ID LERK1_ORYSJ Reviewed; 813 AA.
AC Q7FAZ3; A0A075F7F4; Q0JEU8;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 141.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase LECRK1 {ECO:0000305};
DE Short=OsLecRK1 {ECO:0000303|PubMed:25485617};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=OsRLCK134 {ECO:0000303|PubMed:19825577};
DE Flags: Precursor;
GN Name=LECRK1 {ECO:0000303|PubMed:25485617};
GN OrderedLocusNames=Os04g0201900 {ECO:0000312|EMBL:BAS88070.1},
GN LOC_Os04g12540 {ECO:0000305};
GN ORFNames=OsJ_13804 {ECO:0000312|EMBL:EEE60504.1},
GN OSJNBb0005B05.5 {ECO:0000312|EMBL:CAE03338.2};
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 [MRNA], AND FUNCTION.
RX PubMed=25485617; DOI=10.1038/nbt.3069;
RA Liu Y., Wu H., Chen H., Liu Y., He J., Kang H., Sun Z., Pan G., Wang Q.,
RA Hu J., Zhou F., Zhou K., Zheng X., Ren Y., Chen L., Wang Y., Zhao Z.,
RA Lin Q., Wu F., Zhang X., Guo X., Cheng X., Jiang L., Wu C., Wang H.,
RA Wan J.;
RT "A gene cluster encoding lectin receptor kinases confers broad-spectrum and
RT durable insect resistance in rice.";
RL Nat. Biotechnol. 33:301-305(2015).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP GENE FAMILY.
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).
CC -!- FUNCTION: Involved in innate immunity. Required for the expression of
CC defense-related genes PR1A, LOX2 and CHS1 upon biotic stresses.
CC Required for basal resistance to the fungal blast (M.grisea), bacterial
CC blight (X.oryzae pv. oryzae, Xoo) and the herbivorous insect brown
CC planthopper (N.lugens, BPH). May be involved in several defense
CC signaling pathways. Involved in the promotion of seed germination.
CC Required for the expression of alpha-amylase genes during seed
CC germination (By similarity). Involved in resistance against the
CC herbivorous insect brown planthopper (N.lugens, BPH). Member of the
CC BPH3 (BPH resistance locus 3) cluster which contains LECRK1, LECRK2 and
CC LECRK3 (PubMed:25485617). {ECO:0000250|UniProtKB:A0A075F7E9,
CC ECO:0000269|PubMed:25485617}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF14139.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KF748964; AIE56229.1; -; Genomic_DNA.
DR EMBL; AL606606; CAE03338.2; -; Genomic_DNA.
DR EMBL; AP008210; BAF14139.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014960; BAS88070.1; -; Genomic_DNA.
DR EMBL; CM000141; EEE60504.1; -; Genomic_DNA.
DR RefSeq; XP_015633598.1; XM_015778112.1.
DR AlphaFoldDB; Q7FAZ3; -.
DR SMR; Q7FAZ3; -.
DR STRING; 39947.Q7FAZ3; -.
DR GlyCosmos; Q7FAZ3; 8 sites, No reported glycans.
DR PaxDb; 39947-Q7FAZ3; -.
DR EnsemblPlants; Os04t0201900-01; Os04t0201900-01; Os04g0201900.
DR GeneID; 4335148; -.
DR Gramene; Os04t0201900-01; Os04t0201900-01; Os04g0201900.
DR KEGG; osa:4335148; -.
DR eggNOG; ENOG502QQEW; Eukaryota.
DR HOGENOM; CLU_000288_116_2_1; -.
DR InParanoid; Q7FAZ3; -.
DR OMA; CRIATKK; -.
DR OrthoDB; 339619at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
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:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051707; P:response to other organism; IEA:UniProt.
DR CDD; cd01098; PAN_AP_plant; 1.
DR Gene3D; 2.90.10.10; Bulb-type lectin domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR PANTHER; PTHR47976; G-TYPE LECTIN S-RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD2-5; 1.
DR PANTHER; PTHR47976:SF101; G-TYPE LECTIN S-RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE LECRK1; 1.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000641; SRK; 1.
DR SMART; SM00108; B_lectin; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50927; BULB_LECTIN; 1.
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; Disulfide bond; EGF-like domain; Glycoprotein; Kinase; Lectin;
KW Membrane; Nucleotide-binding; Plant defense; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..813
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase LECRK1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000436165"
FT TOPO_DOM 20..466
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..813
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 22..149
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 293..346
FT /note="EGF-like; atypical"
FT /evidence="ECO:0000305"
FT DOMAIN 354..433
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 523..797
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 647
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 529..537
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 553
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 297..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 309..327
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 329..345
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 391..413
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 395..401
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT CONFLICT 72
FT /note="D -> N (in Ref. 1; AIE56229)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="N -> D (in Ref. 1; AIE56229)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 813 AA; 90495 MW; 95EA7906B38603C5 CRC64;
MVALLLFPML LQLLSPTCAQ TQKNITLGST LAPQSPASSW LSPSGDFAFG FRPVEGNTSF
YLIAVWFNKI SDKTVVWYAK NTDQDPSIVE VPSDSFLQLT NDGALSLKDR SGQEGWNPQV
TSVAYASMRD TGNFVLLGAD GTTKWQTFDM PSDTILPTQV IPCNKTRNKS LRARLDINDY
SSGRFLLDVQ TDGNLALYLV AVPSGSKYQQ YWSTDTTGNG SELVFSETGK VYFALTDGTQ
INISSGAGIG SMADYFHRAT LDPDGVFRQY VYPKKANAGI LGGETWTAVS MQPQNICHAI
VSDVGSGVCG FNSYCTFDGT RNQIASCQCP PWYKFFDEQK KYKGCKQDFQ PHSCDLDEAT
ALAQFELRPI YGVDWPLSDY EKYEPIGQDD CGRLCVIDCF CAMAVYNQST STCWKKKLPL
SNGNMADYVQ RTVLLKVPSS NSSQSMISTS SNKWKRNRKH WVLGSSLILG TSILVNFALI
SIFLFGTYCR IATKKNIPLS QASSKSQLPL KTFTYKELEK ATAGFHEILG AGASGVVYKG
QLEDELKTNI AVKKIDKLQP ETEKEFMVEV ETIGQTFHKN LVRLLGFCNE GAERLLVYEF
MTNGPLNRLL FDNSRPHWNT RVHIALGVAR GLLYLHDECS KQIIHCDIKP QNILLDDNLV
AKISDFGLAK LLLTNQTRTN TGIRGTRGYV APEWFKNIGI STKVDVYSFG VILLELVCCR
RNVELEVVDE EQTIVTYWAN DCYRSGRIDL LVEGDDEAIY NIKKVERFVT VALWCLQEDP
SMRPNMLKVT QMLDGAVAIP SPPDPCSFIS SLP
//
