ID LERK4_ORYSJ Reviewed; 804 AA.
AC Q7FAZ0; A0A0P0W7I0; Q0JEU5;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 149.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase LECRK4 {ECO:0000305};
DE Short=OsLecRK4 {ECO:0000303|PubMed:25485617};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=OsRLCK136 {ECO:0000303|PubMed:19825577};
DE Flags: Precursor;
GN Name=LECRK4 {ECO:0000303|PubMed:25485617};
GN OrderedLocusNames=Os04g0202800 {ECO:0000312|EMBL:BAF14142.2},
GN LOC_Os04g12600 {ECO:0000305};
GN ORFNames=OsJ_13808 {ECO:0000312|EMBL:EAZ29749.1},
GN OSJNBb0005B05.8 {ECO:0000312|EMBL:CAE03341.2};
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 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 [6]
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 [7]
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: Does not seem to be involved in resistance against the
CC herbivorous insect brown planthopper (N.lugens, BPH).
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=BAS88076.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL606606; CAE03341.2; -; Genomic_DNA.
DR EMBL; AP008210; BAF14142.2; -; Genomic_DNA.
DR EMBL; AP014960; BAS88076.1; ALT_INIT; Genomic_DNA.
DR EMBL; CM000141; EAZ29749.1; -; Genomic_DNA.
DR RefSeq; XP_015634539.1; XM_015779053.1.
DR AlphaFoldDB; Q7FAZ0; -.
DR SMR; Q7FAZ0; -.
DR STRING; 39947.Q7FAZ0; -.
DR GlyCosmos; Q7FAZ0; 8 sites, No reported glycans.
DR PaxDb; 39947-Q7FAZ0; -.
DR EnsemblPlants; Os04t0202800-01; Os04t0202800-01; Os04g0202800.
DR GeneID; 4335153; -.
DR Gramene; Os04t0202800-01; Os04t0202800-01; Os04g0202800.
DR KEGG; osa:4335153; -.
DR eggNOG; ENOG502QQEW; Eukaryota.
DR HOGENOM; CLU_000288_116_2_1; -.
DR InParanoid; Q7FAZ0; -.
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: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:SF117; G-TYPE LECTIN S-RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE LECRK4; 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 3: Inferred from homology;
KW ATP-binding; Disulfide bond; EGF-like domain; Glycoprotein; Kinase; Lectin;
KW Membrane; Nucleotide-binding; 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..804
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase LECRK4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000436171"
FT TOPO_DOM 24..458
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..804
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 24..150
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 290..341
FT /note="EGF-like; atypical"
FT /evidence="ECO:0000305"
FT DOMAIN 349..426
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 514..790
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 638
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 520..528
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 544
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 294..311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 305..322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 324..340
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 386..406
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 390..396
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
SQ SEQUENCE 804 AA; 89721 MW; DBF2FECC73B04F46 CRC64;
MAPPLFLLSL QLLVLLSSPS AQAQNISLGT SLTTQGPNNA WLSPSGDFAF GFRPIDGNSS
FYLLAIWFNK ISDKTATWYA KTSEQEPQPI QVPSGSILQF TSTGVLSLRD PTNREVWNPG
ATGAPYASML DTGNFVIAAA GGSTISWETF KNPTDTILVT QALSPGMKLR SRLLTTDYSN
GRFLLNMETQ RAALYTMAVP SGNLYDPYWS TPIDENVTNQ VTNLVFNTTG RIYVSMKNGT
QFNMTSGVIR SMEDYYHRAT LDPDGVFRQY VYPKKPSSMS QAWTAVSIQP ENICNAQTKV
GSGTCGFNSY CMFDGSNNQT SCVCPEQYSF FDEVRKYRGC RPDFELQSCD LDEAASMAQY
EFNLVNNVDW PQADYEWYTP IDMDECRRLC LIDCFCAVAV FHENTCWKKK LPLSNGIMGS
GVQRTVLIKV PKSNSSQPEL RKSRKWKSDK KLWILGSSLL LGGSVIANFA LSSVLLFGTY
CTITRKDVQP LQPSRDPGLP LKAFSYAELE KATDGFKEVL GTGASGIVYK GQLQDELGTY
IAVKKIDKIQ HETEKEFAVE VQTIGRTYHK NLVRMLGFCN EGTERLLVYE FMVNGSLNRF
LFSGVRPLWS LRVQLALGVA RGLLYLHEEC STQIIHCDIK PQNILLDDNF IAKISDFGLA
KLLRTNQTQT YTGIRGTRGY VAPEWFKNVG ITAKVDVYSF GVILLELICC RQNVEMEAAE
EEQSILTYWA NDCYRCGRVD LLVDGDDEAK LNIKKVERFV AVALWCLQEE PTMRPSILKV
TQMLDGADAI PTPPDSSSVV NSFP
//
