CIPK8_ARATH
ID CIPK8_ARATH Reviewed; 445 AA.
AC Q9STV4; A8MR95; Q9C5S5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=CBL-interacting serine/threonine-protein kinase 8;
DE EC=2.7.11.1;
DE AltName: Full=SNF1-related kinase 3.13;
DE AltName: Full=SOS2-like protein kinase PKS11;
GN Name=CIPK8; Synonyms=PKS11, SnRK3.13; OrderedLocusNames=At4g24400;
GN ORFNames=T22A6.230;
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] (ISOFORM 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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] (ISOFORM 1).
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 MUTAGENESIS OF SER-154; THR-162 AND TYR-173, AND TISSUE SPECIFICITY.
RX PubMed=12029080; DOI=10.1074/jbc.m107719200;
RA Gong D., Gong Z., Guo Y., Chen X., Zhu J.-K.;
RT "Biochemical and functional characterization of PKS11, a novel Arabidopsis
RT protein kinase.";
RL J. Biol. Chem. 277:28340-28350(2002).
RN [6]
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 [7]
RP INTERACTION WITH CBL1 AND CBL9.
RX PubMed=14730064; DOI=10.1104/pp.103.033068;
RA Kolukisaoglu U., Weinl S., Blazevic D., Batistic O., Kudla J.;
RT "Calcium sensors and their interacting protein kinases: genomics of the
RT Arabidopsis and rice CBL-CIPK signaling networks.";
RL Plant Physiol. 134:43-58(2004).
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 -!- SUBUNIT: Interacts with CBL1 and CBL9. {ECO:0000269|PubMed:14730064}.
CC -!- INTERACTION:
CC Q9STV4; O81445: CBL1; NbExp=4; IntAct=EBI-2026454, EBI-974530;
CC Q9STV4; Q9LTB8: CBL9; NbExp=8; IntAct=EBI-2026454, EBI-637381;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9STV4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9STV4-2; Sequence=VSP_033982;
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, and, to a lower extent,
CC in leaves, stems, flowers, and siliques. {ECO:0000269|PubMed:12029080}.
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; AF290193; AAK16683.2; -; mRNA.
DR EMBL; AL078637; CAB45075.1; -; Genomic_DNA.
DR EMBL; AL161561; CAB79350.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84899.1; -; Genomic_DNA.
DR EMBL; BT000958; AAN41358.1; -; mRNA.
DR PIR; T09903; T09903.
DR RefSeq; NP_194171.1; NM_118573.4. [Q9STV4-1]
DR AlphaFoldDB; Q9STV4; -.
DR SMR; Q9STV4; -.
DR BioGRID; 13831; 9.
DR IntAct; Q9STV4; 2.
DR STRING; 3702.AT4G24400.1; -.
DR iPTMnet; Q9STV4; -.
DR PaxDb; Q9STV4; -.
DR PRIDE; Q9STV4; -.
DR ProteomicsDB; 246687; -. [Q9STV4-1]
DR EnsemblPlants; AT4G24400.1; AT4G24400.1; AT4G24400. [Q9STV4-1]
DR GeneID; 828542; -.
DR Gramene; AT4G24400.1; AT4G24400.1; AT4G24400. [Q9STV4-1]
DR KEGG; ath:AT4G24400; -.
DR Araport; AT4G24400; -.
DR TAIR; locus:2135962; AT4G24400.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR InParanoid; Q9STV4; -.
DR PhylomeDB; Q9STV4; -.
DR PRO; PR:Q9STV4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9STV4; baseline and differential.
DR Genevisible; Q9STV4; AT.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; TAS:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; HDA:TAIR.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009749; P:response to glucose; TAS:TAIR.
DR GO; GO:0010167; P:response to nitrate; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
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..445
FT /note="CBL-interacting serine/threonine-protein kinase 8"
FT /id="PRO_0000337211"
FT DOMAIN 9..262
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 302..326
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 150..177
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 333..362
FT /note="PPI"
FT /evidence="ECO:0000250"
FT ACT_SITE 132
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 15..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93V58"
FT MOD_RES 166
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
FT VAR_SEQ 388..410
FT /note="VFKVAPSILMVDIQNAAGDAEEY -> QETQKNTLSSTRLFVVSLMTSFGSR
FT QMH (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_033982"
FT MUTAGEN 154
FT /note="S->D: Enhanced kinase activity."
FT /evidence="ECO:0000269|PubMed:12029080"
FT MUTAGEN 162
FT /note="T->D: Strongly enhanced kinase activity, with an
FT optimum pH of 7-7.5 at 30 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:12029080"
FT MUTAGEN 173
FT /note="Y->D: Enhanced kinase activity."
FT /evidence="ECO:0000269|PubMed:12029080"
SQ SEQUENCE 445 AA; 50428 MW; 46636F20F327E709 CRC64;
MVVRKVGKYE LGRTIGEGTF AKVKFAQNTE TGESVAMKIV DRSTIIKRKM VDQIKREISI
MKLVRHPCVV RLYEVLASRT KIYIILEYIT GGELFDKIVR NGRLSESEAR KYFHQLIDGV
DYCHSKGVYH RDLKPENLLL DSQGNLKISD FGLSALPEQG VTILKTTCGT PNYVAPEVLS
HKGYNGAVAD IWSCGVILYV LMAGYLPFDE MDLPTLYSKI DKAEFSCPSY FALGAKSLIN
RILDPNPETR ITIAEIRKDE WFLKDYTPVQ LIDYEHVNLD DVYAAFDDPE EQTYAQDGTR
DTGPLTLNAF DLIILSQGLN LATLFDRGKD SMKHQTRFIS HKPANVVLSS MEVVSQSMGF
KTHIRNYKMR VEGLSANKTS HFSVILEVFK VAPSILMVDI QNAAGDAEEY LKFYKTFCSK
LDDIIWKPPD ASMRNRVTKA KSKRR
