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P62157 (CALM_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calmodulin

Short name=CaM
Gene names
Name:CALM
Synonyms:CAM
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length149 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins 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 CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis By similarity.

Subunit structure

Interacts with CEP97, CCP110, TTN/titin and SRY. Interacts with MYO5A 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 FCHO1. Interacts with MIP in a 1:2 stoichiometry; the interaction with the cytoplasmic domains from two MIP subunits promotes MIP water channel closure. Interacts with ORAI1; this may play a role in the regulation of ORAI1-mediated calcium transport By similarity. Interacts with MYO10 and MYO1C. Ref.9 Ref.10

Subcellular location

Cytoplasm. Cytoplasmcytoskeletonspindle. Cytoplasmcytoskeletonspindle 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 componentCytoplasm
Cytoskeleton
   DomainRepeat
   LigandCalcium
Metal-binding
   PTMAcetylation
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdetection of calcium ion

Inferred from electronic annotation. Source: Ensembl

negative regulation of ryanodine-sensitive calcium-release channel activity

Inferred from direct assay PubMed 19220289. Source: BHF-UCL

positive regulation of cyclic nucleotide metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cyclic-nucleotide phosphodiesterase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphoprotein phosphatase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein dephosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of ryanodine-sensitive calcium-release channel activity

Inferred from direct assay PubMed 19220289. Source: BHF-UCL

regulation of cardiac muscle contraction

Inferred from electronic annotation. Source: Ensembl

regulation of cytokinesis

Inferred from electronic annotation. Source: Ensembl

regulation of heart rate

Inferred from electronic annotation. Source: Ensembl

regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum

Inferred from direct assay PubMed 19220289. Source: BHF-UCL

   Cellular_componentcalcium channel complex

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from electronic annotation. Source: Ensembl

cytosol

Traceable author statement. Source: Reactome

sarcomere

Inferred from electronic annotation. Source: Ensembl

spindle microtubule

Inferred from electronic annotation. Source: Ensembl

spindle pole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from direct assay PubMed 19220289. Source: BHF-UCL

protein phosphatase activator activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ACA8Q9LF7914EBI-397403,EBI-980643From a different organism.
AT4G30490Q8L5174EBI-397403,EBI-4439046From a different organism.
GRB7Q144512EBI-397403,EBI-970191From a different organism.
Hmox2P237113EBI-397403,EBI-2910092From a different organism.
LTFP027882EBI-397403,EBI-1058602From a different organism.
Nos1P294762EBI-397403,EBI-349460From a different organism.
Nos3Q626002EBI-397403,EBI-7052018From a different organism.
NOX5Q96PH1-43EBI-397403,EBI-7305642From a different organism.
STIM1Q135862EBI-397403,EBI-448878From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3 Ref.4 Ref.5 Ref.6
Chain2 – 149148Calmodulin
PRO_0000198222

Regions

Domain8 – 4336EF-hand 1
Domain44 – 7936EF-hand 2
Domain81 – 11636EF-hand 3
Domain117 – 14933EF-hand 4
Calcium binding21 – 32121
Calcium binding57 – 68122
Calcium binding94 – 105123
Calcium binding130 – 141124

Amino acid modifications

Modified residue21N-acetylalanine Ref.5
Modified residue221N6-acetyllysine; alternate By similarity
Modified residue451Phosphothreonine; by CaMK4 By similarity
Modified residue951N6-acetyllysine By similarity
Modified residue1001Phosphotyrosine By similarity
Modified residue1021Phosphoserine By similarity
Modified residue1161N6,N6,N6-trimethyllysine Ref.5 Ref.8
Modified residue1391Phosphotyrosine By similarity
Cross-link22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.6

Secondary structure

......................... 149
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62157 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 6B4BC3FCDE10727B

FASTA14916,838
        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 

« Hide

References

« Hide '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.
PIRMCBO. A90719.
RefSeqNP_001039714.1. NM_001046249.2.
NP_001229501.1. NM_001242572.1.
NP_001229516.1. NM_001242587.1.
UniGeneBt.12896.
Bt.53264.
Bt.61778.
Bt.63542.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A29X-ray2.74A2-148[»]
1AK8NMR-A1-76[»]
1CDMX-ray2.00A5-148[»]
1CM1X-ray2.00A2-149[»]
1CM4X-ray2.00A2-149[»]
1CMFNMR-A77-148[»]
1CMGNMR-A77-148[»]
1DEGX-ray2.90A6-148[»]
1FW4X-ray1.70A79-149[»]
1LINX-ray2.00A2-149[»]
1PRWX-ray1.70A2-148[»]
1QIVX-ray2.64A2-149[»]
1QIWX-ray2.30A/B2-149[»]
1XA5X-ray2.12A2-148[»]
2CLNmodel-A1-149[»]
2F2OX-ray2.17A/B1-149[»]
2F2PX-ray2.60A/B1-149[»]
2FOTX-ray2.45A2-149[»]
3IF7X-ray1.60A2-149[»]
ProteinModelPortalP62157.
SMRP62157. Positions 1-149.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid176895. 1 interaction.
544691. 5 interactions.
DIPDIP-36674N.
IntActP62157. 100 interactions.
MINTMINT-1347941.

Chemistry

BindingDBP62157.
ChEMBLCHEMBL6092.

Proteomic databases

PaxDbP62157.
PRIDEP62157.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000019411; ENSBTAP00000019411; ENSBTAG00000014583.
ENSBTAT00000036194; ENSBTAP00000036057; ENSBTAG00000025644.
GeneID100297344.
520277.
617095.
KEGGbta:100297344.
bta:520277.
bta:617095.

Organism-specific databases

CTD801.
805.
808.

Phylogenomic databases

eggNOGCOG5126.
GeneTreeENSGT00690000101867.
HOVERGENHBG012180.
InParanoidP62157.
KOK02183.
OMAYQEFVKM.
OrthoDBEOG7F7WBV.
TreeFamTF300912.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001125. Recoverin_like.
[Graphical view]
PfamPF13499. EF-hand_7. 2 hits.
[Graphical view]
PRINTSPR00450. RECOVERIN.
SMARTSM00054. EFh. 4 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP62157.
NextBio20873068.

Entry information

Entry nameCALM_BOVIN
AccessionPrimary (citable) accession number: P62157
Secondary accession number(s): P02593 expand/collapse secondary AC list , P70667, P99014, Q08D84, Q2KJE6, Q61379, Q61380
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references