CIPKG_ARATH
ID CIPKG_ARATH Reviewed; 469 AA.
AC Q9SEZ7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=CBL-interacting serine/threonine-protein kinase 16;
DE EC=2.7.11.1;
DE AltName: Full=SNF1-related kinase 3.18;
DE AltName: Full=SOS2-like protein kinase PKS15;
GN Name=CIPK16; Synonyms=PKS15, SnRK3.18; OrderedLocusNames=At2g25090;
GN ORFNames=F13D4.161;
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].
RA Weinl S., Albrecht V., Kudla J.;
RT "Molecular characterization of the CIPK gene family from Arabidopsis
RT thaliana.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, AND INTERACTION WITH AKT1; CBL1; CBL2; CBL3 AND CBL9.
RX PubMed=17898163; DOI=10.1073/pnas.0707912104;
RA Lee S.-C., Lan W.-Z., Kim B.-G., Li L., Cheong Y.H., Pandey G.K., Lu G.,
RA Buchanan B.B., Luan S.;
RT "A protein phosphorylation/dephosphorylation network regulates a plant
RT potassium channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15959-15964(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. Downstream of CBL1, CBL2, CBL3 and CBL9, regulates by
CC phosphorylation the K(+) conductance and uptake of AKT1.
CC {ECO:0000269|PubMed:17898163}.
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: Part of a K(+)-channel calcium-sensing kinase/phosphatase
CC complex composed by a calcium sensor CBL (CBL1, CBL2, CBL3 or CBL9), a
CC kinase CIPK (CIPK6, CIPK16 or CIPK23), a phosphatase PP2C (AIP1) and a
CC K(+)-channel (AKT1). Interacts with AKT1, CBL1, CBL2, CBL3 and CBL9.
CC {ECO:0000269|PubMed:17898163}.
CC -!- INTERACTION:
CC Q9SEZ7; Q17TI5: BRX; NbExp=3; IntAct=EBI-1573415, EBI-4426649;
CC Q9SEZ7; Q9LTB8: CBL9; NbExp=7; IntAct=EBI-1573415, EBI-637381;
CC Q9SEZ7; O22179: MYB70; NbExp=4; IntAct=EBI-1573415, EBI-1238013;
CC Q9SEZ7; O23160: MYB73; NbExp=3; IntAct=EBI-1573415, EBI-25506855;
CC Q9SEZ7; Q38845: PP2AA1; NbExp=3; IntAct=EBI-1573415, EBI-1645478;
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}.
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DR EMBL; AY030304; AAK50348.1; -; mRNA.
DR EMBL; CP002685; AEC07656.1; -; Genomic_DNA.
DR EMBL; BT029241; ABJ98573.1; -; mRNA.
DR PIR; B84644; B84644.
DR RefSeq; NP_180081.1; NM_128066.4.
DR AlphaFoldDB; Q9SEZ7; -.
DR SMR; Q9SEZ7; -.
DR BioGRID; 2399; 15.
DR DIP; DIP-40199N; -.
DR IntAct; Q9SEZ7; 9.
DR STRING; 3702.AT2G25090.1; -.
DR PaxDb; Q9SEZ7; -.
DR PRIDE; Q9SEZ7; -.
DR EnsemblPlants; AT2G25090.1; AT2G25090.1; AT2G25090.
DR GeneID; 817047; -.
DR Gramene; AT2G25090.1; AT2G25090.1; AT2G25090.
DR KEGG; ath:AT2G25090; -.
DR Araport; AT2G25090; -.
DR TAIR; locus:2040219; AT2G25090.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR InParanoid; Q9SEZ7; -.
DR OMA; YLFCEDD; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q9SEZ7; -.
DR PRO; PR:Q9SEZ7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SEZ7; baseline and differential.
DR Genevisible; Q9SEZ7; 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:0042538; P:hyperosmotic salinity response; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; IMP: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..469
FT /note="CBL-interacting serine/threonine-protein kinase 16"
FT /id="PRO_0000337217"
FT DOMAIN 15..278
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 317..342
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 157..193
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 290..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..376
FT /note="PPI"
FT /evidence="ECO:0000250"
FT REGION 447..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 139
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 21..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93V58"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
SQ SEQUENCE 469 AA; 53551 MW; 460E17225D6A7A7A CRC64;
MEESNRSSTV LFDKYNIGRL LGTGNFAKVY HGTEISTGDD VAIKVIKKDH VFKRRGMMEQ
IEREIAVMRL LRHPNVVELR EVMATKKKIF FVMEYVNGGE LFEMIDRDGK LPEDLARKYF
QQLISAVDFC HSRGVFHRDI KPENLLLDGE GDLKVTDFGL SALMMPEGLG GRRGSSDDLL
HTRCGTPAYV APEVLRNKGY DGAMADIWSC GIVLYALLAG FLPFIDENVM TLYTKIFKAE
CEFPPWFSLE SKELLSRLLV PDPEQRISMS EIKMIPWFRK NFTPSVAFSI DETIPSPPEP
PTKKKKKDLN EKEDDGASPR SFNAFQFITS MSSGFDLSNL FEIKRKPKRM FTSKFPAKSV
KERLETAARE MDMRVKHVKD CKMKLQRRTE GRKGRLSVTA EVFEVAPEVS VVEFCKTSGD
TLEYYLFCED DVRPALKDIV WSWQGDDDED DVTTNDNVDT NDNKINNVS
