CDPK1_ARATH
ID CDPK1_ARATH Reviewed; 610 AA.
AC Q06850; Q541W0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Calcium-dependent protein kinase 1;
DE Short=AtCDPK 1;
DE Short=CDPK 1;
DE EC=2.7.11.1;
DE AltName: Full=Calcium-dependent protein kinase isoform AK1;
GN Name=CPK1; Synonyms=AK1; OrderedLocusNames=At5g04870; ORFNames=MUK11.19;
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].
RC STRAIN=cv. Columbia;
RX PubMed=7916621; DOI=10.1021/bi00064a010;
RA Harper J.F., Binder B.M., Sussman M.R.;
RT "Calcium and lipid regulation of an Arabidopsis protein kinase expressed in
RT Escherichia coli.";
RL Biochemistry 32:3282-3290(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=8003490; DOI=10.1021/bi00189a031;
RA Harper J.F., Huang J.F., Lloyd S.J.;
RT "Genetic identification of an autoinhibitor in CDPK, a protein kinase with
RT a calmodulin-like domain.";
RL Biochemistry 33:7267-7277(1994).
RN [7]
RP FUNCTION, AND ACTIVATION BY CALCIUM.
RX PubMed=8855961; DOI=10.1021/bi960498a;
RA Huang J.F., Teyton L., Harper J.F.;
RT "Activation of a Ca(2+)-dependent protein kinase involves intramolecular
RT binding of a calmodulin-like regulatory domain.";
RL Biochemistry 35:13222-13230(1996).
RN [8]
RP INTERACTION WITH 14-3-3 PROTEINS.
RX PubMed=9688575; DOI=10.1016/s0014-5793(98)00696-6;
RA Camoni L., Harper J.F., Palmgren M.G.;
RT "14-3-3 proteins activate a plant calcium-dependent protein kinase
RT (CDPK).";
RL FEBS Lett. 430:381-384(1998).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF PHE-436 AND 443-VAL--ILE-444.
RX PubMed=10747788; DOI=10.1021/bi992373m;
RA Vitart V., Christodoulou J., Huang J.F., Chazin W.J., Harper J.F.;
RT "Intramolecular activation of a Ca(2+)-dependent protein kinase is
RT disrupted by insertions in the tether that connects the calmodulin-like
RT domain to the kinase.";
RL Biochemistry 39:4004-4011(2000).
RN [10]
RP FUNCTION.
RX PubMed=10823962; DOI=10.1073/pnas.97.11.6224;
RA Hwang I., Sze H., Harper J.F.;
RT "A calcium-dependent protein kinase can inhibit a calmodulin-stimulated
RT Ca2+ pump (ACA2) located in the endoplasmic reticulum of Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:6224-6229(2000).
RN [11]
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 [12]
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 [13]
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 [14]
RP SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-2, AND PALMITOYLATION AT CYS-5.
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 [15]
RP CALCIUM-BINDING, AND KINASE ACTIVATION.
RX PubMed=15126505; DOI=10.1074/jbc.m401297200;
RA Christodoulou J., Malmendal A., Harper J.F., Chazin W.J.;
RT "Evidence for differing roles for each lobe of the calmodulin-like domain
RT in a calcium-dependent protein kinase.";
RL J. Biol. Chem. 279:29092-29100(2004).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 428-593 IN COMPLEX WITH CALCIUM
RP ION.
RX PubMed=16430916; DOI=10.1016/j.jmb.2005.11.093;
RA Chandran V., Stollar E.J., Lindorff-Larsen K., Harper J.F., Chazin W.J.,
RA Dobson C.M., Luisi B.F., Christodoulou J.;
RT "Structure of the regulatory apparatus of a calcium-dependent protein
RT kinase (CDPK): a novel mode of calmodulin-target recognition.";
RL J. Mol. Biol. 357:400-410(2006).
CC -!- FUNCTION: May play a role in signal transduction pathways that involve
CC calcium as a second messenger. Phosphorylates the Ca(2+)-ATPase ACA2
CC resulting in the inhibition of its calcium activation.
CC {ECO:0000269|PubMed:10747788, ECO:0000269|PubMed:10823962,
CC ECO:0000269|PubMed:8003490, ECO:0000269|PubMed:8855961}.
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.
CC {ECO:0000269|PubMed:8855961}.
