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SAPK3_ORYSI
ID   SAPK3_ORYSI             Reviewed;         334 AA.
AC   A2ZAB5; B8BIA0; O04062; O24189; Q0IVL6; Q75V63; Q7XC29; Q9AY41;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   03-AUG-2022, entry version 73.
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;
GN   Name=SAPK3; Synonyms=REK; ORFNames=OsI_34678 {ECO:0000312|EMBL:EEC67453.1};
OS   Oryza sativa subsp. indica (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=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND
RP   AUTOPHOSPHORYLATION.
RC   STRAIN=cv. IR36; 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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
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   [3]
RP   NOMENCLATURE.
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).
CC   -!- FUNCTION: May play a role in signal transduction of hyperosmotic
CC       response. {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0C5D6}. Nucleus
CC       {ECO:0000250|UniProtKB:P0C5D6}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves and maturing seeds, but not in
CC       roots and stems of field-grown plants. {ECO:0000269|PubMed:9630507}.
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}.
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DR   EMBL; AB002109; BAA19573.1; -; Genomic_DNA.
DR   EMBL; CM000135; EEC67453.1; -; Genomic_DNA.
DR   PIR; T03403; T03403.
DR   AlphaFoldDB; A2ZAB5; -.
DR   SMR; A2ZAB5; -.
DR   STRING; 39946.A2ZAB5; -.
DR   EnsemblPlants; BGIOSGA031386-TA; BGIOSGA031386-PA; BGIOSGA031386.
DR   Gramene; BGIOSGA031386-TA; BGIOSGA031386-PA; BGIOSGA031386.
DR   HOGENOM; CLU_000288_63_0_1; -.
DR   OMA; DYIIRHE; -.
DR   Proteomes; UP000007015; Chromosome 10.
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; IEA:UniProtKB-KW.
DR   GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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_0000301653"
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        100
FT                   /note="E -> D (in Ref. 1; BAA19573)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        299
FT                   /note="A -> G (in Ref. 1; BAA19573)"
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
 
 
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