SAPK4_ORYSJ
ID SAPK4_ORYSJ Reviewed; 360 AA.
AC Q5N942; A0A0U1UA40; F6M7C8; Q0JHD4; Q943J9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Serine/threonine-protein kinase SAPK4;
DE EC=2.7.11.1;
DE AltName: Full=Osmotic stress/abscisic acid-activated protein kinase 4;
DE AltName: Full=RK2 kinase {ECO:0000312|EMBL:AFK74500.1};
DE AltName: Full=stress-activated protein kinase 4 {ECO:0000303|Ref.8};
DE Short=OsSAPK4 {ECO:0000303|Ref.8};
GN Name=SAPK4; Synonyms=RK2;
GN OrderedLocusNames=Os01g0869900 {ECO:0000312|EMBL:BAF06844.1},
GN LOC_Os01g64970 {ECO:0000305};
GN ORFNames=OsJ_04228 {ECO:0000312|EMBL:EAZ14302.1}, P0039A07.8-1,
GN P0677H08.40-1;
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 [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].
RA Yoon I.S.;
RT "OSRK2 mRNA.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
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 [MRNA] OF 193-360.
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).
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 -!- 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 and abscisic acid (ABA) in leaf
CC blades. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD81709.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD82014.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB125305; BAD18000.1; -; mRNA.
DR EMBL; JQ001817; AFK74500.1; -; mRNA.
DR EMBL; AP003235; BAB64101.1; -; Genomic_DNA.
DR EMBL; AP003235; BAD81709.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP003286; BAB89813.1; -; Genomic_DNA.
DR EMBL; AP003286; BAD82014.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008207; BAF06844.1; -; Genomic_DNA.
DR EMBL; AP014957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000138; EAZ14302.1; -; Genomic_DNA.
DR EMBL; JF733762; AEF00933.1; -; mRNA.
DR RefSeq; XP_015613364.1; XM_015757878.1.
DR AlphaFoldDB; Q5N942; -.
DR SMR; Q5N942; -.
DR STRING; 4530.OS01T0869900-01; -.
DR PaxDb; Q5N942; -.
DR PRIDE; Q5N942; -.
DR EnsemblPlants; Os01t0869900-01; Os01t0869900-01; Os01g0869900.
DR GeneID; 4324934; -.
DR Gramene; Os01t0869900-01; Os01t0869900-01; Os01g0869900.
DR KEGG; osa:4324934; -.
DR eggNOG; KOG0583; Eukaryota.
DR InParanoid; Q5N942; -.
DR OrthoDB; 816341at2759; -.
DR BRENDA; 2.7.11.1; 4460.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IDA:CACAO.
DR GO; GO:0005634; C:nucleus; IDA:CACAO.
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 2: Evidence at transcript level;
KW Abscisic acid signaling pathway; ATP-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Stress response; Transferase.
FT CHAIN 1..360
FT /note="Serine/threonine-protein kinase SAPK4"
FT /id="PRO_0000086631"
FT DOMAIN 4..260
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 303..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..340
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 360 AA; 41979 MW; BA3BEEAAFD3AAF39 CRC64;
MEKYEAVRDI GSGNFGVARL MRNRETRELV AVKCIERGHR IDENVYREII NHRSLRHPNI
IRFKEVILTP THLMIVMEFA AGGELFDRIC DRGRFSEDEA RYFFQQLICG VSYCHHMQIC
HRDLKLENVL LDGSPAPRLK ICDFGYSKSS VLHSRPKSAV GTPAYIAPEV LSRREYDGKL
ADVWSCGVTL YVMLVGAYPF EDQDDPKNIR KTIQRIMSVQ YKIPDYVHIS AECKQLIARI
FVNNPLRRIT MKEIKSHPWF LKNLPRELTE TAQAMYYRRD NSVPSFSDQT SEEIMKIVQE
ARTMPKSSRT GYWSDAGSDE EEKEEEERPE ENEEEEEDEY DKRVKEVHAS GELRMSSLRI
