SAPK3_ORYSJ
ID SAPK3_ORYSJ Reviewed; 334 AA.
AC P0C5D6; A0A0P0XXL3; B9G714; F6M7C7; O04062; O24189; Q0IVL6; Q75V63; Q7XC29;
AC Q9AY41;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Serine/threonine-protein kinase SAPK3;
DE EC=2.7.11.1;
DE AltName: Full=Osmotic stress/abscisic acid-activated protein kinase 3;
DE AltName: Full=Protein kinase REK;
DE AltName: Full=stress-activated protein kinase 3 {ECO:0000303|Ref.3};
DE Short=OsSAPK3 {ECO:0000303|Ref.3};
GN Name=SAPK3; Synonyms=REK; OrderedLocusNames=Os10g0564500, LOC_Os10g41490;
GN ORFNames=OsJ_32488 {ECO:0000312|EMBL:EEE51411.1}, OSJNBa0027P10.6;
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, AND AUTOPHOSPHORYLATION.
RC STRAIN=cv. Nipponbare; TISSUE=Endosperm, and Seed;
RX PubMed=9630507; DOI=10.1016/s0378-1119(98)00207-8;
RA Hotta H., Aoki N., Matsuda T., Adachi T.;
RT "Molecular analysis of a novel protein kinase in maturing rice seed.";
RL Gene 213:47-54(1998).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
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 phosphorylation (By similarity).
CC Activated by hyperosmotic stress. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|Ref.3}. Nucleus
CC {ECO:0000269|Ref.3}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf blades, leaf sheaths and roots of
CC plants grown hydroponically. Expressed in shoots and roots of young
CC seedlings. Expressed in leaves and maturing seeds, but not in roots and
CC stems of field-grown plants. {ECO:0000269|PubMed:15084714,
CC ECO:0000269|PubMed:9630507}.
CC -!- INDUCTION: By abscisic acid (ABA) in leaf blades and leaf sheaths
CC (PubMed:15084714). Induced during incompatible interaction with the
CC bacterial pathogen Xanthomonas oryzae pv. oryzicola (Ref.3).
CC {ECO:0000269|PubMed:15084714, ECO:0000269|Ref.3}.
CC -!- PTM: Autophosphorylated in presence of Ca(2+).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF27249.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAT12096.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D88399; BAA13608.1; -; mRNA.
DR EMBL; AB125304; BAD17999.1; -; mRNA.
DR EMBL; JF733761; AEF00932.1; -; mRNA.
DR EMBL; AC084763; AAG60195.1; -; Genomic_DNA.
DR EMBL; DP000086; AAP55046.1; -; Genomic_DNA.
DR EMBL; AP008216; BAF27249.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014966; BAT12096.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000147; EEE51411.1; -; Genomic_DNA.
DR PIR; T03692; T03692.
DR RefSeq; XP_015614267.1; XM_015758781.1.
DR AlphaFoldDB; P0C5D6; -.
DR SMR; P0C5D6; -.
DR STRING; 4530.OS10T0564500-01; -.
DR PaxDb; P0C5D6; -.
DR PRIDE; P0C5D6; -.
DR GeneID; 4349411; -.
DR KEGG; osa:4349411; -.
DR eggNOG; KOG0583; Eukaryota.
DR InParanoid; P0C5D6; -.
DR OrthoDB; 1017936at2759; -.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000007752; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR Genevisible; P0C5D6; OS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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..334
FT /note="Serine/threonine-protein kinase SAPK3"
FT /id="PRO_0000086630"
FT DOMAIN 5..261
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 124
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 11..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 175
FT /note="K -> E (in Ref. 2; BAD17999 and 3; AEF00932)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="P -> L (in Ref. 1; BAA13608)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="A -> G (in Ref. 1; BAA13608)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 37871 MW; 5C63619DE84EEFAC CRC64;
MEERYEALKE LGAGNFGVAR LVRDKRSKEL VAVKYIERGK KIDENVQREI INHRSLRHPN
IIRFKEVCLT PTHLAIVMEY AAGGELFEQI CTAGRFSEDE ARYFFQQLIS GVSYCHSLEI
CHRDLKLENT LLDGSPTPRV KICDFGYSKS ALLHSKPKST VGTPAYIAPE VLSRKEYDGK
VADVWSCGVT LYVMLVGSYP FEDPGDPRNF RKTISRILGV QYSIPDYVRV SSDCRRLLSQ
IFVADPSKRI TIPEIKKHTW FLKNLPKEIS EREKADYKDT DAAPPTQAVE EIMRIIQEAK
VPGDMAAADP ALLAELAELK SDDEEEAADE YDTY
