SAPK8_ORYSJ
ID SAPK8_ORYSJ Reviewed; 371 AA.
AC Q7Y0B9; A0A0P0W3F8; F6M7D2; Q10EQ3;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Serine/threonine-protein kinase SAPK8;
DE EC=2.7.11.1;
DE AltName: Full=Osmotic stress/abscisic acid-activated protein kinase 8;
DE AltName: Full=stress-activated protein kinase 8 {ECO:0000303|Ref.6};
DE Short=OsSAPK8 {ECO:0000303|Ref.6};
GN Name=SAPK8;
GN OrderedLocusNames=Os03g0764800 {ECO:0000312|EMBL:BAF13285.1},
GN LOC_Os03g55600 {ECO:0000312|EMBL:ABF99034.1}; ORFNames=OSJNBa0079B15.27;
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, DOMAIN, 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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
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 [MRNA] OF 106-371.
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 [7]
RP FUNCTION, INTERACTION WITH PP2C53, AND SUBCELLULAR LOCATION.
RX PubMed=26491145; DOI=10.1093/pcp/pcv154;
RA Li C., Shen H., Wang T., Wang X.;
RT "ABA regulates subcellular redistribution of OsABI-LIKE2, a negative
RT regulator in ABA signaling, to control root architecture and drought
RT resistance in Oryza sativa.";
RL Plant Cell Physiol. 56:2396-2408(2015).
CC -!- FUNCTION: May play a role in signal transduction of hyperosmotic
CC response (Probable). Together with PYL10, PP2C53 and SAPK10, may form
CC an abscisic acid (ABA) signaling module involved in stress response
CC (PubMed:26491145). {ECO:0000269|PubMed:26491145, 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 PP2C53. {ECO:0000269|PubMed:26491145}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26491145}.
CC Nucleus {ECO:0000269|PubMed:26491145}.
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: Neither induced by hyperosmotic stress nor by ABA.
CC {ECO:0000269|PubMed:15084714}.
CC -!- DOMAIN: The C-terminal region is necessary for the kinase activation in
CC response to ABA treatment. {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=BAS86541.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB125309; BAD18004.1; -; mRNA.
DR EMBL; AC099043; AAP50965.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF99034.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF13285.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS86541.1; ALT_SEQ; Genomic_DNA.
DR EMBL; JF733766; AEF00937.1; -; mRNA.
DR RefSeq; XP_015631207.1; XM_015775721.1.
DR AlphaFoldDB; Q7Y0B9; -.
DR SMR; Q7Y0B9; -.
DR STRING; 4530.OS03T0764800-01; -.
DR PaxDb; Q7Y0B9; -.
DR PRIDE; Q7Y0B9; -.
DR EnsemblPlants; Os03t0764800-01; Os03t0764800-01; Os03g0764800.
DR GeneID; 4334218; -.
DR Gramene; Os03t0764800-01; Os03t0764800-01; Os03g0764800.
DR KEGG; osa:4334218; -.
DR eggNOG; KOG0583; Eukaryota.
DR InParanoid; Q7Y0B9; -.
DR OrthoDB; 1017936at2759; -.
DR PlantReactome; R-OSA-3899351; Abscisic acid (ABA) mediated signaling.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR GO; GO:0005829; C:cytosol; 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; IDA: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 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..371
FT /note="Serine/threonine-protein kinase SAPK8"
FT /id="PRO_0000086635"
FT DOMAIN 33..289
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 282..371
FT /note="C-terminal"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 39..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 371 AA; 41723 MW; 8230B1CA070DDAAB CRC64;
MAAAGAGAGA PDRAALTVGP GMDMPIMHDS DRYELVRDIG SGNFGVARLM RDRRTMELVA
VKYIERGEKI DDNVQREIIN HRSLKHPNII RFKEVILTPT HLAIVMEYAS GGELFERICK
NVRFSEDEAR YFFQQLISGV SYCHSMQVCH RDLKLENTLL DGSPAPRLKI CDFGYSKSSV
LHSQPKSTVG TPAYIAPEVL LKKEYDGKTA DVWSCGVTLY VMVVGAYPFE DPEEPKNFRK
TIQRILNVQY SIPENVDISP ECRHLISRIF VGDPSLRITI PEIRSHGWFL KNLPADLMDD
DSMSSQYEEP DQPMQTMDQI MQILTEATIP PACSRINHIL TDGLDLDDDM DDLDSDSDID
VDSSGEIVYA M
