SRK2H_ARATH
ID SRK2H_ARATH Reviewed; 360 AA.
AC Q9FFP9; Q0WT36; Q8LA99;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Serine/threonine-protein kinase SRK2H;
DE EC=2.7.11.1;
DE AltName: Full=OST1-kinase-like 9;
DE AltName: Full=SNF1-related kinase 2.5;
DE Short=SnRK2.5;
GN Name=SRK2H; Synonyms=OSKL9, SNRK2.5; OrderedLocusNames=At5g63650;
GN ORFNames=MBK5.13;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
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 [7]
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).
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 -!- TISSUE SPECIFICITY: Expressed in seedlings.
CC {ECO:0000269|PubMed:15292193}.
CC -!- INDUCTION: By salt and osmotic stress (at protein level).
CC {ECO:0000269|PubMed:15292193}.
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; AB005234; BAB10458.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97781.1; -; Genomic_DNA.
DR EMBL; AK227726; BAE99712.1; -; mRNA.
DR EMBL; AY087955; AAM65503.1; -; mRNA.
DR RefSeq; NP_201170.1; NM_125760.2.
DR AlphaFoldDB; Q9FFP9; -.
DR SMR; Q9FFP9; -.
DR BioGRID; 21727; 2.
DR STRING; 3702.AT5G63650.1; -.
DR iPTMnet; Q9FFP9; -.
DR PaxDb; Q9FFP9; -.
DR PRIDE; Q9FFP9; -.
DR ProteomicsDB; 226731; -.
DR EnsemblPlants; AT5G63650.1; AT5G63650.1; AT5G63650.
DR GeneID; 836485; -.
DR Gramene; AT5G63650.1; AT5G63650.1; AT5G63650.
DR KEGG; ath:AT5G63650; -.
DR Araport; AT5G63650; -.
DR TAIR; locus:2160559; AT5G63650.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q9FFP9; -.
DR OrthoDB; 816341at2759; -.
DR PhylomeDB; Q9FFP9; -.
DR PRO; PR:Q9FFP9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFP9; baseline and differential.
DR Genevisible; Q9FFP9; AT.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; HDA: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; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..360
FT /note="Serine/threonine-protein kinase SRK2H"
FT /id="PRO_0000345162"
FT DOMAIN 4..260
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 298..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..344
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..360
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 174
FT /note="R -> K (in Ref. 3; BAE99712)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="E -> V (in Ref. 3; BAE99712)"
FT /evidence="ECO:0000305"
FT CONFLICT 340..341
FT /note="Missing (in Ref. 4; AAM65503)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 41554 MW; D4ECB111E954A5A8 CRC64;
MDKYEVVKDL GAGNFGVARL LRHKETKELV AMKYIERGRK IDENVAREII NHRSLRHPNI
IRFKEVILTP THLAIVMEYA SGGELFERIC NAGRFSEAEA RYFFQQLICG VDYCHSLQIC
HRDLKLENTL LDGSPAPLLK ICDFGYSKSS LLHSRPKSTV GTPAYIAPEV LSRREYDGKH
ADVWSCGVTL YVMLVGGYPF EDPDDPRNFR KTIQRIMAVQ YKIPDYVHIS QECRHLLSRI
FVTNSAKRIT LKEIKKHPWY LKNLPKELTE PAQAAYYKRE TPSFSLQSVE DIMKIVGEAR
NPAPSSNAVK GFDDDEEDVE DEVEEEEEEE EEEEEEEEEE EDEYEKHVKE AHSCQEPPKA
