CIPKQ_ARATH
ID CIPKQ_ARATH Reviewed; 439 AA.
AC Q84VQ3; Q6ICZ5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=CBL-interacting serine/threonine-protein kinase 26;
DE EC=2.7.11.1;
DE AltName: Full=SNF1-related kinase 3.26;
DE AltName: Full=SOS2-like protein kinase PKS26;
GN Name=CIPK26; Synonyms=PKS26, SnRK3.26; OrderedLocusNames=At5g21326;
GN ORFNames=F13M11;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 220-439.
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP FUNCTION, INTERACTION WITH RBOHF, AND SUBCELLULAR LOCATION.
RX PubMed=23335733; DOI=10.1093/mp/sst009;
RA Drerup M.M., Schluecking K., Hashimoto K., Manishankar P., Steinhorst L.,
RA Kuchitsu K., Kudla J.;
RT "The Calcineurin B-like calcium sensors CBL1 and CBL9 together with their
RT interacting protein kinase CIPK26 regulate the Arabidopsis NADPH oxidase
RT RBOHF.";
RL Mol. Plant 6:559-569(2013).
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. Involved in the calcium-dependent regulation of reactive oxygen
CC species production by the NADPH oxidase RBOHF.
CC {ECO:0000269|PubMed:23335733}.
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: Interacts with RBOHF (via N-terminus).
CC {ECO:0000269|PubMed:23335733}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23335733}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO73884.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC140977; AAO73884.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92948.1; -; Genomic_DNA.
DR EMBL; BT014878; AAT41861.1; -; mRNA.
DR RefSeq; NP_850861.2; NM_180530.3.
DR AlphaFoldDB; Q84VQ3; -.
DR SMR; Q84VQ3; -.
DR BioGRID; 17521; 13.
DR STRING; 3702.AT5G21326.1; -.
DR iPTMnet; Q84VQ3; -.
DR PaxDb; Q84VQ3; -.
DR PRIDE; Q84VQ3; -.
DR ProteomicsDB; 246692; -.
DR EnsemblPlants; AT5G21326.1; AT5G21326.1; AT5G21326.
DR GeneID; 832246; -.
DR Gramene; AT5G21326.1; AT5G21326.1; AT5G21326.
DR KEGG; ath:AT5G21326; -.
DR Araport; AT5G21326; -.
DR TAIR; locus:1005716172; AT5G21326.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR OMA; HGRMMEN; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q84VQ3; -.
DR PRO; PR:Q84VQ3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84VQ3; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; 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; Cell membrane; Kinase; Manganese; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..439
FT /note="CBL-interacting serine/threonine-protein kinase 26"
FT /id="PRO_0000337226"
FT DOMAIN 13..268
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 306..330
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 154..183
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 336..365
FT /note="PPI"
FT /evidence="ECO:0000250"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 19..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93V58"
FT MOD_RES 172
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
SQ SEQUENCE 439 AA; 49629 MW; 305C6FBBCBE23C60 CRC64;
MNRPKVQRRV GKYEVGKTLG QGTFAKVRCA VNTETGERVA LKILDKEKVL KHKMAEQIRR
EICTMKLINH PNVVRLYEVL ASKTKIYIVL EFGTGGELFD KIVHDGRLKE ENARKYFQQL
INAVDYCHSR GVYHRDLKPE NLLLDAQGNL KVSDFGLSAL SRQVRGDGLL HTACGTPNYA
APEVLNDQGY DGATADLWSC GVILFVLLAG YLPFEDSNLM TLYKKIIAGE YHCPPWLSPG
AKNLIVRILD PNPMTRITIP EVLGDAWFKK NYKPAVFEEK EEANLDDVDA VFKDSEEHHV
TEKKEEQPTS MNAFELISMS RALDLGNLFE EEEGFKRETR FAAKGAANDL VQKIEEASKP
LGFDIQKKNY KMRLENVTAG RKGNLRVATE IFQVSPSLHM IEVRKTKGDT LEFHKFYKKL
STSLNDVVWK SGESSGLSK
