LERK1_ORYSI
ID LERK1_ORYSI Reviewed; 813 AA.
AC A0A075F7E9; A0A075F413; A2XQD1; T1SG84;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 2.
DT 03-AUG-2022, entry version 36.
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:0000305};
DE Flags: Precursor;
GN Name=LECRK1 {ECO:0000303|PubMed:25485617};
GN Synonyms=LECRK {ECO:0000303|PubMed:24033867};
GN ORFNames=OsI_14840 {ECO:0000312|EMBL:EAY93041.1};
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ADF4, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=24033867; DOI=10.1111/tpj.12328;
RA Cheng X., Wu Y., Guo J., Du B., Chen R., Zhu L., He G.;
RT "A rice lectin receptor-like kinase that is involved in innate immune
RT responses also contributes to seed germination.";
RL Plant J. 76:687-698(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
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).
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 (O.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 (PubMed:15685292). Involved in resistance against the brown
CC planthopper (BPH). Member of the BPH3 (BPH resistance locus 3) cluster
CC which contains LECRK1, LECRK2 and LECRK3 (PubMed:25485617).
CC {ECO:0000269|PubMed:15685292, 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 -!- SUBUNIT: Interacts (via kinase domain) with ADF4.
CC {ECO:0000269|PubMed:24033867}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in plumules, radicles and panicles.
CC {ECO:0000269|PubMed:24033867}.
CC -!- INDUCTION: Induced by infection with the fungal blast (M.grisea) and
CC bacterial blight (X.oryzae pv. oryzae, Xoo).
CC {ECO:0000269|PubMed:24033867}.
CC -!- MISCELLANEOUS: Seeds silencing LECRK1 show decreased germination rates
CC due to decreased alpha-amylase activity during seed germination. Plants
CC silencing LECRK1 have increased susceptibility to infection by the
CC fungal blast (M.grisea), bacterial blight (X.oryzae pv. oryzae, Xoo)
CC and the herbivorous insect brown planthopper (N.lugens, BPH). Plants
CC silencing LECRK1 display reduced induction of the defense-related genes
CC PR1A, LOX2 and CHS1 after exposure to biotic stresses.
CC {ECO:0000269|PubMed:24033867}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AGT37611.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC Sequence=EAY93041.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KC131131; AGT37611.1; ALT_SEQ; mRNA.
DR EMBL; KF748957; AIE56222.1; -; Genomic_DNA.
DR EMBL; KF748958; AIE56223.1; -; Genomic_DNA.
DR EMBL; KF748959; AIE56224.1; -; Genomic_DNA.
DR EMBL; KF748960; AIE56225.1; -; Genomic_DNA.
DR EMBL; KF748961; AIE56226.1; -; Genomic_DNA.
DR EMBL; KF748962; AIE56227.1; -; Genomic_DNA.
DR EMBL; KF748963; AIE56228.1; -; Genomic_DNA.
DR EMBL; CM000129; EAY93041.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A0A075F7E9; -.
DR SMR; A0A075F7E9; -.
DR STRING; 39946.A0A075F7E9; -.
DR Proteomes; UP000007015; Chromosome 4.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate 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:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 2.90.10.10; -; 2.
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 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; SSF51110; 1.
DR SUPFAM; SSF56112; SSF56112; 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 1: Evidence at protein 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_0000436166"
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 90
FT /note="E -> K (in Ref. 1; AGT37611 and 2; AIE56222/
FT AIE56223/AIE56224/AIE56225/AIE56226/AIE56227/AIE56228)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="R -> C (in Ref. 1; AGT37611 and 2; AIE56222/
FT AIE56223/AIE56224/AIE56225/AIE56226/AIE56227/AIE56228)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="E -> G (in Ref. 1; AGT37611)"
FT /evidence="ECO:0000305"
FT CONFLICT 761
FT /note="D -> N (in Ref. 1; AGT37611 and 2; AIE56222/
FT AIE56223/AIE56224/AIE56225/AIE56226/AIE56227/AIE56228)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 813 AA; 90770 MW; DF0114F5E41EC3DB CRC64;
MVALLLFPML LQLLSPTCAQ TQKNITLGST LAPQGPASSW LSPSGDFAFG FRPVEGNTSF
YLIAVWFNKI SDKTVVWYAK NTDQDPSIVE VPSDSFLQLT NDGALSLKDR SGQEGWNPQV
TGVAYASMRD TGNFVLLGAD GTTKWQTFDM PSDTILPTQV IPCNKTRNKS LRARLDIDDY
SSGRFLLDVQ TDGNLALYLV AVPSGSKYQQ YWSTDTTGNG SELVFSETGK VYFALTDGTQ
INISSDAGIG SMADYFHRAT LDPDGVFRQY VYPKKANAGI LGGETWTALS MQPQNICHAI
VSDVGSGVCG FNSYCTFDGT RNQIASCQCP PWYKFFDEQK KYKGCKQDFQ PHSCDLEEAT
ALAQFELRPI YGVDWPLSDY EKYEPIGQDD CGRLCVIECF CAMAVYNQST STCWKKKLPL
SNGNMADYVQ RTVLLKVPSS NSSQFMISTS SNKWKRNRKH WVLGSSLILG TSILVNFALI
SIFLFGTYCR ITTKKNIPLS QASSKSQLPL KTFTYKELEK ATAGFHEILG AGASGVVYKG
QLEDELKTNI AVKTIHKLQP ETEKEFMVEV ETIGQTFHKN LVRLLGFCNE RAERLLVYEF
MTNGPLNRLL FDNSRPHWNT RVHIALGVAR GFLYLHDECS KQIIHCDIKP QNILLDDNLV
AKISDFGLAK LLLTNQTRTK TGIRGTRGYV APEWFKNIGI STKVDVYSFG VILLELVCCR
RNVELEVVDE EQTIVTYWAN DCYRSGRIDL LVEGDDEAIY DIKKVERFVT VALWCLQEDP
SMRPNMLKVT QMLDGAVAIP SPPDPCSFIS SLP
