RK185_ORYSJ
ID RK185_ORYSJ Reviewed; 491 AA.
AC Q6I5Q6; Q0DIQ0;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Receptor-like cytoplasmic kinase 185 {ECO:0000303|PubMed:19825577};
DE Short=OsRLCK185 {ECO:0000303|PubMed:19825577};
DE EC=2.7.11.1 {ECO:0000305};
GN Name=RLCK185 {ECO:0000303|PubMed:19825577};
GN OrderedLocusNames=Os05g0372100 {ECO:0000312|EMBL:BAS93696.1},
GN LOC_Os05g30870 {ECO:0000305};
GN ORFNames=OSJNBa0025P09.5 {ECO:0000312|EMBL:AAT58829.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19825577; DOI=10.1093/mp/ssn047;
RA Vij S., Giri J., Dansana P.K., Kapoor S., Tyagi A.K.;
RT "The receptor-like cytoplasmic kinase (OsRLCK) gene family in rice:
RT organization, phylogenetic relationship, and expression during development
RT and stress.";
RL Mol. Plant 1:732-750(2008).
RN [6]
RP FUNCTION, INTERACTION WITH CERK1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP SER-240; THR-241 AND THR-246, AND MUTAGENESIS OF LYS-108; SER-240; THR-241
RP AND THR-246.
RX PubMed=23498959; DOI=10.1016/j.chom.2013.02.007;
RA Yamaguchi K., Yamada K., Ishikawa K., Yoshimura S., Hayashi N.,
RA Uchihashi K., Ishihama N., Kishi-Kaboshi M., Takahashi A., Tsuge S.,
RA Ochiai H., Tada Y., Shimamoto K., Yoshioka H., Kawasaki T.;
RT "A receptor-like cytoplasmic kinase targeted by a plant pathogen effector
RT is directly phosphorylated by the chitin receptor and mediates rice
RT immunity.";
RL Cell Host Microbe 13:347-357(2013).
CC -!- FUNCTION: Functions as an immediate downstream signaling partner of
CC CERK1 in the microbial peptidoglycans (PGNs) and fungal chitin
CC signaling pathways that mediate innate immunity. Is required for
CC chitin-induced activation of MPK3 and MPK6. Participates in the
CC activation of defense genes during response to PGN and chitin.
CC {ECO:0000269|PubMed:23498959}.
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:0000305};
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:0000305};
CC -!- SUBUNIT: Interacts with CERK1. {ECO:0000269|PubMed:23498959}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23498959};
CC Peripheral membrane protein {ECO:0000255}.
CC -!- PTM: Phosphorylated at Ser-240, Thr-241 and Thr-246 by CERK1 in
CC response to chitin elicitation. {ECO:0000269|PubMed:23498959}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF17273.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAS93695.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC119289; AAT58829.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF17273.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014961; BAS93695.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014961; BAS93696.1; -; Genomic_DNA.
DR RefSeq; XP_015639740.1; XM_015784254.1.
DR AlphaFoldDB; Q6I5Q6; -.
DR SMR; Q6I5Q6; -.
DR STRING; 4530.OS05T0372100-01; -.
DR iPTMnet; Q6I5Q6; -.
DR PaxDb; Q6I5Q6; -.
DR PRIDE; Q6I5Q6; -.
DR EnsemblPlants; Os05t0372100-01; Os05t0372100-01; Os05g0372100.
DR EnsemblPlants; Os05t0372100-04; Os05t0372100-04; Os05g0372100.
DR GeneID; 4338592; -.
DR Gramene; Os05t0372100-01; Os05t0372100-01; Os05g0372100.
DR Gramene; Os05t0372100-04; Os05t0372100-04; Os05g0372100.
DR KEGG; osa:4338592; -.
DR eggNOG; KOG1187; Eukaryota.
DR InParanoid; Q6I5Q6; -.
DR OMA; CISWEDI; -.
DR OrthoDB; 684563at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR ExpressionAtlas; Q6I5Q6; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP 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:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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 Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 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 ATP-binding; Cell membrane; Immunity; Innate immunity; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Plant defense; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..491
FT /note="Receptor-like cytoplasmic kinase 185"
FT /id="PRO_0000440895"
FT DOMAIN 80..356
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 206
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 86..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23498959"
FT MOD_RES 241
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:23498959"
FT MOD_RES 246
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:23498959"
FT MUTAGEN 108
FT /note="K->E: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:23498959"
FT MUTAGEN 240
FT /note="S->A: Abolishes phosphorylation and activation by
FT CERK1; when associated with A-241 and A-246."
FT /evidence="ECO:0000269|PubMed:23498959"
FT MUTAGEN 241
FT /note="T->A: Abolishes phosphorylation and activation by
FT CERK1; when associated with A-240 and A-246."
FT /evidence="ECO:0000269|PubMed:23498959"
FT MUTAGEN 246
FT /note="T->A: Abolishes phosphorylation and activation by
FT CERK1; when associated with A-240 and A-241."
FT /evidence="ECO:0000269|PubMed:23498959"
SQ SEQUENCE 491 AA; 53704 MW; 336AAEFB7D09BA52 CRC64;
MGCFPCFGSG GKGEAKKGGG GRKDGGSADR RVARVGSDKS KSQGGLDSRK DAFIPRDANG
QPIAAHTFTF RELAAATKNF RQDCLLGEGG FGRVYKGHLE NGQAVAVKQL DRNGLQGNRE
FLVEVLMLSL LHHDNLVNLI GYCADGDQRL LVYEFMPLGS LEDHLHDIPP DKEPLDWNTR
MKIAAGAAKG LEFLHDKANP PVIYRDFKSS NILLGEGYHP KLSDFGLAKL GPVGDKTHVS
TRVMGTYGYC APEYAMTGQL TVKSDVYSFG VVFLELITGR KAIDNTKPLG EQNLVAWARP
LFKDRRKFPK MADPLLAGRF PMRGLYQALA VAAMCLQEQA ATRPFIGDVV TALSYLASQT
YDPNTPVQHS RSNASTPRAR NRVGANFDQR RLHSPNHQQS PDLRKEGTTT SKYEAEVSRT
NSGSGSGRRA GLDSMDVTGS QMGSPAHAGR KRESSRSTDR QRAVAEAKTW GENSRERKWP
NARGSFDSTN E
