CALM_DROME
ID CALM_DROME Reviewed; 149 AA.
AC P62152; P07181; Q9V3T4;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Calmodulin;
DE Short=CaM;
GN Name=Cam; ORFNames=CG8472;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Canton-S, and Oregon-R; TISSUE=Embryo;
RX PubMed=3106931; DOI=10.1093/nar/15.8.3335;
RA Yamanaka M.K., Saugstad J.A., Hanson-Painton O., McCarthy B.J., Tobin S.L.;
RT "Structure and expression of the Drosophila calmodulin gene.";
RL Nucleic Acids Res. 15:3335-3348(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3119855; DOI=10.1016/0022-2836(87)90025-8;
RA Smith V.L., Doyle K.E., Maune J.F., Munjaal R.P., Beckingham K.;
RT "Structure and sequence of the Drosophila melanogaster calmodulin gene.";
RL J. Mol. Biol. 196:471-485(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2113585; DOI=10.1016/s0022-2836(05)80245-1;
RA Doyle K.E., Kovalick G.E., Lee E., Beckingham K.;
RT "Drosophila melanogaster contains a single calmodulin gene. Further
RT structure and expression studies.";
RL J. Mol. Biol. 213:599-605(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-141.
RX PubMed=3035324; DOI=10.1016/0076-6879(87)39089-5;
RA Beckingham K., Doyle K.E., Maune J.F.;
RT "The calmodulin gene of Drosophila melanogaster.";
RL Methods Enzymol. 139:230-247(1987).
RN [9]
RP AMINO-ACID COMPOSITION.
RX PubMed=11001594; DOI=10.1016/0167-4838(85)90337-1;
RA Gorlach M., Dieter P., Seydewitz H.H., Kaiser C., Witt I., Marme D.;
RT "Characterisation of calmodulin from Drosophila heads.";
RL Biochim. Biophys. Acta 832:228-232(1985).
RN [10]
RP INTERACTION WITH STAC.
RX PubMed=9813038; DOI=10.1074/jbc.273.47.31297;
RA Xu X.-Z.S., Wes P.D., Chen H., Li H.-S., Yu M., Morgan S., Liu Y.,
RA Montell C.;
RT "Retinal targets for calmodulin include proteins implicated in synaptic
RT transmission.";
RL J. Biol. Chem. 273:31297-31307(1998).
RN [11]
RP INTERACTION WITH AKAP200.
RX PubMed=10480937; DOI=10.1074/jbc.274.38.27201;
RA Rossi E.A., Li Z., Feng H., Rubin C.S.;
RT "Characterization of the targeting, binding, and phosphorylation site
RT domains of an A kinase anchor protein and a myristoylated alanine-rich C
RT kinase substrate-like analog that are encoded by a single gene.";
RL J. Biol. Chem. 274:27201-27210(1999).
RN [12]
RP METHYLATION AT LYS-95.
RC TISSUE=Eye;
RX PubMed=17610210; DOI=10.1002/pmic.200700343;
RA Takemori N., Komori N., Thompson J.N. Jr., Yamamoto M.T., Matsumoto H.;
RT "Novel eye-specific calmodulin methylation characterized by protein mapping
RT in Drosophila melanogaster.";
RL Proteomics 7:2651-2658(2007).
RN [13]
RP INTERACTION WITH CRAG, AND SUBCELLULAR LOCATION.
RX PubMed=18331716; DOI=10.1016/j.devcel.2007.12.012;
RA Denef N., Chen Y., Weeks S.D., Barcelo G., Schuepbach T.;
RT "Crag regulates epithelial architecture and polarized deposition of
RT basement membrane proteins in Drosophila.";
RL Dev. Cell 14:354-364(2008).
RN [14]
RP FUNCTION.
RX PubMed=23226104; DOI=10.1371/journal.pbio.1001438;
RA Xiong B., Bayat V., Jaiswal M., Zhang K., Sandoval H., Charng W.L., Li T.,
RA David G., Duraine L., Lin Y.Q., Neely G.G., Yamamoto S., Bellen H.J.;
RT "Crag is a GEF for Rab11 required for rhodopsin trafficking and maintenance
RT of adult photoreceptor cells.";
RL PLoS Biol. 10:E1001438-E1001438(2012).
RN [15]
RP DISRUPTION PHENOTYPE.
