CIPK1_ARATH
ID CIPK1_ARATH Reviewed; 444 AA.
AC Q8RWC9; Q3EB49; Q9FUK2; Q9LUP6;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=CBL-interacting serine/threonine-protein kinase 1;
DE EC=2.7.11.1;
DE AltName: Full=SNF1-related kinase 3.16;
DE AltName: Full=SOS2-like protein kinase PKS13;
GN Name=CIPK1; Synonyms=PKS13, SnRK3.16; OrderedLocusNames=At3g17510;
GN ORFNames=MKP6.6;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND INTERACTION
RP WITH CBL1.
RX PubMed=10590166; DOI=10.2307/3870963;
RA Shi J., Kim K.-N., Ritz O., Albrecht V., Gupta R., Harter K., Luan S.,
RA Kudla J.;
RT "Novel protein kinases associated with calcineurin B-like calcium sensors
RT in Arabidopsis.";
RL Plant Cell 11:2393-2405(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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] (ISOFORM 1).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH CBL1 AND CBL3.
RC STRAIN=cv. Columbia;
RX PubMed=11115898; DOI=10.1104/pp.124.4.1844;
RA Kim K.-N., Cheong Y.H., Gupta R., Luan S.;
RT "Interaction specificity of Arabidopsis calcineurin B-like calcium sensors
RT and their target kinases.";
RL Plant Physiol. 124:1844-1853(2000).
RN [7]
RP INTERACTION WITH CBL2 AND CBL3.
RX PubMed=11230129; DOI=10.1093/emboj/20.5.1051;
RA Albrecht V., Ritz O., Linder S., Harter K., Kudla J.;
RT "The NAF domain defines a novel protein-protein interaction module
RT conserved in Ca(2+)-regulated kinases.";
RL EMBO J. 20:1051-1063(2001).
RN [8]
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 [9]
RP INTERACTION WITH CBL1 AND CBL9.
RX PubMed=14730064; DOI=10.1104/pp.103.033068;
RA Kolukisaoglu U., Weinl S., Blazevic D., Batistic O., Kudla J.;
RT "Calcium sensors and their interacting protein kinases: genomics of the
RT Arabidopsis and rice CBL-CIPK signaling networks.";
RL Plant Physiol. 134:43-58(2004).
RN [10]
RP INTERACTION WITH ECT1 AND ECT2.
RC STRAIN=cv. Columbia;
RX PubMed=16113215; DOI=10.1104/pp.105.065649;
RA Ok S.H., Jeong H.J., Bae J.M., Shin J.S., Luan S., Kim K.N.;
RT "Novel CIPK1-associated proteins in Arabidopsis contain an evolutionarily
RT conserved C-terminal region that mediates nuclear localization.";
RL Plant Physiol. 139:138-150(2005).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP PHOSPHORYLATION.
RX PubMed=22253446; DOI=10.1074/jbc.m111.279331;
RA Hashimoto K., Eckert C., Anschuetz U., Scholz M., Held K., Waadt R.,
RA Reyer A., Hippler M., Becker D., Kudla J.;
RT "Phosphorylation of calcineurin B-like (CBL) calcium sensor proteins by
RT their CBL-interacting protein kinases (CIPKs) is required for full activity
RT of CBL-CIPK complexes toward their target proteins.";
RL J. Biol. Chem. 287:7956-7968(2012).
CC -!- FUNCTION: CIPK serine-threonine protein kinases interact with CBL
CC proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK
CC protein lead to the activation of the kinase in a calcium-dependent
CC manner. {ECO:0000269|PubMed:22253446}.
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 Evidence={ECO:0000269|PubMed:22253446};
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; Evidence={ECO:0000269|PubMed:22253446};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:22253446};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15.2 uM for synthetic substrate {ECO:0000269|PubMed:22253446};
CC Vmax=146.1 pmol/min/mg enzyme {ECO:0000269|PubMed:22253446};
CC -!- SUBUNIT: Interacts with CBL1 (PubMed:10590166, PubMed:11115898,
CC PubMed:14730064). Interacts with CBL2 (PubMed:11230129). Interacts with
CC CBL3 (PubMed:11115898, PubMed:11230129). Interacts with CBL9
CC (PubMed:14730064). Interacts with ECT1 and ECT2 (PubMed:16113215).
CC {ECO:0000269|PubMed:10590166, ECO:0000269|PubMed:11115898,
CC ECO:0000269|PubMed:11230129, ECO:0000269|PubMed:14730064,
CC ECO:0000269|PubMed:16113215}.
