P62157 (CALM_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calmodulin
Short name=CaM

Gene names

Name:	CALM
Synonyms:	CAM

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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, TTN/titin and SRY. Interacts with MYO1C and RRAD By similarity. Interacts with USP6; the interaction is calcium dependent By similarity. Interacts with CDK5RAP2. Interacts with SCN5A. Interacts with RYR1 and RYR2 By similarity. Interacts with MYO10. Interacts with FCHO1 By similarity. Ref.9 Ref.10
Subcellular location	Cytoplasm. 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. 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	negative regulation of ryanodine-sensitive calcium-release channel activity Inferred from direct assay PubMed 19220289. Source: BHF-UCL positive regulation of ryanodine-sensitive calcium-release channel activity Inferred from direct assay PubMed 19220289. Source: BHF-UCL regulation of cytokinesis Inferred from electronic annotation. Source: Compara regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Inferred from direct assay PubMed 19220289. Source: BHF-UCL response to calcium ion 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 direct assay PubMed 19220289. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACA8	Q9LF79	14	EBI-397403,EBI-980643	From a different organism.
GRB7	Q14451	2	EBI-397403,EBI-970191	From a different organism.
Hmox2	P23711	3	EBI-397403,EBI-2910092	From a different organism.
LTF	P02788	2	EBI-397403,EBI-1058602	From a different organism.
STIM1	Q13586	2	EBI-397403,EBI-448878	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.3 Ref.4 Ref.5 Ref.6

Chain

2 – 149

148

Calmodulin

PRO_0000198222

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.5

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 By similarity

Modified residue

102

1

Phosphoserine By similarity

Modified residue

116

1

N6,N6,N6-trimethyllysine Ref.5 Ref.8

Modified residue

139

1

Phosphotyrosine By similarity

Cross-link

22

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

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.

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.

.

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.

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.

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149

Helix Strand Turn

Details...

Helix

7 – 20

14

Turn

21 – 23

3

Beta strand

25 – 28

4

Helix

30 – 39

10

Helix

46 – 56

11

Beta strand

61 – 65

5

Helix

66 – 75

10

Beta strand

79 – 82

4

Helix

83 – 93

11

Beta strand

98 – 101

4

Helix

103 – 112

10

Helix

119 – 129

11

Beta strand

131 – 138

8

Helix

139 – 146

8

Sequences

	Sequence		Length	Mass (Da)
	P62157 [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]	"Characterization of gene expression profiles in early bovine pregnancy using a custom cDNA microarray." Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H., Takahashi T., Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y., Tsujimoto G., Izaike Y., Todoroki J., Hashizume K. Mol. Reprod. Dev. 65:9-18(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus and Hereford. Tissue: Fetal pons, Ileum and Uterus.
[3]	"The amino acid sequence of the troponin C-like protein (modulator protein) from bovine uterus." Grand R.J.A., Perry S.V. FEBS Lett. 92:137-142(1978) Cited for: PROTEIN SEQUENCE OF 2-149. Tissue: Uterus.
[4]	"Determination of the complete amino acid sequence of calmodulin (phenylalanine-rich acidic protein II) from bovine brain." Kasai H., Kato Y., Isobe T., Kawasaki H., Okuyama T. Biomed. Res. 1:248-264(1980) Cited for: PROTEIN SEQUENCE OF 2-149. Tissue: Brain.
[5]	"The complete amino acid sequence of the Ca2+-dependent modulator protein (calmodulin) of bovine brain." Watterson D.M., Sharief F., Vanaman T.C. J. Biol. Chem. 255:962-975(1980) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-149, ACETYLATION AT ALA-2, METHYLATION AT LYS-116. Tissue: Brain.
[6]	"Modulation of calmodulin function by ubiquitin-calmodulin ligase and identification of the responsible ubiquitylation site in vertebrate calmodulin." Laub M., Steppuhn J.A., Blueggel M., Immler D., Meyer H.E., Jennissen H.P. Eur. J. Biochem. 255:422-431(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-28, UBIQUITINATION AT LYS-22.
[7]	"Heat-resistant inhibitors of protein kinase C from bovine brain." Pribilla I., Krueger H., Buchner K., Otto H., Schiebler W., Tripier D., Hucho F. Eur. J. Biochem. 177:657-664(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 39-61.
[8]	Weise C. Unpublished observations (OCT-2002) Cited for: METHYLATION AT LYS-116.
[9]	"Domain Structure of a mammalian myosin I-beta." Reizes O., Barylko B., Li C., Suedhof T.C., Albenisi J.P. Proc. Natl. Acad. Sci. U.S.A. 91:6349-6353(1994) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MYO1C.
[10]	"Motor function and regulation of myosin X." Homma K., Saito J., Ikebe R., Ikebe M. J. Biol. Chem. 276:34348-34354(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MYO10.
[11]	"Two trifluoperazine-binding sites on calmodulin predicted from comparative molecular modeling with troponin-C." Strynadka N.C.J., James M.N.G. Proteins 3:1-17(1988) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF TRIMETHYLATED CALMODULIN.
[12]	"Solution structure of the paramagnetic complex of the N-terminal domain of calmodulin with two Ce3+ ions by 1H NMR." Bentrop D., Bertini I., Cremonini M.A., Forsen S., Luchinat C., Malmendal A. Biochemistry 36:11605-11618(1997) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-75.
[13]	"The structure of apo-calmodulin. A 1H NMR examination of the carboxy-terminal domain." Finn B.E., Drakenberg T., Forsen S. FEBS Lett. 336:368-374(1993) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 77-149.
[14]	"Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex." Meador W.E., Means A.R., Quiocho F.A. Science 257:1251-1255(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[15]	"Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures." Meador W.E., Means A.R., Quiocho F.A. Science 262:1718-1721(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-148.
[16]	"The linker of des-Glu84-calmodulin is bent." Raghunathan S., Chandross R.J., Cheng B.P., Persechini A., Sobottka S.E., Kretsinger R.H. Proc. Natl. Acad. Sci. U.S.A. 90:6869-6873(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 6-148 GLU-85 DEL.
[17]	"Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex." Cook W.J., Walter L.J., Walter M.R. Biochemistry 33:15259-15265(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
[18]	"Trifluoperazine-induced conformational change in Ca(2+)-calmodulin." Vandonselaar M., Hickie R.A., Quail J.W., Delbaere L.T. Nat. Struct. Biol. 1:795-801(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 4-149.
[19]	"Motions of calmodulin characterized using both Bragg and diffuse X-ray scattering." Wall M.E., Clarage J.B., Phillips G.N. Structure 5:1599-1612(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-147.
[20]	"Structure of Escherichia coli fragment TR2C from calmodulin to 1.7 A resolution." Olsson L.L., Sjolin L. Acta Crystallogr. D 57:664-669(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 79-149.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB099053 mRNA. Translation: BAC56543.1.
BC105380 mRNA. Translation: AAI05381.1.
BC120080 mRNA. Translation: AAI20081.1.
BC123890 mRNA. Translation: AAI23891.1.

