P62204 (CALM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calmodulin
Short name=CaM

Gene names

Name:	Calm1
Synonyms:	Calm, Cam, Cam1
AND
Name:	Calm2
Synonyms:	Cam2, Camb
AND
Name:	Calm3
Synonyms:	Cam3, Camc

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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. Together with CEP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis By similarity.
Subunit structure	Interacts with CEP97, CEP110, MYO1C, TTN/titin and SRY. Interacts with MYO10. Interacts with RRAD By similarity. Interacts with USP6; the interaction is calcium dependent By similarity. Interacts with CDK5RAP2. Interacts with SCN5A By similarity. Interacts with RYR1 and RYR2. Interacts with FCHO1 By similarity. Ref.9
Subcellular location	Cytoplasm › cytoskeleton › spindle. Cytoplasm › cytoskeleton › spindle pole. Note: Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules By similarity.
Post-translational modification	Ubiquitination results in a strongly decreased activity By similarity. Phosphorylation results in a decreased activity By similarity.
Miscellaneous	This protein has four functional calcium-binding sites.
Sequence similarities	Belongs to the calmodulin family. Contains 4 EF-hand domains.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Domain	Repeat
Ligand	Calcium Metal-binding
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	regulation of cytokinesis Inferred from electronic annotation. Source: Compara response to amphetamine Inferred from electronic annotation. Source: Compara response to calcium ion Inferred from electronic annotation. Source: Compara response to corticosterone stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	centrosome Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome spindle microtubule Inferred from electronic annotation. Source: Compara spindle pole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Ccp110	Q7TSH4	4	EBI-397460,EBI-646843
Kcnma1	Q08460	4	EBI-397460,EBI-1633915
PPEF1	O14829	2	EBI-397460,EBI-2931238	From a different organism.
PPEF2	O14830	2	EBI-397460,EBI-2931306	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 149

148

Calmodulin

PRO_0000198224

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

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.7

Modified residue

22

1

N6-acetyllysine By similarity

Modified residue

45

1

Phosphothreonine; by CaMK4 By similarity

Modified residue

95

1

N6-acetyllysine By similarity

Modified residue

100

1

Phosphotyrosine Ref.10

Modified residue

102

1

Phosphoserine By similarity

Modified residue

116

1

N6,N6,N6-trimethyllysine By similarity

Modified residue

139

1

Phosphotyrosine By similarity

Cross-link

22

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict

26

1

G → N in AAA66182. Ref.1

Sequence conflict

55

1

E → V in BAE41271. Ref.5

Sequence conflict

69

1

F → L in BAE40191. Ref.5

Sequence conflict

82

1

S → G in BAE31439. Ref.5

Sequence conflict

82

1

S → G in BAE31644. Ref.5

Sequence conflict

82

1

S → G in BAE31442. Ref.5

Sequence conflict

126

1

I → T in BAE31579. Ref.5

Sequence conflict

142

1

F → S in BAC39089. Ref.5

Sequence conflict

143

1

V → L in BAB28959. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

149

Helix Strand Turn

Details...

