CIPK9_ARATH
ID CIPK9_ARATH Reviewed; 447 AA.
AC Q9MAM1; Q3EDL5; Q94F03; Q9C5P5; Q9C5S4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=CBL-interacting serine/threonine-protein kinase 9;
DE EC=2.7.11.1;
DE AltName: Full=SNF1-related kinase 3.12;
DE AltName: Full=SOS2-like protein kinase PKS6;
GN Name=CIPK9; Synonyms=PKS6, SnRK3.12; OrderedLocusNames=At1g01140;
GN ORFNames=F6F3.28, T25K16.13;
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 2), AND INTERACTION WITH CBL2.
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] (ISOFORM 4), AND TISSUE SPECIFICITY.
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM 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 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 [7]
RP FUNCTION, INTERACTION WITH CBL2 AND CBL3, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=23109687; DOI=10.1104/pp.112.206896;
RA Liu L.L., Ren H.M., Chen L.Q., Wang Y., Wu W.H.;
RT "A protein kinase, calcineurin B-like protein-interacting protein Kinase9,
RT interacts with calcium sensor calcineurin B-like Protein3 and regulates
RT potassium homeostasis under low-potassium stress in Arabidopsis.";
RL Plant Physiol. 161:266-277(2013).
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. Involved in K(+) homeostasis under low-K(+) stress.
CC {ECO:0000269|PubMed:23109687}.
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 CBL2 and CBL3. {ECO:0000269|PubMed:11230129,
CC ECO:0000269|PubMed:23109687}.
CC -!- INTERACTION:
CC Q9MAM1; Q17TI5: BRX; NbExp=4; IntAct=EBI-1765282, EBI-4426649;
CC Q9MAM1; Q9LTB8: CBL9; NbExp=4; IntAct=EBI-1765282, EBI-637381;
CC Q9MAM1; O22179: MYB70; NbExp=4; IntAct=EBI-1765282, EBI-1238013;
CC Q9MAM1; O23160: MYB73; NbExp=5; IntAct=EBI-1765282, EBI-25506855;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23109687}. Nucleus
CC {ECO:0000269|PubMed:23109687}. Note=Targeted to the tonoplast when
CC interacting with CBL2 or CBL3.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=3;
CC IsoId=Q9MAM1-3; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9MAM1-1; Sequence=VSP_033983, VSP_033984;
CC Name=2;
CC IsoId=Q9MAM1-2; Sequence=VSP_033983;
CC Name=4;
CC IsoId=Q9MAM1-4; Sequence=VSP_033984;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots and shoots.
CC Detected in root vascular bundles and in the leaf vascular tissue and
CC hydathode, but not in root tips. {ECO:0000269|PubMed:11402167,
CC ECO:0000269|PubMed:23109687}.
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 1]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be due to a competing donor 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; AF295664; AAK16684.1; -; mRNA.
DR EMBL; AF339147; AAK26845.1; -; mRNA.
DR EMBL; AC007323; AAF26468.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27243.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27244.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27245.1; -; Genomic_DNA.
DR EMBL; AF386999; AAK62444.1; -; mRNA.
DR EMBL; AY093242; AAM13241.1; -; mRNA.
DR PIR; G86141; G86141.
DR RefSeq; NP_171622.1; NM_099996.4. [Q9MAM1-3]
DR RefSeq; NP_849570.1; NM_179239.1. [Q9MAM1-2]
DR RefSeq; NP_849571.1; NM_179240.1. [Q9MAM1-4]
DR AlphaFoldDB; Q9MAM1; -.
DR SMR; Q9MAM1; -.
DR BioGRID; 24584; 26.
DR IntAct; Q9MAM1; 19.
DR STRING; 3702.AT1G01140.3; -.
DR iPTMnet; Q9MAM1; -.
DR PaxDb; Q9MAM1; -.
DR PRIDE; Q9MAM1; -.
DR ProteomicsDB; 246688; -. [Q9MAM1-3]
DR EnsemblPlants; AT1G01140.1; AT1G01140.1; AT1G01140. [Q9MAM1-3]
DR EnsemblPlants; AT1G01140.2; AT1G01140.2; AT1G01140. [Q9MAM1-2]
DR EnsemblPlants; AT1G01140.3; AT1G01140.3; AT1G01140. [Q9MAM1-4]
DR GeneID; 839349; -.
DR Gramene; AT1G01140.1; AT1G01140.1; AT1G01140. [Q9MAM1-3]
DR Gramene; AT1G01140.2; AT1G01140.2; AT1G01140. [Q9MAM1-2]
DR Gramene; AT1G01140.3; AT1G01140.3; AT1G01140. [Q9MAM1-4]
DR KEGG; ath:AT1G01140; -.
DR Araport; AT1G01140; -.
DR TAIR; locus:2035367; AT1G01140.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR InParanoid; Q9MAM1; -.
DR OMA; KEMMGMA; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q9MAM1; -.
DR PRO; PR:Q9MAM1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MAM1; baseline and differential.
DR Genevisible; Q9MAM1; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0051365; P:cellular response to potassium ion starvation; IMP:TAIR.
DR GO; GO:0055075; P:potassium ion homeostasis; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0043266; P:regulation of potassium ion transport; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0010555; P:response to mannitol; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
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; Cytoplasm; Kinase; Manganese;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..447
FT /note="CBL-interacting serine/threonine-protein kinase 9"
FT /id="PRO_0000337212"
FT DOMAIN 19..274
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 312..336
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 160..189
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 343..372
FT /note="PPI"
FT /evidence="ECO:0000250"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 25..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93V58"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
FT VAR_SEQ 231
FT /note="R -> RVR (in isoform 1 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230129"
FT /id="VSP_033983"
FT VAR_SEQ 422
FT /note="K -> KVCDS (in isoform 1 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11402167"
FT /id="VSP_033984"
FT CONFLICT 33
FT /note="V -> A (in Ref. 5; AAK62444/AAM13241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 447 AA; 50505 MW; 5E1A9B8DD37A0E32 CRC64;
MSGSRRKATP ASRTRVGNYE MGRTLGEGSF AKVKYAKNTV TGDQAAIKIL DREKVFRHKM
VEQLKREIST MKLIKHPNVV EIIEVMASKT KIYIVLELVN GGELFDKIAQ QGRLKEDEAR
RYFQQLINAV DYCHSRGVYH RDLKPENLIL DANGVLKVSD FGLSAFSRQV REDGLLHTAC
GTPNYVAPEV LSDKGYDGAA ADVWSCGVIL FVLMAGYLPF DEPNLMTLYK RICKAEFSCP
PWFSQGAKRV IKRILEPNPI TRISIAELLE DEWFKKGYKP PSFDQDDEDI TIDDVDAAFS
NSKECLVTEK KEKPVSMNAF ELISSSSEFS LENLFEKQAQ LVKKETRFTS QRSASEIMSK
MEETAKPLGF NVRKDNYKIK MKGDKSGRKG QLSVATEVFE VAPSLHVVEL RKTGGDTLEF
HKFYKNFSSG LKDVVWNTDA AAEEQKQ
