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RK176_ORYSJ
ID   RK176_ORYSJ             Reviewed;         395 AA.
AC   Q65XV8; Q94HI7;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Receptor-like cytoplasmic kinase 176 {ECO:0000303|PubMed:19825577};
DE            Short=OsRLCK176 {ECO:0000303|PubMed:19825577};
DE            EC=2.7.11.1 {ECO:0000305};
GN   Name=RLCK176 {ECO:0000303|PubMed:19825577};
GN   OrderedLocusNames=Os05g0110900 {ECO:0000312|EMBL:BAF16358.1},
GN   LOC_Os05g02020 {ECO:0000305};
GN   ORFNames=OsJ_16858 {ECO:0000312|EMBL:EEE62074.1},
GN   P0016H04.10 {ECO:0000312|EMBL:AAU44204.1};
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=16261349; DOI=10.1007/s00438-005-0039-y;
RA   Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA   Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA   Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT   "A fine physical map of the rice chromosome 5.";
RL   Mol. Genet. Genomics 274:337-345(2005).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
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   [8]
RP   FUNCTION, AND INTERACTION WITH CERK1.
RX   PubMed=25335639; DOI=10.1111/tpj.12710;
RA   Ao Y., Li Z., Feng D., Xiong F., Liu J., Li J.F., Wang M., Wang J., Liu B.,
RA   Wang H.B.;
RT   "OsCERK1 and OsRLCK176 play important roles in peptidoglycan and chitin
RT   signaling in rice innate immunity.";
RL   Plant J. 80:1072-1084(2014).
CC   -!- FUNCTION: Functions downstream of CERK1 in the microbial peptidoglycans
CC       (PGNs) and fungal chitin signaling pathways that mediate innate
CC       immunity. Participates in the activation of defense genes during
CC       response to PGN and chitin. {ECO:0000269|PubMed:25335639}.
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   -!- SUBUNIT: Interacts with CERK1. {ECO:0000269|PubMed:25335639}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AC079022; AAK73157.1; -; Genomic_DNA.
DR   EMBL; AC079356; AAU44204.1; -; Genomic_DNA.
DR   EMBL; AP008211; BAF16358.1; -; Genomic_DNA.
DR   EMBL; AP014961; BAS91920.1; -; Genomic_DNA.
DR   EMBL; CM000142; EEE62074.1; -; Genomic_DNA.
DR   EMBL; AK073169; BAG93323.1; -; mRNA.
DR   RefSeq; XP_015638719.1; XM_015783233.1.
DR   AlphaFoldDB; Q65XV8; -.
DR   SMR; Q65XV8; -.
DR   STRING; 4530.OS05T0110900-01; -.
DR   PaxDb; Q65XV8; -.
DR   PRIDE; Q65XV8; -.
DR   EnsemblPlants; Os05t0110900-01; Os05t0110900-01; Os05g0110900.
DR   GeneID; 4337593; -.
DR   Gramene; Os05t0110900-01; Os05t0110900-01; Os05g0110900.
DR   KEGG; osa:4337593; -.
DR   eggNOG; KOG1187; Eukaryota.
DR   HOGENOM; CLU_000288_21_4_1; -.
DR   InParanoid; Q65XV8; -.
DR   OMA; AIWARTF; -.
DR   OrthoDB; 684563at2759; -.
DR   PlantReactome; R-OSA-9611432; Recognition of fungal and bacterial pathogens and immunity response.
DR   Proteomes; UP000000763; Chromosome 5.
DR   Proteomes; UP000007752; Chromosome 5.
DR   Proteomes; UP000059680; Chromosome 5.
DR   GO; GO:0005524; F:ATP 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:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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   SUPFAM; SSF56112; SSF56112; 1.
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; Immunity; Innate immunity; Kinase; Nucleotide-binding;
KW   Plant defense; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..395
FT                   /note="Receptor-like cytoplasmic kinase 176"
FT                   /id="PRO_0000440894"
FT   DOMAIN          70..355
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          359..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..386
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        205
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         76..84
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         108
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   395 AA;  43242 MW;  9892C5237B2A9F66 CRC64;
     MGNCWGAKIS SESPCRSASS PSGGTSKYAS NSSVSAASVP PTPRSEDEIL EAANVKAFAF
     NELRTATRNF RPDSVLGEGG FGSVFKGWID EKTLAPTKPG TGMVIAVKKL NQEGHQGHRE
     WLAEVNYLGQ LSHPYLVRLV GYCVEDEQRL LVYEFMPRGS LENHLFRRST HFQPLSWNLR
     MKIALGAAKG LAFLHSDKVK VIYRDFKTSN VLLDANYDAK LSDFGLAKDG PTGDKSHVST
     RVMGTYGYAA PEYLATGHLT TKSDVYSFGV VLLEMLSGRR ALDKNRPTGE HNLVEWARPY
     LMSKRRIFRI LDARLGGQYS LAKAQKAATL ALQCISVEAK NRPNMEQVVA VLEQLQDSKE
     TGANPQLQKK SSSKNAGSNG SKPSSKGKPA NARLV
 
 
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