CC -!- INTERACTION:
CC Q8RWC9; O81445: CBL1; NbExp=10; IntAct=EBI-1748677, EBI-974530;
CC Q8RWC9; Q8LAS7: CBL2; NbExp=4; IntAct=EBI-1748677, EBI-485991;
CC Q8RWC9; Q8LEM7: CBL3; NbExp=4; IntAct=EBI-1748677, EBI-637358;
CC Q8RWC9; O81223: CBL4; NbExp=3; IntAct=EBI-1748677, EBI-537541;
CC Q8RWC9; Q9LTB8: CBL9; NbExp=5; IntAct=EBI-1748677, EBI-637381;
CC Q8RWC9; Q3MK94: ECT1; NbExp=4; IntAct=EBI-1748677, EBI-2368594;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8RWC9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8RWC9-2; Sequence=VSP_026063, VSP_026064;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10590166}.
CC -!- DOMAIN: The activation loop within the kinase domain is the target of
CC phosphorylation/activation by upstream protein kinases. The PPI motif
CC mediates the interaction with the ABI (abscisic acid-insensitive)
CC phosphatases (By similarity). {ECO:0000250}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:22253446}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02040.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF302112; AAG28776.1; -; mRNA.
DR EMBL; AB022219; BAB02040.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75962.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75963.1; -; Genomic_DNA.
DR EMBL; AY093177; AAM13176.1; -; mRNA.
DR EMBL; BT029495; ABL66752.1; -; mRNA.
DR RefSeq; NP_566580.1; NM_112631.3. [Q8RWC9-1]
DR RefSeq; NP_974328.1; NM_202599.2. [Q8RWC9-2]
DR AlphaFoldDB; Q8RWC9; -.
DR SMR; Q8RWC9; -.
DR BioGRID; 6349; 18.
DR IntAct; Q8RWC9; 10.
DR STRING; 3702.AT3G17510.1; -.
DR PaxDb; Q8RWC9; -.
DR PRIDE; Q8RWC9; -.
DR EnsemblPlants; AT3G17510.1; AT3G17510.1; AT3G17510. [Q8RWC9-1]
DR EnsemblPlants; AT3G17510.2; AT3G17510.2; AT3G17510. [Q8RWC9-2]
DR GeneID; 821016; -.
DR Gramene; AT3G17510.1; AT3G17510.1; AT3G17510. [Q8RWC9-1]
DR Gramene; AT3G17510.2; AT3G17510.2; AT3G17510. [Q8RWC9-2]
DR KEGG; ath:AT3G17510; -.
DR Araport; AT3G17510; -.
DR TAIR; locus:2090537; AT3G17510.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR InParanoid; Q8RWC9; -.
DR OMA; KVMQEHK; -.
DR PhylomeDB; Q8RWC9; -.
DR SABIO-RK; Q8RWC9; -.
DR PRO; PR:Q8RWC9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8RWC9; baseline and differential.
DR Genevisible; Q8RWC9; AT.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018451; NAF/FISL_domain.
DR InterPro; IPR004041; NAF_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF03822; NAF; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50816; NAF; 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 Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..444
FT /note="CBL-interacting serine/threonine-protein kinase 1"
FT /id="PRO_0000085861"
FT DOMAIN 20..275
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 313..337
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 161..190
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 343..372
FT /note="PPI"
FT /evidence="ECO:0000250"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 26..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93V58"
FT MOD_RES 179
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
FT VAR_SEQ 1..80
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_026063"
FT VAR_SEQ 81..85
FT /note="VRLHE -> MVIMQ (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_026064"
FT CONFLICT 179
FT /note="T -> N (in Ref. 1; AAG28776)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="D -> N (in Ref. 4; AAM13176)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="K -> N (in Ref. 1; AAG28776)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="N -> T (in Ref. 1; AAG28776)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 444 AA; 49933 MW; 63DB8AF69CCAA5C9 CRC64;
MVRRQEEEKK AEKGMRLGKY ELGRTLGEGN FGKVKFAKDT VSGHSFAVKI IDKSRIADLN
FSLQIKREIR TLKMLKHPHI VRLHEVLASK TKINMVMELV TGGELFDRIV SNGKLTETDG
RKMFQQLIDG ISYCHSKGVF HRDLKLENVL LDAKGHIKIT DFGLSALPQH FRDDGLLHTT
CGSPNYVAPE VLANRGYDGA ASDIWSCGVI LYVILTGCLP FDDRNLAVLY QKICKGDPPI
PRWLSPGART MIKRMLDPNP VTRITVVGIK ASEWFKLEYI PSIPDDDDEE EVDTDDDAFS
IQELGSEEGK GSDSPTIINA FQLIGMSSFL DLSGFFEQEN VSERRIRFTS NSSAKDLLEK
IETAVTEMGF SVQKKHAKLR VKQEERNQKG QVGLSVTAEV FEIKPSLNVV ELRKSYGDSC
LYRQLYERLL KDVGTSSPEQ EIVT
