEN GTTLSVINQN LNSSIAPYDQ
INFDPILRYN SNIKDKDRIQ MGSRVLVPFP CECQPGDFLG HNFSYSVRQE DTYERVAISN
YANLTTMESL QARNPFPATN IPLSATLNVL VNCSCGDESV SKDFGLFVTY PLRPEDSLSS
IARSSGVSAD ILQRYNPGVN FNSGNGIVYV PGRDPNGAFP PFKSSKQDGV GAGVIAGIVI
GVIVALLLIL FIVYYAYRKN KSKGDSFSSS IPLSTKADHA SSTSLQSGGL GGAGVSPGIA
AISVDKSVEF SLEELAKATD NFNLSFKIGQ GGFGAVYYAE LRGEKAAIKK MDMEASKQFL
AELKVLTRVH HVNLVRLIGY CVEGSLFLVY EYVENGNLGQ HLHGSGREPL PWTKRVQIAL
DSARGLEYIH EHTVPVYVHR DIKSANILID QKFRAKVADF GLTKLTEVGG SATRGAMGTF
GYMAPETVYG EVSAKVDVYA FGVVLYELIS AKGAVVKMTE AVGEFRGLVG VFEESFKETD
KEEALRKIID PRLGDSYPFD SVYKMAELGK ACTQENAQLR PSMRYIVVAL STLFSSTGNW
DVGNFQNEDL VSLMSGR
