SAPK9_ORYSJ
ID SAPK9_ORYSJ Reviewed; 361 AA.
AC Q75V57; F6M7D3; Q2QMY2;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Serine/threonine-protein kinase SAPK9;
DE EC=2.7.11.1;
DE AltName: Full=Osmotic stress/abscisic acid-activated protein kinase 9;
DE AltName: Full=stress-activated protein kinase 9 {ECO:0000303|Ref.2};
DE Short=OsSAPK9 {ECO:0000303|Ref.2};
GN Name=SAPK9; OrderedLocusNames=Os12g0586100, LOC_Os12g39630;
GN ORFNames=OOSJNBa0017N12.8;
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], INDUCTION BY XANTHOMONAS ORYZAE, AND
RP SUBCELLULAR LOCATION.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
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 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 [8]
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 BZIP46 in vitro
CC (PubMed:22301130). {ECO:0000269|PubMed:22301130, 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 and abscisic acid
CC (ABA).
CC -!- SUBUNIT: Interacts with BZIP46. {ECO:0000269|PubMed:22301130}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|Ref.2}. Nucleus
CC {ECO:0000269|Ref.2}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf sheaths and roots. Expressed in
CC shoots of young seedlings. {ECO:0000269|PubMed:15084714}.
CC -!- INDUCTION: Down-regulated by ABA in roots (PubMed:15084714). Induced
CC during incompatible interaction with the bacterial pathogen Xanthomonas
CC oryzae pv. oryzicola (Ref.2). {ECO:0000269|PubMed:15084714,
CC ECO:0000269|Ref.2}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB125310; BAD18005.1; -; mRNA.
DR EMBL; JF733767; AEF00938.1; -; mRNA.
DR EMBL; DP000011; ABA99733.1; -; Genomic_DNA.
DR EMBL; AP008218; BAF30174.1; -; Genomic_DNA.
DR EMBL; AP014968; BAT17851.1; -; Genomic_DNA.
DR EMBL; AK069697; BAG91556.1; -; mRNA.
DR RefSeq; XP_015619839.1; XM_015764353.1.
DR AlphaFoldDB; Q75V57; -.
DR SMR; Q75V57; -.
DR BioGRID; 821697; 2.
DR STRING; 4530.OS12T0586100-01; -.
DR PaxDb; Q75V57; -.
DR PRIDE; Q75V57; -.
DR EnsemblPlants; Os12t0586100-01; Os12t0586100-01; Os12g0586100.
DR GeneID; 4352660; -.
DR Gramene; Os12t0586100-01; Os12t0586100-01; Os12g0586100.
DR KEGG; osa:4352660; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q75V57; -.
DR OMA; ICLWMEI; -.
DR OrthoDB; 1017936at2759; -.
DR PlantReactome; R-OSA-3899351; Abscisic acid (ABA) mediated signaling.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR Genevisible; Q75V57; OS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
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; Cytoplasm; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..361
FT /note="Serine/threonine-protein kinase SAPK9"
FT /id="PRO_0000086636"
FT DOMAIN 22..278
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 28..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 361 AA; 40628 MW; 86D981639A8DA0E0 CRC64;
MERAAAGPLG MEMPIMHDGD RYELVKEIGS GNFGVARLMR NRASGDLVAV KYIDRGEKID
ENVQREIINH RSLRHPNIIR FKEVILTPTH LAIVMEYASG GELFERICSA GRFSEDEARF
FFQQLISGVS YCHSMQVCHR DLKLENTLLD GSTAPRLKIC DFGYSKSSVL HSQPKSTVGT
PAYIAPEVLL KKEYDGKIAD VWSCGVTLYV MLVGAYPFED PEDPKNFRKT IQKILGVQYS
IPDYVHISPE CRDLITRIFV GNPASRITMP EIKNHPWFMK NIPADLMDDG MVSNQYEEPD
QPMQNMNEIM QILAEATIPA AGTSGINQFL TDSLDLDDDM EDMDSDLDLD IESSGEIVYA
M
