LERK2_ORYSI
ID LERK2_ORYSI Reviewed; 811 AA.
AC A2XQD3; A0A075F418; A6N110; Q25AF4;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase LECRK2 {ECO:0000305};
DE Short=OsLecRK2 {ECO:0000303|PubMed:25485617};
DE EC=2.7.11.1 {ECO:0000305};
DE Flags: Precursor;
GN Name=LECRK2 {ECO:0000303|PubMed:25485617};
GN ORFNames=H0512B01.10 {ECO:0000312|EMBL:CAH67715.1},
GN OsI_14842 {ECO:0000312|EMBL:EAY93043.1};
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Guang-Lu-Ai No.4;
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. 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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 141-448.
RC TISSUE=Shoot;
RA Kumari S., Panjabi V., Singla-Pareek S.L., Sopory S.K., Pareek A.;
RT "A comparative transcriptome map of early and late salinity stress
RT responses in contrasting genotypes of Oryza sativa L.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in resistance against the herbivorous insect brown
CC planthopper (N.lugens, BPH). Member of the BPH3 (BPH resistance locus
CC 3) cluster which contains LECRK1, LECRK2 and LECRK3.
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}.
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DR EMBL; KF748965; AIE56230.1; -; Genomic_DNA.
DR EMBL; KF748966; AIE56231.1; -; Genomic_DNA.
DR EMBL; KF748967; AIE56232.1; -; Genomic_DNA.
DR EMBL; KF748968; AIE56233.1; -; Genomic_DNA.
DR EMBL; KF748969; AIE56234.1; -; Genomic_DNA.
DR EMBL; KF748970; AIE56235.1; -; Genomic_DNA.
DR EMBL; AL442110; CAH67715.1; -; Genomic_DNA.
DR EMBL; KF748971; AIE56236.1; -; Genomic_DNA.
DR EMBL; CM000129; EAY93043.1; -; Genomic_DNA.
DR EMBL; EF576342; ABR25930.1; -; mRNA.
DR AlphaFoldDB; A2XQD3; -.
DR SMR; A2XQD3; -.
DR EnsemblPlants; BGIOSGA015600-TA; BGIOSGA015600-PA; BGIOSGA015600.
DR Gramene; BGIOSGA015600-TA; BGIOSGA015600-PA; BGIOSGA015600.
DR HOGENOM; CLU_000288_116_2_1; -.
DR OMA; VIWYAKT; -.
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; -; 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 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; 2.
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 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..811
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase LECRK2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000436168"
FT TOPO_DOM 24..464
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 486..811
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 24..153
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 292..344
FT /note="EGF-like; atypical"
FT /evidence="ECO:0000305"
FT DOMAIN 352..436
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 521..795
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 645
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 527..535
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 551
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 59
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 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 237
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 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 296..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 308..325
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 327..343
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 389..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 393..399
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT CONFLICT 151
FT /note="S -> P (in Ref. 1; AIE56230/AIE56231/AIE56232/
FT AIE56233/AIE56234/AIE56235/AIE56236)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="R -> K (in Ref. 2; CAH67715)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="D -> N (in Ref. 1; AIE56230/AIE56231/AIE56232/
FT AIE56233/AIE56234/AIE56235/AIE56236)"
FT /evidence="ECO:0000305"
FT CONFLICT 695
FT /note="N -> K (in Ref. 2; CAH67715)"
FT /evidence="ECO:0000305"
FT CONFLICT 751
FT /note="A -> E (in Ref. 2; CAH67715)"
FT /evidence="ECO:0000305"
FT CONFLICT 758
FT /note="F -> L (in Ref. 1; AIE56230/AIE56231/AIE56232/
FT AIE56233/AIE56234/AIE56235/AIE56236)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 811 AA; 90588 MW; 99866EA2ED3D962E CRC64;
MAPILFLPIL QILLIYCTKS AQAQLNISIG SSLTPQEVNN SWISPSSDFA FGFRAVDGNS
SSYLLAVWFN KIADKTVIWY AKTSSNGQDD TIPVQVQSGS VLKLADGALS LRDPSGNEVW
NPRVTDVGYA RMLNTGNFRL LGTDGATKWE SFGDPSDTIL PTQVLPLGTA LHSRLLATDY
SNGRFQLNVQ DDGNLVLYLV AVPSAYYHDP YWASNTVGNG SQLVFNETGR IYFTLTNGSQ
INITSAGVDS MGDFFHRATL DTDGVFRQYI YPKSKQARSL WQEQWRAVDA LPENICQTIQ
TKVGSGACGF NSYCTFDGTK NTTNCLCPQR YKFFDNERTY KGCRPDFEPQ SCDLDETAAM
VQYEMTPIDR INWPLSDYEQ YSPIDETECR RLCVIDCFCS VAVFNKPSNT CYKKKLPLSN
GNMDSSLQAT VLLKVPRSTN SPSMISSGSS KWKKDKKYWI LGSSLFFGSS VLVNFLLIFV
LLFGTYCSIT SRKKTQLSQL PSNSGLPSKI FTYRELEKAT GGFHEVLGTG ASGIVYKGQL
QDECGTNIAV KKIEKLQQEA QKEFLVEVQT IGQTFHRNLV RLLGFCNEGT EKLLVYEFMS
NGSLNTFLFN DTHPHWSLRV QVALGVSRGL LYLHEECNKQ IIHCDMKPQN ILLDDNFVAK
ISDFGLAKLL PVNQTQTNTG IRGTRGYVAP EWFKNIGITS KVDVYSFGVI LLELVCCRKN
VELEVADEEQ TILTYWANDC YRCGRIDLLV AGDDEAIFNI KKVERFVAVA LWCLQEEPSM
RPTMHKVMQM LDGAVQIPTP PDPSSYISSL A
