LERK3_ORYSJ
ID LERK3_ORYSJ Reviewed; 811 AA.
AC Q0JEU6; Q7FAZ1;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 2.
DT 03-AUG-2022, entry version 106.
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:0000303|PubMed:19825577};
DE Flags: Precursor;
GN Name=LECRK3 {ECO:0000303|PubMed:25485617};
GN OrderedLocusNames=Os04g0202500 {ECO:0000312|EMBL:BAF14141.1},
GN LOC_Os04g12580 {ECO:0000305};
GN ORFNames=OSJNBb0005B05.7 {ECO:0000312|EMBL:CAE03340.2};
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 [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 [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.
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.
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).
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=BAF14141.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF14141.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAS88074.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAS88074.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAE03340.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAE03340.2; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL606606; CAE03340.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008210; BAF14141.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014960; BAS88074.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q0JEU6; -.
DR SMR; Q0JEU6; -.
DR STRING; 4530.OS04T0202500-00; -.
DR PRIDE; Q0JEU6; -.
DR InParanoid; Q0JEU6; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000059680; 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_0000436169"
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"
SQ SEQUENCE 811 AA; 90376 MW; 23EAB29997528951 CRC64;
MAHLLFLPIL QLLLLYCTKS AQAQLNISIG SSLTPQGVNN SWISPSADFA FGFLAVDGNS
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 RLCVTDCFCA VAVFDKASST CWKKRFPLSN
GKMDVNVPRT VLIKVPRSTN SPSVFSSGSS KWKEDQKYWI LGSSLLFGSS VLVNFLLISV
MLFGTYCSIT SRKKTQLSQP SNNSGLPPKI FTYSELEKAT GGFQEVLGTG ASGVVYKGQL
QDEFGTNIAV KKIEKLQQEA QKEFLVEVQT IGQTFHRNLV RLLGFCNEGT ERLLVYEFMS
NGSLNTFLFS DTHPHWSLRV QVALGVARGL LYLHEECNKQ IIHCDMKPQN ILLDDNFVAK
ISDFGLAKLL PVNQTQTNTG IRGTRGYVAP EWFKNIGITS KVDVYSFGVI LLELVCCRKN
VELEVLDEEQ TILTYWANDC YKCGRIDLLV AGDDEAIFNI KKVERFVAVA LWCLQEEPSM
RPTMLKVTQM LDGAVQIPTP PDPSSYISSL A
