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 27-MAR-2024, entry version 78.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; QSTNHYY; -.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14662; STKc_SnRK2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR24343; SERINE/THREONINE KINASE; 1.
DR PANTHER; PTHR24343:SF403; SERINE_THREONINE-PROTEIN KINASE SAPK3; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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
//