Helix

7 – 20

14

Beta strand

24 – 29

6

Helix

30 – 32

3

Helix

33 – 39

7

Helix

46 – 54

9

Beta strand

63 – 65

3

Helix

66 – 78

13

Helix

83 – 91

9

Helix

103 – 112

10

Beta strand

113 – 115

3

Helix

119 – 128

10

Beta strand

135 – 137

3

Helix

139 – 145

7

Sequences

	Sequence		Length	Mass (Da)
	P62204 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 6B4BC3FCDE10727B	FASTA	149	16,838
	10 20 30 40 50 60 MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG 70 80 90 100 110 120 NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE 130 140 EVDEMIREAD IDGDGQVNYE EFVQMMTAK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The abundance of calmodulin mRNAs is regulated in phosphorylase kinase-deficient skeletal muscle." Bender P.K., Dedman J.R., Emerson C.P. Jr. J. Biol. Chem. 263:9733-9737(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning and expression of mouse-brain calmodulin as an activator of Bordetella pertussis adenylate cyclase in Escherichia coli." Danchin A., Sezer O., Glaser P., Chalon P., Caput D. Gene 80:145-149(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]	"Genome-wide isolation of growth and obesity QTL using mouse speed congenic strains." Farber C.R., Corva P.M., Medrano J.F. BMC Genomics 7:102-102(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: CAST/EiJ. Tissue: Brain.
[4]	"A collection of cDNA clones with specific expression patterns in mouse brain." Kato K. Eur. J. Neurosci. 2:704-711(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: BALB/c. Tissue: Brain.
[5]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J, DBA/2 and NOD. Tissue: Amnion, Bone marrow, Colon, Hippocampus, Kidney, Liver, Lung, Mammary gland, Ovary, Placenta, Stomach, Testis, Thymus and Tongue.
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: 129, C57BL/6 and Czech II. Tissue: Brain, Mammary tumor, Placenta and Spinal ganglion.
[7]	Bienvenut W.V. Submitted (JUL-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Liver.
[8]	Lubec G., Klug S., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 15-31; 79-87 AND 92-107, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
[9]	"S100A1 and calmodulin compete for the same binding site on ryanodine receptor." Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F., Weber D.J. J. Biol. Chem. 283:26676-26683(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RYR1 AND RYR2.
[10]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, MASS SPECTROMETRY. Tissue: Brain.
[11]	"Crystal structure of apo-calmodulin bound to the first two IQ motifs of myosin V reveals essential recognition features." Houdusse A., Gaucher J.F., Krementsova E., Mui S., Trybus K.M., Cohen C. Proc. Natl. Acad. Sci. U.S.A. 103:19326-19331(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 3-147 IN COMPLEX WITH MYO5A.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M19380 mRNA. Translation: AAA66181.1.
M19381 mRNA. Translation: AAA66182.1.
L31642 mRNA. Translation: AAA65934.1.
M27844 Genomic DNA. Translation: AAA37365.1.
AY902353 Genomic DNA. Translation: AAY21063.1.
X61432 mRNA. Translation: CAA43674.1.
AK004673 mRNA. Translation: BAB23462.1.
AK012247 mRNA. Translation: BAB28116.1.
AK012564 mRNA. Translation: BAB28319.1.
AK013068 mRNA. Translation: BAB28631.1.
AK013695 mRNA. Translation: BAB28959.1.
AK083996 mRNA. Translation: BAC39089.2.
AK088141 mRNA. Translation: BAC40168.1.
AK150288 mRNA. Translation: BAE29443.1.
AK150978 mRNA. Translation: BAE30007.1.
AK151001 mRNA. Translation: BAE30025.1.
AK151552 mRNA. Translation: BAE30497.1.
AK151610 mRNA. Translation: BAE30549.1.
AK151784 mRNA. Translation: BAE30686.1.
AK151923 mRNA. Translation: BAE30801.1.
AK151992 mRNA. Translation: BAE30856.1.
AK152148 mRNA. Translation: BAE30984.1.
AK152303 mRNA. Translation: BAE31109.1.
AK152715 mRNA. Translation: BAE31439.1.
AK152719 mRNA. Translation: BAE31442.1.
AK152754 mRNA. Translation: BAE31469.1.
AK152850 mRNA. Translation: BAE31543.1.
AK152897 mRNA. Translation: BAE31579.1.
AK153004 mRNA. Translation: BAE31644.1.
AK153179 mRNA. Translation: BAE31782.1.
AK153348 mRNA. Translation: BAE31924.1.
AK153426 mRNA. Translation: BAE31985.1.
AK153546 mRNA. Translation: BAE32083.1.
AK159762 mRNA. Translation: BAE35353.1.
AK160057 mRNA. Translation: BAE35595.1.
AK160508 mRNA. Translation: BAE35832.1.
AK160636 mRNA. Translation: BAE35930.1.
AK161268 mRNA. Translation: BAE36280.1.
AK161302 mRNA. Translation: BAE36309.1.
AK161984 mRNA. Translation: BAE36667.1.
AK162314 mRNA. Translation: BAE36849.1.
AK166308 mRNA. Translation: BAE38695.1.
AK167353 mRNA. Translation: BAE39452.1.
AK168002 mRNA. Translation: BAE39990.1.
AK168241 mRNA. Translation: BAE40191.1.
AK168663 mRNA. Translation: BAE40516.1.
AK168741 mRNA. Translation: BAE40582.1.
AK168803 mRNA. Translation: BAE40633.1.
AK169027 mRNA. Translation: BAE40819.1.
AK169055 mRNA. Translation: BAE40843.1.
AK169640 mRNA. Translation: BAE41271.1.
BC010730 mRNA. Translation: AAH10730.1.
BC021347 mRNA. Translation: AAH21347.1.
BC050926 mRNA. Translation: AAH50926.1.
BC051444 mRNA. Translation: AAH51444.1.
BC054805 mRNA. Translation: AAH54805.1.
BC100301 mRNA. Translation: AAI00302.1.

