(data stored in ACNUC13479 zone)

SWISSPROT: 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   30-AUG-2017, entry version 127.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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=10.1105/tpc.13.6.1383;
RA   Guo Y., Halfter U., Ishitani M., Zhu J.-K.;
RT   "Molecular characterization of functional domains in the protein
RT   kinase 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.,
RA   Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA   Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA   Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA   Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA   Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA   Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA   Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA   Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA   Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA   Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA   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.,
RA   Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA   Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA   van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA   Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA   Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:823-826(2000).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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.,
RA   Hayashizaki Y., 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
RP   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
RT   regulators 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.,
RA   Halford N., Kudla J., Luan S., Nimmo H.G., Sussman M.R., Thomas M.,
RA   Walker-Simmons K., 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
CC       CIPK protein lead to the activation of the kinase in a calcium-
CC       dependent manner. {ECO:0000269|PubMed:12194854}.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
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   -!- 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
CC       cells. {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
CC       of phosphorylation/activation by upstream protein kinases. The PPI
CC       motif mediates the interaction with the ABI (abscisic acid-
CC       insensitive) phosphatases (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. SNF1 subfamily. {ECO:0000305}.
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   UniGene; At.20284; -.
DR   ProteinModelPortal; P92937; -.
DR   SMR; P92937; -.
DR   BioGrid; 15835; 8.
DR   IntAct; P92937; 2.
DR   STRING; 3702.AT5G01810.1; -.
DR   PaxDb; 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.
DR   Gramene; AT5G01810.2; AT5G01810.2; AT5G01810.
DR   KEGG; ath:AT5G01810; -.
DR   Araport; AT5G01810; -.
DR   TAIR; locus:2181047; AT5G01810.
DR   eggNOG; KOG0583; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   HOGENOM; HOG000233016; -.
DR   InParanoid; P92937; -.
DR   OMA; FVMEHVK; -.
DR   OrthoDB; EOG093608Y0; -.
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:0005622; C:intracellular; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; ISS:TAIR.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR   InterPro; IPR020636; Ca/CaM-dep_Ca-dep_prot_Kinase.
DR   InterPro; IPR011009; Kinase-like_dom.
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   PANTHER; PTHR24347; PTHR24347; 1.
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;
DR   PRODOM; P92937.
DR   SWISS-2DPAGE; P92937.
KW   Alternative splicing; ATP-binding; Complete proteome; Kinase;
KW   Manganese; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    421       CBL-interacting serine/threonine-protein
FT                                kinase 15.
FT                                /FTId=PRO_0000085876.
FT   DOMAIN       12    266       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   DOMAIN      299    323       NAF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00256}.
FT   NP_BIND      18     26       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   REGION      152    181       Activation loop. {ECO:0000250}.
FT   REGION      328    357       PPI. {ECO:0000250}.
FT   ACT_SITE    134    134       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING      41     41       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     156    156       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q93V58}.
FT   MOD_RES     170    170       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q38997}.
FT   CONFLICT    176    178       AYV -> TYC (in Ref. 1, 2 and 3).
FT                                {ECO:0000305}.
FT   CONFLICT    230    230       K -> R (in Ref. 6; BAF00779).
FT                                {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
//

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