CDPKU_ARATH
ID CDPKU_ARATH Reviewed; 541 AA.
AC Q9SSF8; Q9SBZ3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Calcium-dependent protein kinase 30;
DE EC=2.7.11.1;
DE AltName: Full=Calcium-dependent protein kinase isoform CDPK1a;
DE Short=AtCDPK1a;
GN Name=CPK30; Synonyms=CDPK1A; OrderedLocusNames=At1g74740;
GN ORFNames=F25A4.29;
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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-322, FUNCTION, AND MUTAGENESIS OF LYS-92.
RX PubMed=8943201; DOI=10.1126/science.274.5294.1900;
RA Sheen J.;
RT "Ca2+-dependent protein kinases and stress signal transduction in plants.";
RL Science 274:1900-1902(1996).
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).
CC -!- FUNCTION: May play a role in signal transduction pathways that involve
CC calcium as a second messenger. May be a positive regulator controlling
CC stress signal transduction. Acts as a calcium sensor involved in the
CC hormone-signaling pathways. {ECO:0000269|PubMed:8943201}.
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 -!- INTERACTION:
CC Q9SSF8; P25854: CAM4; NbExp=2; IntAct=EBI-1235738, EBI-1235664;
CC Q9SSF8; P59220: CAM7; NbExp=2; IntAct=EBI-1235738, EBI-1236031;
CC Q9SSF8; Q9S744: CML9; NbExp=2; IntAct=EBI-1235738, EBI-1236048;
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
CC -!- TISSUE SPECIFICITY: Highly expressed in root.
CC -!- INDUCTION: Induced by ABA, IAA, 2,4-D, GA(3) and 6-BA treatment.
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 (323-353) 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}.
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DR EMBL; AC008263; AAD55274.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35628.1; -; Genomic_DNA.
DR EMBL; AY140016; AAM98158.1; -; mRNA.
DR EMBL; BT008900; AAP68339.1; -; mRNA.
DR EMBL; U73610; AAF14337.1; -; mRNA.
DR PIR; F96776; F96776.
DR RefSeq; NP_177612.2; NM_106132.4.
DR AlphaFoldDB; Q9SSF8; -.
DR SMR; Q9SSF8; -.
DR BioGRID; 29032; 11.
DR IntAct; Q9SSF8; 10.
DR STRING; 3702.AT1G74740.1; -.
DR iPTMnet; Q9SSF8; -.
DR PaxDb; Q9SSF8; -.
DR PRIDE; Q9SSF8; -.
DR ProteomicsDB; 224396; -.
DR EnsemblPlants; AT1G74740.1; AT1G74740.1; AT1G74740.
DR GeneID; 843813; -.
DR Gramene; AT1G74740.1; AT1G74740.1; AT1G74740.
DR KEGG; ath:AT1G74740; -.
DR Araport; AT1G74740; -.
DR TAIR; locus:2027227; AT1G74740.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_4_1; -.
DR InParanoid; Q9SSF8; -.
DR OMA; VIIDIMR; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q9SSF8; -.
DR PRO; PR:Q9SSF8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SSF8; baseline and differential.
DR Genevisible; Q9SSF8; 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; IBA:GO_Central.
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:0004672; F:protein kinase activity; TAS:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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: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; 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.
PE 1: Evidence at protein level;
KW ATP-binding; Calcium; Kinase; Lipoprotein; Membrane; Metal-binding;
KW Myristate; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..541
FT /note="Calcium-dependent protein kinase 30"
FT /id="PRO_0000304515"
FT DOMAIN 59..317
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 360..395
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 396..431
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 432..467
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 468..503
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 11..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..353
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 14..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 65..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 373
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 375
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 377
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 379
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 415
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 420
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 445
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 449
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 451
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 456
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 481
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 485
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 487
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 492
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW4"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW4"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT MUTAGEN 92
FT /note="K->M: Loss of function."
FT /evidence="ECO:0000269|PubMed:8943201"
FT CONFLICT 50..53
FT /note="SHQS -> ANQT (in Ref. 4; AAF14337)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="N -> T (in Ref. 4; AAF14337)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="D -> G (in Ref. 4; AAF14337)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 61404 MW; 7D170F76BAFCB4C4 CRC64;
MGNCIACVKF DPDNSKPNQK KKPPRGRQRN PYDDPDGLRT HAPLRVIPMS HQSQISDKYI
LGRELGRGEF GITYLCTDRE TREALACKSI SKRKLRTAVD VEDVRREVTI MSTLPEHPNV
VKLKATYEDN ENVHLVMELC EGGELFDRIV ARGHYTERAA ATVARTIAEV VRMCHVNGVM
HRDLKPENFL FANKKENSAL KAIDFGLSVL FKPGERFTEI VGSPYYMAPE VLKRNYGPEV
DVWSAGVILY ILLCGVPPFW AETEQGVALA ILRGVLDFKR DPWSQISESA KSLVKQMLEP
DSTKRLTAQQ VLDHPWIQNA KKAPNVPLGD IVRSRLKQFS MMNRLKKKAL RVIAEHLSIQ
EVEVIRNMFT LMDDDNDGKI SYLELRAGLR KVGSQLGEPE IKLLMEVADV NGNGCLDYGE
FVAVIIHLQK MENDEHFRQA FMFFDKDGSG YIESEELREA LTDELGEPDN SVIIDIMREV
DTDKDGKINY DEFVVMMKAG TDWRKASRQY SRERFKSLSL NLMKDGSMHL HDALTGQSIA
V
