SRK2F_ARATH
ID SRK2F_ARATH Reviewed; 350 AA.
AC Q9SMQ4;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Serine/threonine-protein kinase SRK2F;
DE EC=2.7.11.1;
DE AltName: Full=OST1-kinase-like 5;
DE AltName: Full=SNF1-related kinase 2.7;
DE Short=SnRK2.7;
GN Name=SRK2F; Synonyms=OSKL5, SNRK2.7; OrderedLocusNames=At4g40010;
GN ORFNames=T5J17.180;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 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 [4]
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 [5]
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 -!- TISSUE SPECIFICITY: Expressed in seedlings.
CC {ECO:0000269|PubMed:15292193}.
CC -!- INDUCTION: By abscisic acid (ABA), salt, and osmotic stress (at protein
CC level). {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; AL035708; CAB38914.1; -; Genomic_DNA.
DR EMBL; AL161596; CAB80664.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87152.1; -; Genomic_DNA.
DR PIR; T06107; T06107.
DR RefSeq; NP_195711.1; NM_120165.2.
DR AlphaFoldDB; Q9SMQ4; -.
DR SMR; Q9SMQ4; -.
DR BioGRID; 15442; 4.
DR STRING; 3702.AT4G40010.1; -.
DR iPTMnet; Q9SMQ4; -.
DR PaxDb; Q9SMQ4; -.
DR PRIDE; Q9SMQ4; -.
DR ProteomicsDB; 226875; -.
DR EnsemblPlants; AT4G40010.1; AT4G40010.1; AT4G40010.
DR GeneID; 830162; -.
DR Gramene; AT4G40010.1; AT4G40010.1; AT4G40010.
DR KEGG; ath:AT4G40010; -.
DR Araport; AT4G40010; -.
DR TAIR; locus:2140104; AT4G40010.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q9SMQ4; -.
DR OMA; PEIEKHP; -.
DR OrthoDB; 888395at2759; -.
DR PhylomeDB; Q9SMQ4; -.
DR PRO; PR:Q9SMQ4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SMQ4; baseline and differential.
DR Genevisible; Q9SMQ4; 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:0016301; F:kinase activity; IDA: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; Coiled coil; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..350
FT /note="Serine/threonine-protein kinase SRK2F"
FT /id="PRO_0000345161"
FT DOMAIN 4..260
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT COILED 270..303
FT /evidence="ECO:0000255"
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"
SQ SEQUENCE 350 AA; 39775 MW; 214A067623BA9C9A CRC64;
MERYDILRDL GSGNFGVAKL VREKANGEFY AVKYIERGLK IDEHVQREII NHRDLKHPNI
IRFKEVFVTP THLAIVMEYA AGGELFERIC NAGRFSEDEG RYYFKQLISG VSYCHAMQIC
HRDLKLENTL LDGSPSSHLK ICDFGYSKSS VLHSQPKSTV GTPAYVAPEV LSRKEYNGKI
ADVWSCGVTL YVMLVGAYPF EDPEDPRNIR NTIQRILSVH YTIPDYVRIS SECKHLLSRI
FVADPDKRIT VPEIEKHPWF LKGPLVVPPE EEKCDNGVEE EEEEEEKCRQ SVEEIVKIIE
EARKGVNGTD NNGGLGLIDG SIDLDDIDDA DIYDDVDDDE ERNGDFVCAL