IPI

IPI00695508.

PIR

MCBO. A90719.

RefSeq

NP_001039714.1. NM_001046249.2.
NP_001229501.1. NM_001242572.1.
NP_001229516.1. NM_001242587.1.

UniGene

Bt.12896.
Bt.53264.
Bt.61778.
Bt.63542.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A29	X-ray	2.74	A	2-148	[»]
1AK8	NMR	-	A	1-76	[»]
1CDM	X-ray	2.00	A	5-148	[»]
1CM1	X-ray	2.00	A	2-149	[»]
1CM4	X-ray	2.00	A	2-149	[»]
1CMF	NMR	-	A	77-148	[»]
1CMG	NMR	-	A	77-148	[»]
1DEG	X-ray	2.90	A	6-148	[»]
1FW4	X-ray	1.70	A	79-149	[»]
1LIN	X-ray	2.00	A	2-149	[»]
1PRW	X-ray	1.70	A	2-148	[»]
1QIV	X-ray	2.64	A	2-149	[»]
1QIW	X-ray	2.30	A/B	2-149	[»]
1XA5	X-ray	2.12	A	2-148	[»]
2CLN	model	-	A	1-149	[»]
2F2O	X-ray	2.17	A/B	1-149	[»]
2F2P	X-ray	2.60	A/B	1-149	[»]
2FOT	X-ray	2.45	A	2-149	[»]
3IF7	X-ray	1.60	A	2-149	[»]

ProteinModelPortal

P62157.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36674N.

IntAct

P62157. 94 interactions.

MINT

MINT-1347941.

Proteomic databases

PaxDb

P62157.

PRIDE

P62157.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000019411; ENSBTAP00000019411; ENSBTAG00000014583.
ENSBTAT00000036194; ENSBTAP00000036057; ENSBTAG00000025644.

GeneID

100297344.
520277.
617095.

KEGG

bta:100297344.
bta:520277.
bta:617095.

Organism-specific databases

CTD

801.
805.
808.

Phylogenomic databases

eggNOG

COG5126.

GeneTree

ENSGT00690000101867.

HOVERGEN

HBG012180.

InParanoid

P62157.

KO

K02183.

OMA

MIREADN.

OrthoDB

EOG4001KK.

Enzyme and pathway databases

BioCyc

CATTLE:520277-MONOMER.

Reactome

REACT_108745. Immune System.
REACT_114534. Signal Transduction.
REACT_29717. Muscle contraction.
REACT_86149. Disease.

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

P62157.

ChEMBL

CHEMBL6092.

EvolutionaryTrace

P62157.

NextBio

20873068.

Entry information

Entry name

CALM_BOVIN

Accession

Primary (citable) accession number: P62157
Secondary accession number(s): P02593 , P70667, P99014, Q08D84, Q2KJE6, Q61379, Q61380

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program