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 27-MAR-2024, entry version 182. 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}. 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; 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 PDB; 7CQH; X-ray; 2.15 A; B=79-149. 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 PDBsum; 7CQH; -. 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; 7227-FBpp0293502; -. 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 AGR; FB:FBgn0000253; -. 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; 22601at2759; -. DR PhylomeDB; P62152; -. DR Reactome; R-DME-6798695; Neutrophil degranulation. 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 cell types or tissues. DR ExpressionAtlas; P62152; baseline and differential. 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:0016247; F:channel regulator activity; IMP: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: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:0006468; P:protein phosphorylation; 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 Gene3D; 1.10.238.10; EF-hand; 3. DR IDEAL; IID50080; -. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR002048; EF_hand_dom. DR PANTHER; PTHR23050:SF523; AT16150P-RELATED; 1. DR PANTHER; PTHR23050; CALCIUM BINDING PROTEIN; 1. DR Pfam; PF13499; EF-hand_7; 2. DR SMART; SM00054; EFh; 4. DR SUPFAM; SSF47473; EF-hand; 1. DR PROSITE; PS00018; EF_HAND_1; 4. DR PROSITE; PS50222; EF_HAND_2; 4. DR Genevisible; P62152; DM. 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 //