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P62152 (CALM_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calmodulin

Short name=CaM
Gene names
Name:Cam
ORF Names:CG8472
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length149 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca2+. Among the enzymes to be stimulated by the calmodulin-Ca2+ complex are a number of protein kinases and phosphatases.

Post-translational modification

Trimethylation of Lys-116 observed in other calmodulins is absent here, but does occur at Lys-95 specifically in the compound eye.

Miscellaneous

This protein has four functional calcium-binding sites.

Two alternative gene models exist that generate identical translations.

Sequence similarities

Belongs to the calmodulin family.

Contains 4 EF-hand domains.

Ontologies

Keywords
   DomainRepeat
   LigandCalcium
Metal-binding
   PTMAcetylation
Methylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament-based movement

Inferred from direct assay PubMed 15980429. Source: FlyBase

adaptation of rhodopsin mediated signaling

Traceable author statement PubMed 10611962. Source: FlyBase

centriole replication

Inferred from mutant phenotype PubMed 18798690. Source: FlyBase

deactivation of rhodopsin mediated signaling

Traceable author statement PubMed 10611962. Source: FlyBase

kinetochore organization

Inferred from mutant phenotype PubMed 17412918. Source: FlyBase

lateral inhibition

Inferred from mutant phenotype PubMed 19363474. Source: FlyBase

metarhodopsin inactivation

Inferred from genetic interaction PubMed 9363946. Source: FlyBase

mitotic spindle organization

Inferred from mutant phenotype PubMed 17412918. Source: FlyBase

muscle cell cellular homeostasis

Inferred from genetic interaction PubMed 21256839. Source: FlyBase

photoreceptor cell axon guidance

Inferred from mutant phenotype PubMed 21943192. Source: FlyBase

positive regulation of NFAT protein import into nucleus

Inferred from mutant phenotype PubMed 17293345. Source: FlyBase

protein phosphorylation

Inferred from mutant phenotype PubMed 9363946. Source: FlyBase

regulation of light-activated channel activity

Inferred from mutant phenotype PubMed 9363946. Source: FlyBase

regulation of response to DNA damage stimulus

Inferred from genetic interaction PubMed 18612247. Source: FlyBase

rhabdomere development

Inferred from mutant phenotype PubMed 21943192. Source: FlyBase

rhodopsin mediated signaling pathway

Inferred from mutant phenotype PubMed 9159171. Source: FlyBase

sensory perception of sound

Inferred from mutant phenotype PubMed 22939627. Source: FlyBase

   Cellular_componentcentriole

Inferred from direct assay PubMed 18798690. Source: FlyBase

cytoplasm

Inferred from direct assay PubMed 8235618. Source: FlyBase

microtubule associated complex

Inferred from direct assay PubMed 18433294. Source: FlyBase

midbody

Inferred from direct assay PubMed 18798690. Source: FlyBase

myosin V complex

Inferred from physical interaction PubMed 15178316. Source: FlyBase

myosin VI complex

Inferred from physical interaction PubMed 16790438. Source: FlyBase

rhabdomere

Inferred from direct assay PubMed 8235618. Source: FlyBase

spindle

Inferred from direct assay PubMed 18798690. Source: FlyBase

spindle pole

Inferred from direct assay PubMed 17412918. Source: FlyBase

   Molecular_functioncalcium ion binding

Inferred from direct assay PubMed 15178316. Source: FlyBase

calmodulin binding

Inferred from direct assay PubMed 18331716. Source: FlyBase

myosin V binding

Inferred from physical interaction PubMed 15178316. Source: FlyBase

myosin VI head/neck binding

Inferred from physical interaction PubMed 16790438. Source: FlyBase

myosin heavy chain binding

Inferred from physical interaction PubMed 15980429. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 149148Calmodulin
PRO_0000198278

Regions

Domain8 – 4336EF-hand 1
Domain44 – 7936EF-hand 2
Domain81 – 11636EF-hand 3
Domain117 – 14933EF-hand 4
Calcium binding21 – 32121
Calcium binding57 – 68122
Calcium binding94 – 105123
Calcium binding130 – 141124

Sites

Site1161Not N6-methylated

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue951N6,N6,N6-trimethyllysine Ref.10

Secondary structure

........................ 149
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62152 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 6B44A8917FC7027B

FASTA14916,811
        10         20         30         40         50         60 
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG 

        70         80         90        100        110        120 
NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGF ISAAELRHVM TNLGEKLTDE 

