SAPK2_ORYSJ
ID SAPK2_ORYSJ Reviewed; 339 AA.
AC Q0D4J7; B7EIN4; Q84TC6; Q8LH98;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Serine/threonine-protein kinase SAPK2;
DE EC=2.7.11.1;
DE AltName: Full=Osmotic stress/abscisic acid-activated protein kinase 2;
DE AltName: Full=stress-activated protein kinase 2 {ECO:0000303|Ref.2};
DE Short=OsSAPK2 {ECO:0000303|Ref.2};
GN Name=SAPK2; OrderedLocusNames=Os07g0622000, LOC_Os07g42940;
GN ORFNames=OsJ_25167 {ECO:0000312|EMBL:EEE67612.1}, P0594D10.134;
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], ACTIVITY REGULATION, PHOSPHORYLATION, TISSUE
RP SPECIFICITY, INDUCTION, DOMAIN, AND 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].
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=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 [4]
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 [5]
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 [6]
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 [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, INTERACTION WITH ABI5 AND PP2C30, SUBCELLULAR LOCATION, AND
RP INDUCTION BY ABSCISIC ACID.
RX PubMed=22071266; DOI=10.1093/jxb/err338;
RA Kim H., Hwang H., Hong J.W., Lee Y.N., Ahn I.P., Yoon I.S., Yoo S.D.,
RA Lee S., Lee S.C., Kim B.G.;
RT "A rice orthologue of the ABA receptor, OsPYL/RCAR5, is a positive
RT regulator of the ABA signal transduction pathway in seed germination and
RT early seedling growth.";
RL J. Exp. Bot. 63:1013-1024(2012).
RN [9]
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).
RN [10]
RP INTERACTION WITH PP2C51, AND SUBCELLULAR LOCATION.
RX PubMed=28000033; DOI=10.1007/s11103-016-0568-2;
RA Bhatnagar N., Min M.K., Choi E.H., Kim N., Moon S.J., Yoon I., Kwon T.,
RA Jung K.H., Kim B.G.;
RT "The protein phosphatase 2C clade A protein OsPP2C51 positively regulates
RT seed germination by directly inactivating OsbZIP10.";
RL Plant Mol. Biol. 93:389-401(2017).
CC -!- FUNCTION: May play a role in signal transduction of hyperosmotic
CC response (Probable). Can phosphorylate BZIP46 in vitro
CC (PubMed:22301130). Together with ABI5, PP2C30 and PYL5, is part of an
CC abscisic acid (ABA) signaling unit that modulates seed germination and
CC early seedling growth (PubMed:22071266). {ECO:0000269|PubMed:22071266,
CC 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 phosphorylation in response to
CC hyperosmotic stress within 5 minutes. {ECO:0000269|PubMed:15084714}.
CC -!- SUBUNIT: Interacts with BZIP46 (PubMed:22301130). Interacts with ABI5
CC and PP2C30 (PubMed:22071266). Interacts with PP2C51 (PubMed:28000033).
CC {ECO:0000269|PubMed:22071266, ECO:0000269|PubMed:22301130,
CC ECO:0000269|PubMed:28000033}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22071266}. Nucleus
CC {ECO:0000269|PubMed:22071266, ECO:0000269|PubMed:28000033}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf blades, leaf sheaths and roots.
CC Expressed in shoots and roots of young seedlings.
CC {ECO:0000269|PubMed:15084714}.
CC -!- INDUCTION: By hyperosmotic stress in leaf blades and leaf sheaths, but
CC not in roots (PubMed:15084714). Induced by abscisic acid (ABA)
CC (PubMed:22071266). {ECO:0000269|PubMed:15084714,
CC ECO:0000269|PubMed:22071266}.
CC -!- DOMAIN: The C-terminal region is necessary for the kinase activation in
CC response to hyperosmotic stress. {ECO:0000269|PubMed:15084714}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:15084714}.
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; AB125303; BAD17998.1; -; mRNA.
DR EMBL; JF733760; AEF00931.1; -; mRNA.
DR EMBL; AP004380; BAC10192.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF22226.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT02704.1; -; Genomic_DNA.
DR EMBL; CM000144; EEE67612.1; -; Genomic_DNA.
DR EMBL; AK070965; BAG92231.1; -; mRNA.
DR RefSeq; XP_015646374.1; XM_015790888.1.
DR AlphaFoldDB; Q0D4J7; -.
DR SMR; Q0D4J7; -.
DR STRING; 4530.OS07T0622000-01; -.
DR PaxDb; Q0D4J7; -.
DR PRIDE; Q0D4J7; -.
DR EnsemblPlants; Os07t0622000-01; Os07t0622000-01; Os07g0622000.
DR GeneID; 4343944; -.
DR Gramene; Os07t0622000-01; Os07t0622000-01; Os07g0622000.
DR KEGG; osa:4343944; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q0D4J7; -.
DR OMA; FPKSCTA; -.
DR OrthoDB; 888395at2759; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR Genevisible; Q0D4J7; OS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0009845; P:seed germination; IMP:UniProtKB.
DR GO; GO:0090351; P:seedling development; IMP: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; Cytoplasm; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Stress response; Transferase.
FT CHAIN 1..339
FT /note="Serine/threonine-protein kinase SAPK2"
FT /id="PRO_0000086629"
FT DOMAIN 4..260
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 253..339
FT /note="C-terminal"
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 339 AA; 38538 MW; BFD71BAF45CE46BF CRC64;
MERYEVIKDI GSGNFGVAKL VRDVRTKELF AVKFIERGQK IDENVQREIM NHRSLRHPNI
VRFKEVVLTP THLAIVMEYA AGGELFERIC SAGRFSEDEA RFFFQQLISG VSYCHSMQIC
HRDLKLENTL LDGSIAPRLK ICDFGYSKSS LLHSQPKSTV GTPAYIAPEV LARKEYDGKV
ADVWSCGVTL YVMLVGAYPF EDPDEPRNFR KTITRILSVQ YMVPDYVRVS MECRHLLSRI
FVANPEQRIT IPEIKNHPWF LKNLPIEMTD EYQMSVQMND INTPSQGLEE IMAIIQEARK
PGDGSKFSGQ IPGLGSMELD DVDTDDIDVE DSGDFVCAL
