CRK6_ORYSJ
ID CRK6_ORYSJ Reviewed; 695 AA.
AC Q0D5R3; Q84S61;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Cysteine-rich receptor-like protein kinase 6 {ECO:0000305};
DE Short=Cysteine-rich RLK6 {ECO:0000305};
DE EC=2.7.11.- {ECO:0000305};
DE Flags: Precursor;
GN Name=CRK6 {ECO:0000303|PubMed:27176732};
GN OrderedLocusNames=Os07g0541400 {ECO:0000312|EMBL:BAF21810.1},
GN LOC_Os07g35690 {ECO:0000305};
GN ORFNames=OJ1008_E09.114 {ECO:0000312|EMBL:BAD30125.1},
GN P0458H05.131 {ECO:0000312|EMBL:BAC65053.1};
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 FUNCTION, INDUCTION BY BENZOTHIADIAZOLE, AND MUTAGENESIS OF ASP-488.
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. Possesses kinase activity in vitro.
CC {ECO:0000269|PubMed:27176732}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Induced by benzothiadiazole (BTH).
CC {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=BAC65053.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD30125.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP003736; BAD30125.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP005786; BAC65053.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008213; BAF21810.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT01968.1; -; Genomic_DNA.
DR RefSeq; XP_015644888.1; XM_015789402.1.
DR RefSeq; XP_015644889.1; XM_015789403.1.
DR AlphaFoldDB; Q0D5R3; -.
DR SMR; Q0D5R3; -.
DR STRING; 4530.OS07T0541400-01; -.
DR PaxDb; Q0D5R3; -.
DR PRIDE; Q0D5R3; -.
DR EnsemblPlants; Os07t0541400-01; Os07t0541400-01; Os07g0541400.
DR GeneID; 4343500; -.
DR Gramene; Os07t0541400-01; Os07t0541400-01; Os07g0541400.
DR KEGG; osa:4343500; -.
DR eggNOG; ENOG502QWDY; Eukaryota.
DR HOGENOM; CLU_000288_35_7_1; -.
DR InParanoid; Q0D5R3; -.
DR OMA; CAPYPPS; -.
DR OrthoDB; 345452at2759; -.
DR Proteomes; UP000000763; 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:0004672; F:protein kinase activity; IDA:UniProtKB.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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 1: Evidence at protein 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..31
FT /evidence="ECO:0000255"
FT CHAIN 32..695
FT /note="Cysteine-rich receptor-like protein kinase 6"
FT /evidence="ECO:0000255"
FT /id="PRO_5007318556"
FT TOPO_DOM 32..294
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..695
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 38..142
FT /note="Gnk2-homologous 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 151..261
FT /note="Gnk2-homologous 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 363..634
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 658..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 488
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 369..377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 96..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 108..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 215..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 227..252
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT MUTAGEN 488
FT /note="D->N: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:27176732"
SQ SEQUENCE 695 AA; 76461 MW; AB3270ED6076F822 CRC64;
MRRHRPYLDG VAAAAATFLL AVLLHAPLAA GEDEPPPWVL CGPYPPSGNY SKNGTYQVNL
DLLSTTLPKN TSSSPAMYAT GTVGDVPDKV YGLALCRGDA NASACERCVA AALRDAPRRC
PLVKDVLVFY DLCQLRYSNR DFFLDDDYFV TTYTLQRSRR VGAAAAAAFD AAVAVLVNAT
ADYAAADSSR RYGTGEEEGV DGDSDRPKIY ALAQCTPDKT PEVCRTCLST VIGQLPKEFS
GRTGGGMFGV WCNFRYEVFP FFSGRPLLQL PAFVETPPPP PSPSATSGEK TKNRIGTVLA
IVMPAIAAIL LMVVACFCCW KRIKKRRPEE QTFLSYSVSS DDIQSIDSLI LDLPTIRVAT
DDFADTKMIG QGGFGMVYKG VLPDGQEIAV KRLCQSSRQG IGELKSELIL VAKLYHKNLV
RLIGVCLEQQ EKILVYEYMP NGSLDIVLFD TDKNRELDWG KRFKIINGIA RGLQYLHEDS
QLKIVHRDLK ASNILLDFDY SPKISDFGLA KIFGGDQSED VTNRIAGTYG YMAPEYAMRG
NYSIKSDVFS FGVLVLEIIT GRRNTGSYDS GQDVDLLNLV WEHWTRGNVV ELIDPSMGDH
PPIEQMLKCI HIGLLCVQKK PASRPTISSV NIMLSSNTVR LPSLSRPAFC IQEVSASDSS
NPYSERYPRP RHSGYSDNST VVSSNDLSIT ELVPR
