ID CDPK8_ARATH Reviewed; 533 AA. AC Q42438; Q0WUS5; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 180. DE RecName: Full=Calcium-dependent protein kinase 8; DE EC=2.7.11.1; DE AltName: Full=Calcium-dependent protein kinase isoform CDPK19; DE Short=AtCDPK19; GN Name=CPK8; Synonyms=CDPK19; OrderedLocusNames=At5g19450; GN ORFNames=F7K24.200; 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 [GENOMIC DNA / MRNA] (ISOFORM 1). RC STRAIN=Columbia; RX PubMed=8704134; DOI=10.1007/bf00019557; RA Hong Y., Takano M., Liu C.-M., Gasch A., Chye M.-L., Chua N.-H.; RT "Expression of three members of the calcium-dependent protein kinase gene RT family in Arabidopsis thaliana."; RL Plant Mol. Biol. 30:1259-1275(1996). RN [2] 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 [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 2). 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 [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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=cv. La-0; RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200; RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.; RT "Large-scale analysis of in vivo phosphorylated membrane proteins by RT immobilized metal ion affinity chromatography and mass spectrometry."; RL Mol. Cell. Proteomics 2:1234-1243(2003). RN [8] 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 [9] RP SUBCELLULAR LOCATION. RX PubMed=12913141; DOI=10.1104/pp.103.020008; RA Dammann C., Ichida A., Hong B., Romanowsky S.M., Hrabak E.M., Harmon A.C., RA Pickard B.G., Harper J.F.; RT "Subcellular targeting of nine calcium-dependent protein kinase isoforms RT from Arabidopsis."; RL Plant Physiol. 132:1840-1848(2003). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15308754; DOI=10.1105/tpc.104.023150; RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.; RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new RT phosphorylation site database."; RL Plant Cell 16:2394-2405(2004). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=cv. Columbia; RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004; RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., RA Rathjen J.P., Peck S.C.; RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis RT thaliana."; RL J. Proteomics 72:439-451(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19376835; DOI=10.1104/pp.109.138677; RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., RA Grossmann J., Gruissem W., Baginsky S.; RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel RT chloroplast kinase substrates and phosphorylation networks."; RL Plant Physiol. 150:889-903(2009). CC -!- FUNCTION: May play a role in signal transduction pathways that involve CC calcium as a second messenger. 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12913141}; CC Lipid-anchor {ECO:0000269|PubMed:12913141}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q42438-1; Sequence=Displayed; CC Name=2; CC IsoId=Q42438-2; Sequence=VSP_036290; 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 (321-351) inactivates kinase CC activity under calcium-free conditions (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. CDPK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}. 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; U20624; AAA67655.1; -; mRNA. DR EMBL; U20627; AAA67658.1; -; Genomic_DNA. DR EMBL; AF296837; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CP002688; AED92708.1; -; Genomic_DNA. DR EMBL; CP002688; AED92709.1; -; Genomic_DNA. DR EMBL; AK227066; BAE99123.1; -; mRNA. DR PIR; S71778; S71778. DR RefSeq; NP_197446.1; NM_121950.3. [Q42438-1] DR RefSeq; NP_850853.1; NM_180522.3. [Q42438-1] DR AlphaFoldDB; Q42438; -. DR SMR; Q42438; -. DR BioGRID; 17341; 5. DR STRING; 3702.Q42438; -. DR iPTMnet; Q42438; -. DR SwissPalm; Q42438; -. DR PaxDb; 3702-AT5G19450-2; -. DR ProteomicsDB; 220468; -. [Q42438-1] DR EnsemblPlants; AT5G19450.1; AT5G19450.1; AT5G19450. [Q42438-1] DR EnsemblPlants; AT5G19450.2; AT5G19450.2; AT5G19450. [Q42438-1] DR GeneID; 832065; -. DR Gramene; AT5G19450.1; AT5G19450.1; AT5G19450. [Q42438-1] DR Gramene; AT5G19450.2; AT5G19450.2; AT5G19450. [Q42438-1] DR KEGG; ath:AT5G19450; -. DR Araport; AT5G19450; -. DR TAIR; AT5G19450; CDPK19. DR eggNOG; KOG0032; Eukaryota. DR HOGENOM; CLU_000288_37_4_1; -. DR InParanoid; Q42438; -. DR OMA; RMNESEM; -. DR OrthoDB; 655312at2759; -. DR PhylomeDB; Q42438; -. DR PRO; PR:Q42438; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; Q42438; baseline and differential. DR Genevisible; Q42438; AT. DR GO; GO:0005886; C:plasma membrane; HDA:TAIR. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. 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:SF553; CALCIUM-DEPENDENT PROTEIN KINASE 8; 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; 3. 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. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Calcium; Cell membrane; Kinase; KW Lipoprotein; Membrane; Metal-binding; Myristate; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Repeat; KW Serine/threonine-protein kinase; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000255" FT CHAIN 2..533 FT /note="Calcium-dependent protein kinase 8" FT /id="PRO_0000363333" FT DOMAIN 57..315 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 358..394 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 395..430 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 431..466 FT /note="EF-hand 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 467..502 FT /note="EF-hand 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 321..351 FT /note="Autoinhibitory domain" FT /evidence="ECO:0000250" FT ACT_SITE 181 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 63..71 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 86 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 371 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 375 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 377 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 382 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 408 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 410 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="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 414 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 419 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 444 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="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 448 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 450 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 455 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 480 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 482 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 484 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 486 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 491 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT MOD_RES 221 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9FKW4" FT MOD_RES 488 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9FKW4" FT MOD_RES 526 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19376835" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..55 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_036290" SQ SEQUENCE 533 AA; 59941 MW; 8E9D9DD090C9FD1A CRC64; MGNCCASPGS ETGSKKGKPK IKSNPFYSEA YTTNGSGTGF KLSVLKDPTG HDISLMYDLG REVGRGEFGI TYLCTDIKTG EKYACKSISK KKLRTAVDIE DVRREVEIMK HMPRHPNIVS LKDAFEDDDA VHIVMELCEG GELFDRIVAR GHYTERAAAA VMKTILEVVQ ICHKHGVMHR DLKPENFLFA NKKETSALKA IDFGLSVFFK PGEGFNEIVG SPYYMAPEVL RRNYGPEVDI WSAGVILYIL LCGVPPFWAE TEQGVAQAII RSVIDFKRDP WPRVSETAKD LVRKMLEPDP KKRLSAAQVL EHSWIQNAKK APNVSLGETV KARLKQFSVM NKLKKRALRV IAEHLSVEEV AGIKEAFEMM DSKKTGKINL EELKFGLHKL GQQQIPDTDL QILMEAADVD GDGTLNYGEF VAVSVHLKKM ANDEHLHKAF SFFDQNQSDY IEIEELREAL NDEVDTNSEE VVAAIMQDVD TDKDGRISYE EFAAMMKAGT DWRKASRQYS RERFNSLSLK LMREGSLQLE GEN //