CC -!- SUBUNIT: Interacts with 14-3-3 proteins. {ECO:0000269|PubMed:16430916,
CC ECO:0000269|PubMed:9688575}.
CC -!- INTERACTION:
CC Q06850; Q946J8: LHP1; NbExp=3; IntAct=EBI-2357775, EBI-2309089;
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000269|PubMed:12913141}; Lipid-anchor
CC {ECO:0000269|PubMed:12913141}.
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 (414-444) inactivates kinase
CC activity under calcium-free conditions. {ECO:0000269|PubMed:10747788}.
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; L14771; AAA32761.1; -; mRNA.
DR EMBL; AB008271; BAB08991.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90798.1; -; Genomic_DNA.
DR EMBL; AK118706; BAC43300.1; -; mRNA.
DR EMBL; BT005932; AAO64867.1; -; mRNA.
DR PIR; A49082; A49082.
DR RefSeq; NP_196107.1; NM_120569.3.
DR PDB; 2AAO; X-ray; 2.00 A; A/B=428-593.
DR PDBsum; 2AAO; -.
DR AlphaFoldDB; Q06850; -.
DR BMRB; Q06850; -.
DR SMR; Q06850; -.
DR BioGRID; 15645; 65.
DR IntAct; Q06850; 2.
DR STRING; 3702.AT5G04870.1; -.
DR iPTMnet; Q06850; -.
DR PaxDb; Q06850; -.
DR PRIDE; Q06850; -.
DR ProteomicsDB; 241221; -.
DR EnsemblPlants; AT5G04870.1; AT5G04870.1; AT5G04870.
DR GeneID; 830366; -.
DR Gramene; AT5G04870.1; AT5G04870.1; AT5G04870.
DR KEGG; ath:AT5G04870; -.
DR Araport; AT5G04870; -.
DR TAIR; locus:2175503; AT5G04870.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_1_1; -.
DR InParanoid; Q06850; -.
DR OMA; PPEHLTM; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q06850; -.
DR BRENDA; 2.7.11.1; 399.
DR EvolutionaryTrace; Q06850; -.
DR PRO; PR:Q06850; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q06850; baseline and differential.
DR Genevisible; Q06850; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0010857; F:calcium-dependent protein kinase activity; IDA:UniProtKB.
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; 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: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; IDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:0010941; P:regulation of cell death; IMP:TAIR.
DR GO; GO:1900055; P:regulation of leaf senescence; IMP:TAIR.
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 3D-structure; ATP-binding; Calcium; Kinase; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Nucleotide-binding; Palmitate; Peroxisome;
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..610
FT /note="Calcium-dependent protein kinase 1"
FT /id="PRO_0000085827"
FT DOMAIN 150..408
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 451..486
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 487..522
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 523..558
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 559..592
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 17..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..444
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000269|PubMed:10747788"
FT COMPBIAS 70..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 274
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 156..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 464
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15126505, ECO:0000269|PubMed:16430916,
FT ECO:0007744|PDB:2AAO"
FT BINDING 466
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15126505, ECO:0000269|PubMed:16430916,
FT ECO:0007744|PDB:2AAO"
FT BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15126505, ECO:0000269|PubMed:16430916,
FT ECO:0007744|PDB:2AAO"
FT BINDING 470
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15126505, ECO:0000269|PubMed:16430916,
FT ECO:0007744|PDB:2AAO"
FT BINDING 475
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15126505, ECO:0000269|PubMed:16430916,
FT ECO:0007744|PDB:2AAO"
FT BINDING 500
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15126505, ECO:0000269|PubMed:16430916,
FT ECO:0007744|PDB:2AAO"
FT BINDING 502
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15126505, ECO:0000269|PubMed:16430916,
FT ECO:0007744|PDB:2AAO"
FT BINDING 504
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15126505, ECO:0000269|PubMed:16430916,
FT ECO:0007744|PDB:2AAO"
FT BINDING 506
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15126505, ECO:0000269|PubMed:16430916,
FT ECO:0007744|PDB:2AAO"
FT BINDING 511
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15126505, ECO:0000269|PubMed:16430916,
FT ECO:0007744|PDB:2AAO"
FT BINDING 536
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15126505, ECO:0000269|PubMed:16430916,
FT ECO:0007744|PDB:2AAO"
FT BINDING 538
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15126505, ECO:0000269|PubMed:16430916,
FT ECO:0007744|PDB:2AAO"
FT BINDING 540
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15126505, ECO:0000269|PubMed:16430916,
FT ECO:0007744|PDB:2AAO"
FT BINDING 542
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15126505, ECO:0000269|PubMed:16430916,
FT ECO:0007744|PDB:2AAO"
FT BINDING 547
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15126505, ECO:0000269|PubMed:16430916,
FT ECO:0007744|PDB:2AAO"
FT BINDING 570
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15126505, ECO:0000269|PubMed:16430916,
FT ECO:0007744|PDB:2AAO"
FT BINDING 572
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15126505, ECO:0000269|PubMed:16430916,
FT ECO:0007744|PDB:2AAO"
FT BINDING 574
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15126505, ECO:0000269|PubMed:16430916,
FT ECO:0007744|PDB:2AAO"
FT BINDING 576
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15126505, ECO:0000269|PubMed:16430916,
FT ECO:0007744|PDB:2AAO"
FT BINDING 581
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15126505, ECO:0000269|PubMed:16430916,
FT ECO:0007744|PDB:2AAO"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW4"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:12913141"
FT LIPID 5
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:12913141"
FT MUTAGEN 436
FT /note="F->A: Abolishes activation by calcium."
