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 28-FEB-2018, entry version 146. 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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 RT gene 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., 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 [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Portal (Araport); RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. 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., 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 [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., 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). 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., RA Harmon A.C., Pickard B.G., Harper J.F.; RT "Subcellular targeting of nine calcium-dependent protein kinase RT isoforms 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., RA Andreasson E., Rathjen J.P., Peck S.C.; RT "Phosphoproteomic analysis of nuclei-enriched fractions from RT Arabidopsis thaliana."; RL J. Proteomics 72:439-451(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526, AND IDENTIFICATION RP BY 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 CC involve calcium as a second messenger. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- ENZYME REGULATION: Activated by calcium. Autophosphorylation may CC play an important role in the regulation of the kinase activity CC (By 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 Note=No experimental confirmation available.; CC -!- DOMAIN: There are 3 contiguous domains conserved in the CDPK CC subfamily: a kinase domain, an autoinhibitory (junction) domain CC and a calmodulin-like domain. The autoinhibitory domain (321-351) CC inactivates kinase activity under calcium-free conditions (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr CC protein kinase family. CDPK subfamily. {ECO:0000255|PROSITE- CC 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 UniGene; At.433; -. DR ProteinModelPortal; Q42438; -. DR SMR; Q42438; -. DR BioGrid; 17341; 1. DR STRING; 3702.AT5G19450.1; -. DR iPTMnet; Q42438; -. DR SwissPalm; Q42438; -. DR PaxDb; Q42438; -. DR PRIDE; Q42438; -. 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; locus:2150230; AT5G19450. DR eggNOG; KOG0032; Eukaryota. DR eggNOG; ENOG410XRMJ; LUCA. DR HOGENOM; HOG000233030; -. DR KO; K13412; -. DR OMA; SWIQNAK; -. DR OrthoDB; EOG093605YU; -. DR PhylomeDB; Q42438; -. DR Reactome; R-ATH-3371571; HSF1-dependent transactivation. DR Reactome; R-ATH-4086398; Ca2+ pathway. DR Reactome; R-ATH-442729; CREB phosphorylation through the activation of CaMKII. DR Reactome; R-ATH-5578775; Ion homeostasis. DR Reactome; R-ATH-936837; Ion transport by P-type ATPases. DR PRO; PR:Q42438; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; Q42438; baseline and differential. DR Genevisible; Q42438; AT. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; 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:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central. DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central. DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IBA:GO_Central. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central. DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central. DR CDD; cd00051; EFh; 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 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; SSF47473; 1. DR SUPFAM; SSF56112; SSF56112; 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; KW Complete proteome; Kinase; Lipoprotein; Membrane; Metal-binding; KW Myristate; Nucleotide-binding; Phosphoprotein; Reference proteome; KW Repeat; Serine/threonine-protein kinase; Transferase. FT INIT_MET 1 1 Removed. {ECO:0000255}. FT CHAIN 2 533 Calcium-dependent protein kinase 8. FT /FTId=PRO_0000363333. FT DOMAIN 57 315 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT DOMAIN 358 394 EF-hand 1. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT DOMAIN 395 430 EF-hand 2. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT DOMAIN 431 466 EF-hand 3. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT DOMAIN 467 502 EF-hand 4. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT NP_BIND 63 71 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT CA_BIND 371 382 1. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT CA_BIND 408 419 2. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT CA_BIND 444 455 3. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT CA_BIND 480 491 4. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT REGION 321 351 Autoinhibitory domain. {ECO:0000250}. FT ACT_SITE 181 181 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027}. FT BINDING 86 86 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT MOD_RES 221 221 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9FKW4}. FT MOD_RES 488 488 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9FKW4}. FT MOD_RES 526 526 Phosphoserine. FT {ECO:0000244|PubMed:19376835}. FT LIPID 2 2 N-myristoyl glycine. {ECO:0000255}. FT VAR_SEQ 1 55 Missing (in isoform 2). FT {ECO:0000303|Ref.4}. FT /FTId=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 //