RX PubMed=29444420; DOI=10.1016/j.celrep.2018.01.049;
RA Parkhurst S.J., Adhikari P., Navarrete J.S., Legendre A., Manansala M.,
RA Wolf F.W.;
RT "Perineurial Barrier Glia Physically Respond to Alcohol in an Akap200-
RT Dependent Manner to Promote Tolerance.";
RL Cell Rep. 22:1647-1656(2018).
RN [16]
RP STRUCTURE BY NMR.
RX PubMed=1909892; DOI=10.1021/bi00102a013;
RA Ikura M., Spera S., Barbato G., Kay L.E., Krinks M., Bax A.;
RT "Secondary structure and side-chain 1H and 13C resonance assignments of
RT calmodulin in solution by heteronuclear multidimensional NMR
RT spectroscopy.";
RL Biochemistry 30:9216-9228(1991).
RN [17]
RP STRUCTURE BY NMR OF 7-147 IN INTERACTION WITH MYLK2.
RX PubMed=1585175; DOI=10.1126/science.1585175;
RA Ikura M., Clore G.M., Gronenborn A.M., Zhu G., Klee C.B., Bax A.;
RT "Solution structure of a calmodulin-target peptide complex by
RT multidimensional NMR.";
RL Science 256:632-638(1992).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=1939171; DOI=10.2210/pdb4cln/pdb;
RA Taylor D.A., Sack J.S., Maune J.F., Beckingham K., Quiocho F.A.;
RT "Structure of a recombinant calmodulin from Drosophila melanogaster refined
RT at 2.2-A resolution.";
RL J. Biol. Chem. 266:21375-21380(1991).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=12475216; DOI=10.1021/bi026660t;
RA Clapperton J.A., Martin S.R., Smerdon S.J., Gamblin S.J., Bayley P.M.;
RT "Structure of the complex of calmodulin with the target sequence of
RT calmodulin-dependent protein kinase I: studies of the kinase activation
RT mechanism.";
RL Biochemistry 41:14669-14679(2002).
CC -!- FUNCTION: Calmodulin mediates the control of a large number of enzymes,
CC ion channels and other proteins by Ca(2+) (By similarity). Among the
CC enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number
CC of protein kinases and phosphatases (By similarity). In photoreceptor
CC cells, light-induced Ca(2+) influx activates calmodulin, which in turn
CC is likely to promote Crag activity in trafficking of newly synthesized
CC ninaE (Rh1) from the trans-Golgi network to rhabdomere membranes
CC (PubMed:23226104). Together with Akap200, regulates PKA activity and
CC ethanol-induced sensitivity and tolerance (PubMed:10480937,
CC PubMed:29444420). {ECO:0000250|UniProtKB:P02599,
CC ECO:0000269|PubMed:10480937, ECO:0000269|PubMed:23226104,
CC ECO:0000269|PubMed:29444420}.
CC -!- SUBUNIT: Interacts with Crag (PubMed:18331716). Interacts with stac
CC (PubMed:9813038). Interacts with Akap200; the interaction is calcium-
CC dependent and is inhibited by PKC-mediated phosphorylation of Akap200
CC (PubMed:10480937). {ECO:0000269|PubMed:10480937,
CC ECO:0000269|PubMed:18331716, ECO:0000269|PubMed:9813038}.
CC -!- INTERACTION:
CC P62152; Q9V3Z6: ck; NbExp=3; IntAct=EBI-182924, EBI-15762145;
CC P62152; Q9VGC1: Rsbp15; NbExp=3; IntAct=EBI-182924, EBI-98046;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:18331716}.
CC -!- PTM: Trimethylation of Lys-116 observed in other calmodulins is absent
CC here, but does occur at Lys-95 specifically in the compound eye.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the perineurial glia
CC increases ethanol sedation resistance and decreases ethanol tolerance.
CC {ECO:0000269|PubMed:29444420}.
CC -!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
CC -!- MISCELLANEOUS: Two alternative gene models exist that generate
CC identical translations.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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DR EMBL; Y00133; CAA68327.1; -; mRNA.
DR EMBL; X05948; CAA29380.1; -; Genomic_DNA.
DR EMBL; X05949; CAA29381.1; -; Genomic_DNA.
DR EMBL; X05950; CAB51566.1; -; Genomic_DNA.
DR EMBL; X05951; CAA29383.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58542.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58543.1; -; Genomic_DNA.
DR EMBL; AY118890; AAM50750.1; -; mRNA.
