CIPKB_ARATH
ID CIPKB_ARATH Reviewed; 435 AA.
AC O22932; Q7FYB7; Q944I6;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=CBL-interacting serine/threonine-protein kinase 11;
DE EC=2.7.11.1;
DE AltName: Full=SNF1-related kinase 3.22;
DE AltName: Full=SOS2-like protein kinase PKS5;
DE AltName: Full=SOS3-interacting protein 4;
GN Name=CIPK11; Synonyms=PKS5, SIP4, SnRK3.22; OrderedLocusNames=At2g30360;
GN ORFNames=T9D9.17;
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 CBL1; CBL2; CBL3 AND CBL5.
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=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].
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 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 [7]
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 [8]
RP FUNCTION, INTERACTION WITH CBL2, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, INDUCTION, COFACTOR, AND AUTOPHOSPHORYLATION.
RX PubMed=17483306; DOI=10.1105/tpc.105.035626;
RA Fuglsang A.T., Guo Y., Cuin T.A., Qiu Q., Song C., Kristiansen K.A.,
RA Bych K., Schulz A., Shabala S., Schumaker K.S., Palmgren M.G., Zhu J.K.;
RT "Arabidopsis protein kinase PKS5 inhibits the plasma membrane H+ -ATPase by
RT preventing interaction with 14-3-3 protein.";
RL Plant Cell 19:1617-1634(2007).
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. Acts as a negative regulator of the plasma membrane proton pump
CC AHA2 by preventing its interaction with 14-3-3 protein.
CC {ECO:0000269|PubMed:17483306}.
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;
CC Evidence={ECO:0000269|PubMed:17483306};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17483306};
CC -!- SUBUNIT: Interacts with CBL1, CBL2, CBL3, CBL4/SOS3, and CBL5.
CC {ECO:0000269|PubMed:10725350, ECO:0000269|PubMed:11230129,
CC ECO:0000269|PubMed:17483306}.
CC -!- INTERACTION:
CC O22932; P19456: AHA2; NbExp=3; IntAct=EBI-537638, EBI-2293350;
CC O22932; Q8LAS7: CBL2; NbExp=5; IntAct=EBI-537638, EBI-485991;
CC O22932; Q9LTB8: CBL9; NbExp=5; IntAct=EBI-537638, EBI-637381;
CC O22932; O23160: MYB73; NbExp=3; IntAct=EBI-537638, EBI-25506855;
CC -!- TISSUE SPECIFICITY: Expressed in roots and stems, but barely detectable
CC in flowers and siliques. {ECO:0000269|PubMed:11402167,
CC ECO:0000269|PubMed:17483306}.
CC -!- DEVELOPMENTAL STAGE: Expressed in hypocotyls and roots upon
CC germination. As seedlings mature, detected in the vascular tissue of
CC both the stem and leaf. {ECO:0000269|PubMed:17483306}.
CC -!- INDUCTION: Up-regulated by salt, drought, abscisic acid and glucose,
CC but not by cold. {ECO:0000269|PubMed:11402167,
CC ECO:0000269|PubMed:17483306}.
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 -!- DISRUPTION PHENOTYPE: Increased proton extrusion and resistance to high
CC external pH. {ECO:0000269|PubMed:17483306}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL16166.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF295666; AAK16686.1; -; mRNA.
DR EMBL; AF339146; AAK26844.1; -; mRNA.
DR EMBL; AC002338; AAC16938.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08375.1; -; Genomic_DNA.
DR EMBL; AF370595; AAK43914.1; -; mRNA.
DR EMBL; AF428398; AAL16166.1; ALT_FRAME; mRNA.
DR EMBL; BT002478; AAO00838.1; -; mRNA.
DR EMBL; BT006582; AAP31926.1; -; mRNA.
DR PIR; E84707; E84707.
DR RefSeq; NP_180595.1; NM_128589.2.
DR AlphaFoldDB; O22932; -.
DR SMR; O22932; -.
DR BioGRID; 2935; 38.
DR IntAct; O22932; 9.
DR STRING; 3702.AT2G30360.1; -.
DR PaxDb; O22932; -.
DR PRIDE; O22932; -.
DR EnsemblPlants; AT2G30360.1; AT2G30360.1; AT2G30360.
DR GeneID; 817586; -.
DR Gramene; AT2G30360.1; AT2G30360.1; AT2G30360.
DR KEGG; ath:AT2G30360; -.
DR Araport; AT2G30360; -.
DR TAIR; locus:2065781; AT2G30360.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR InParanoid; O22932; -.
DR OMA; IFYDEDC; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; O22932; -.
DR PRO; PR:O22932; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22932; differential.
DR Genevisible; O22932; AT.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
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; IDA:TAIR.
DR GO; GO:0051592; P:response to calcium ion; IEP:TAIR.
DR GO; GO:0009268; P:response to pH; IMP: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 ATP-binding; Kinase; Magnesium; Manganese; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..435
FT /note="CBL-interacting serine/threonine-protein kinase 11"
FT /id="PRO_0000085875"
FT DOMAIN 21..277
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 163..192
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 333..362
FT /note="PPI"
FT /evidence="ECO:0000250"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 27..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93V58"
FT MOD_RES 181
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
SQ SEQUENCE 435 AA; 49017 MW; 50C256B3C2B7D900 CRC64;
MPEIEIAAGS GDNNDALFGK YELGKLLGCG AFAKVFHARD RRTGQSVAVK ILNKKKLLTN
PALANNIKRE ISIMRRLSHP NIVKLHEVMA TKSKIFFAME FVKGGELFNK ISKHGRLSED
LSRRYFQQLI SAVGYCHARG VYHRDLKPEN LLIDENGNLK VSDFGLSALT DQIRPDGLLH
TLCGTPAYVA PEILSKKGYE GAKVDVWSCG IVLFVLVAGY LPFNDPNVMN MYKKIYKGEY
RFPRWMSPDL KRFVSRLLDI NPETRITIDE ILKDPWFVRG GFKQIKFHDD EIEDQKVESS
LEAVKSLNAF DLISYSSGLD LSGLFAGCSN SSGESERFLS EKSPEMLAEE VEGFAREENL
RMKKKKEEEY GFEMEGQNGK FGIGICISRL NDLLVVVEAR RRGGDGDCYK EMWNGKLRVQ
LIRVCDQTSS TNAAI
