CDPK3_ARATH
ID CDPK3_ARATH Reviewed; 529 AA.
AC Q42479; Q941A2;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Calcium-dependent protein kinase 3 {ECO:0000303|PubMed:12068094};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Calcium-dependent protein kinase isoform CDPK6 {ECO:0000303|PubMed:8704134};
DE Short=AtCDPK6 {ECO:0000303|PubMed:8704134};
GN Name=CPK3 {ECO:0000303|PubMed:12068094};
GN Synonyms=CDPK6 {ECO:0000303|PubMed:8704134};
GN OrderedLocusNames=At4g23650 {ECO:0000312|Araport:AT4G23650};
GN ORFNames=F9D16.120 {ECO:0000312|EMBL:CAA23031.1};
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].
RC STRAIN=cv. 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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [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 FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17032064; DOI=10.1371/journal.pbio.0040327;
RA Mori I.C., Murata Y., Yang Y., Munemasa S., Wang Y.-F., Andreoli S.,
RA Tiriac H., Alonso J.M., Harper J.F., Ecker J.R., Kwak J.M., Schroeder J.I.;
RT "CDPKs CPK6 and CPK3 function in ABA regulation of guard cell S-type
RT anion- and Ca(2+)-permeable channels and stomatal closure.";
RL PLoS Biol. 4:E327-E327(2006).
RN [11]
RP IDENTIFICATION 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).
RN [12]
RP INTERACTION WITH GHR1.
RC STRAIN=cv. Columbia, and cv. Columbia GL1;
RX PubMed=30361234; DOI=10.1105/tpc.18.00441;
RA Sierla M., Horak H., Overmyer K., Waszczak C., Yarmolinsky D.,
RA Maierhofer T., Vainonen J.P., Denessiouk K., Salojaervi J., Laanemets K.,
RA Toldsepp K., Vahisalu T., Gauthier A., Puukko T., Paulin L., Auvinen P.,
RA Geiger D., Hedrich R., Kollist H., Kangasjaervi J.;
RT "The receptor-like pseudokinase GHR1 is required for stomatal closure.";
RL Plant Cell 30:2813-2837(2018).
CC -!- FUNCTION: May play a role in signal transduction pathways that involve
CC calcium as a second messenger. Functions in abscisic acid (ABA)
CC regulation of guard cell S-type anion- and Ca(2+)-permeable channels
CC and stomatal closure. {ECO:0000269|PubMed:17032064}.
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 Evidence={ECO:0000255|PROSITE-ProRule:PRU00159};
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; Evidence={ECO:0000255|PROSITE-ProRule:PRU00159};
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 GHR1. {ECO:0000269|PubMed:30361234}.
CC -!- INTERACTION:
CC Q42479; Q03509: CAM6; NbExp=2; IntAct=EBI-1235782, EBI-1236097;
CC Q42479; P59220: CAM7; NbExp=2; IntAct=EBI-1235782, EBI-1236031;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12913141}. Nucleus
CC {ECO:0000269|PubMed:12913141}.
CC -!- TISSUE SPECIFICITY: Expressed in both guard cells and mesophyll cells.
CC {ECO:0000269|PubMed:17032064}.
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 (342-372) 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; U20623; AAA67654.1; -; mRNA.
DR EMBL; U20625; AAA67656.1; -; Genomic_DNA.
DR EMBL; AL035394; CAA23031.1; -; Genomic_DNA.
DR EMBL; AL161559; CAB79320.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84789.1; -; Genomic_DNA.
DR EMBL; AF385710; AAK60302.1; -; mRNA.
DR EMBL; AF446863; AAL38596.1; -; mRNA.
DR EMBL; AY052319; AAK96512.1; -; mRNA.
DR EMBL; AY081732; AAL87385.1; -; mRNA.
DR EMBL; BT000736; AAN31878.1; -; mRNA.
DR EMBL; AY087637; AAM65176.1; -; mRNA.
DR PIR; T05597; S71774.
DR RefSeq; NP_194096.1; NM_118496.4.
DR AlphaFoldDB; Q42479; -.
DR SMR; Q42479; -.
DR BioGRID; 13754; 35.
DR IntAct; Q42479; 18.
DR STRING; 3702.AT4G23650.1; -.
DR iPTMnet; Q42479; -.
DR PaxDb; Q42479; -.
DR PRIDE; Q42479; -.
DR ProteomicsDB; 220381; -.
DR EnsemblPlants; AT4G23650.1; AT4G23650.1; AT4G23650.
DR GeneID; 828465; -.
DR Gramene; AT4G23650.1; AT4G23650.1; AT4G23650.
DR KEGG; ath:AT4G23650; -.
DR Araport; AT4G23650; -.
DR TAIR; locus:2128409; AT4G23650.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_4_1; -.
DR InParanoid; Q42479; -.
DR OMA; TCVAYQL; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q42479; -.
DR PRO; PR:Q42479; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q42479; baseline and differential.
DR Genevisible; Q42479; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
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: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:0009738; P:abscisic acid-activated signaling pathway; IMP: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; HDA:TAIR.
DR GO; GO:0010359; P:regulation of anion channel activity; IMP:TAIR.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR CDD; cd00051; EFh; 2.
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; Cytoplasm; Kinase; Lipoprotein; Metal-binding;
KW Myristate; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..529
FT /note="Calcium-dependent protein kinase 3"
FT /id="PRO_0000363330"
FT DOMAIN 78..336
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 379..414
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 415..450
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 451..485
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 486..521
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..372
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250|UniProtKB:Q06850"
FT COMPBIAS 11..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 84..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 396
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 428
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 430
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 432
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 434
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 439
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 464
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 466
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 470
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 475
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 499
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 501
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 503
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 505
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 510
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW4"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT CONFLICT 315
FT /note="K -> E (in Ref. 4; AAL38596/AAK96512)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 529 AA; 59336 MW; 290259B0F428D376 CRC64;
MGHRHSKSKS SDPPPSSSSS SSGNVVHHVK PAGERRGSSG SGTVGSSGSG TGGSRSTTST
QQNGRILGRP MEEVRRTYEF GRELGRGQFG VTYLVTHKET KQQVACKSIP TRRLVHKDDI
EDVRREVQIM HHLSGHRNIV DLKGAYEDRH SVNLIMELCE GGELFDRIIS KGLYSERAAA
DLCRQMVMVV HSCHSMGVMH RDLKPENFLF LSKDENSPLK ATDFGLSVFF KPGDKFKDLV
GSAYYVAPEV LKRNYGPEAD IWSAGVILYI LLSGVPPFWG ENETGIFDAI LQGQLDFSAD
PWPALSDGAK DLVRKMLKYD PKDRLTAAEV LNHPWIREDG EASDKPLDNA VLSRMKQFRA
MNKLKKMALK VIAENLSEEE IIGLKEMFKS LDTDNNGIVT LEELRTGLPK LGSKISEAEI
RQLMEAADMD GDGSIDYLEF ISATMHMNRI EREDHLYTAF QFFDNDNSGY ITMEELELAM
KKYNMGDDKS IKEIIAEVDT DRDGKINYEE FVAMMKKGNP ELVPNRRRM
