Reviewed, UniProtKB/Swiss-Prot P62152 (CALM_DROME)

Names and origin

Protein names

Recommended name:
    Calmodulin
      Short name=CaM

Gene names

Name:	Cam
ORF Names:	CG8472

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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 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.
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
PTM	Acetylation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	adaptation of rhodopsin mediated signaling Traceable author statement. Source: FlyBase centriole replication Inferred from mutant phenotype. Source: FlyBase kinetochore organization Inferred from mutant phenotype. Source: FlyBase metarhodopsin inactivation Inferred from genetic interaction. Source: FlyBase mitotic spindle organization Inferred from mutant phenotype. Source: FlyBase positive regulation of NFAT protein import into nucleus Inferred from mutant phenotype. Source: FlyBase protein amino acid phosphorylation Inferred from mutant phenotype. Source: FlyBase regulation of light-activated channel activity Inferred from mutant phenotype. Source: FlyBase
Cellular component	cytoplasm Inferred from direct assay. Source: FlyBase rhabdomere Inferred from direct assay. Source: FlyBase spindle pole Inferred from direct assay. Source: FlyBase
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW myosin heavy chain binding Inferred from physical interaction. Source: FlyBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q9VB28	1	EBI-182924,EBI-188872
	Q9VGC1	1	EBI-182924,EBI-98046
	Q9VJM6	1	EBI-182924,EBI-113648
	Q9VQQ3	1	EBI-182924,EBI-130419
	Q9VSS9	1	EBI-182924,EBI-91244
BG:DS07486.4	Q9NK71	1	EBI-182924,EBI-92608

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

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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

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)
	P62152-1 [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: 3106931] [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: 3119855] [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: 2113585] [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: 10731132] [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: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[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: 12537569] [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: 3035324] [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: 11001594] [Abstract] Cited for: AMINO-ACID COMPOSITION.
[10]	"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: 1909892] [Abstract] Cited for: STRUCTURE BY NMR.
[11]	"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: 1585175] [Abstract] Cited for: STRUCTURE BY NMR OF 7-147 IN INTERACTION WITH MYLK2.
[12]	"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: 1939171] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[13]	"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: 12475216] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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_523710.1.
NP_725120.1.

UniGene

Dm.577

3D structure databases

PDBPDBe

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	[»]
3GN4	X-ray	2.70	B/D/F/H	1-149	[»]
4CLN	X-ray	2.20	A	2-149	[»]

DisProt

DP00344.

ModBase

Search...

Protein-protein interaction databases

IntAct

P62152. 26 interactions.

STRING

P62152.

Genome annotation databases

Ensembl

FBtr0088001; FBpp0087109; FBgn0000253; Drosophila melanogaster. [Genome view]
FBtr0088002; FBpp0087110; FBgn0000253; Drosophila melanogaster. [Genome view]

GeneID

36329.

KEGG

dme:Dmel_CG8472.

UCSC

CG8472-RA. d. melanogaster.

Organism-specific databases

CTD

36329.

FlyBase

FBgn0000253. Cam.

Phylogenomic databases

HOGENOM

P62152.

OMA

DEQIAEF

Gene expression databases

ArrayExpress

P62152.

GermOnline

CG8472. Drosophila melanogaster.

Family and domain databases

InterPro

IPR011992. EF-Hand_type.
IPR018247. EF_Hand_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca_bd.
IPR018248. EF_Hand_dom.
[Graphical view]

Gene3D

G3DSA:1.10.238.10. EF-Hand_type. 1 hit.

Pfam

PF00036. efhand. 4 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 Resources

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:	November 24, 2009
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project