DR EMBL; BT003282; AAO25039.1; -; mRNA.
DR PIR; S01173; MCFF.
DR RefSeq; NP_001246276.1; NM_001259347.2.
DR RefSeq; NP_001246277.1; NM_001259348.3.
DR RefSeq; NP_001286337.1; NM_001299408.1.
DR RefSeq; NP_523710.1; NM_078986.3.
DR RefSeq; NP_725120.1; NM_165870.2.
DR PDB; 1MXE; X-ray; 1.70 A; A/B=2-149.
DR PDB; 2BBM; NMR; -; A=2-149.
DR PDB; 2BBN; NMR; -; A=2-149.
DR PDB; 2BKH; X-ray; 2.40 A; B=2-148.
DR PDB; 2VAS; X-ray; 2.40 A; B=1-149.
DR PDB; 2X51; X-ray; 2.20 A; B=1-149.
DR PDB; 3GN4; X-ray; 2.70 A; B/D/F/H=1-149.
DR PDB; 3L9I; X-ray; 2.20 A; C=1-149.
DR PDB; 4ANJ; X-ray; 2.60 A; B=1-149.
DR PDB; 4CLN; X-ray; 2.20 A; A=2-149.
DR PDB; 4DBP; X-ray; 2.20 A; C=1-149.
DR PDB; 4DBQ; X-ray; 2.60 A; B=1-149.
DR PDB; 4PJJ; X-ray; 2.40 A; B=1-149.
DR PDBsum; 1MXE; -.
DR PDBsum; 2BBM; -.
DR PDBsum; 2BBN; -.
DR PDBsum; 2BKH; -.
DR PDBsum; 2VAS; -.
DR PDBsum; 2X51; -.
DR PDBsum; 3GN4; -.
DR PDBsum; 3L9I; -.
DR PDBsum; 4ANJ; -.
DR PDBsum; 4CLN; -.
DR PDBsum; 4DBP; -.
DR PDBsum; 4DBQ; -.
DR PDBsum; 4PJJ; -.
DR AlphaFoldDB; P62152; -.
DR SMR; P62152; -.
DR BioGRID; 62106; 64.
DR DIP; DIP-42091N; -.
DR ELM; P62152; -.
DR IntAct; P62152; 63.
DR MINT; P62152; -.
DR STRING; 7227.FBpp0293502; -.
DR PaxDb; P62152; -.
DR PRIDE; P62152; -.
DR DNASU; 36329; -.
DR EnsemblMetazoa; FBtr0088001; FBpp0087109; FBgn0000253.
DR EnsemblMetazoa; FBtr0088002; FBpp0087110; FBgn0000253.
DR EnsemblMetazoa; FBtr0304963; FBpp0293502; FBgn0000253.
DR EnsemblMetazoa; FBtr0304964; FBpp0293503; FBgn0000253.
DR EnsemblMetazoa; FBtr0345018; FBpp0311269; FBgn0000253.
DR GeneID; 36329; -.
DR KEGG; dme:Dmel_CG8472; -.
DR UCSC; CG8472-RA; d. melanogaster.
DR CTD; 36329; -.
DR FlyBase; FBgn0000253; Cam.
DR VEuPathDB; VectorBase:FBgn0000253; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000162930; -.
DR HOGENOM; CLU_061288_2_0_1; -.
DR InParanoid; P62152; -.
DR OMA; SCDRHPP; -.
DR OrthoDB; 1386217at2759; -.
DR PhylomeDB; P62152; -.
DR Reactome; R-DME-111932; CaMK IV-mediated phosphorylation of CREB.
DR Reactome; R-DME-111933; Calmodulin induced events.
DR Reactome; R-DME-111957; Cam-PDE 1 activation.
DR Reactome; R-DME-114608; Platelet degranulation.
DR Reactome; R-DME-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-DME-163615; PKA activation.
DR Reactome; R-DME-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-DME-2025928; Calcineurin activates NFAT.
DR Reactome; R-DME-203615; eNOS activation.
DR Reactome; R-DME-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-DME-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-DME-4086398; Ca2+ pathway.
DR Reactome; R-DME-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-DME-442729; CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde.
DR Reactome; R-DME-451308; Activation of Ca-permeable Kainate Receptor.
DR Reactome; R-DME-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-DME-5578775; Ion homeostasis.
