※ dbPPT Protein Information
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UniProt Accession | |||||||||||||||||||||||||||||||||||
Theoretical PI | 6.36 | ||||||||||||||||||||||||||||||||||
Molecular Weight | 67314.83 | ||||||||||||||||||||||||||||||||||
Genbank Protein ID | |||||||||||||||||||||||||||||||||||
Genbank Nucleotide ID | |||||||||||||||||||||||||||||||||||
Protein Name | Chitin elicitor receptor kinase 1; AtCERK1; LysM domain receptor-like kinase 1; LysM RLK1; LysM-containing receptor-like kinase 1 | ||||||||||||||||||||||||||||||||||
Gene Name | CERK1; LYK1; RLK1; At3g21630; MIL23.20 | ||||||||||||||||||||||||||||||||||
Created Date | 2013-01-09 | ||||||||||||||||||||||||||||||||||
Organism | Arabidopsis thaliana(Mouse-ear cress) | ||||||||||||||||||||||||||||||||||
NCBI Taxa ID | 3702 | ||||||||||||||||||||||||||||||||||
Phosphorylation Sites |
Functional Description Lysin motif (LysM) receptor kinase that functions as a cell surface receptor in chitin elicitor (chitooligosaccharides) signaling leading to innate immunity toward both biotic and abiotic stresses (e.g. tolerance to salinity, heavy-metal stresses, and Botrytis cinerea infection). Recognizes microbe-derived N-acetylglucosamine (NAG)-containing ligands. Involved in the resistance to pathogenic fungi Alternaria brassicicola and Erysiphe cichoracearum, probably by sensing microbe-associated molecular patterns (MAMP) and pathogen-associated molecular patterns (PAMP). Plays an essential role in detecting peptidoglycans (e.g. PGNs) and restricting bacterial growth. Target of the bacterial type III effector E3-ligase protein hopAB2/avrPtoB of Pseudomonas syringae pv. tomato DC3000 that mediates ubiquitination and subsequent proteolysis, thus blocking all defense responses by suppressing PAMP-triggered immunity (PTI). Sequence Annotation signal peptide 1 23 chain 24 617 Chitin elicitor receptor kinase 1 topological domain 24 232 Extracellular transmembrane region 233 253 Helical; topological domain 254 617 Cytoplasmic repeat 46 74 LysM 1; degenerate repeat 108 140 LysM 2; degenerate repeat 173 200 LysM 3 domain 322 594 Protein kinase nucleotide phosphate-binding region 328 336 ATP region of interest 109 115 Chitin-binding region of interest 137 143 Chitin-binding active site 441 Proton acceptor binding site 349 ATP modified residue 266 Phosphoserine modified residue 268 Phosphoserine modified residue 270 Phosphoserine modified residue 274 Phosphoserine modified residue 519 Phosphothreonine glycosylation site 40 N-linked (GlcNAc...) glycosylation site 52 N-linked (GlcNAc...) glycosylation site 102 N-linked (GlcNAc...) glycosylation site 123 N-linked (GlcNAc...) glycosylation site 152 N-linked (GlcNAc...) disulfide bond 25 93 disulfide bond 29 155 disulfide bond 91 153 strand 32 37 helix 44 50 strand 54 56 helix 64 67 strand 84 89 strand 92 94 turn 95 97 strand 98 106 helix 113 118 turn 119 123 helix 127 133 helix 138 140 strand 146 152 turn 158 160 strand 167 171 helix 178 185 helix 189 195 strand 205 211 Keyword 3D-structure,ATP-binding,Cell membrane,Chitin-binding,Complete proteome,Disulfide bond,Glycoprotein,Kinase,Membrane,Nucleotide-binding,Phosphoprotein,Plant defense,Receptor,Reference proteome,Repeat,Serine/threonine-protein kinase,Signal,Transferase,Transmembrane,Transmembrane helix,Ubl conjugation Sequence Source UniProt Protein Sequence MKLKISLIAP ILLLFSFFFA VESKCRTSCP LALASYYLEN GTTLSVINQN LNSSIAPYDQ 60 INFDPILRYN SNIKDKDRIQ MGSRVLVPFP CECQPGDFLG HNFSYSVRQE DTYERVAISN 120 YANLTTMESL QARNPFPATN IPLSATLNVL VNCSCGDESV SKDFGLFVTY PLRPEDSLSS 180 IARSSGVSAD ILQRYNPGVN FNSGNGIVYV PGRDPNGAFP PFKSSKQDGV GAGVIAGIVI 240 GVIVALLLIL FIVYYAYRKN KSKGDSFSSS IPLSTKADHA SSTSLQSGGL GGAGVSPGIA 300 AISVDKSVEF SLEELAKATD NFNLSFKIGQ GGFGAVYYAE LRGEKAAIKK MDMEASKQFL 360 AELKVLTRVH HVNLVRLIGY CVEGSLFLVY EYVENGNLGQ HLHGSGREPL PWTKRVQIAL 420 DSARGLEYIH EHTVPVYVHR DIKSANILID QKFRAKVADF GLTKLTEVGG SATRGAMGTF 480 GYMAPETVYG EVSAKVDVYA FGVVLYELIS AKGAVVKMTE AVGEFRGLVG VFEESFKETD 540 KEEALRKIID PRLGDSYPFD SVYKMAELGK ACTQENAQLR PSMRYIVVAL STLFSSTGNW 600 DVGNFQNEDL VSLMSGR 617 Gene Ontology GO:0016021; C: integral component of membrane; IEA: UniProtKB-KW GO:0005886; C: plasma membrane; IDA: TAIR GO:0005524; F: ATP binding; IEA: UniProtKB-KW GO:0008061; F: chitin binding; IDA: UniProtKB GO:2001080; F: chitosan binding; IDA: UniProtKB GO:0005515; F: protein binding; IPI: UniProtKB GO:0042803; F: protein homodimerization activity; IDA: UniProtKB GO:0043621; F: protein self-association; ISS: UniProtKB GO:0004674; F: protein serine/threonine kinase activity; IDA: UniProtKB GO:0019199; F: transmembrane receptor protein kinase activity; IDA: TAIR GO:0002752; P: cell surface pattern recognition receptor signaling pathway; IDA: UniProtKB GO:0016998; P: cell wall macromolecule catabolic process; IEA: InterPro GO:0071323; P: cellular response to chitin; IEP: UniProtKB GO:0071219; P: cellular response to molecule of bacterial origin; IEP: UniProtKB GO:0042742; P: defense response to bacterium; IDA: UniProtKB GO:0009817; P: defense response to fungus, incompatible interaction; IMP: TAIR GO:0032491; P: detection of molecule of fungal origin; IMP: TAIR GO:0032499; P: detection of peptidoglycan; IMP: TAIR GO:0045087; P: innate immune response; IMP: TAIR GO:0035556; P: intracellular signal transduction; IDA: TAIR GO:0046777; P: protein autophosphorylation; IDA: UniProtKB GO:0010200; P: response to chitin; IMP: TAIR Interpro InterPro; IPR013320; ConA-like_subgrp InterPro; IPR011009; Kinase-like_dom InterPro; IPR018392; LysM_dom InterPro; IPR000719; Prot_kinase_dom InterPro; IPR017441; Protein_kinase_ATP_BS InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom InterPro; IPR008271; Ser/Thr_kinase_AS InterPro; IPR027789; Syndecan/Neurexin_dom Pfam SMART PROSITE PRINTS |