SAPK7_ORYSJ
ID SAPK7_ORYSJ Reviewed; 359 AA.
AC Q7XQP4; A0A0U1T2M5; Q0JD46; Q7XQP3;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Serine/threonine-protein kinase SAPK7;
DE EC=2.7.11.1;
DE AltName: Full=Osmotic stress/abscisic acid-activated protein kinase 7;
DE AltName: Full=RK4 kinase {ECO:0000312|EMBL:AFK74498.1};
DE AltName: Full=stress-activated protein kinase 7 {ECO:0000303|Ref.2};
DE Short=OsSAPK7 {ECO:0000303|Ref.2};
GN Name=SAPK7; Synonyms=RK4; OrderedLocusNames=Os04g0432000, LOC_Os04g35240;
GN ORFNames=OsJ_14855, OSJNBa0084A10.12;
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 [MRNA].
RA Yoon I.S.;
RT "OSRK4 mRNA.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [5]
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 [6]
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 [7]
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 [8]
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).
CC -!- FUNCTION: May play a role in signal transduction of hyperosmotic
CC response.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|Ref.2}. Nucleus
CC {ECO:0000269|Ref.2}.
CC -!- TISSUE SPECIFICITY: Weakly expressed in roots. Expressed in roots of
CC young seedlings. {ECO:0000269|PubMed:15084714}.
CC -!- INDUCTION: By hyperosmotic stress in roots. Weakly induced by
CC hyperosmotic stress and abscisic acid (ABA) in leaf blades
CC (PubMed:15084714). Accumulates upon incompatible interaction with
CC Xanthomonas 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 -!- SEQUENCE CAUTION:
CC Sequence=CAE03037.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB125308; BAD18003.1; -; mRNA.
DR EMBL; JF733765; AEF00936.1; -; mRNA.
DR EMBL; JN848808; AFK74498.1; -; mRNA.
DR EMBL; AL606458; CAE03037.3; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008210; BAF14741.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS89270.1; -; Genomic_DNA.
DR EMBL; CM000141; EEE61026.1; -; Genomic_DNA.
DR RefSeq; XP_015636932.1; XM_015781446.1.
DR AlphaFoldDB; Q7XQP4; -.
DR SMR; Q7XQP4; -.
DR STRING; 4530.OS04T0432000-02; -.
DR PaxDb; Q7XQP4; -.
DR PRIDE; Q7XQP4; -.
DR EnsemblPlants; Os04t0432000-02; Os04t0432000-02; Os04g0432000.
DR GeneID; 4335877; -.
DR Gramene; Os04t0432000-02; Os04t0432000-02; Os04g0432000.
DR KEGG; osa:4335877; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q7XQP4; -.
DR OMA; EETIFLM; -.
DR OrthoDB; 816341at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR ExpressionAtlas; Q7XQP4; baseline and differential.
DR Genevisible; Q7XQP4; 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; IBA:GO_Central.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEP:UniProtKB.
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 2: Evidence at transcript 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..359
FT /note="Serine/threonine-protein kinase SAPK7"
FT /id="PRO_0000086634"
FT DOMAIN 4..260
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 299..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..342
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 359 AA; 41325 MW; A7DBD41F3425203E CRC64;
MERYELLKDI GAGNFGVARL MRNKETKELV AMKYIPRGLK IDENVAREII NHRSLRHPNI
IRFKEVVVTP THLAIVMEYA AGGELFDRIC NAGRFSEDEA RYFFQQLICG VSYCHFMQIC
HRDLKLENTL LDGSPAPRLK ICDFGYSKSS LLHSKPKSTV GTPAYIAPEV LSRREYDGKT
ADVWSCGVTL YVMLVGAYPF EDPDDPKNFR KTIGRIMSIQ YKIPEYVHVS QDCRQLLSRI
FVANPAKRIT IREIRNHPWF LKNLPRELTE AAQAMYYKKD NSAPTYSVQS VEEIMKIVEE
ARTPPRSSTP VAGFGWQEED EQEDNSKKPE EEQEEEEDAE DEYDKQVKQV HASGEFQLS