       130        140 
EVDEMIREAD IDGDGQVNYE EFVTMMTSK 

« Hide

References

« Hide 'large scale' references
[1]"Structure and expression of the Drosophila calmodulin gene."
Yamanaka M.K., Saugstad J.A., Hanson-Painton O., McCarthy B.J., Tobin S.L.
Nucleic Acids Res. 15:3335-3348(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Canton-S and Oregon-R.
Tissue: Embryo.
[2]"Structure and sequence of the Drosophila melanogaster calmodulin gene."
Smith V.L., Doyle K.E., Maune J.F., Munjaal R.P., Beckingham K.
J. Mol. Biol. 196:471-485(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Drosophila melanogaster contains a single calmodulin gene. Further structure and expression studies."
Doyle K.E., Kovalick G.E., Lee E., Beckingham K.
J. Mol. Biol. 213:599-605(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[5]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[6]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[7]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Berkeley.
Tissue: Embryo.
[8]"The calmodulin gene of Drosophila melanogaster."
Beckingham K., Doyle K.E., Maune J.F.
Methods Enzymol. 139:230-247(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-141.
[9]"Characterisation of calmodulin from Drosophila heads."
Gorlach M., Dieter P., Seydewitz H.H., Kaiser C., Witt I., Marme D.
Biochim. Biophys. Acta 832:228-232(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: AMINO-ACID COMPOSITION.
[10]"Novel eye-specific calmodulin methylation characterized by protein mapping in Drosophila melanogaster."
Takemori N., Komori N., Thompson J.N. Jr., Yamamoto M.T., Matsumoto H.
Proteomics 7:2651-2658(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-95.
Tissue: Eye.
[11]"Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR spectroscopy."
Ikura M., Spera S., Barbato G., Kay L.E., Krinks M., Bax A.
Biochemistry 30:9216-9228(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[12]"Solution structure of a calmodulin-target peptide complex by multidimensional NMR."
Ikura M., Clore G.M., Gronenborn A.M., Zhu G., Klee C.B., Bax A.
Science 256:632-638(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 7-147 IN INTERACTION WITH MYLK2.
[13]"Structure of a recombinant calmodulin from Drosophila melanogaster refined at 2.2-A resolution."
Taylor D.A., Sack J.S., Maune J.F., Beckingham K., Quiocho F.A.
J. Biol. Chem. 266:21375-21380(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[14]"Structure of the complex of calmodulin with the target sequence of calmodulin-dependent protein kinase I: studies of the kinase activation mechanism."
Clapperton J.A., Martin S.R., Smerdon S.J., Gamblin S.J., Bayley P.M.
Biochemistry 41:14669-14679(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00133 mRNA. Translation: CAA68327.1.
X05948 Genomic DNA. Translation: CAA29380.1.
X05949 Genomic DNA. Translation: CAA29381.1.
X05950 Genomic DNA. Translation: CAB51566.1.
X05951 Genomic DNA. Translation: CAA29383.1.
AE013599 Genomic DNA. Translation: AAF58542.1.
AE013599 Genomic DNA. Translation: AAF58543.1.
AY118890 mRNA. Translation: AAM50750.1.
BT003282 mRNA. Translation: AAO25039.1.
PIRMCFF. S01173.
RefSeqNP_001246276.1. NM_001259347.2.
NP_001246277.1. NM_001259348.2.
NP_523710.1. NM_078986.3.
NP_725120.1. NM_165870.1.
UniGeneDm.577.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MXEX-ray1.70A/B2-149[»]
2BBMNMR-A2-149[»]
2BBNNMR-A2-149[»]
2BKHX-ray2.40B2-147[»]
2VASX-ray2.40B1-149[»]
2X51X-ray2.20B1-149[»]
3GN4X-ray2.70B/D/F/H1-149[»]
3L9IX-ray2.20C1-149[»]
4ANJX-ray2.60B1-149[»]
4CLNX-ray2.20A2-149[»]
4DBPX-ray2.20C1-149[»]
4DBQX-ray2.60B1-149[»]
DisProtDP00344.
ProteinModelPortalP62152.
SMRP62152. Positions 5-148.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid62106. 28 interactions.
DIPDIP-42091N.
IntActP62152. 6 interactions.
MINTMINT-279657.

Proteomic databases

PaxDbP62152.
PRIDEP62152.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0088001; FBpp0087109; FBgn0000253.
FBtr0088002; FBpp0087110; FBgn0000253.
FBtr0304963; FBpp0293502; FBgn0000253.
FBtr0304964; FBpp0293503; FBgn0000253.
GeneID36329.
KEGGdme:Dmel_CG8472.
UCSCCG8472-RA. d. melanogaster.

Organism-specific databases

CTD36329.
FlyBaseFBgn0000253. Cam.

Phylogenomic databases

eggNOGCOG5126.
GeneTreeENSGT00690000101867.
InParanoidP62152.
KOK02183.
OMANEVDEMI.
OrthoDBEOG7F7WBV.
PhylomeDBP62152.

Gene expression databases

BgeeP62152.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamPF13499. EF-hand_7. 2 hits.
[Graphical view]
SMARTSM00054. EFh. 4 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCam. drosophila.
EvolutionaryTraceP62152.
GenomeRNAi36329.
NextBio797939.

Entry information

Entry nameCALM_DROME
AccessionPrimary (citable) accession number: P62152
Secondary accession number(s): P07181, Q9V3T4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase