SRK2C_ARATH
ID SRK2C_ARATH Reviewed; 343 AA.
AC Q9M9E9; Q8L8P8;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Serine/threonine-protein kinase SRK2C;
DE EC=2.7.11.1;
DE AltName: Full=OST1-kinase-like 4;
DE AltName: Full=SNF1-related kinase 2.8;
DE Short=SnRK2.8;
GN Name=SRK2C; Synonyms=OSKL4, SNRK2.8; OrderedLocusNames=At1g78290;
GN ORFNames=F3F9.17;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12805596; DOI=10.1104/pp.102.011999;
RA Hrabak E.M., Chan C.W.M., Gribskov M., Harper J.F., Choi J.H., Halford N.,
RA Kudla J., Luan S., Nimmo H.G., Sussman M.R., Thomas M., Walker-Simmons K.,
RA Zhu J.-K., Harmon A.C.;
RT "The Arabidopsis CDPK-SnRK superfamily of protein kinases.";
RL Plant Physiol. 132:666-680(2003).
RN [7]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15292193; DOI=10.1074/jbc.m405259200;
RA Boudsocq M., Barbier-Brygoo H., Lauriere C.;
RT "Identification of nine sucrose nonfermenting 1-related protein kinases 2
RT activated by hyperosmotic and saline stresses in Arabidopsis thaliana.";
RL J. Biol. Chem. 279:41758-41766(2004).
RN [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=15561775; DOI=10.1073/pnas.0407758101;
RA Umezawa T., Yoshida R., Maruyama K., Yamaguchi-Shinozaki K., Shinozaki K.;
RT "SRK2C, a SNF1-related protein kinase 2, improves drought tolerance by
RT controlling stress-responsive gene expression in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:17306-17311(2004).
RN [9]
RP GENE FAMILY.
RX PubMed=16365038; DOI=10.1074/jbc.m509820200;
RA Yoshida R., Umezawa T., Mizoguchi T., Takahashi S., Takahashi F.,
RA Shinozaki K.;
RT "The regulatory domain of SRK2E/OST1/SnRK2.6 interacts with ABI1 and
RT integrates abscisic acid (ABA) and osmotic stress signals controlling
RT stomatal closure in Arabidopsis.";
RL J. Biol. Chem. 281:5310-5318(2006).
RN [10]
RP INTERACTION WITH I-2 AND TOPP1.
RX PubMed=26943172; DOI=10.1371/journal.pgen.1005835;
RA Hou Y.J., Zhu Y., Wang P., Zhao Y., Xie S., Batelli G., Wang B., Duan C.G.,
RA Wang X., Xing L., Lei M., Yan J., Zhu X., Zhu J.K.;
RT "Type one protein phosphatase 1 and its regulatory protein inhibitor 2
RT negatively regulate ABA signaling.";
RL PLoS Genet. 12:E1005835-E1005835(2016).
CC -!- FUNCTION: Involved in gene regulation and confers tolerance to drought
CC and osmotic stress. {ECO:0000269|PubMed:15561775}.
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 -!- SUBUNIT: Interacts with I-2 and TOPP1. {ECO:0000269|PubMed:26943172}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings.
CC {ECO:0000269|PubMed:15292193}.
CC -!- INDUCTION: By abscisic acid (ABA), cold, H(2)O(2), salt, and osmotic
CC stress (at protein level). {ECO:0000269|PubMed:15292193,
CC ECO:0000269|PubMed:15561775}.
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; AC013430; AAF71802.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36091.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36092.1; -; Genomic_DNA.
DR EMBL; AF411782; AAL06472.1; -; mRNA.
DR EMBL; BT020608; AAW80881.1; -; mRNA.
DR EMBL; AY088883; AAM67189.1; -; mRNA.
DR RefSeq; NP_001077839.1; NM_001084370.2.
DR RefSeq; NP_974170.1; NM_202441.3.
DR AlphaFoldDB; Q9M9E9; -.
DR SMR; Q9M9E9; -.
DR BioGRID; 29383; 2.
DR DIP; DIP-48987N; -.
DR IntAct; Q9M9E9; 3.
DR STRING; 3702.AT1G78290.2; -.
DR iPTMnet; Q9M9E9; -.
DR PaxDb; Q9M9E9; -.
DR PRIDE; Q9M9E9; -.
DR ProteomicsDB; 226872; -.
DR EnsemblPlants; AT1G78290.2; AT1G78290.2; AT1G78290.
DR EnsemblPlants; AT1G78290.3; AT1G78290.3; AT1G78290.
DR GeneID; 844164; -.
DR Gramene; AT1G78290.2; AT1G78290.2; AT1G78290.
DR Gramene; AT1G78290.3; AT1G78290.3; AT1G78290.
DR KEGG; ath:AT1G78290; -.
DR Araport; AT1G78290; -.
DR TAIR; locus:2032075; AT1G78290.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q9M9E9; -.
DR OMA; FPKSCTA; -.
DR OrthoDB; 888395at2759; -.
DR PhylomeDB; Q9M9E9; -.
DR PRO; PR:Q9M9E9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M9E9; baseline and differential.
DR Genevisible; Q9M9E9; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0006970; P:response to osmotic stress; IGI:TAIR.
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 ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..343
FT /note="Serine/threonine-protein kinase SRK2C"
FT /id="PRO_0000345158"
FT DOMAIN 4..260
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 123
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 158
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
FT CONFLICT 232
FT /note="E -> K (in Ref. 5; AAM67189)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 343 AA; 38250 MW; 4557AAC98EAD02AB CRC64;
MERYEIVKDI GSGNFGVAKL VRDKFSKELF AVKFIERGQK IDEHVQREIM NHRSLIHPNI
IRFKEVLLTA THLALVMEYA AGGELFGRIC SAGRFSEDEA RFFFQQLISG VNYCHSLQIC
HRDLKLENTL LDGSEAPRVK ICDFGYSKSG VLHSQPKTTV GTPAYIAPEV LSTKEYDGKI
ADVWSCGVTL YVMLVGAYPF EDPSDPKDFR KTIGRILKAQ YAIPDYVRVS DECRHLLSRI
FVANPEKRIT IEEIKNHSWF LKNLPVEMYE GSLMMNGPST QTVEEIVWII EEARKPITVA
TGLAGAGGSG GSSNGAIGSS SMDLDDLDTD FDDIDTADLL SPL