DR Reactome; R-DME-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR Reactome; R-DME-5673000; RAF activation.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-70221; Glycogen breakdown (glycogenolysis).
DR Reactome; R-DME-8876725; Protein methylation.
DR Reactome; R-DME-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-DME-936837; Ion transport by P-type ATPases.
DR Reactome; R-DME-9619229; Activation of RAC1 downstream of NMDARs.
DR Reactome; R-DME-9648002; RAS processing.
DR BioGRID-ORCS; 36329; 2 hits in 3 CRISPR screens.
DR ChiTaRS; Cam; fly.
DR EvolutionaryTrace; P62152; -.
DR GenomeRNAi; 36329; -.
DR PRO; PR:P62152; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0000253; Expressed in second segment of antenna (Drosophila) and 66 other tissues.
DR ExpressionAtlas; P62152; baseline and differential.
DR Genevisible; P62152; DM.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005814; C:centriole; IDA:FlyBase.
DR GO; GO:0005813; C:centrosome; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0030496; C:midbody; IDA:FlyBase.
DR GO; GO:0072686; C:mitotic spindle; IDA:FlyBase.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:FlyBase.
DR GO; GO:0031475; C:myosin V complex; IPI:FlyBase.
DR GO; GO:0031476; C:myosin VI complex; IPI:FlyBase.
DR GO; GO:0031477; C:myosin VII complex; IPI:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; HDA:FlyBase.
DR GO; GO:0016028; C:rhabdomere; IDA:FlyBase.
DR GO; GO:0005819; C:spindle; IDA:FlyBase.
DR GO; GO:0005509; F:calcium ion binding; IDA:FlyBase.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0032036; F:myosin heavy chain binding; IPI:FlyBase.
DR GO; GO:0031489; F:myosin V binding; IPI:FlyBase.
DR GO; GO:0070855; F:myosin VI head/neck binding; IPI:FlyBase.
DR GO; GO:0030048; P:actin filament-based movement; IDA:FlyBase.
DR GO; GO:0016062; P:adaptation of rhodopsin mediated signaling; TAS:FlyBase.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:InterPro.
DR GO; GO:0071361; P:cellular response to ethanol; IMP:UniProtKB.
DR GO; GO:0007099; P:centriole replication; IMP:FlyBase.
DR GO; GO:0016059; P:deactivation of rhodopsin mediated signaling; TAS:FlyBase.
DR GO; GO:0051383; P:kinetochore organization; IMP:FlyBase.
DR GO; GO:0016060; P:metarhodopsin inactivation; IGI:FlyBase.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IGI:FlyBase.
DR GO; GO:0072499; P:photoreceptor cell axon guidance; IMP:FlyBase.
DR GO; GO:2001259; P:positive regulation of cation channel activity; IDA:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IMP:FlyBase.
DR GO; GO:0016061; P:regulation of light-activated channel activity; IMP:FlyBase.
DR GO; GO:0042052; P:rhabdomere development; IMP:FlyBase.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; IMP:FlyBase.
DR GO; GO:0035071; P:salivary gland cell autophagic cell death; IMP:FlyBase.
DR GO; GO:0007608; P:sensory perception of smell; IDA:FlyBase.
DR GO; GO:0007605; P:sensory perception of sound; IMP:FlyBase.
DR CDD; cd00051; EFh; 2.
DR DisProt; DP00344; -.
DR IDEAL; IID50080; -.
DR InterPro; IPR039030; Calmodulin.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR23050:SF401; PTHR23050:SF401; 1.
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 3D-structure; Acetylation; Calcium; Cytoplasm; Metal-binding; Methylation;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..149
FT /note="Calmodulin"
FT /id="PRO_0000198278"
FT DOMAIN 8..43
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 44..79
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 81..116
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 117..149
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
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 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
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 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT SITE 116
FT /note="Not N6-methylated"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250"
FT MOD_RES 95
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:17610210"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:1MXE"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1MXE"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:1MXE"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:1MXE"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1MXE"
FT HELIX 66..79
FT /evidence="ECO:0007829|PDB:1MXE"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:1MXE"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:4CLN"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1MXE"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:1MXE"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:1MXE"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:1MXE"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:1MXE"
SQ SEQUENCE 149 AA; 16811 MW; 6B44A8917FC7027B CRC64;
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGF ISAAELRHVM TNLGEKLTDE
EVDEMIREAD IDGDGQVNYE EFVTMMTSK
