LERK3_ORYSI
ID LERK3_ORYSI Reviewed; 811 AA.
AC Q25AG3; A0A075F7G5; A2XQD5;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase LECRK3 {ECO:0000305};
DE Short=OsLecRK3 {ECO:0000303|PubMed:25485617};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=OsRLCK135 {ECO:0000305};
DE Flags: Precursor;
GN Name=LECRK3 {ECO:0000303|PubMed:25485617};
GN ORFNames=H0512B01.11 {ECO:0000312|EMBL:CAH67716.1},
GN OsI_14844 {ECO:0000312|EMBL:EAY93045.1},
GN OSIGBa0147O06.1 {ECO:0000312|EMBL:CAH66271.1};
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).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAY93045.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KF748973; AIE56238.1; -; Genomic_DNA.
DR EMBL; KF748974; AIE56239.1; -; Genomic_DNA.
DR EMBL; KF748975; AIE56240.1; -; Genomic_DNA.
DR EMBL; KF748976; AIE56241.1; -; Genomic_DNA.
DR EMBL; KF748977; AIE56242.1; -; Genomic_DNA.
DR EMBL; KF748978; AIE56243.1; -; Genomic_DNA.
DR EMBL; KF748979; AIE56244.1; -; Genomic_DNA.
DR EMBL; AL442110; CAH67716.1; -; Genomic_DNA.
DR EMBL; CR855078; CAH66271.1; -; Genomic_DNA.
DR EMBL; CM000129; EAY93045.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q25AG3; -.
DR SMR; Q25AG3; -.
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; 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 3: Inferred from homology;
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 LECRK3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000436170"
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..430
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 74
FT /note="D -> E (in Ref. 2; CAH67716/CAH66271)"
FT CONFLICT 88..92
FT /note="KDDTI -> QGDTM (in Ref. 1; AIE56238/AIE56239/
FT AIE56240/AIE56241/AIE56242/AIE56243/AIE56244)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="V -> A (in Ref. 1; AIE56238/AIE56239/AIE56240/
FT AIE56241/AIE56242/AIE56243/AIE56244)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="K -> N (in Ref. 2; CAH67716/CAH66271 and 1;
FT AIE56238/AIE56239/AIE56240/AIE56241/AIE56242/AIE56243/
FT AIE56244)"
FT CONFLICT 546
FT /note="I -> T (in Ref. 2; CAH67716/CAH66271 and 1;
FT AIE56238/AIE56239/AIE56240/AIE56241/AIE56242/AIE56243/
FT AIE56244)"
FT CONFLICT 627
FT /note="A -> S (in Ref. 2; CAH67716/CAH66271)"
FT CONFLICT 658
FT /note="A -> V (in Ref. 2; CAH67716/CAH66271 and 1;
FT AIE56238/AIE56239/AIE56240/AIE56241/AIE56242/AIE56243/
FT AIE56244)"
SQ SEQUENCE 811 AA; 90441 MW; 8F81933DB14836C4 CRC64;
MAHLLFLPIL QLLLLYCTKS AQAQLNISIG SSLTPQGVNN SWISPSADFA FGFRAVDGNS
SSYLLAVWFN KIADKTVVWY ARTSSNGKDD TIPVQVQSGS VLKLADGALS LRDPSGNEVW
NPQVTDVGYA RMLDTGNFRL LGTDGATKWE SFGDPSDTIL PTQVLSLGTA LHSRLLATDY
SNGRFQLKVQ RDGNLVMYPD AVPSGYLYDP YWASNTVDNG SQLVFNETGR IYFTIINGSQ
VNITSAGVDS MGDFFHRATL DTDGVFRQYV YPKNIHARPL WPEQWTAVDV LPENICQSIQ
TMVGSGACGF NSYCTIDGTK NTTSCLCPQN YKFIDDKRKY KGCRPDFEPQ NCDLDETTAM
LQYDMAPIDR VDWPLSDYEQ YNPIDQTECR RLCVIDCFCA VAVFDKASST CWKKRFPLSN
GKMDVNVPRT VLIKVPRSTN SPSVFSSGSS KWKEDKKYWI LGSSLLFGSS VLVNFLLISV
MLFGTYCSIT SRKKIQLSQP SNKSGLPPKI FTYSELEKAT GGFQEVLGTG ASGVVYKGQL
QDEFGINIAV KKIEKLQQEA QKEFLVEVQT IGQTFHRNLV RLLGFCNEGT ERLLVYEFMS
NGSLNTFLFS DTHPHWSLRV QVALGVARGL LYLHEECNKQ IIHCDMKPQN ILLDDNFAAK
ISDFGLAKLL PVNQTQTNTG IRGTRGYVAP EWFKNIGITS KVDVYSFGVI LLELVCCRKN
VELEVLDEEQ TILTYWANDC YKCGRIDLLV AGDDEAIFNI KKVERFVAVA LWCLQEEPSM
RPTMLKVTQM LDGAVQIPTP PDPSSYISSL A
