CALM_DICDI
ID CALM_DICDI Reviewed; 152 AA.
AC P02599; Q54WM2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Calmodulin;
DE Short=CaM;
GN Name=calA; Synonyms=camA; ORFNames=DDB_G0279407;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=1493336; DOI=10.1091/mbc.3.12.1403;
RA Liu T., Williams J.G., Clarke M.;
RT "Inducible expression of calmodulin antisense RNA in Dictyostelium cells
RT inhibits the completion of cytokinesis.";
RL Mol. Biol. Cell 3:1403-1413(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP PROTEIN SEQUENCE OF 2-152, FUNCTION, AND BLOCKAGE OF N-TERMINUS.
RC STRAIN=AX3;
RX PubMed=6087882; DOI=10.1021/bi00308a007;
RA Marshak D.R., Clarke M., Roberts D.M., Watterson D.M.;
RT "Structural and functional properties of calmodulin from the eukaryotic
RT microorganism Dictyostelium discoideum.";
RL Biochemistry 23:2891-2899(1984).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-152.
RX PubMed=3785182; DOI=10.1128/mcb.6.5.1851-1854.1986;
RA Goldhagen H., Clarke M.;
RT "Identification of the single gene for calmodulin in Dictyostelium
RT discoideum.";
RL Mol. Cell. Biol. 6:1851-1854(1986).
RN [5]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=6243626; DOI=10.1128/jb.141.1.397-400.1980;
RA Clarke M., Bazari W.L., Kayman S.C.;
RT "Isolation and properties of calmodulin from Dictyostelium discoideum.";
RL J. Bacteriol. 141:397-400(1980).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=1629238; DOI=10.1083/jcb.118.2.347;
RA Zhu Q., Clarke M.;
RT "Association of calmodulin and an unconventional myosin with the
RT contractile vacuole complex of Dictyostelium discoideum.";
RL J. Cell Biol. 118:347-358(1992).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=11923193; DOI=10.1242/dev.129.7.1543;
RA Van Driessche N., Shaw C., Katoh M., Morio T., Sucgang R., Ibarra M.,
RA Kuwayama H., Saito T., Urushihara H., Maeda M., Takeuchi I., Ochiai H.,
RA Eaton W., Tollett J., Halter J., Kuspa A., Tanaka Y., Shaulsky G.;
RT "A transcriptional profile of multicellular development in Dictyostelium
RT discoideum.";
RL Development 129:1543-1552(2002).
RN [8]
RP INTERACTION WITH NUMA.
RX PubMed=11919178; DOI=10.1074/jbc.m109717200;
RA Myre M.A., O'Day D.H.;
RT "Nucleomorphin. A novel, acidic, nuclear calmodulin-binding protein from
RT Dictyostelium that regulates nuclear number.";
RL J. Biol. Chem. 277:19735-19744(2002).
RN [9]
RP DEVELOPMENTAL STAGE.
RX PubMed=12912885; DOI=10.1128/ec.2.4.664-670.2003;
RA Iranfar N., Fuller D., Loomis W.F.;
RT "Genome-wide expression analyses of gene regulation during early
RT development of Dictyostelium discoideum.";
RL Eukaryot. Cell 2:664-670(2003).
RN [10]
RP INTERACTION WITH PGKA.
RX PubMed=15363631; DOI=10.1016/j.bbamcr.2004.08.003;
RA Myre M.A., O'Day D.H.;
RT "Calmodulin binds to and inhibits the activity of phosphoglycerate
RT kinase.";
RL Biochim. Biophys. Acta 1693:177-183(2004).
RN [11]
RP INTERACTION WITH DWWA.
RX PubMed=14595117; DOI=10.1091/mbc.e03-05-0329;
RA Nagasaki A., Uyeda T.Q.P.;
RT "DWWA, a novel protein containing two WW domains and an IQ motif, is
RT required for scission of the residual cytoplasmic bridge during cytokinesis
RT in Dictyostelium.";
RL Mol. Biol. Cell 15:435-446(2004).
RN [12]
RP INTERACTION WITH THYB.
RX PubMed=15883042; DOI=10.1016/j.bbrc.2005.04.074;
RA O'Day D.H., Chatterjee-Chakraborty M., Wagler S., Myre M.A.;
RT "Isolation and characterization of Dictyostelium thymidine kinase 1 as a
RT calmodulin-binding protein.";
RL Biochem. Biophys. Res. Commun. 331:1494-1502(2005).
RN [13]
RP INTERACTION WITH CMBB.
RX PubMed=16777069; DOI=10.1016/j.bbrc.2006.05.204;
RA O'Day D.H., Suhre K., Myre M.A., Chatterjee-Chakraborty M., Chavez S.E.;
RT "Isolation, characterization, and bioinformatic analysis of calmodulin-
RT binding protein cmbB reveals a novel tandem IP22 repeat common to many
RT Dictyostelium and Mimivirus proteins.";
RL Biochem. Biophys. Res. Commun. 346:879-888(2006).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16782229; DOI=10.1016/j.ejcb.2006.05.008;
RA Koch K.V., Reinders Y., Ho T.-H., Sickmann A., Graef R.;
RT "Identification and isolation of Dictyostelium microtubule-associated
RT protein interactors by tandem affinity purification.";
RL Eur. J. Cell Biol. 85:1079-1090(2006).
CC -!- FUNCTION: Calmodulin mediates the control of a large number of enzymes,
CC ion channels and other proteins by Ca(2+). Among the enzymes to be
CC stimulated by the calmodulin-Ca(2+) complex are a number of protein
CC kinases and phosphatases. {ECO:0000269|PubMed:1493336,
CC ECO:0000269|PubMed:6087882, ECO:0000269|PubMed:6243626}.
