SRK2G_ARATH
ID SRK2G_ARATH Reviewed; 353 AA.
AC P43292; Q24JK3; Q9FNM9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Serine/threonine-protein kinase SRK2G;
DE EC=2.7.11.1;
DE AltName: Full=Arabidopsis protein SK1;
DE AltName: Full=OST1-kinase-like 8;
DE AltName: Full=SNF1-related kinase 2.1;
DE Short=SnRK2.1;
GN Name=SRK2G; Synonyms=ASK2, OSKL8, SNRK2.1; OrderedLocusNames=At5g08590;
GN ORFNames=MAH20.15;
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 [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=8393717; DOI=10.1007/bf00047402;
RA Park Y.S., Hong S.W., Oh S.A., Kwak J.M., Lee H.H., Nam H.G.;
RT "Two putative protein kinases from Arabidopsis thaliana contain highly
RT acidic domains.";
RL Plant Mol. Biol. 22:615-624(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 148-174, AND SUBCELLULAR LOCATION.
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
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 GENE FAMILY, AND INDUCTION.
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).
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 -!- INTERACTION:
CC P43292; Q9C9W9: ADO3; NbExp=3; IntAct=EBI-401174, EBI-401228;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18433157}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings.
CC {ECO:0000269|PubMed:15292193}.
CC -!- INDUCTION: By abscisic acid (ABA), salt, and osmotic stress.
CC {ECO:0000269|PubMed:15292193, ECO:0000269|PubMed:16365038}.
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; Z12120; CAA78106.1; -; mRNA.
DR EMBL; AB006697; BAB10008.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91326.1; -; Genomic_DNA.
DR EMBL; BT024886; ABD85157.1; -; mRNA.
DR PIR; S24586; S24586.
DR RefSeq; NP_196476.1; NM_120946.5.
DR AlphaFoldDB; P43292; -.
DR SMR; P43292; -.
DR IntAct; P43292; 3.
DR STRING; 3702.AT5G08590.1; -.
DR iPTMnet; P43292; -.
DR PaxDb; P43292; -.
DR PRIDE; P43292; -.
DR ProteomicsDB; 226730; -.
DR EnsemblPlants; AT5G08590.1; AT5G08590.1; AT5G08590.
DR GeneID; 830760; -.
DR Gramene; AT5G08590.1; AT5G08590.1; AT5G08590.
DR KEGG; ath:AT5G08590; -.
DR Araport; AT5G08590; -.
DR TAIR; locus:2159597; AT5G08590.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; P43292; -.
DR OMA; LMACHEK; -.
DR OrthoDB; 816341at2759; -.
DR PhylomeDB; P43292; -.
DR BRENDA; 2.7.11.1; 399.
DR PRO; PR:P43292; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P43292; baseline and differential.
DR Genevisible; P43292; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IDA:TAIR.
DR GO; GO:0004672; F:protein kinase activity; TAS:TAIR.
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; IDA:TAIR.
DR GO; GO:0009651; P:response to salt stress; IDA: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; Direct protein sequencing; Kinase; Nucleotide-binding;
KW Nucleus; Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..353
FT /note="Serine/threonine-protein kinase SRK2G"
FT /id="PRO_0000085637"
FT DOMAIN 4..260
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 299..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..337
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 CONFLICT 55
FT /note="L -> F (in Ref. 1; CAA78106)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="S -> A (in Ref. 1; CAA78106)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 40198 MW; 7176CE43659FCCA4 CRC64;
MDKYDVVKDL GAGNFGVARL LRHKDTKELV AMKYIERGRK IDENVAREII NHRSLKHPNI
IRFKEVILTP THLAIVMEYA SGGELFDRIC TAGRFSEAEA RYFFQQLICG VDYCHSLQIC
HRDLKLENTL LDGSPAPLLK ICDFGYSKSS ILHSRPKSTV GTPAYIAPEV LSRREYDGKH
ADVWSCGVTL YVMLVGAYPF EDPNDPKNFR KTIQRIMAVQ YKIPDYVHIS QECKHLLSRI
FVTNSAKRIT LKEIKNHPWY LKNLPKELLE SAQAAYYKRD TSFSLQSVED IMKIVGEARN
PAPSTSAVKS SGSGADEEEE EDVEAEVEEE EDDEDEYEKH VKEAQSCQES DKA