FT /evidence="ECO:0000269|PubMed:10747788"
FT MUTAGEN 443..444
FT /note="VI->AA: Abolishes activation by calcium."
FT /evidence="ECO:0000269|PubMed:10747788"
FT HELIX 434..447
FT /evidence="ECO:0007829|PDB:2AAO"
FT HELIX 450..463
FT /evidence="ECO:0007829|PDB:2AAO"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:2AAO"
FT HELIX 473..479
FT /evidence="ECO:0007829|PDB:2AAO"
FT HELIX 480..483
FT /evidence="ECO:0007829|PDB:2AAO"
FT HELIX 489..499
FT /evidence="ECO:0007829|PDB:2AAO"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:2AAO"
FT HELIX 509..516
FT /evidence="ECO:0007829|PDB:2AAO"
FT HELIX 520..523
FT /evidence="ECO:0007829|PDB:2AAO"
FT HELIX 526..535
FT /evidence="ECO:0007829|PDB:2AAO"
FT STRAND 540..543
FT /evidence="ECO:0007829|PDB:2AAO"
FT HELIX 545..551
FT /evidence="ECO:0007829|PDB:2AAO"
FT HELIX 565..569
FT /evidence="ECO:0007829|PDB:2AAO"
FT STRAND 574..577
FT /evidence="ECO:0007829|PDB:2AAO"
FT HELIX 579..586
FT /evidence="ECO:0007829|PDB:2AAO"
SQ SEQUENCE 610 AA; 68254 MW; 41868DF12B0DF9FB CRC64;
MGNTCVGPSR NGFLQSVSAA MWRPRDGDDS ASMSNGDIAS EAVSGELRSR LSDEVQNKPP
EQVTMPKPGT DVETKDREIR TESKPETLEE ISLESKPETK QETKSETKPE SKPDPPAKPK
KPKHMKRVSS AGLRTESVLQ RKTENFKEFY SLGRKLGQGQ FGTTFLCVEK TTGKEFACKS
IAKRKLLTDE DVEDVRREIQ IMHHLAGHPN VISIKGAYED VVAVHLVMEC CAGGELFDRI
IQRGHYTERK AAELTRTIVG VVEACHSLGV MHRDLKPENF LFVSKHEDSL LKTIDFGLSM
FFKPDDVFTD VVGSPYYVAP EVLRKRYGPE ADVWSAGVIV YILLSGVPPF WAETEQGIFE
QVLHGDLDFS SDPWPSISES AKDLVRKMLV RDPKKRLTAH QVLCHPWVQV DGVAPDKPLD
SAVLSRMKQF SAMNKFKKMA LRVIAESLSE EEIAGLKEMF NMIDADKSGQ ITFEELKAGL
KRVGANLKES EILDLMQAAD VDNSGTIDYK EFIAATLHLN KIEREDHLFA AFTYFDKDGS
GYITPDELQQ ACEEFGVEDV RIEELMRDVD QDNDGRIDYN EFVAMMQKGS ITGGPVKMGL
EKSFSIALKL
