ID CDPKB_ARATH Reviewed; 495 AA. AC Q39016; Q949P0; Q9LQH7; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 03-MAY-2011, sequence version 2. DT 27-MAR-2024, entry version 179. DE RecName: Full=Calcium-dependent protein kinase 11; DE EC=2.7.11.1; DE AltName: Full=Calcium-dependent protein kinase isoform CDPK2; DE Short=AtCDPK2; GN Name=CPK11; Synonyms=CDPK2; OrderedLocusNames=At1g35670; GN ORFNames=F15O4.8; 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], FUNCTION, AND INDUCTION. RX PubMed=8078458; DOI=10.1007/bf00286684; RA Urao T., Katagiri T., Mizoguchi T., Yamaguchi-Shinozaki K., Hayashida N., RA Shinozaki K.; RT "Two genes that encode Ca(2+)-dependent protein kinases are induced by RT drought and high-salt stresses in Arabidopsis thaliana."; RL Mol. Gen. Genet. 244:331-340(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., RA Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."; RL Nature 408:816-820(2000). 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. RA Harmon A.C., Gribskov M., Gubrium E., Harper J.F.; RT "The CDPK superfamily of protein kinases."; RL New Phytol. 151:175-183(2001). RN [6] RP GENE FAMILY, AND NOMENCLATURE. RX PubMed=12068094; DOI=10.1104/pp.005645; RA Cheng S.-H., Willmann M.R., Chen H.-C., Sheen J.; RT "Calcium signaling through protein kinases. The Arabidopsis calcium- RT dependent protein kinase gene family."; RL Plant Physiol. 129:469-485(2002). RN [7] 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 [8] RP INTERACTION WITH DI19, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-150; RP ASP-171 AND PHE-306. RX PubMed=16438971; DOI=10.1016/j.febslet.2006.01.013; RA Rodriguez Milla M.A., Uno Y., Chang I.-F., Townsend J., Maher E.A., RA Quilici D., Cushman J.C.; RT "A novel yeast two-hybrid approach to identify CDPK substrates: RT characterization of the interaction between AtCPK11 and AtDi19, a nuclear RT zinc finger protein."; RL FEBS Lett. 580:904-911(2006). RN [9] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=17921317; DOI=10.1105/tpc.107.050666; RA Zhu S.-Y., Yu X.-C., Wang X.-J., Zhao R., Li Y., Fan R.-C., Shang Y., RA Du S.-Y., Wang X.-F., Wu F.-Q., Xu Y.-H., Zhang X.-Y., Zhang D.-P.; RT "Two calcium-dependent protein kinases, CPK4 and CPK11, regulate abscisic RT acid signal transduction in Arabidopsis."; RL Plant Cell 19:3019-3036(2007). CC -!- FUNCTION: May play a role in signal transduction pathways that involve CC calcium as a second messenger. Functions as a regulator of the calcium- CC mediated abscisic acid (ABA) signaling pathway. Phosphorylates ABA- CC responsive transcription factors ABF1 and ABF4 in vitro. CC {ECO:0000269|PubMed:17921317, ECO:0000269|PubMed:8078458}. 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 -!- ACTIVITY REGULATION: Activated by calcium. Autophosphorylation may play CC an important role in the regulation of the kinase activity (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with Di19. {ECO:0000269|PubMed:16438971}. CC -!- INTERACTION: CC Q39016; Q9ZSK4: ADF3; NbExp=5; IntAct=EBI-979321, EBI-2009725; CC Q39016; Q9C944: At1g52740; NbExp=9; IntAct=EBI-979321, EBI-1537419; CC Q39016; Q27GK5: At3g26510; NbExp=5; IntAct=EBI-979321, EBI-2297208; CC Q39016; Q940C2: At5g52550; NbExp=6; IntAct=EBI-979321, EBI-2298422; CC Q39016; Q94BN0: BT2; NbExp=7; IntAct=EBI-979321, EBI-540986; CC Q39016; Q9CA67: CHLP; NbExp=5; IntAct=EBI-979321, EBI-2298544; CC Q39016; Q39083: DI19-1; NbExp=25; IntAct=EBI-979321, EBI-979339; CC Q39016; O23338: HSP1; NbExp=6; IntAct=EBI-979321, EBI-2296482; CC Q39016; O80800: MTACP2; NbExp=4; IntAct=EBI-979321, EBI-2298689; CC Q39016; O23680: TOC33; NbExp=4; IntAct=EBI-979321, EBI-639377; CC Q39016; O04482: UCH2; NbExp=4; IntAct=EBI-979321, EBI-2298606; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16438971}. Nucleus CC {ECO:0000269|PubMed:16438971}. CC -!- INDUCTION: By drought and high-slat stress, but not by low-temperature, CC heat stress or abscisic acid treatment. {ECO:0000269|PubMed:8078458}. CC -!- DOMAIN: There are 3 contiguous domains conserved in the CDPK subfamily: CC a kinase domain, an autoinhibitory (junction) domain and a calmodulin- CC like domain. The autoinhibitory domain (290-320) inactivates kinase CC activity under calcium-free conditions (By similarity). {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: Mutant cpk11-2 shows reduced ABA and salt CC responsiveness in seed germination. {ECO:0000269|PubMed:17921317}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. CDPK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF79386.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D21806; BAA04830.1; -; mRNA. DR EMBL; AC007887; AAF79386.