IPI

IPI00761696.

PIR

I49567.
S37707.

RefSeq

NP_031615.1. NM_007589.5.
NP_031616.1. NM_007590.3.
NP_033920.1. NM_009790.4.

UniGene

Mm.285993.
Mm.288630.
Mm.329243.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DFS	electron microscopy	24.00	B/C/D/E/F/G/N/O/P/Q/R/S	2-148	[»]
2IX7	X-ray	2.50	A/B	3-147	[»]
4HEX	X-ray	2.00	A/B	1-149	[»]

ProteinModelPortal

P62204.

ModBase

Search...

Protein-protein interaction databases

IntAct

P62204. 19 interactions.

PTM databases

PhosphoSite

P62204.

2D gel databases

REPRODUCTION-2DPAGE

P62204.

SWISS-2DPAGE

P62204.

Proteomic databases

PaxDb

P62204.

PRIDE

P62204.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000019514; ENSMUSP00000019514; ENSMUSG00000019370.
ENSMUST00000040440; ENSMUSP00000048857; ENSMUSG00000036438.
ENSMUST00000110082; ENSMUSP00000105709; ENSMUSG00000001175.

GeneID

12313.
12314.
12315.

KEGG

mmu:12313.
mmu:12314.
mmu:12315.

UCSC

uc007osq.1. mouse.

Organism-specific databases

CTD

801.
805.
808.

MGI

MGI:88251. Calm1.
MGI:103250. Calm2.
MGI:103249. Calm3.

Phylogenomic databases

eggNOG

COG5126.

GeneTree

ENSGT00690000101867.

HOVERGEN

HBG012180.

InParanoid

P62204.

KO

K02183.

OMA

ELEDMIN.

OrthoDB

EOG4001KK.

Enzyme and pathway databases

Reactome

REACT_118809. Calcineurin Dephosphorylates Nfatc2.
REACT_147847. Translocation of Glut4 to the Plasma Membrane.
REACT_88307. Membrane Trafficking.

Gene expression databases

ArrayExpress

P62204.

Bgee

P62204.

CleanEx

MM_CALM1.
MM_CALM2.
MM_CALM3.

Genevestigator

P62204.

GermOnline

ENSMUSG00000001175. Mus musculus.
ENSMUSG00000019370. Mus musculus.
ENSMUSG00000036438. Mus musculus.

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.
IPR001125. Recoverin.
[Graphical view]

Pfam

PF13499. EF_hand_5. 2 hits.
[Graphical view]

PRINTS

PR00450. RECOVERIN.

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

BindingDB

P62204.

ChiTaRS

CALM1. mouse.
CALM2. mouse.
CALM3. mouse.

EvolutionaryTrace

P62204.

NextBio

280868.

SOURCE

Search...

Entry information

Entry name

CALM_MOUSE

Accession

Primary (citable) accession number: P62204
Secondary accession number(s): P02593 , P70667, P99014, Q3TEH7, Q3THK5, Q3U6Z5, Q3U7C7, Q498A3, Q61379, Q61380, Q8BNC9, Q91VQ9, Q9D6G4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program