CRK10_ORYSJ
ID CRK10_ORYSJ Reviewed; 645 AA.
AC Q0D5R2; A3BKS4; Q84S59;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Cysteine-rich receptor-like protein kinase 10 {ECO:0000305};
DE Short=Cysteine-rich RLK10 {ECO:0000305};
DE EC=2.7.11.- {ECO:0000305};
DE Flags: Precursor;
GN Name=CRK10 {ECO:0000303|PubMed:27176732};
GN OrderedLocusNames=Os07g0541500 {ECO:0000312|EMBL:BAF21811.1},
GN LOC_Os07g35700 {ECO:0000305};
GN ORFNames=OJ1008_E09.116 {ECO:0000312|EMBL:BAD30127.1},
GN OsJ_24608 {ECO:0000312|EMBL:EAZ40163.1},
GN P0458H05.133 {ECO:0000312|EMBL:BAC65055.1};
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=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 [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, AND INDUCTION BY BENZOTHIADIAZOLE.
RX PubMed=27176732; DOI=10.1371/journal.pgen.1006049;
RA Chern M., Xu Q., Bart R.S., Bai W., Ruan D., Sze-To W.H., Canlas P.E.,
RA Jain R., Chen X., Ronald P.C.;
RT "A genetic screen identifies a requirement for cysteine-rich-receptor-like
RT kinases in rice NH1 (OsNPR1)-mediated immunity.";
RL PLoS Genet. 12:E1006049-E1006049(2016).
CC -!- FUNCTION: Involved in disease resistance. Required for NPR1/NH1-
CC mediated immunity to the bacterial blight pathogen Xanthomomas oryzae
CC pv. oryzae (Xoo). Required for the benzothiadiazole (BTH)-induced
CC immune response. Probably regulated by the transcription factor TGA2.1.
CC {ECO:0000269|PubMed:16100779}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: By benzothiadiazole (BTH). {ECO:0000269|PubMed:27176732}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CRK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65055.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD30127.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAZ40163.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP003736; BAD30127.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP005786; BAC65055.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP008213; BAF21811.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT01969.1; -; Genomic_DNA.
DR EMBL; CM000144; EAZ40163.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_015645020.1; XM_015789534.1.
DR AlphaFoldDB; Q0D5R2; -.
DR SMR; Q0D5R2; -.
DR STRING; 4530.OS07T0541500-01; -.
DR PaxDb; Q0D5R2; -.
DR PRIDE; Q0D5R2; -.
DR EnsemblPlants; Os07t0541500-01; Os07t0541500-01; Os07g0541500.
DR GeneID; 4343501; -.
DR Gramene; Os07t0541500-01; Os07t0541500-01; Os07g0541500.
DR KEGG; osa:4343501; -.
DR eggNOG; ENOG502QWDY; Eukaryota.
DR HOGENOM; CLU_000288_35_7_1; -.
DR InParanoid; Q0D5R2; -.
DR OMA; YHANIQY; -.
DR OrthoDB; 684563at2759; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR Gene3D; 3.30.430.20; -; 2.
DR InterPro; IPR002902; GNK2.
DR InterPro; IPR038408; GNK2_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 Pfam; PF00069; Pkinase; 1.
DR Pfam; PF01657; Stress-antifung; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51473; GNK2; 2.
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; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Plant defense; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..645
FT /note="Cysteine-rich receptor-like protein kinase 10"
FT /evidence="ECO:0000255"
FT /id="PRO_5007318542"
FT TOPO_DOM 28..283
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..645
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 28..132
FT /note="Gnk2-homologous 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 140..251
FT /note="Gnk2-homologous 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 348..619
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 473
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 354..362
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 86..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 98..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 204..213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 216..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT CONFLICT 352
FT /note="K -> Q (in Ref. 4; EAZ40163)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 645 AA; 70478 MW; FAABFC4AE6C45022 CRC64;
MSMACYYLAA AAAGLALLLL HAPLTDAQTL VPLCGDSGNY TEHGTYHANI QYLATSLPSY
ASSSPSLFAS GSSGTVPDAI YALALCRGDT NSSSCATCVA AAIQSAQELC PLVKTVIVYD
DTCILRFAND AFPISPTSNS QGMVVAWKAQ NVSAAVAPAF EAAVVRLINT TADYAATDSV
RRFGTGEEAF DETTFPKIYS LAQCTPDMAA TACRSCLEDI VGRMVSGNLI GRMGGRVLGV
RCNLWFEVYP FFSGRSLLQL PGPSPSPAPP VTAAGERSKN KRSAILAISM PTIALVLATI
AAWFCSTSWR RRRLARKTLR PKSSEDEMQS FASLVLDLQT LRTATDNFSE HKRLGEGGFG
VVYKGDLPEG QEIAVKRLAQ TSRQGIEELK TELLLVAKLN HNNLVRLIGV CLEENEKILA
YEYMPNRSLD TILFDAERIK ELDWGQRFKI INGIARGLQY LHEDSQLKIV HRDLKASNVL
LDSAYNPKIS DFGLAKIFER DQSQVITHRI AGTYGYMSPE YAMRGQYSMK LDVYSFGVLV
LEIITGRRNF GSYGSDHVVD LIYVTWEHWT SDKAIELIDP SLGNHYPVDK VLKCIHIGLL
CVQPKPADRP LMSAVNAMLS STGTVRLPCL SRPSFWVQEI GATAS