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002684; AEE31822.1; -; Genomic_DNA. DR EMBL; AY050981; AAK93658.1; -; mRNA. DR EMBL; AY113986; AAM45034.1; -; mRNA. DR PIR; S46284; S46284. DR RefSeq; NP_174807.1; NM_103271.4. DR AlphaFoldDB; Q39016; -. DR SMR; Q39016; -. DR BioGRID; 25703; 35. DR IntAct; Q39016; 25. DR MINT; Q39016; -. DR STRING; 3702.Q39016; -. DR iPTMnet; Q39016; -. DR PaxDb; 3702-AT1G35670-1; -. DR ProteomicsDB; 224453; -. DR EnsemblPlants; AT1G35670.1; AT1G35670.1; AT1G35670. DR GeneID; 840471; -. DR Gramene; AT1G35670.1; AT1G35670.1; AT1G35670. DR KEGG; ath:AT1G35670; -. DR Araport; AT1G35670; -. DR TAIR; AT1G35670; CDPK2. DR eggNOG; KOG0032; Eukaryota. DR HOGENOM; CLU_000288_37_4_1; -. DR InParanoid; Q39016; -. DR OMA; HINWISH; -. DR OrthoDB; 655312at2759; -. DR PRO; PR:Q39016; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q39016; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:TAIR. DR GO; GO:0005634; C:nucleus; IDA:TAIR. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA:TAIR. DR GO; GO:0004672; F:protein kinase activity; IDA: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:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:TAIR. DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR. DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR. DR GO; GO:1901979; P:regulation of inward rectifier potassium channel activity; IDA:TAIR. DR GO; GO:0080092; P:regulation of pollen tube growth; IMP:TAIR. DR CDD; cd00051; EFh; 1. DR CDD; cd05117; STKc_CAMK; 1. DR Gene3D; 1.10.238.10; EF-hand; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR002048; EF_hand_dom. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24349:SF192; CALCIUM-DEPENDENT PROTEIN KINASE 11; 1. DR PANTHER; PTHR24349; SERINE/THREONINE-PROTEIN KINASE; 1. DR Pfam; PF13499; EF-hand_7; 2. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00054; EFh; 4. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF47473; EF-hand; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00018; EF_HAND_1; 4. DR PROSITE; PS50222; EF_HAND_2; 4. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; Q39016; AT. PE 1: Evidence at protein level; KW ATP-binding; Calcium; Cytoplasm; Kinase; Metal-binding; Nucleotide-binding; KW Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..495 FT /note="Calcium-dependent protein kinase 11" FT /id="PRO_0000304513" FT DOMAIN 26..284 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 327..362 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 363..398 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 399..434 FT /note="EF-hand 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 438..468 FT /note="EF-hand 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT REGION 290..320 FT /note="Autoinhibitory domain" 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 32..40 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 55 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 340 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 342 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 344 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 346 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 351 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 376 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 378 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 380 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 382 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 387 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 412 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 414 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 416 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 418 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 423 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 446 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 448 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 450 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 452 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 457 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT MOD_RES 190 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9FKW4" FT MUTAGEN 150 FT /note="D->A: Loss of activity." FT /evidence="ECO:0000269|PubMed:16438971" FT MUTAGEN 171 FT /note="D->A: Loss of activity." FT /evidence="ECO:0000269|PubMed:16438971" FT MUTAGEN 306 FT /note="F->A: Constitutive activity." FT /evidence="ECO:0000269|PubMed:16438971" FT CONFLICT 403 FT /note="N -> I (in Ref. 1; BAA04830)" FT /evidence="ECO:0000305" FT CONFLICT 410 FT /note="Y -> D (in Ref. 1; BAA04830)" FT /evidence="ECO:0000305" SQ SEQUENCE 495 AA; 55916 MW; 2DD0ED8C234EF2F7 CRC64; METKPNPRRP SNTVLPYQTP RLRDHYLLGK KLGQGQFGTT YLCTEKSTSA NYACKSIPKR KLVCREDYED VWREIQIMHH LSEHPNVVRI KGTYEDSVFV HIVMEVCEGG ELFDRIVSKG HFSEREAVKL IKTILGVVEA CHSLGVMHRD LKPENFLFDS PKDDAKLKAT DFGLSVFYKP GQYLYDVVGS PYYVAPEVLK KCYGPEIDVW SAGVILYILL SGVPPFWAET ESGIFRQILQ GKLDFKSDPW PTISEAAKDL IYKMLERSPK KRISAHEALC HPWIVDEQAA PDKPLDPAVL SRLKQFSQMN KIKKMALRVI AERLSEEEIG GLKELFKMID TDNSGTITFE ELKAGLKRVG SELMESEIKS LMDAADIDNS GTIDYGEFLA ATLHMNKMER EENLVAAFSY FDKDGSGYIT IDELQSACTE FGLCDTPLDD MIKEIDLDND GKIDFSEFTA MMRKGDGVGR SRTMMKNLNF NIADAFGVDG EKSDD //