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Serine/threonine-protein kinase SRK2A (EC 2.7.11.1) (Arabidopsis protein SK1) (OST1-kinase-like 7) (SNF1-related kinase 2.4) (SnRK2.4)

 SRK2A_ARATH             Reviewed;         363 AA.
P43291;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
05-DEC-2018, entry version 158.
RecName: Full=Serine/threonine-protein kinase SRK2A;
EC=2.7.11.1;
AltName: Full=Arabidopsis protein SK1;
AltName: Full=OST1-kinase-like 7;
AltName: Full=SNF1-related kinase 2.4;
Short=SnRK2.4;
Name=SRK2A; Synonyms=ASK1, OSKL7, SNRK2.4;
OrderedLocusNames=At1g10940; ORFNames=T19D16.14;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia; TISSUE=Leaf;
PubMed=8393717; DOI=10.1007/BF00047402;
Park Y.S., Hong S.W., Oh S.A., Kwak J.M., Lee H.H., Nam H.G.;
"Two putative protein kinases from Arabidopsis thaliana contain highly
acidic domains.";
Plant Mol. Biol. 22:615-624(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
GENE FAMILY, AND NOMENCLATURE.
PubMed=12805596; DOI=10.1104/pp.102.011999;
Hrabak E.M., Chan C.W.M., Gribskov M., Harper J.F., Choi J.H.,
Halford N., Kudla J., Luan S., Nimmo H.G., Sussman M.R., Thomas M.,
Walker-Simmons K., Zhu J.-K., Harmon A.C.;
"The Arabidopsis CDPK-SnRK superfamily of protein kinases.";
Plant Physiol. 132:666-680(2003).
[7]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=15292193; DOI=10.1074/jbc.M405259200;
Boudsocq M., Barbier-Brygoo H., Lauriere C.;
"Identification of nine sucrose nonfermenting 1-related protein
kinases 2 activated by hyperosmotic and saline stresses in Arabidopsis
thaliana.";
J. Biol. Chem. 279:41758-41766(2004).
[8]
GENE FAMILY.
PubMed=16365038; DOI=10.1074/jbc.M509820200;
Yoshida R., Umezawa T., Mizoguchi T., Takahashi S., Takahashi F.,
Shinozaki K.;
"The regulatory domain of SRK2E/OST1/SnRK2.6 interacts with ABI1 and
integrates abscisic acid (ABA) and osmotic stress signals controlling
stomatal closure in Arabidopsis.";
J. Biol. Chem. 281:5310-5318(2006).
[9]
INTERACTION WITH TOPP1.
PubMed=26943172; DOI=10.1371/journal.pgen.1005835;
Hou Y.J., Zhu Y., Wang P., Zhao Y., Xie S., Batelli G., Wang B.,
Duan C.G., Wang X., Xing L., Lei M., Yan J., Zhu X., Zhu J.K.;
"Type one protein phosphatase 1 and its regulatory protein inhibitor 2
negatively regulate ABA signaling.";
PLoS Genet. 12:E1005835-E1005835(2016).
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
EC=2.7.11.1;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.1;
-!- SUBUNIT: Interacts with TOPP1. {ECO:0000269|PubMed:26943172}.
-!- INTERACTION:
Q9SKK0:EBF1; NbExp=2; IntAct=EBI-401164, EBI-401198;
Q708Y0:EBF2; NbExp=2; IntAct=EBI-401164, EBI-593623;
Q39090:UFO; NbExp=3; IntAct=EBI-401164, EBI-590758;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=P43291-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Expressed in seedlings.
{ECO:0000269|PubMed:15292193}.
-!- INDUCTION: By abscisic acid (ABA), salt, and osmotic stress (at
protein level). {ECO:0000269|PubMed:15292193}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M91548; AAA02840.1; -; mRNA.
EMBL; U95973; AAB65483.1; -; Genomic_DNA.
EMBL; CP002684; AEE28666.1; -; Genomic_DNA.
EMBL; AY093130; AAM13129.1; -; mRNA.
EMBL; BT008850; AAP68289.1; -; mRNA.
EMBL; AY084221; AAM60822.1; -; mRNA.
PIR; S36944; S36944.
RefSeq; NP_172563.1; NM_100969.4. [P43291-1]
UniGene; At.23750; -.
ProteinModelPortal; P43291; -.
SMR; P43291; -.
BioGrid; 22877; 7.
DIP; DIP-31342N; -.
IntAct; P43291; 14.
STRING; 3702.AT1G10940.2; -.
iPTMnet; P43291; -.
PaxDb; P43291; -.
PRIDE; P43291; -.
EnsemblPlants; AT1G10940.1; AT1G10940.1; AT1G10940. [P43291-1]
GeneID; 837637; -.
Gramene; AT1G10940.1; AT1G10940.1; AT1G10940. [P43291-1]
KEGG; ath:AT1G10940; -.
Araport; AT1G10940; -.
eggNOG; KOG0583; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000233016; -.
InParanoid; P43291; -.
KO; K14498; -.
PhylomeDB; P43291; -.
BRENDA; 2.7.11.1; 399.
Reactome; R-ATH-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-ATH-8953750; Transcriptional Regulation by E2F6.
PRO; PR:P43291; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; P43291; baseline and differential.
Genevisible; P43291; AT.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Kinase;
Nucleotide-binding; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 363 Serine/threonine-protein kinase SRK2A.
/FTId=PRO_0000085636.
DOMAIN 4 260 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 10 18 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 319 348 Asp/Glu-rich (acidic).
ACT_SITE 123 123 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 33 33 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SEQUENCE 363 AA; 41169 MW; 89C31C87AB6C6E78 CRC64;
MDKYELVKDI GAGNFGVARL MKVKNSKELV AMKYIERGPK IDENVAREII NHRSLRHPNI
IRFKEVVLTP THLAIAMEYA AGGELFERIC SAGRFSEDEA RYFFQQLISG VSYCHAMQIC
HRDLKLENTL LDGSPAPRLK ICDFGYSKSS LLHSRPKSTV GTPAYIAPEV LSRREYDGKM
ADVWSCGVTL YVMLVGAYPF EDQEDPKNFR KTIQKIMAVQ YKIPDYVHIS QDCKNLLSRI
FVANSLKRIT IAEIKKHSWF LKNLPRELTE TAQAAYFKKE NPTFSLQTVE EIMKIVADAK
TPPPVSRSIG GFGWGGNGDA DGKEEDAEDV EEEEEEVEEE EDDEDEYDKT VKEVHASGEV
RIS


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