CIPK7_ARATH
ID CIPK7_ARATH Reviewed; 429 AA.
AC Q9XIW0; Q93Y18; Q9FZN7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=CBL-interacting serine/threonine-protein kinase 7;
DE EC=2.7.11.1;
DE AltName: Full=SNF1-related kinase 3.10;
DE AltName: Full=SOS2-like protein kinase PKS7;
DE AltName: Full=Serine/threonine-protein kinase SR2;
DE Short=AtSR2;
DE Short=AtSRPK1;
GN Name=CIPK7; Synonyms=PKS7, SnRK3.10, SR2, SRPK1;
GN OrderedLocusNames=At3g23000; ORFNames=MXC7.3;
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], AND 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AUTOPHOSPHORYLATION, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=11212922; DOI=10.1007/s004380000354;
RA Chikano H., Ogawa M., Ikeda Y., Koizumi N., Kusano T., Sano H.;
RT "Two novel genes encoding SNF-1 related protein kinases from Arabidopsis
RT thaliana: differential accumulation of AtSR1 and AtSR2 transcripts in
RT response to cytokinins and sugars, and phosphorylation of sucrose synthase
RT by AtSR2.";
RL Mol. Gen. Genet. 264:674-681(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nanmori T., Matsuoka D., Kono T.;
RT "Arabidopsis thaliana mRNA for a novel SNF1 related protein kinase
RT (ATSRPK1), partial cds.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=11402167; DOI=10.2307/3871302;
RA Guo Y., Halfter U., Ishitani M., Zhu J.-K.;
RT "Molecular characterization of functional domains in the protein kinase
RT SOS2 that is required for plant salt tolerance.";
RL Plant Cell 13:1383-1400(2001).
RN [5]
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 [6]
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [9]
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 [10]
RP INTERACTION WITH CBL1.
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 [11]
RP FUNCTION, INTERACTION WITH CBL1, INDUCTION BY COLD, AND TISSUE SPECIFICITY.
RX PubMed=21600398; DOI=10.1016/j.plantsci.2011.03.011;
RA Huang C., Ding S., Zhang H., Du H., An L.;
RT "CIPK7 is involved in cold response by interacting with CBL1 in Arabidopsis
RT thaliana.";
RL Plant Sci. 181:57-64(2011).
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 (By similarity). Phosphorylates the rice sucrose synthase (SuSy)
CC in vitro in an allosteric manner. Involved in cold response.
CC {ECO:0000250, ECO:0000269|PubMed:11212922,
CC ECO:0000269|PubMed:21600398}.
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 CBL1, CBL2 and CBL3.
CC {ECO:0000269|PubMed:11230129, ECO:0000269|PubMed:14730064,
CC ECO:0000269|PubMed:21600398}.
CC -!- INTERACTION:
CC Q9XIW0; O81445: CBL1; NbExp=3; IntAct=EBI-1765255, EBI-974530;
CC -!- TISSUE SPECIFICITY: Strongly expressed in leaves, but barely expressed
CC in roots, stems or flowers. {ECO:0000269|PubMed:11402167,
CC ECO:0000269|PubMed:21600398}.
CC -!- INDUCTION: By sucrose, glucose and fructose. Repressed in roots by salt
CC stress. Up-regulated by cold stress. {ECO:0000269|PubMed:11212922,
CC ECO:0000269|PubMed:11402167, ECO:0000269|PubMed:21600398}.
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.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {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; AF290192; AAK16682.1; -; mRNA.
DR EMBL; AB035148; BAB11738.1; -; mRNA.
DR EMBL; AB027153; BAA77716.2; -; mRNA.
DR EMBL; AF339148; AAK26846.1; -; mRNA.
DR EMBL; AB026655; BAB02091.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76704.1; -; Genomic_DNA.
DR EMBL; AY054686; AAK96877.1; -; mRNA.
DR EMBL; BT020492; AAW38993.1; -; mRNA.
DR EMBL; BT028967; ABI54342.1; -; mRNA.
DR RefSeq; NP_188940.1; NM_113200.3.
DR AlphaFoldDB; Q9XIW0; -.
DR SMR; Q9XIW0; -.
DR BioGRID; 7206; 7.
DR IntAct; Q9XIW0; 8.
DR STRING; 3702.AT3G23000.1; -.
DR PaxDb; Q9XIW0; -.
DR PRIDE; Q9XIW0; -.
DR ProteomicsDB; 246685; -.
DR EnsemblPlants; AT3G23000.1; AT3G23000.1; AT3G23000.
DR GeneID; 821874; -.
DR Gramene; AT3G23000.1; AT3G23000.1; AT3G23000.
DR KEGG; ath:AT3G23000; -.
DR Araport; AT3G23000; -.
DR TAIR; locus:2094553; AT3G23000.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR InParanoid; Q9XIW0; -.
DR OMA; RFSHQDG; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q9XIW0; -.
DR PRO; PR:Q9XIW0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9XIW0; baseline and differential.
DR Genevisible; Q9XIW0; 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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009409; P:response to cold; IEP: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 ATP-binding; Kinase; Manganese; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..429
FT /note="CBL-interacting serine/threonine-protein kinase 7"
FT /id="PRO_0000337210"
FT DOMAIN 25..280
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 302..326
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 167..195
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 330..363
FT /note="PPI"
FT /evidence="ECO:0000250"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 31..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93V58"
FT MOD_RES 184
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
FT CONFLICT 25
FT /note="Y -> H (in Ref. 2; BAB11738)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="V -> A (in Ref. 7; AAK96877)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="T -> P (in Ref. 7; AAK96877)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 429 AA; 48266 MW; 5D6703058ACF4A75 CRC64;
MESLPQPQNQ SSPATTPAKI LLGKYELGRR LGSGSFAKVH LARSIESDEL VAVKIIEKKK
TIESGMEPRI IREIDAMRRL RHHPNILKIH EVMATKSKIY LVMELASGGE LFSKVLRRGR
LPESTARRYF QQLASALRFS HQDGVAHRDV KPQNLLLDEQ GNLKVSDFGL SALPEHLQNG
LLHTACGTPA YTAPEVISRR GYDGAKADAW SCGVILFVLL VGDVPFDDSN IAAMYRKIHR
RDYRFPSWIS KQAKSIIYQM LDPNPVTRMS IETVMKTNWF KKSLETSEFH RNVFDSEVEM
KSSVNSITAF DLISLSSGLD LSGLFEAKKK KERRFTAKVS GVEVEEKAKM IGEKLGYVVK
KKMMKKEGEV KVVGLGRGRT VIVVEAVELT VDVVVVEVKV VEGEEDDSRW SDLITELEDI
VLSWHNDIM
