CIPK3_ARATH
ID CIPK3_ARATH Reviewed; 441 AA.
AC Q2V452; Q0WM53; Q2V451; Q8RWU8; Q93VA4; Q9LKC9; Q9ZVD9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=CBL-interacting serine/threonine-protein kinase 3;
DE EC=2.7.11.1;
DE AltName: Full=SNF1-related kinase 3.17;
DE AltName: Full=SOS2-like protein kinase PKS12;
GN Name=CIPK3; Synonyms=PKS12, SnRK3.17; OrderedLocusNames=At2g26980;
GN ORFNames=T20P8.3;
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 5), AND INTERACTION WITH 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Albrecht V., Weinl S., Kudla J.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 170-441 (ISOFORMS 1 AND 2).
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 [7]
RP FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=12566581; DOI=10.1105/tpc.006858;
RA Kim K.-N., Cheong Y.H., Grant J.J., Pandey G.K., Luan S.;
RT "CIPK3, a calcium sensor-associated protein kinase that regulates abscisic
RT acid and cold signal transduction in Arabidopsis.";
RL Plant Cell 15:411-423(2003).
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 FUNCTION, AND INTERACTION WITH CBL9.
RX PubMed=19825536; DOI=10.1093/mp/ssn003;
RA Pandey G.K., Grant J.J., Cheong Y.H., Kim B.G., Li L., Luan S.;
RT "Calcineurin-B-like protein CBL9 interacts with target kinase CIPK3 in the
RT regulation of ABA response in seed germination.";
RL Mol. Plant 1:238-248(2008).
CC -!- FUNCTION: Involved in the resistance to some abiotic stresses (e.g.
CC high salt, hyperosmotic stress) in young seedlings, by regulating the
CC expression of several stress-inducible genes (cold- and salt-induced
CC genes but not drought-responsive genes). Required for the ABA response
CC during germination. CIPK serine-threonine protein kinases interact with
CC CBL proteins. Binding of a CBL protein to the regulatory NAF domain of
CC CIPK protein lead to the activation of the kinase in a calcium-
CC dependent manner. The CBL9/CIPK3 complex acts in the regulation of
CC abscisic acid response in seed germination.
CC {ECO:0000269|PubMed:12566581, ECO:0000269|PubMed:19825536}.
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with CBL3 and CBL9. {ECO:0000269|PubMed:11115898,
CC ECO:0000269|PubMed:19825536}.
CC -!- INTERACTION:
CC Q2V452; Q9LTB8: CBL9; NbExp=5; IntAct=EBI-1748724, EBI-637381;
CC Q2V452; Q94AW5: ERF003; NbExp=3; IntAct=EBI-1748724, EBI-15202166;
CC Q2V452; Q38845: PP2AA1; NbExp=3; IntAct=EBI-1748724, EBI-1645478;
CC Q2V452; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-1748724, EBI-15192297;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=2;
CC IsoId=Q2V452-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q2V452-1; Sequence=VSP_038051;
CC Name=3;
CC IsoId=Q2V452-3; Sequence=VSP_033979, VSP_038050;
CC Name=4;
CC IsoId=Q2V452-4; Sequence=VSP_033981;
CC Name=5;
CC IsoId=Q2V452-5; Sequence=VSP_033980, VSP_038049;
CC -!- TISSUE SPECIFICITY: Mostly expressed in germinating seeds and young
CC seedlings. Detected at low levels in roots, stems, leaves and flowers.
CC {ECO:0000269|PubMed:12566581}.
CC -!- INDUCTION: By stresses such as cold, drought, high salt, wounding, and
CC abscisic acid (ABA). {ECO:0000269|PubMed:12566581}.
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 -!- MISCELLANEOUS: [Isoform 3]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
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DR EMBL; AF286051; AAF86507.1; -; mRNA.
DR EMBL; AY266298; AAP22036.1; -; mRNA.
DR EMBL; AC005623; AAC77856.2; -; Genomic_DNA.
DR EMBL; AC005623; AAM15068.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07915.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07916.1; -; Genomic_DNA.
