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Protein

Calmodulin

Gene

Cam

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei116 – 1161Not N6-methylated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi21 – 32121Add
BLAST
Calcium bindingi57 – 68122Add
BLAST
Calcium bindingi94 – 105123Add
BLAST
Calcium bindingi130 – 141124Add
BLAST

GO - Molecular functioni

  • calcium ion binding Source: FlyBase
  • myosin heavy chain binding Source: FlyBase
  • myosin V binding Source: FlyBase
  • myosin VI head/neck binding Source: FlyBase

GO - Biological processi

  • actin filament-based movement Source: FlyBase
  • adaptation of rhodopsin mediated signaling Source: FlyBase
  • centriole replication Source: FlyBase
  • deactivation of rhodopsin mediated signaling Source: FlyBase
  • kinetochore organization Source: FlyBase
  • lateral inhibition Source: FlyBase
  • metarhodopsin inactivation Source: FlyBase
  • mitotic spindle assembly Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • muscle cell cellular homeostasis Source: FlyBase
  • photoreceptor cell axon guidance Source: FlyBase
  • positive regulation of cation channel activity Source: FlyBase
  • positive regulation of NFAT protein import into nucleus Source: FlyBase
  • protein phosphorylation Source: FlyBase
  • regulation of light-activated channel activity Source: FlyBase
  • regulation of response to DNA damage stimulus Source: FlyBase
  • rhabdomere development Source: FlyBase
  • rhodopsin mediated signaling pathway Source: FlyBase
  • salivary gland cell autophagic cell death Source: FlyBase
  • sensory perception of smell Source: FlyBase
  • sensory perception of sound Source: FlyBase
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_272812. eNOS activation.
REACT_275007. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_278006. Platelet degranulation.
REACT_278791. Glycogen breakdown (glycogenolysis).
REACT_298215. Ca2+ pathway.
REACT_302578. FCERI mediated Ca+2 mobilization.
REACT_305295. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
REACT_310206. Translocation of GLUT4 to the plasma membrane.
REACT_314692. CREB phosphorylation through the activation of CaMKII.
REACT_323252. CaM pathway.
REACT_323764. DARPP-32 events.
REACT_324131. Smooth Muscle Contraction.
REACT_328493. Calmodulin induced events.
REACT_331453. VEGFR2 mediated vascular permeability.
REACT_342163. VEGFR2 mediated cell proliferation.
REACT_360805. CLEC7A (Dectin-1) induces NFAT activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Calmodulin
Short name:
CaM
Gene namesi
Name:Cam
ORF Names:CG8472
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0000253. Cam.

Subcellular locationi

GO - Cellular componenti

  • centriole Source: FlyBase
  • centrosome Source: FlyBase
  • cytoplasm Source: FlyBase
  • cytosol Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • midbody Source: FlyBase
  • myosin V complex Source: FlyBase
  • myosin VI complex Source: FlyBase
  • nucleoplasm Source: FlyBase
  • rhabdomere Source: FlyBase
  • spindle Source: FlyBase
  • spindle pole Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 149148CalmodulinPRO_0000198278Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei95 – 951N6,N6,N6-trimethyllysine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

PaxDbiP62152.
PRIDEiP62152.

Expressioni

Gene expression databases

BgeeiP62152.
ExpressionAtlasiP62152. differential.
GenevisibleiP62152. DM.

Interactioni

Protein-protein interaction databases

BioGridi62106. 28 interactions.
DIPiDIP-42091N.
IntActiP62152. 61 interactions.
MINTiMINT-279657.
STRINGi7227.FBpp0293502.

Structurei

Secondary structure

1
149
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2014Combined sources
Beta strandi25 – 284Combined sources
Helixi30 – 3910Combined sources
Helixi46 – 5611Combined sources
Beta strandi61 – 655Combined sources
Helixi66 – 7914Combined sources
Helixi82 – 9312Combined sources
Turni94 – 963Combined sources
Beta strandi98 – 1014Combined sources
Helixi103 – 11210Combined sources
Helixi119 – 12911Combined sources
Beta strandi133 – 1386Combined sources
Helixi139 – 1479Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MXEX-ray1.70A/B2-149[»]
2BBMNMR-A2-149[»]
2BBNNMR-A2-149[»]
2BKHX-ray2.40B2-148[»]
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[»]
4PJJX-ray2.40B1-149[»]
DisProtiDP00344.
ProteinModelPortaliP62152.
SMRiP62152. Positions 5-148.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62152.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 4336EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini44 – 7936EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini81 – 11636EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini117 – 14933EF-hand 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the calmodulin family.Curated
Contains 4 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5126.
GeneTreeiENSGT00760000118901.
InParanoidiP62152.
KOiK02183.
OMAiHRISGKA.
OrthoDBiEOG7F7WBV.
PhylomeDBiP62152.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 2 hits.
[Graphical view]
SMARTiSM00054. EFh. 4 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62152-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ
60 70 80 90 100
DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGF
110 120 130 140
ISAAELRHVM TNLGEKLTDE EVDEMIREAD IDGDGQVNYE EFVTMMTSK
Length:149
Mass (Da):16,811
Last modified:January 23, 2007 - v2
Checksum:i6B44A8917FC7027B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS01173. MCFF.
RefSeqiNP_001246276.1. NM_001259347.2.
NP_001246277.1. NM_001259348.3.
NP_001286337.1. NM_001299408.1.
NP_523710.1. NM_078986.3.
NP_725120.1. NM_165870.2.
UniGeneiDm.577.