CC -!- SUBUNIT: Interacts with cmbB, numA/nucleomorphin, pgkA/phosphoglycerate
CC kinase, and thyB/thymidine kinase in the presence of Ca(2+). Interacts
CC with dwwA in the absence of Ca(2+). {ECO:0000269|PubMed:11919178,
CC ECO:0000269|PubMed:14595117, ECO:0000269|PubMed:15363631,
CC ECO:0000269|PubMed:15883042, ECO:0000269|PubMed:16777069}.
CC -!- INTERACTION:
CC P02599; Q9GPK9: AF318287; NbExp=2; IntAct=EBI-1808395, EBI-6256975;
CC P02599; P54657: cadA; NbExp=4; IntAct=EBI-1808395, EBI-8446773;
CC -!- SUBCELLULAR LOCATION: Contractile vacuole {ECO:0000269|PubMed:1629238}.
CC -!- DEVELOPMENTAL STAGE: Expressed during development. Expression levels
CC decrease steadily from the initiation of development until late
CC culmination. {ECO:0000269|PubMed:11923193,
CC ECO:0000269|PubMed:12912885}.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Trimethylation of Lys-118 observed in other calmodulins is absent
CC here.
CC -!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
CC -!- MISCELLANEOUS: Loss-of-function mutant (antisense inhibition) fail to
CC complete the final step of cytokinesis and form multinucleated cells.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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; M64089; AAA33172.1; -; Genomic_DNA.
DR EMBL; AAFI02000031; EAL67642.1; -; Genomic_DNA.
DR EMBL; M13009; AAA33171.1; -; mRNA.
DR PIR; A03029; MCDO.
DR RefSeq; XP_641695.1; XM_636603.1.
DR AlphaFoldDB; P02599; -.
DR SMR; P02599; -.
DR BioGRID; 1247107; 3.
DR ELM; P02599; -.
DR IntAct; P02599; 4.
DR MINT; P02599; -.
DR STRING; 44689.DDB0214955; -.
DR PaxDb; P02599; -.
DR EnsemblProtists; EAL67642; EAL67642; DDB_G0279407.
DR GeneID; 8622104; -.
DR KEGG; ddi:DDB_G0279407; -.
DR dictyBase; DDB_G0279407; calA.
DR eggNOG; KOG0027; Eukaryota.
DR HOGENOM; CLU_061288_2_0_1; -.
DR InParanoid; P02599; -.
DR OMA; SCDRHPP; -.
DR PhylomeDB; P02599; -.
DR Reactome; R-DDI-111932; CaMK IV-mediated phosphorylation of CREB.
DR Reactome; R-DDI-111957; Cam-PDE 1 activation.
DR Reactome; R-DDI-114608; Platelet degranulation.
DR Reactome; R-DDI-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-DDI-163615; PKA activation.
DR Reactome; R-DDI-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-DDI-203615; eNOS activation.
DR Reactome; R-DDI-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-DDI-4086398; Ca2+ pathway.
DR Reactome; R-DDI-442729; CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde.
DR Reactome; R-DDI-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-DDI-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR Reactome; R-DDI-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-DDI-9619229; Activation of RAC1 downstream of NMDARs.
DR Reactome; R-DDI-9648002; RAS processing.
DR PRO; PR:P02599; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0000331; C:contractile vacuole; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0031012; C:extracellular matrix; IDA:dictyBase.
DR GO; GO:0005615; C:extracellular space; IDA:dictyBase.
DR GO; GO:0005634; C:nucleus; IDA:dictyBase.
DR GO; GO:0005509; F:calcium ion binding; IDA:dictyBase.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:dictyBase.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:dictyBase.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0019900; F:kinase binding; IPI:dictyBase.
DR GO; GO:0017024; F:myosin I binding; IDA:dictyBase.
DR GO; GO:0019901; F:protein kinase binding; IPI:dictyBase.
DR GO; GO:0031013; F:troponin I binding; IDA:dictyBase.
DR GO; GO:0072666; P:establishment of protein localization to vacuole; IDA:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:1903665; P:negative regulation of asexual reproduction; IDA:dictyBase.
DR GO; GO:0045861; P:negative regulation of proteolysis; IDA:dictyBase.
DR GO; GO:0001778; P:plasma membrane repair; IDA:dictyBase.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:dictyBase.
DR GO; GO:0051343; P:positive regulation of cyclic-nucleotide phosphodiesterase activity; IDA:dictyBase.
DR GO; GO:0061122; P:positive regulation of positive chemotaxis to cAMP; IDA:dictyBase.
DR GO; GO:0051284; P:positive regulation of sequestering of calcium ion; IMP:dictyBase.
DR GO; GO:0006611; P:protein export from nucleus; IMP:dictyBase.
DR GO; GO:0043549; P:regulation of kinase activity; IDA:dictyBase.
DR GO; GO:0031285; P:regulation of sorocarp stalk cell differentiation; IMP:dictyBase.
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 Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Cell cycle; Cell division; Direct protein sequencing;
KW Metal-binding; Reference proteome; Repeat; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6087882"
FT CHAIN 2..152
FT /note="Calmodulin"
FT /id="PRO_0000198252"
FT DOMAIN 10..45
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 46..81
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 83..118
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 119..152
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT SITE 118
FT /note="Not N6-methylated"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 152 AA; 17151 MW; ABD99139F0FECB4C CRC64;
MASQESLTEE QIAEFKEAFS LFDKDGDGSI TTKELGTVMR SLGQNPTEAE LQDMINEVDA
DGNGNIDFPE FLTMMARKMQ DTDTEEEIRE AFKVFDKDGN GYISAAELRH VMTSLGEKLT
NEEVDEMIRE ADLDGDGQVN YDEFVKMMIV RN