DR EMBL; AF367290; AAK56278.1; -; mRNA.
DR EMBL; AY059163; AAL15388.1; -; mRNA.
DR EMBL; AY091098; AAM14049.1; -; mRNA.
DR EMBL; AY142671; AAN13209.1; -; mRNA.
DR EMBL; AK229978; BAF01803.1; -; mRNA.
DR PIR; C84667; C84667.
DR RefSeq; NP_850092.1; NM_179761.2. [Q2V452-3]
DR RefSeq; NP_850094.1; NM_179763.4. [Q2V452-2]
DR AlphaFoldDB; Q2V452; -.
DR SMR; Q2V452; -.
DR BioGRID; 2592; 13.
DR IntAct; Q2V452; 6.
DR STRING; 3702.AT2G26980.4; -.
DR iPTMnet; Q2V452; -.
DR PaxDb; Q2V452; -.
DR ProteomicsDB; 246790; -. [Q2V452-2]
DR EnsemblPlants; AT2G26980.1; AT2G26980.1; AT2G26980. [Q2V452-3]
DR EnsemblPlants; AT2G26980.3; AT2G26980.3; AT2G26980. [Q2V452-2]
DR GeneID; 817240; -.
DR Gramene; AT2G26980.1; AT2G26980.1; AT2G26980. [Q2V452-3]
DR Gramene; AT2G26980.3; AT2G26980.3; AT2G26980. [Q2V452-2]
DR KEGG; ath:AT2G26980; -.
DR Araport; AT2G26980; -.
DR eggNOG; KOG0583; Eukaryota.
DR InParanoid; Q2V452; -.
DR OMA; HHVTEKT; -.
DR PhylomeDB; Q2V452; -.
DR PRO; PR:Q2V452; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q2V452; baseline and differential.
DR Genevisible; Q2V452; AT.
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:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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; Manganese; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..441
FT /note="CBL-interacting serine/threonine-protein kinase 3"
FT /id="PRO_0000337206"
FT DOMAIN 14..269
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 307..331
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 155..184
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 337..366
FT /note="PPI"
FT /evidence="ECO:0000250"
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 20..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1
FT /note="M -> MLIPNKKLRE (in isoform 1)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_038051"
FT VAR_SEQ 373..382
FT /note="MRLENVKAGR -> VSENSVTEMK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_033979"
FT VAR_SEQ 373..375
FT /note="MRL -> YIT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11115898"
FT /id="VSP_033980"
FT VAR_SEQ 376..441
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11115898"
FT /id="VSP_038049"
FT VAR_SEQ 383..441
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_038050"
FT VAR_SEQ 392..441
FT /note="IFQVAPSLHMVQVSKSKGDTLEFHKFYKKLSNSLEQVVWTNNEVKKETAK
FT -> VCYMRLDIQESVGDGLLNQCVFCLYGVTTSRYS (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_033981"
SQ SEQUENCE 441 AA; 50600 MW; 1B9D9CB78E178138 CRC64;
MNRRQQVKRR VGKYEVGRTI GEGTFAKVKF ARNSETGEPV ALKILDKEKV LKHKMAEQIR
REIATMKLIK HPNVVQLYEV MASKTKIFII LEYVTGGELF DKIVNDGRMK EDEARRYFQQ
LIHAVDYCHS RGVYHRDLKP ENLLLDSYGN LKISDFGLSA LSQQVRDDGL LHTSCGTPNY
VAPEVLNDRG YDGATADMWS CGVVLYVLLA GYLPFDDSNL MNLYKKISSG EFNCPPWLSL
GAMKLITRIL DPNPMTRVTP QEVFEDEWFK KDYKPPVFEE RDDSNMDDID AVFKDSEEHL
VTEKREEQPA AINAFEIISM SRGLNLENLF DPEQEFKRET RITLRGGANE IIEKIEEAAK
PLGFDVQKKN YKMRLENVKA GRKGNLNVAT EIFQVAPSLH MVQVSKSKGD TLEFHKFYKK
LSNSLEQVVW TNNEVKKETA K
