CERK1_PHYPA
ID CERK1_PHYPA Reviewed; 640 AA.
AC A9TXT1;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Chitin elicitor receptor kinase 1 {ECO:0000305};
DE Short=PpCERK1 {ECO:0000303|PubMed:27268428};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:A8R7E6};
DE AltName: Full=Chitin receptor CERK1 {ECO:0000303|PubMed:27268428};
DE AltName: Full=LysM domain receptor-like kinase 1 {ECO:0000305};
DE AltName: Full=LysM-containing receptor-like kinase 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=CERK1 {ECO:0000303|PubMed:27268428};
GN ORFNames=PHYPADRAFT_1279 {ECO:0000312|EMBL:EDQ51753.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Gransden 2004 {ECO:0000303|PubMed:27268428};
RX PubMed=27268428; DOI=10.1105/tpc.15.00774;
RA Bressendorff S., Azevedo R., Kenchappa C.S., Ponce de Leon I., Olsen J.V.,
RA Rasmussen M.W., Erbs G., Newman M.A., Petersen M., Mundy J.;
RT "An innate immunity pathway in the Moss Physcomitrella patens.";
RL Plant Cell 28:1328-1342(2016).
RN [2] {ECO:0000312|EMBL:EDQ51753.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (PARTIAL).
RC STRAIN=cv. Gransden 2004;
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
CC -!- FUNCTION: Lysin motif (LysM) receptor kinase required as a cell surface
CC receptor for chitin elicitor (chitooligosaccharides) signaling leading
CC to innate immunity in response to biotic stresses (By similarity). The
CC CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in
CC pathogen defense. The pathway induces rapid growth inhibition, cell
CC wall depositions and accumulation of defense-related transcripts. This
CC protein is required for response to chitin. Is able to complement the
CC A.thaliana cerk1 mutant (PubMed:27268428).
CC {ECO:0000250|UniProtKB:A0A0P0XII1, ECO:0000269|PubMed:27268428}.
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:0000250|UniProtKB:A8R7E6};
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:0000250|UniProtKB:A8R7E6};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A8R7E6};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:A8R7E6}.
CC -!- INDUCTION: Up-regulated in response to chitosan.
CC {ECO:0000269|PubMed:27268428}.
CC -!- DISRUPTION PHENOTYPE: Chitin treatment does not lead to growth
CC inhibition or reduced cell wall-associated depositions in contrast to
CC the wild-type. No chitin-, chitosan- or chitin hexamer-induced MPK
CC phosphorylation. Peptidyl glycan (PGN) from S.aureus does not induce
CC MPK phosphorylation either. Reduced accumulation of PAL4 and CHS
CC transcripts in response to chitin. Tissues fail to exhibit enhanced
CC conductivity in an electrolyte leakage assay.
CC {ECO:0000269|PubMed:27268428}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDQ51753.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS545251; EDQ51753.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001783413.1; XM_001783361.1.
DR AlphaFoldDB; A9TXT1; -.
DR SMR; A9TXT1; -.
DR STRING; 3218.PP1S364_10V6.1; -.
DR eggNOG; ENOG502QPX8; Eukaryota.
DR HOGENOM; CLU_000288_99_3_1; -.
DR InParanoid; A9TXT1; -.
DR Proteomes; UP000006727; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0019199; F:transmembrane receptor protein kinase activity; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.10.350.10; -; 1.
DR InterPro; IPR044812; CERK1/LYK3-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR46204; PTHR46204; 1.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00257; LysM; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51782; LYSM; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Chitin-binding; Disulfide bond; Kinase;
KW Membrane; Nucleotide-binding; Plant defense; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..640
FT /note="Chitin elicitor receptor kinase 1"
FT /id="PRO_0000443381"
FT TOPO_DOM 32..248
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..640
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 53..98
FT /note="LysM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 113..160
FT /note="LysM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 179..227
FT /note="LysM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 330..612
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 286..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 452
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 119..125
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000250|UniProtKB:A8R7E6"
FT BINDING 148..154
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000250|UniProtKB:A8R7E6"
FT BINDING 336..344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DISULFID 43..104
FT /evidence="ECO:0000250|UniProtKB:A8R7E6"
FT DISULFID 49..166
FT /evidence="ECO:0000250|UniProtKB:A8R7E6"
FT DISULFID 102..164
FT /evidence="ECO:0000250|UniProtKB:A8R7E6"
FT CONFLICT 236..238
FT /note="YVL -> SSG (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 240..243
FT /note="TVHW -> GSS (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 640 AA; 70884 MW; 9D7C2A7B4D034D22 CRC64;
MKFQMKMKSE LCRTYKYWLI LLVLWLSGVT QRETGVLIVD ADCIPPNGCK ALAYYRLKQG
DDLEKLQGRF QTNNSEVLAY NPQLVDANSI QAGTNIYLPF DCLCLNGELV HRFSYTVTTN
DTAEKVVDVT YQKLTTVGAV RSASNSGDLS SIYSGQSLTI PVRCYCGDPN VDPKYGLFST
YVVQADDQLT SLSTNFSVDA DVISKFNSDT RNLSPDSIIF IPSKAANGSF PPFSGYVLGT
VHWRSNVGII VGVVVGGIVL AVLLLFALIF GFKHFRRRKL AKEPTMQQSG LLSSSSMAGS
KPSRSGSTML PVPKSVEFTY EELAAATDNF SLAKKIGQGG FASVYYGVIR DQKLAIKKMT
LQCTKEFLAE LQVLTNVHHT NLVQLIGYCT TNSLFLVYEY IENGTLDHHL RRRKSDDKPP
LSWLQRVQIC LDSARGLEYI HEHTKPTYIH RDIKSANILL DDNFRAKVAD FGLAKLAEEG
TGTGIVGTFG YMPPEYALYG EVSPKLDVYA FGVVLFEIIS GRVAISSALP SENDQQSPAQ
NRESRTLTSF FEPVLNDPDG KTLLPKCIDP ALNGEYSLDA VWKMAQLARR CTHQSPDMRP
TMRFAVVQLM TLASVTQEWD VGYFSRASSQ SQPPSGNDQL
