SRK2D_ARATH
ID SRK2D_ARATH Reviewed; 362 AA.
AC Q39192; Q8LAA1; Q93ZE6;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Serine/threonine-protein kinase SRK2D;
DE EC=2.7.11.1;
DE AltName: Full=OST1-kinase-like 3;
DE AltName: Full=Protein ATHPROKIN A;
DE AltName: Full=SNF1-related kinase 2.2;
DE Short=SnRK2.2;
GN Name=SRK2D; Synonyms=OSKL3, SNRK2.2, SPK2; OrderedLocusNames=At3g50500;
GN ORFNames=T20E23.100;
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;
RA Gallois P.;
RT "Two new protein kinases in Arabidopsis.";
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
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 [9]
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).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17307925; DOI=10.1105/tpc.106.048538;
RA Fujii H., Verslues P.E., Zhu J.-K.;
RT "Identification of two protein kinases required for abscisic acid
RT regulation of seed germination, root growth, and gene expression in
RT Arabidopsis.";
RL Plant Cell 19:485-494(2007).
RN [11]
RP INTERACTION WITH ABI1.
RX PubMed=19874541; DOI=10.1111/j.1365-313x.2009.04054.x;
RA Nishimura N., Sarkeshik A., Nito K., Park S.-Y., Wang A., Carvalho P.C.,
RA Lee S., Caddell D.F., Cutler S.R., Chory J., Yates J.R., Schroeder J.I.;
RT "PYR/PYL/RCAR family members are major in-vivo ABI1 protein phosphatase 2C-
RT interacting proteins in Arabidopsis.";
RL Plant J. 61:290-299(2010).
RN [12]
RP INTERACTION WITH I-2; TOPP1 AND TOPP2.
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).
RN [13]
RP FUNCTION, AND INTERACTION WITH FREE1.
RX PubMed=30962512; DOI=10.1038/s41477-019-0400-5;
RA Li H., Li Y., Zhao Q., Li T., Wei J., Li B., Shen W., Yang C., Zeng Y.,
RA Rodriguez P.L., Zhao Y., Jiang L., Wang X., Gao C.;
RT "The plant ESCRT component FREE1 shuttles to the nucleus to attenuate
RT abscisic acid signalling.";
RL Nat. Plants 5:512-524(2019).
CC -!- FUNCTION: Together with SRK2I, key component and activator of the
CC abscisic acid (ABA) signaling pathway that regulates numerous ABA
CC responses, such as seed germination, Pro accumulation, root growth
CC inhibition, dormancy and seedling growth, and, to a lesser extent,
CC stomatal closure (PubMed:17307925). In response to ABA, phosphorylates
CC the ESCRT-I complex component FREE1, which is required for ABA-induced
CC FREE1 nuclear import (PubMed:30962512). {ECO:0000269|PubMed:17307925,
CC ECO:0000269|PubMed:30962512}.
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 ABI1 (PubMed:19874541). Interacts with I-2,
CC TOPP1 and TOPP2 (PubMed:26943172). Interacts with FREE1 (via C-
CC terminus) (PubMed:30962512). {ECO:0000269|PubMed:19874541,
CC ECO:0000269|PubMed:26943172, ECO:0000269|PubMed:30962512}.
CC -!- INTERACTION:
CC Q39192; P49597: ABI1; NbExp=7; IntAct=EBI-2363308, EBI-782526;
CC Q39192; O04719-1: ABI2; NbExp=2; IntAct=EBI-2363308, EBI-15803514;
CC Q39192; Q9FLI3: AHG1; NbExp=2; IntAct=EBI-2363308, EBI-2363348;
CC Q39192; Q9CAJ0: HAB1; NbExp=2; IntAct=EBI-2363308, EBI-2309302;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q39192-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in seeds, seedlings, roots (especially in
CC tips), stems, leaves, shoots, flowers and siliques.
CC {ECO:0000269|PubMed:15292193, ECO:0000269|PubMed:17307925}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL14386.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L05561; AAA32845.1; -; mRNA.
DR EMBL; AL133363; CAB62479.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78672.1; -; Genomic_DNA.
DR EMBL; AY057591; AAL14386.1; ALT_FRAME; mRNA.
DR EMBL; BT025246; ABF18999.1; -; mRNA.
DR EMBL; AY087953; AAM65501.1; -; mRNA.
DR PIR; S56718; S56718.
DR RefSeq; NP_190619.1; NM_114910.3. [Q39192-1]
DR AlphaFoldDB; Q39192; -.
DR SMR; Q39192; -.
DR BioGRID; 9532; 16.
DR DIP; DIP-48985N; -.
DR IntAct; Q39192; 15.
DR STRING; 3702.AT3G50500.2; -.
DR iPTMnet; Q39192; -.
DR PaxDb; Q39192; -.
DR PRIDE; Q39192; -.
DR ProteomicsDB; 226873; -. [Q39192-1]
DR EnsemblPlants; AT3G50500.1; AT3G50500.1; AT3G50500. [Q39192-1]
DR GeneID; 824214; -.
DR Gramene; AT3G50500.1; AT3G50500.1; AT3G50500. [Q39192-1]
DR KEGG; ath:AT3G50500; -.
DR Araport; AT3G50500; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q39192; -.
DR PhylomeDB; Q39192; -.
DR PRO; PR:Q39192; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q39192; baseline and differential.
DR Genevisible; Q39192; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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 Abscisic acid signaling pathway; Alternative splicing; ATP-binding; Kinase;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..362
FT /note="Serine/threonine-protein kinase SRK2D"
FT /id="PRO_0000345159"
FT DOMAIN 23..279
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 29..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 37
FT /note="A -> T (in Ref. 6; AAM65501)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="Y -> C (in Ref. 6; AAM65501)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="R -> Q (in Ref. 6; AAM65501)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 41207 MW; 043E44E476E17119 CRC64;
MDPATNSPIM PIDLPIMHDS DRYDFVKDIG SGNFGVARLM TDRVTKELVA VKYIERGEKI
DENVQREIIN HRSLRHPNIV RFKEVILTPS HLAIVMEYAA GGELYERICN AGRFSEDEAR
FFFQQLISGV SYCHAMQICH RDLKLENTLL DGSPAPRLKI CDFGYSKSSV LHSQPKSTVG
TPAYIAPEIL LRQEYDGKLA DVWSCGVTLY VMLVGAYPFE DPQEPRDYRK TIQRILSVTY
SIPEDLHLSP ECRHLISRIF VADPATRITI PEITSDKWFL KNLPGDLMDE NRMGSQFQEP
EQPMQSLDTI MQIISEATIP TVRNRCLDDF MADNLDLDDD MDDFDSESEI DVDSSGEIVY
AL
