CIPKA_ARATH
ID CIPKA_ARATH Reviewed; 479 AA.
AC Q9C562; Q9LVL3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=CBL-interacting serine/threonine-protein kinase 10;
DE EC=2.7.11.1;
DE AltName: Full=SNF1-related kinase 3.8;
DE AltName: Full=SOS2-like protein kinase PKS2;
DE AltName: Full=SOS3-interacting protein 1;
GN Name=CIPK10; Synonyms=PKS2, SIP1, SnRK3.8; OrderedLocusNames=At5g58380;
GN ORFNames=MCK7.25;
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].
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], 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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].
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].
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 INTERACTION WITH CBL4.
RX PubMed=10725350; DOI=10.1073/pnas.97.7.3735;
RA Halfter U., Ishitani M., Zhu J.-K.;
RT "The Arabidopsis SOS2 protein kinase physically interacts with and is
RT activated by the calcium-binding protein SOS3.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3735-3740(2000).
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).
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). {ECO:0000250}.
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 CBL4/SOS3. {ECO:0000269|PubMed:10725350}.
CC -!- INTERACTION:
CC Q9C562; O81445: CBL1; NbExp=3; IntAct=EBI-537572, EBI-974530;
CC Q9C562; Q9LTB8: CBL9; NbExp=9; IntAct=EBI-537572, EBI-637381;
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots.
CC {ECO:0000269|PubMed:11402167}.
CC -!- INDUCTION: By salt stress. {ECO:0000269|PubMed:11402167}.
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA96929.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF295665; AAK16685.1; -; mRNA.
DR EMBL; AF339143; AAK26841.1; -; mRNA.
DR EMBL; AB019228; BAA96929.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97046.1; -; Genomic_DNA.
DR EMBL; AY094414; AAM19789.1; -; mRNA.
DR EMBL; AY124002; AAM74510.1; -; mRNA.
DR EMBL; AY125530; AAM78040.1; -; mRNA.
DR EMBL; AK226938; BAE99008.1; -; mRNA.
DR RefSeq; NP_568878.1; NM_125224.3.
DR AlphaFoldDB; Q9C562; -.
DR SMR; Q9C562; -.
DR BioGRID; 21195; 7.
DR IntAct; Q9C562; 5.
DR STRING; 3702.AT5G58380.1; -.
DR iPTMnet; Q9C562; -.
DR PaxDb; Q9C562; -.
DR PRIDE; Q9C562; -.
DR ProteomicsDB; 246510; -.
DR EnsemblPlants; AT5G58380.1; AT5G58380.1; AT5G58380.
DR GeneID; 835951; -.
DR Gramene; AT5G58380.1; AT5G58380.1; AT5G58380.
DR KEGG; ath:AT5G58380; -.
DR Araport; AT5G58380; -.
DR TAIR; locus:2161273; AT5G58380.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR InParanoid; Q9C562; -.
DR OMA; KEGRMGI; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q9C562; -.
DR PRO; PR:Q9C562; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9C562; baseline and differential.
DR Genevisible; Q9C562; 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 ATP-binding; Kinase; Manganese; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..479
FT /note="CBL-interacting serine/threonine-protein kinase 10"
FT /id="PRO_0000337213"
FT DOMAIN 12..266
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 322..346
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 152..181
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 286..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..379
FT /note="PPI"
FT /evidence="ECO:0000250"
FT REGION 456..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93V58"
FT MOD_RES 170
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
SQ SEQUENCE 479 AA; 54589 MW; 07203C4F6D83ED1B CRC64;
MENKPSVLTD KYDVGRLLGQ GTFAKVYYGR SILTNQSVAI KMIDKEKVMK VGLIEQIKRE
ISVMRIARHP NVVELYEVMA TKTRIYFVME YCKGGELFNK VAKGKLRDDV AWKYFYQLIN
AVDFCHSREV YHRDIKPENL LLDDNENLKV SDFGLSALAD CKRQDGLLHT TCGTPAYVAP
EVINRKGYDG TKADIWSCGV VLFVLLAGYL PFHDSNLMEM YRKIGKADFK APSWFAPEVR
RLLCKMLDPN PETRITIARI RESSWFRKGL HMKQKKMEKR VKEINSVEAG TAGTNENGAG
PSENGAGPSE NGDRVTEENH TDEPTNLNAF DLIALSAGFD LAGLFGDDNK RESRFTSQKP
ASVIISKLEE VAQRLKLSIR KREAGLFKLE RLKEGRKGIL SMDAEIFQVT PNFHLVEVKK
SNGDTLEYQK LVAEDLRPAL SDIVWVWQGE KDELTSQQET EYQQQQQQEQ QEQEEPLKF
