CIPKJ_ARATH
ID CIPKJ_ARATH Reviewed; 483 AA.
AC Q9FJ55;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=CBL-interacting serine/threonine-protein kinase 19;
DE EC=2.7.11.1;
DE AltName: Full=SNF1-related kinase 3.5;
DE AltName: Full=SOS2-like protein kinase PKS21;
GN Name=CIPK19; Synonyms=PKS21, SnRK3.5; OrderedLocusNames=At5g45810;
GN ORFNames=K15I22.1;
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=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;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
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).
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 -!- INTERACTION:
CC Q9FJ55; Q9ZR37: DSPTP1; NbExp=3; IntAct=EBI-16967606, EBI-25512239;
CC Q9FJ55; Q38845: PP2AA1; NbExp=3; IntAct=EBI-16967606, EBI-1645478;
CC Q9FJ55; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-16967606, EBI-15192297;
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; AY030303; AAK50347.1; -; mRNA.
DR EMBL; AB016870; BAB09309.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95302.1; -; Genomic_DNA.
DR EMBL; DQ447041; ABE66223.1; -; mRNA.
DR RefSeq; NP_199393.1; NM_123949.2.
DR AlphaFoldDB; Q9FJ55; -.
DR SMR; Q9FJ55; -.
DR BioGRID; 19870; 4.
DR IntAct; Q9FJ55; 4.
DR STRING; 3702.AT5G45810.1; -.
DR PaxDb; Q9FJ55; -.
DR PRIDE; Q9FJ55; -.
DR ProteomicsDB; 246861; -.
DR EnsemblPlants; AT5G45810.1; AT5G45810.1; AT5G45810.
DR GeneID; 834621; -.
DR Gramene; AT5G45810.1; AT5G45810.1; AT5G45810.
DR KEGG; ath:AT5G45810; -.
DR Araport; AT5G45810; -.
DR TAIR; locus:2152370; AT5G45810.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR InParanoid; Q9FJ55; -.
DR OMA; MEYDEFC; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q9FJ55; -.
DR PRO; PR:Q9FJ55; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJ55; baseline and differential.
DR Genevisible; Q9FJ55; 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..483
FT /note="CBL-interacting serine/threonine-protein kinase 19"
FT /id="PRO_0000337220"
FT DOMAIN 28..282
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 340..364
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 168..197
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 313..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..396
FT /note="PPI"
FT /evidence="ECO:0000250"
FT REGION 459..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 150
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 34..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93V58"
FT MOD_RES 186
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
SQ SEQUENCE 483 AA; 54616 MW; 2CF0E948F2A07BF9 CRC64;
MADLLRKVKS IKKKQDQSNH QALILGKYEM GRLLGHGTFA KVYLARNAQS GESVAIKVID
KEKVLKSGLI AHIKREISIL RRVRHPNIVQ LFEVMATKSK IYFVMEYVKG GELFNKVAKG
RLKEEMARKY FQQLISAVSF CHFRGVYHRD LKPENLLLDE NGNLKVSDFG LSAVSDQIRQ
DGLFHTFCGT PAYVAPEVLA RKGYDGAKVD IWSCGVILFV LMAGFLPFHD RNVMAMYKKI
YRGDFRCPRW FPVEINRLLI RMLETKPERR FTMPDIMETS WFKKGFKHIK FYVEDDHQLC
NVADDDEIES IESVSGRSST VSEPEDFESF DGRRRGGSMP RPASLNAFDL ISFSPGFDLS
GLFEDDGEGS RFVSGAPVGQ IISKLEEIAR IVSFTVRKKD CKVSLEGSRE GSMKGPLSIA
AEIFELTPAL VVVEVKKKGG DKMEYDEFCN KELKPKLQNL SSENGQRVSG SRSLPSFLLS
DTD