Genome annotation databases

EnsemblMetazoaiFBtr0088001; FBpp0087109; FBgn0000253.
FBtr0088002; FBpp0087110; FBgn0000253.
FBtr0304963; FBpp0293502; FBgn0000253.
FBtr0304964; FBpp0293503; FBgn0000253.
FBtr0345018; FBpp0311269; FBgn0000253.
GeneIDi36329.
KEGGidme:Dmel_CG8472.
UCSCiCG8472-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS01173. MCFF.
RefSeqiNP_001246276.1. NM_001259347.2.
NP_001246277.1. NM_001259348.3.
NP_001286337.1. NM_001299408.1.
NP_523710.1. NM_078986.3.
NP_725120.1. NM_165870.2.
UniGeneiDm.577.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MXEX-ray1.70A/B2-149[»]
2BBMNMR-A2-149[»]
2BBNNMR-A2-149[»]
2BKHX-ray2.40B2-148[»]
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[»]
4PJJX-ray2.40B1-149[»]
DisProtiDP00344.
ProteinModelPortaliP62152.
SMRiP62152. Positions 5-148.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62106. 28 interactions.
DIPiDIP-42091N.
IntActiP62152. 61 interactions.
MINTiMINT-279657.
STRINGi7227.FBpp0293502.

Proteomic databases

PaxDbiP62152.
PRIDEiP62152.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0088001; FBpp0087109; FBgn0000253.
FBtr0088002; FBpp0087110; FBgn0000253.
FBtr0304963; FBpp0293502; FBgn0000253.
FBtr0304964; FBpp0293503; FBgn0000253.
FBtr0345018; FBpp0311269; FBgn0000253.
GeneIDi36329.
KEGGidme:Dmel_CG8472.
UCSCiCG8472-RA. d. melanogaster.

Organism-specific databases

CTDi36329.
FlyBaseiFBgn0000253. Cam.

Phylogenomic databases

eggNOGiCOG5126.
GeneTreeiENSGT00760000118901.
InParanoidiP62152.
KOiK02183.
OMAiHRISGKA.
OrthoDBiEOG7F7WBV.
PhylomeDBiP62152.

Enzyme and pathway databases

ReactomeiREACT_272812. eNOS activation.
REACT_275007. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_278006. Platelet degranulation.
REACT_278791. Glycogen breakdown (glycogenolysis).
REACT_298215. Ca2+ pathway.
REACT_302578. FCERI mediated Ca+2 mobilization.
REACT_305295. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
REACT_310206. Translocation of GLUT4 to the plasma membrane.
REACT_314692. CREB phosphorylation through the activation of CaMKII.
REACT_323252. CaM pathway.
REACT_323764. DARPP-32 events.
REACT_324131. Smooth Muscle Contraction.
REACT_328493. Calmodulin induced events.
REACT_331453. VEGFR2 mediated vascular permeability.
REACT_342163. VEGFR2 mediated cell proliferation.
REACT_360805. CLEC7A (Dectin-1) induces NFAT activation.

Miscellaneous databases

ChiTaRSiCam. fly.
EvolutionaryTraceiP62152.
GenomeRNAii36329.
NextBioi797939.
PROiP62152.

Gene expression databases

BgeeiP62152.
ExpressionAtlasiP62152. differential.
GenevisibleiP62152. DM.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 2 hits.
[Graphical view]
SMARTiSM00054. EFh. 4 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  7. 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).

Entry informationi

Entry nameiCALM_DROME
AccessioniPrimary (citable) accession number: P62152
Secondary accession number(s): P07181, Q9V3T4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

This protein has four functional calcium-binding sites.
Two alternative gene models exist that generate identical translations.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.