CIPKM_ARATH
ID CIPKM_ARATH Reviewed; 431 AA.
AC O80902; F4ISZ4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=CBL-interacting serine/threonine-protein kinase 22;
DE EC=2.7.11.1;
DE AltName: Full=SNF1-related kinase 3.19;
DE AltName: Full=SOS2-like protein kinase PKS14;
GN Name=CIPK22; Synonyms=PKS14, SnRK3.19; OrderedLocusNames=At2g38490;
GN ORFNames=T19C21.2, T6A23.31;
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 (NOV-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;
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 [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 O80902; O80575: At2g44050; NbExp=3; IntAct=EBI-4453230, EBI-4473692;
CC O80902; Q8H0T5: ERF073; NbExp=4; IntAct=EBI-4453230, EBI-4475239;
CC O80902; Q9CA27: ERF118; NbExp=5; IntAct=EBI-4453230, EBI-25513289;
CC O80902; Q9LUA2: ERF119; NbExp=3; IntAct=EBI-4453230, EBI-15393651;
CC O80902; Q38829: IAA11; NbExp=4; IntAct=EBI-4453230, EBI-2367923;
CC O80902; Q8H174: IAA31; NbExp=3; IntAct=EBI-4453230, EBI-3946408;
CC O80902; Q9SSA8: RAP2-12; NbExp=3; IntAct=EBI-4453230, EBI-4441057;
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; AF450478; AAL47845.1; -; mRNA.
DR EMBL; AC004683; AAM14992.1; -; Genomic_DNA.
DR EMBL; AC005499; AAC67369.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09543.2; -; Genomic_DNA.
DR EMBL; AY091782; AAM10329.1; -; mRNA.
DR EMBL; BT000597; AAN18166.1; -; mRNA.
DR PIR; T02496; T02496.
DR RefSeq; NP_181383.3; NM_129406.4.
DR AlphaFoldDB; O80902; -.
DR SMR; O80902; -.
DR BioGRID; 3773; 15.
DR IntAct; O80902; 14.
DR STRING; 3702.AT2G38490.1; -.
DR PaxDb; O80902; -.
DR PRIDE; O80902; -.
DR ProteomicsDB; 246520; -.
DR DNASU; 818431; -.
DR EnsemblPlants; AT2G38490.1; AT2G38490.1; AT2G38490.
DR GeneID; 818431; -.
DR Gramene; AT2G38490.1; AT2G38490.1; AT2G38490.
DR KEGG; ath:AT2G38490; -.
DR Araport; AT2G38490; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR InParanoid; O80902; -.
DR OMA; TIHEARN; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; O80902; -.
DR PRO; PR:O80902; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80902; baseline and differential.
DR Genevisible; O80902; 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..431
FT /note="CBL-interacting serine/threonine-protein kinase 22"
FT /id="PRO_0000337223"
FT DOMAIN 28..282
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 303..327
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 168..197
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 333..363
FT /note="PPI"
FT /evidence="ECO:0000250"
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 58
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 431 AA; 48680 MW; 24B5E2F89E88FE72 CRC64;
MAEDSNSSES IIVNVTGDDN KSALFGKYDL GKLLGSGAFA KVYQAEDLQN GGESVAIKVV
QKKRLKDGLT AHVKREISVM RRLRHPHIVL LSEVLATKTK IYFVMELAKG GELFSRVTSN
RFTESLSRKY FRQLISAVRY CHARGVFHRD LKPENLLLDE NRDLKVSDFG LSAMKEQIHP
DGMLHTLCGT PAYVAPELLL KKGYDGSKAD IWSCGVVLFL LNAGYLPFRD PNIMGLYRKI
HKAQYKLPDW TSSDLRKLLR RLLEPNPELR ITVEEILKDP WFNHGVDPSE IIGIQADDYD
LEENGKILNA FDLISSASSS NLSGLFGNFV TPDHCDQFVS DESTAVIMRK VEEVAKQLNL
RIAKKKERAI KLEGPHGVAN VVVKVRRLTN ELVMVEMKNK QRDVGLVWAD ALRQKLRRLI
NQPVYKVPDK P
