SRK2I_ARATH
ID SRK2I_ARATH Reviewed; 361 AA.
AC Q39193; Q8RWG9;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Serine/threonine-protein kinase SRK2I;
DE EC=2.7.11.1;
DE AltName: Full=OST1-kinase-like 2;
DE AltName: Full=Protein ATHPROKIN B;
DE AltName: Full=SNF1-related kinase 2.3;
DE Short=SnRK2.3;
GN Name=SRK2I; Synonyms=41K, OSKL2, SNRK2.3; OrderedLocusNames=At5g66880;
GN ORFNames=MUD21.14;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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] OF 7-361.
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 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, 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 [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [10]
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 [11]
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).
RN [12]
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).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), ACTIVITY REGULATION, AND
RP AUTOPHOSPHORYLATION.
RX PubMed=22160701; DOI=10.1073/pnas.1118651109;
RA Ng L.M., Soon F.F., Zhou X.E., West G.M., Kovach A., Suino-Powell K.M.,
RA Chalmers M.J., Li J., Yong E.L., Zhu J.K., Griffin P.R., Melcher K.,
RA Xu H.E.;
RT "Structural basis for basal activity and autoactivation of abscisic acid
RT (ABA) signaling SnRK2 kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:21259-21264(2011).
CC -!- FUNCTION: Together with SRK2D, 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 -!- ACTIVITY REGULATION: Activated by autophosphorylation of its activation
CC loop. {ECO:0000269|PubMed:22160701}.
CC -!- SUBUNIT: Interacts with ABI1 (PubMed:19874541). Interacts with I-2 and
CC TOPP1 (PubMed:26943172). Interacts with FREE1 (via C-terminus)
CC (PubMed:30962512). {ECO:0000269|PubMed:19874541,
CC ECO:0000269|PubMed:26943172, ECO:0000269|PubMed:30962512}.
CC -!- INTERACTION:
CC Q39193; P49597: ABI1; NbExp=8; IntAct=EBI-2620383, EBI-782526;
CC Q39193; O04719-1: ABI2; NbExp=2; IntAct=EBI-2620383, EBI-15803514;
CC Q39193; Q9FLI3: AHG1; NbExp=2; IntAct=EBI-2620383, EBI-2363348;
CC Q39193; Q9CAJ0: HAB1; NbExp=2; IntAct=EBI-2620383, EBI-2309302;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in seeds, seedlings, roots
CC (especially in 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 -!- PTM: Autophosphorylated in vitro. {ECO:0000269|PubMed:22160701}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM13097.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; L05562; AAA32846.1; -; mRNA.
DR EMBL; AB010700; BAB08630.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98274.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70143.1; -; Genomic_DNA.
DR EMBL; AY093098; AAM13097.1; ALT_INIT; mRNA.
DR EMBL; BT002082; AAN72093.1; -; mRNA.
DR PIR; S71172; S71172.
DR RefSeq; NP_001318893.1; NM_001345807.1.
DR RefSeq; NP_201489.1; NM_126087.5.
DR PDB; 3UC3; X-ray; 1.90 A; A=1-361.
DR PDBsum; 3UC3; -.
DR AlphaFoldDB; Q39193; -.
DR SMR; Q39193; -.
DR BioGRID; 22064; 15.
DR DIP; DIP-48986N; -.
DR IntAct; Q39193; 13.
DR STRING; 3702.AT5G66880.1; -.
DR iPTMnet; Q39193; -.
DR PaxDb; Q39193; -.
DR PRIDE; Q39193; -.
DR ProteomicsDB; 226876; -.
DR EnsemblPlants; AT5G66880.1; AT5G66880.1; AT5G66880.
DR EnsemblPlants; AT5G66880.2; AT5G66880.2; AT5G66880.
DR GeneID; 836822; -.
DR Gramene; AT5G66880.1; AT5G66880.1; AT5G66880.
DR Gramene; AT5G66880.2; AT5G66880.2; AT5G66880.
DR KEGG; ath:AT5G66880; -.
DR Araport; AT5G66880; -.
DR TAIR; locus:2174999; AT5G66880.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q39193; -.
DR OMA; EYITDSC; -.
DR OrthoDB; 1017936at2759; -.
DR PhylomeDB; Q39193; -.
DR PRO; PR:Q39193; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q39193; baseline and differential.
DR Genevisible; Q39193; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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:0004672; F:protein 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:0009738; P:abscisic acid-activated signaling pathway; TAS:TAIR.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0010029; P:regulation of seed germination; IGI:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IDA:TAIR.
DR GO; GO:0009739; P:response to gibberellin; IGI:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IDA:TAIR.
DR GO; GO:0009651; P:response to salt stress; IDA:TAIR.
DR GO; GO:0009414; P:response to water deprivation; 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 3D-structure; Abscisic acid signaling pathway; ATP-binding; Kinase;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..361
FT /note="Serine/threonine-protein kinase SRK2I"
FT /id="PRO_0000345163"
FT DOMAIN 22..278
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 28..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 262
FT /note="D -> N (in Ref. 4; AAN72093/AAM13097)"
FT /evidence="ECO:0000305"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:3UC3"
FT STRAND 22..31
FT /evidence="ECO:0007829|PDB:3UC3"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:3UC3"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:3UC3"
FT STRAND 47..56
FT /evidence="ECO:0007829|PDB:3UC3"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:3UC3"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:3UC3"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:3UC3"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:3UC3"
FT HELIX 115..134
FT /evidence="ECO:0007829|PDB:3UC3"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:3UC3"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:3UC3"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:3UC3"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3UC3"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:3UC3"
FT HELIX 196..213
FT /evidence="ECO:0007829|PDB:3UC3"
FT HELIX 227..235
FT /evidence="ECO:0007829|PDB:3UC3"
FT HELIX 249..258
FT /evidence="ECO:0007829|PDB:3UC3"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:3UC3"
FT HELIX 269..273
FT /evidence="ECO:0007829|PDB:3UC3"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:3UC3"
FT HELIX 306..316
FT /evidence="ECO:0007829|PDB:3UC3"
SQ SEQUENCE 361 AA; 41085 MW; 01200388CD0124B9 CRC64;
MDRAPVTTGP LDMPIMHDSD RYDFVKDIGS GNFGVARLMR DKLTKELVAV KYIERGDKID
ENVQREIINH RSLRHPNIVR FKEVILTPTH LAIIMEYASG GELYERICNA GRFSEDEARF
FFQQLLSGVS YCHSMQICHR DLKLENTLLD GSPAPRLKIC DFGYSKSSVL HSQPKSTVGT
PAYIAPEVLL RQEYDGKIAD VWSCGVTLYV MLVGAYPFED PEEPRDYRKT IQRILSVKYS
IPDDIRISPE CCHLISRIFV ADPATRISIP EIKTHSWFLK NLPADLMNES NTGSQFQEPE
QPMQSLDTIM QIISEATIPA VRNRCLDDFM TDNLDLDDDM DDFDSESEID IDSSGEIVYA
L
