P62152 (CALM_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calmodulin
Short name=CaM

Gene names

Name:	Cam
ORF Names:	CG8472

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	149 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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
Domain	Repeat
Ligand	Calcium Metal-binding
PTM	Acetylation Methylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin 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 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 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 sensory perception of sound Inferred from mutant phenotype PubMed 22939627. Source: FlyBase
Cellular_component	centriole Inferred from direct assay PubMed 18798690. 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 pole Inferred from direct assay PubMed 17412918. Source: FlyBase
Molecular_function	calcium ion binding Inferred from direct assay PubMed 15178316. Source: FlyBase calmodulin binding Inferred from direct assay PubMed 18331716. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 149

148

Calmodulin

PRO_0000198278

Regions

Domain

8 – 43

36

EF-hand 1

Domain

44 – 79

36

EF-hand 2

Domain

81 – 116

36

EF-hand 3

Domain

117 – 149

33

EF-hand 4

Calcium binding

21 – 32

12

1

Calcium binding

57 – 68

12

2

Calcium binding

94 – 105

12

3

Calcium binding

130 – 141

12

4

Sites

Site

116

1

Not N6-methylated

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Modified residue

95

1

N6,N6,N6-trimethyllysine Ref.10

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

.

.

.

.

.

149

Helix Strand Turn

Details...

Helix

7 – 20

14

Beta strand

25 – 28

4

Helix

30 – 39

10

Helix

46 – 56

11

Beta strand

61 – 65

5

Helix

66 – 79

14

Helix

82 – 93

12

Turn

94 – 96

3

Beta strand

98 – 101

4

Helix

103 – 112

10

Helix

119 – 129

11

Beta strand

133 – 138

6

Helix

139 – 147

9

Sequences

	Sequence		Length	Mass (Da)
	P62152 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 6B44A8917FC7027B	FASTA	149	16,811
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.

PIR

MCFF. S01173.

RefSeq

NP_001246276.1. NM_001259347.2.
NP_001246277.1. NM_001259348.2.
NP_523710.1. NM_078986.3.
NP_725120.1. NM_165870.1.

UniGene

Dm.577.

3D structure databases

PDBe
RCSB PDB
PDBj

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	2-147	[»]
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	[»]

DisProt

DP00344.

ProteinModelPortal

P62152.

SMR

P62152. Positions 5-148.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-42091N.

IntAct

P62152. 6 interactions.

MINT

MINT-279657.

Proteomic databases

PaxDb

P62152.

PRIDE

P62152.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0088001; FBpp0087109; FBgn0000253.
FBtr0088002; FBpp0087110; FBgn0000253.
FBtr0304963; FBpp0293502; FBgn0000253.
FBtr0304964; FBpp0293503; FBgn0000253.

GeneID

36329.

KEGG

dme:Dmel_CG8472.

UCSC

CG8472-RA. d. melanogaster.

Organism-specific databases

CTD

36329.

FlyBase

FBgn0000253. Cam.

Phylogenomic databases

eggNOG

COG5126.

GeneTree

ENSGT00690000101867.

InParanoid

P62152.

KO

K02183.

OMA

ELEDMIN.

OrthoDB

EOG4R4XK2.

PhylomeDB

P62152.

Gene expression databases

Bgee

P62152.

GermOnline

CG8472. Drosophila melanogaster.

Family and domain databases

Gene3D

1.10.238.10. 2 hits.

InterPro

IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]

Pfam

PF13499. EF_hand_5. 2 hits.
[Graphical view]

SMART

SM00054. EFh. 4 hits.
[Graphical view]

PROSITE

PS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

Cam. drosophila.

EvolutionaryTrace

P62152.

GenomeRNAi

36329.

NextBio

797939.

Entry information

Entry name

CALM_DROME

Accession

Primary (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:	May 1, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project