CIPKK_ARATH
ID CIPKK_ARATH Reviewed; 439 AA.
AC Q9FJ54;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=CBL-interacting serine/threonine-protein kinase 20;
DE EC=2.7.11.1;
DE AltName: Full=SNF1-related kinase 3.6;
DE AltName: Full=SOS2-like protein kinase PKS18;
GN Name=CIPK20; Synonyms=PKS18, SnRK3.6; OrderedLocusNames=At5g45820;
GN ORFNames=K15I22.2;
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 (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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 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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, MUTAGENESIS OF THR-170, AUTOPHOSPHORYLATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12198122; DOI=10.1074/jbc.m205504200;
RA Gong D., Zhang C., Chen X., Gong Z., Zhu J.-K.;
RT "Constitutive activation and transgenic evaluation of the function of an
RT arabidopsis PKS protein kinase.";
RL J. Biol. Chem. 277:42088-42096(2002).
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).
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). Required for the abscisic acid-mediated (ABA)
CC signaling pathway involved in seed germination and growth elongation
CC inhibition. {ECO:0000250, ECO:0000269|PubMed:12198122}.
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 -!- INTERACTION:
CC Q9FJ54; Q9LTB8: CBL9; NbExp=5; IntAct=EBI-25514480, EBI-637381;
CC -!- TISSUE SPECIFICITY: Confined to mature leaves.
CC {ECO:0000269|PubMed:12198122}.
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}.
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DR EMBL; AY035225; AAK61493.1; -; mRNA.
DR EMBL; AB016870; BAB09310.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95303.1; -; Genomic_DNA.
DR EMBL; AK221510; BAD94760.1; -; mRNA.
DR EMBL; BT028970; ABI54345.1; -; mRNA.
DR RefSeq; NP_199394.1; NM_123950.4.
DR AlphaFoldDB; Q9FJ54; -.
DR SMR; Q9FJ54; -.
DR BioGRID; 19871; 3.
DR IntAct; Q9FJ54; 1.
DR STRING; 3702.AT5G45820.1; -.
DR PaxDb; Q9FJ54; -.
DR PRIDE; Q9FJ54; -.
DR ProteomicsDB; 246518; -.
DR EnsemblPlants; AT5G45820.1; AT5G45820.1; AT5G45820.
DR GeneID; 834622; -.
DR Gramene; AT5G45820.1; AT5G45820.1; AT5G45820.
DR KEGG; ath:AT5G45820; -.
DR Araport; AT5G45820; -.
DR TAIR; locus:2152380; AT5G45820.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR InParanoid; Q9FJ54; -.
DR OMA; GSINTKH; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q9FJ54; -.
DR PRO; PR:Q9FJ54; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJ54; baseline and differential.
DR Genevisible; Q9FJ54; 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:0009737; P:response to abscisic acid; 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; Manganese; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..439
FT /note="CBL-interacting serine/threonine-protein kinase 20"
FT /id="PRO_0000337221"
FT DOMAIN 12..266
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 297..322
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 152..181
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 326..356
FT /note="PPI"
FT /evidence="ECO:0000250"
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"
FT MUTAGEN 170
FT /note="T->D: Strongly enhanced kinase activity, and higher
FT autophosphorylation, with an optimal pH of 7.5."
FT /evidence="ECO:0000269|PubMed:12198122"
FT MUTAGEN 303..323
FT /note="Missing: Enhanced kinase activity, and higher
FT autophosphorylation."
SQ SEQUENCE 439 AA; 50168 MW; AE9FB6C013192D20 CRC64;
MDKNGIVLMR KYELGRLLGQ GTFAKVYHAR NIKTGESVAI KVIDKQKVAK VGLIDQIKRE
ISVMRLVRHP HVVFLHEVMA SKTKIYFAME YVKGGELFDK VSKGKLKENI ARKYFQQLIG
AIDYCHSRGV YHRDLKPENL LLDENGDLKI SDFGLSALRE SKQQDGLLHT TCGTPAYVAP
EVIGKKGYDG AKADVWSCGV VLYVLLAGFL PFHEQNLVEM YRKITKGEFK CPNWFPPEVK
KLLSRILDPN PNSRIKIEKI MENSWFQKGF KKIETPKSPE SHQIDSLISD VHAAFSVKPM
SYNAFDLISS LSQGFDLSGL FEKEERSESK FTTKKDAKEI VSKFEEIATS SERFNLTKSD
VGVKMEDKRE GRKGHLAIDV EIFEVTNSFH MVEFKKSGGD TMEYKQFCDR ELRPSLKDIV
WKWQGNNNNS NNEKIEVIH
