SAPK6_ORYSJ
ID SAPK6_ORYSJ Reviewed; 365 AA.
AC Q6ZI44; Q0E0H5;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Serine/threonine-protein kinase SAPK6;
DE EC=2.7.11.1;
DE AltName: Full=Osmotic stress/abscisic acid-activated protein kinase 6;
DE AltName: Full=stress-activated protein kinase 6 {ECO:0000303|Ref.3};
DE Short=OsSAPK6 {ECO:0000303|Ref.3};
GN Name=SAPK6 {ECO:0000303|Ref.3}; Synonyms=RK1 {ECO:0000303|PubMed:16977424};
GN OrderedLocusNames=Os02g0551100, LOC_Os02g34600;
GN ORFNames=OJ1004_H01.2, OsJ_07099 {ECO:0000312|EMBL:EEE57169.1},
GN P0451A10.35;
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 [MRNA], TISSUE SPECIFICITY, INDUCTION, AND
RP NOMENCLATURE.
RC STRAIN=cv. Nipponbare;
RX PubMed=15084714; DOI=10.1105/tpc.019943;
RA Kobayashi Y., Yamamoto S., Minami H., Kagaya Y., Hattori T.;
RT "Differential activation of the rice sucrose nonfermenting1-related protein
RT kinase2 family by hyperosmotic stress and abscisic acid.";
RL Plant Cell 16:1163-1177(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Ilpoombyeo;
RX PubMed=16977424; DOI=10.1007/s11103-006-9079-x;
RA Chae M.J., Lee J.S., Nam M.H., Cho K., Hong J.Y., Yi S.A., Suh S.C.,
RA Yoon I.S.;
RT "A rice dehydration-inducible SNF1-related protein kinase 2 phosphorylates
RT an abscisic acid responsive element-binding factor and associates with ABA
RT signaling.";
RL Plant Mol. Biol. 63:151-169(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX DOI=10.1007/s11105-013-0559-2;
RA Xu M.-R., Huang L.-Y., Zhang F., Zhu L.-H., Zhou Y.-L., Li Z.-K.;
RT "Genome-wide phylogenetic analysis of stress-activated protein kinase genes
RT in rice (OsSAPKs) and expression profiling in response to Xanthomonas
RT oryzae pv. oryzicola infection.";
RL Plant Mol. Biol. Rep. 31:877-885(2013).
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP FUNCTION.
RX PubMed=21055780; DOI=10.1016/j.phytochem.2010.10.005;
RA Hong J.Y., Chae M.J., Lee I.S., Lee Y.N., Nam M.H., Kim D.Y., Byun M.O.,
RA Yoon I.S.;
RT "Phosphorylation-mediated regulation of a rice ABA responsive element
RT binding factor.";
RL Phytochemistry 72:27-36(2011).
RN [10]
RP FUNCTION, AND INTERACTION WITH BZIP46.
RX PubMed=22301130; DOI=10.1104/pp.111.190389;
RA Tang N., Zhang H., Li X., Xiao J., Xiong L.;
RT "Constitutive activation of transcription factor OsbZIP46 improves drought
RT tolerance in rice.";
RL Plant Physiol. 158:1755-1768(2012).
CC -!- FUNCTION: May play a role in signal transduction of hyperosmotic
CC response (Probable). Can phosphorylate ABI5 in vitro (PubMed:21055780).
CC Can phosphorylate BZIP46 in vitro (PubMed:22301130).
CC {ECO:0000269|PubMed:21055780, ECO:0000269|PubMed:22301130,
CC ECO:0000305}.
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 -!- 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;
CC -!- ACTIVITY REGULATION: Activated by hyperosmotic stress.
CC -!- SUBUNIT: Interacts with BZIP46. {ECO:0000269|PubMed:22301130}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf blades and leaf sheaths.
CC Expressed in shoots and roots of young seedlings.
CC {ECO:0000269|PubMed:15084714}.
CC -!- INDUCTION: Weakly induced by hyperosmotic stress in leaf blades, leaf
CC sheaths and roots. Weakly induced by abscisic acid (ABA) in leaf blades
CC and roots. {ECO:0000269|PubMed:15084714}.
CC -!- PTM: May be phosphorylated. {ECO:0000250}.
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; AB125307; BAD18002.1; -; mRNA.
DR EMBL; DQ285022; ABB89146.1; -; mRNA.
DR EMBL; JF733764; AEF00935.1; -; mRNA.
DR EMBL; AP004038; BAD15474.1; -; Genomic_DNA.
DR EMBL; AP004775; BAD33270.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09013.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS79168.1; -; Genomic_DNA.
DR EMBL; CM000139; EEE57169.1; -; Genomic_DNA.
DR EMBL; AK067395; BAG90400.1; -; mRNA.
DR RefSeq; XP_015626727.1; XM_015771241.1.
DR AlphaFoldDB; Q6ZI44; -.
DR SMR; Q6ZI44; -.
DR STRING; 4530.OS02T0551100-01; -.
DR PaxDb; Q6ZI44; -.
DR PRIDE; Q6ZI44; -.
DR EnsemblPlants; Os02t0551100-01; Os02t0551100-01; Os02g0551100.
DR GeneID; 4329630; -.
DR Gramene; Os02t0551100-01; Os02t0551100-01; Os02g0551100.
DR KEGG; osa:4329630; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q6ZI44; -.
DR OMA; FCARGEL; -.
DR OrthoDB; 816341at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6ZI44; OS.
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; IDA:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
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 SMART; SM00220; S_TKc; 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 Abscisic acid signaling pathway; ATP-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..365
FT /note="Serine/threonine-protein kinase SAPK6"
FT /id="PRO_0000086633"
FT DOMAIN 4..260
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 298..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..346
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 123
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 365 AA; 41803 MW; 802F7B0DA65A04BD CRC64;
MEKYELLKDI GSGNFGVARL MRNRETKELV AMKYIPRGLK IDENVAREII NHRSLRHPNI
IRFKEVVLTP THLAIVMEYA AGGELFDRIC SAGRFSEDES RYFFQQLICG VSYCHFMQIC
HRDLKLENTL LDGSPAPRLK ICDFGYSKSS LLHSKPKSTV GTPAYIAPEV LSRREYDGKM
ADVWSCGVTL YVMLVGAYPF EDPDDPKNFR KTIGRIVSIQ YKIPEYVHIS QDCRQLLSRI
FVANPAKRIT IREIRNHPWF MKNLPRELTE AAQAKYYKKD NSARTFSDQT VDEIMKIVQE
AKTPPPSSTP VAGFGWTEEE EQEDGKNPDD DEGDRDEEEG EEGDSEDEYT KQVKQAHASC
DLQKS
