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P62152

- CALM_DROME

UniProt

P62152 - CALM_DROME

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Protein
Calmodulin
Gene
Cam, CG8472
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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 – 32121
Add
BLAST
Calcium bindingi57 – 68122
Add
BLAST
Calcium bindingi94 – 105123
Add
BLAST
Calcium bindingi130 – 141124
Add
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: FlyBase
  2. calmodulin binding Source: FlyBase
  3. myosin V binding Source: FlyBase
  4. myosin VI head/neck binding Source: FlyBase
  5. myosin heavy chain binding Source: FlyBase
  6. protein binding Source: FlyBase

GO - Biological processi

  1. actin filament-based movement Source: FlyBase
  2. adaptation of rhodopsin mediated signaling Source: FlyBase
  3. centriole replication Source: FlyBase
  4. deactivation of rhodopsin mediated signaling Source: FlyBase
  5. kinetochore organization Source: FlyBase
  6. lateral inhibition Source: FlyBase
  7. metarhodopsin inactivation Source: FlyBase
  8. mitotic spindle organization Source: FlyBase
  9. muscle cell cellular homeostasis Source: FlyBase
  10. photoreceptor cell axon guidance Source: FlyBase
  11. positive regulation of NFAT protein import into nucleus Source: FlyBase
  12. protein phosphorylation Source: FlyBase
  13. regulation of light-activated channel activity Source: FlyBase
  14. regulation of response to DNA damage stimulus Source: FlyBase
  15. rhabdomere development Source: FlyBase
  16. rhodopsin mediated signaling pathway Source: FlyBase
  17. sensory perception of sound Source: FlyBase
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_180317. CREB phosphorylation through the activation of CaMKII.
REACT_180765. Synthesis of IP3 and IP4 in the cytosol.
REACT_180852. Translocation of GLUT4 to the plasma membrane.
REACT_181514. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_184321. Ca2+ pathway.
REACT_203584. FCERI mediated Ca+2 mobilization.
REACT_209150. Calmodulin induced events.
REACT_211028. Smooth Muscle Contraction.
REACT_213958. DARPP-32 events.
REACT_224224. Glycogen breakdown (glycogenolysis).
REACT_226300. CaM pathway.
REACT_227109. Inactivation, recovery and regulation of the phototransduction cascade.

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: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0000253. Cam.

Subcellular locationi

GO - Cellular componenti

  1. centriole Source: FlyBase
  2. cytoplasm Source: FlyBase
  3. microtubule associated complex Source: FlyBase
  4. midbody Source: FlyBase
  5. myosin V complex Source: FlyBase
  6. myosin VI complex Source: FlyBase
  7. rhabdomere Source: FlyBase
  8. spindle Source: FlyBase
  9. spindle pole Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 149148Calmodulin
PRO_0000198278Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By 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.

Interactioni

Protein-protein interaction databases

BioGridi62106. 28 interactions.
DIPiDIP-42091N.
IntActiP62152. 6 interactions.
MINTiMINT-279657.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
DisProtiDP00344.
ProteinModelPortaliP62152.
SMRiP62152. Positions 5-148.

Miscellaneous databases

EvolutionaryTraceiP62152.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Belongs to the calmodulin family.
Contains 4 EF-hand domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5126.
GeneTreeiENSGT00690000101867.
InParanoidiP62152.
KOiK02183.
OMAiSKECILE.
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

MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ    50
DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGF 100
ISAAELRHVM TNLGEKLTDE EVDEMIREAD IDGDGQVNYE EFVTMMTSK 149
Length:149
Mass (Da):16,811
Last modified:January 23, 2007 - v2
Checksum:i6B44A8917FC7027B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_001259348.2.
NP_523710.1. NM_078986.3.
NP_725120.1. NM_165870.1.
UniGeneiDm.577.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi S01173. MCFF.
RefSeqi NP_001246276.1. NM_001259347.2.
NP_001246277.1. NM_001259348.2.
NP_523710.1. NM_078986.3.
NP_725120.1. NM_165870.1.
UniGenei Dm.577.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MXE X-ray 1.70 A/B 2-149 [» ]
2BBM NMR - A 2-149 [» ]
2BBN NMR - A 2-149 [» ]
2BKH X-ray 2.40 B 2-148 [» ]
2VAS X-ray 2.40 B 1-149 [» ]
2X51 X-ray 2.20 B 1-149 [» ]
3GN4 X-ray 2.70 B/D/F/H 1-149 [» ]
3L9I X-ray 2.20 C 1-149 [» ]
4ANJ X-ray 2.60 B 1-149 [» ]
4CLN X-ray 2.20 A 2-149 [» ]
4DBP X-ray 2.20 C 1-149 [» ]
4DBQ X-ray 2.60 B 1-149 [» ]
DisProti DP00344.
ProteinModelPortali P62152.
SMRi P62152. Positions 5-148.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 62106. 28 interactions.
DIPi DIP-42091N.
IntActi P62152. 6 interactions.
MINTi MINT-279657.

Proteomic databases

PaxDbi P62152.
PRIDEi P62152.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0088001 ; FBpp0087109 ; FBgn0000253 .
FBtr0088002 ; FBpp0087110 ; FBgn0000253 .
FBtr0304963 ; FBpp0293502 ; FBgn0000253 .
FBtr0304964 ; FBpp0293503 ; FBgn0000253 .
GeneIDi 36329.
KEGGi dme:Dmel_CG8472.
UCSCi CG8472-RA. d. melanogaster.

Organism-specific databases

CTDi 36329.
FlyBasei FBgn0000253. Cam.

Phylogenomic databases

eggNOGi COG5126.
GeneTreei ENSGT00690000101867.
InParanoidi P62152.
KOi K02183.
OMAi SKECILE.
OrthoDBi EOG7F7WBV.
PhylomeDBi P62152.

Enzyme and pathway databases

Reactomei REACT_180317. CREB phosphorylation through the activation of CaMKII.
REACT_180765. Synthesis of IP3 and IP4 in the cytosol.
REACT_180852. Translocation of GLUT4 to the plasma membrane.
REACT_181514. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_184321. Ca2+ pathway.
REACT_203584. FCERI mediated Ca+2 mobilization.
REACT_209150. Calmodulin induced events.
REACT_211028. Smooth Muscle Contraction.
REACT_213958. DARPP-32 events.
REACT_224224. Glycogen breakdown (glycogenolysis).
REACT_226300. CaM pathway.
REACT_227109. Inactivation, recovery and regulation of the phototransduction cascade.

Miscellaneous databases

ChiTaRSi Cam. drosophila.
EvolutionaryTracei P62152.
GenomeRNAii 36329.
NextBioi 797939.

Gene expression databases

Bgeei P62152.

Family and domain databases

Gene3Di 1.10.238.10. 2 hits.
InterProi IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view ]
Pfami PF13499. EF-hand_7. 2 hits.
[Graphical view ]
SMARTi SM00054. EFh. 4 hits.
[Graphical view ]
PROSITEi PS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 111 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

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