CIPKF_ARATH
ID CIPKF_ARATH Reviewed; 421 AA.
AC P92937; Q0D240; Q0WQ20; Q9LZW5;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=CBL-interacting serine/threonine-protein kinase 15;
DE EC=2.7.11.1;
DE AltName: Full=SNF1-related kinase 3.1;
DE AltName: Full=SOS-interacting protein 2;
DE AltName: Full=SOS2-like protein kinase PKS3;
DE AltName: Full=Serine/threonine-protein kinase ATPK10;
GN Name=CIPK15; Synonyms=ATPK10, PKS3, SIP2, SnRK3.1;
GN OrderedLocusNames=At5g01810; ORFNames=T20L15_80;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=7824653; DOI=10.1104/pp.106.3.1229;
RA Mizoguchi T., Hayashida N., Yamaguchi-Shinozaki K., Kamada H.,
RA Shinozaki K.;
RT "Cloning and sequencing of a novel serine/threonine protein kinase in
RT Arabidopsis thaliana.";
RL Plant Physiol. 106:1229-1230(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11230129; DOI=10.1093/emboj/20.5.1051;
RA Albrecht V., Ritz O., Linder S., Harter K., Kudla J.;
RT "The NAF domain defines a novel protein-protein interaction module
RT conserved in Ca(2+)-regulated kinases.";
RL EMBO J. 20:1051-1063(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=11402167; DOI=10.2307/3871302;
RA Guo Y., Halfter U., Ishitani M., Zhu J.-K.;
RT "Molecular characterization of functional domains in the protein kinase
RT SOS2 that is required for plant salt tolerance.";
RL Plant Cell 13:1383-1400(2001).
RN [4]
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 [5]
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 [6]
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP INTERACTION WITH CBL4.
RX PubMed=10725350; DOI=10.1073/pnas.97.7.3735;
RA Halfter U., Ishitani M., Zhu J.-K.;
RT "The Arabidopsis SOS2 protein kinase physically interacts with and is
RT activated by the calcium-binding protein SOS3.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3735-3740(2000).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH CBL1; ABI1 AND ABI2.
RX PubMed=12194854; DOI=10.1016/s1534-5807(02)00229-0;
RA Guo Y., Xiong L., Song C.-P., Gong D., Halfter U., Zhu J.-K.;
RT "A calcium sensor and its interacting protein kinase are global regulators
RT of abscisic acid signaling in Arabidopsis.";
RL Dev. Cell 3:233-244(2002).
RN [10]
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. {ECO:0000269|PubMed:12194854}.
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 CBL1/SCaBP5, CBL4/SOS3, ABI1 and ABI2.
CC {ECO:0000269|PubMed:10725350, ECO:0000269|PubMed:12194854}.
CC -!- INTERACTION:
CC P92937; O80575: At2g44050; NbExp=3; IntAct=EBI-537592, EBI-4473692;
CC P92937; Q9LUI0: At3g22810; NbExp=3; IntAct=EBI-537592, EBI-25518150;
CC P92937; Q9LTB8: CBL9; NbExp=3; IntAct=EBI-537592, EBI-637381;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P92937-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Co-expressed with CBL1 in guard cells.
CC {ECO:0000269|PubMed:11402167, ECO:0000269|PubMed:12194854,
CC ECO:0000269|PubMed:7824653}.
CC -!- INDUCTION: Slightly repressed by salt stress.
CC {ECO:0000269|PubMed:11402167}.
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; D30622; BAA06311.1; -; mRNA.
DR EMBL; AF302111; AAK16692.1; -; mRNA.
DR EMBL; AF339144; AAK26842.1; -; mRNA.
DR EMBL; AL162351; CAB82751.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90394.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90395.1; -; Genomic_DNA.
DR EMBL; AK228889; BAF00779.1; -; mRNA.
DR EMBL; BT028964; ABI54339.1; -; mRNA.
DR PIR; T48202; T48202.
DR RefSeq; NP_001031820.1; NM_001036743.1. [P92937-1]
DR RefSeq; NP_195801.1; NM_120259.4. [P92937-1]
DR AlphaFoldDB; P92937; -.
DR SMR; P92937; -.
DR BioGRID; 15835; 11.
DR IntAct; P92937; 5.
DR STRING; 3702.AT5G01810.2; -.
DR PaxDb; P92937; -.
DR PRIDE; P92937; -.
DR EnsemblPlants; AT5G01810.1; AT5G01810.1; AT5G01810. [P92937-1]
DR EnsemblPlants; AT5G01810.2; AT5G01810.2; AT5G01810. [P92937-1]
DR GeneID; 830556; -.
DR Gramene; AT5G01810.1; AT5G01810.1; AT5G01810. [P92937-1]
DR Gramene; AT5G01810.2; AT5G01810.2; AT5G01810. [P92937-1]
DR KEGG; ath:AT5G01810; -.
DR Araport; AT5G01810; -.
DR TAIR; locus:2181047; AT5G01810.
DR eggNOG; KOG0583; Eukaryota.
DR InParanoid; P92937; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; P92937; -.
DR PRO; PR:P92937; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P92937; baseline and differential.
DR Genevisible; P92937; AT.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISS:TAIR.
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:0009738; P:abscisic acid-activated signaling pathway; TAS:TAIR.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
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 Alternative splicing; ATP-binding; Kinase; Manganese; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..421
FT /note="CBL-interacting serine/threonine-protein kinase 15"
FT /id="PRO_0000085876"
FT DOMAIN 12..266
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 299..323
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 152..181
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 328..357
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 CONFLICT 176..178
FT /note="AYV -> TYC (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="K -> R (in Ref. 6; BAF00779)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 421 AA; 47928 MW; FE109AA564776B34 CRC64;
MEKKGSVLML RYEVGKFLGQ GTFAKVYHAR HLKTGDSVAI KVIDKERILK VGMTEQIKRE
ISAMRLLRHP NIVELHEVMA TKSKIYFVME HVKGGELFNK VSTGKLREDV ARKYFQQLVR
AVDFCHSRGV CHRDLKPENL LLDEHGNLKI SDFGLSALSD SRRQDGLLHT TCGTPAYVAP
EVISRNGYDG FKADVWSCGV ILFVLLAGYL PFRDSNLMEL YKKIGKAEVK FPNWLAPGAK
RLLKRILDPN PNTRVSTEKI MKSSWFRKGL QEEVKESVEE ETEVDAEAEG NASAEKEKKR
CINLNAFEII SLSTGFDLSG LFEKGEEKEE MRFTSNREAS EITEKLVEIG KDLKMKVRKK
EHEWRVKMSA EATVVEAEVF EIAPSYHMVV LKKSGGDTAE YKRVMKESIR PALIDFVLAW
H
