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P62149 (CALM_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 99. 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·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
ORF Names:RCJMB04_24e7
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

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 and other proteins by Ca2+. Among the enzymes to be stimulated by the calmodulin-Ca2+ complex are a number of protein kinases and phosphatases.

Miscellaneous

This protein has four functional calcium-binding sites.

Sequence similarities

Belongs to the calmodulin family.

Contains 4 EF-hand domains.

Ontologies

Keywords
   DomainRepeat
   LigandCalcium
Metal-binding
   PTMAcetylation
Methylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdetection of calcium ion

Inferred from electronic annotation. Source: Ensembl

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 electronic annotation. Source: Ensembl

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 electronic annotation. Source: Ensembl

   Cellular_componentcalcium channel complex

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from electronic annotation. Source: Ensembl

sarcomere

Inferred from electronic annotation. Source: Ensembl

spindle microtubule

Inferred from electronic annotation. Source: Ensembl

spindle pole

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

protein phosphatase activator activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 149148Calmodulin
PRO_0000198230

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 By similarity
Modified residue1161N6,N6,N6-trimethyllysine By similarity

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P62149 [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]"Chicken calmodulin genes. A species comparison of cDNA sequences and isolation of a genomic clone."
Putkey J.A., Ts'Ui K.F., Tanaka T., Lagace L., Stein J.P., Lai E.C., Means A.R.
J. Biol. Chem. 258:11864-11870(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The structural organization of the chicken calmodulin gene."
Simmen R.C.M., Tanaka T., Ts'Ui K.F., Putkey J.A., Scott M.J., Lai E.C., Means A.R.
J. Biol. Chem. 260:907-912(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]Erratum
Simmen R.C.M., Tanaka T., Ts'Ui K.F., Putkey J.A., Scott M.J., Lai E.C., Means A.R.
J. Biol. Chem. 262:4928-4929(1987)
[4]"cDNA sequences and molecular evolution of calmodulin genes of chicken and eel."
Iida Y.
Bull. Chem. Soc. Jpn. 57:2667-2668(1984)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Full-length cDNAs from chicken bursal lymphocytes to facilitate gene function analysis."
Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.
Genome Biol. 6:R6.1-R6.9(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: CB.
Tissue: Bursa of Fabricius.
[6]"The structure of a calmodulin mutant with a deletion in the central helix: implications for molecular recognition and protein binding."
Tabernero L., Taylor D.A., Chandross R.J., VanBerkum M.F.A., Means A.R., Quiocho F.A., Sack J.S.
Structure 5:613-622(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L00101 expand/collapse EMBL AC list , L00096, L00097, L00098, L00099, L00100 Genomic DNA. Translation: AAA48653.1.
M36167 mRNA. Translation: AAA48650.1.
AJ720728 mRNA. Translation: CAG32387.1.
PIRMCCH. A92394.
UniGeneGga.11685.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AHRX-ray1.80A2-147[»]
1UP5X-ray1.90A/B2-149[»]
2BCXX-ray2.00A2-148[»]
2BKIX-ray2.90B/D2-148[»]
2KZ2NMR-A77-149[»]
2M3SNMR-A1-149[»]
2O5GX-ray1.08A2-149[»]
2O60X-ray1.55A2-149[»]
2VB6X-ray2.30B1-147[»]
3GOFX-ray1.45A/B2-149[»]
3GP2X-ray1.46A2-148[»]
ProteinModelPortalP62149.
SMRP62149. Positions 1-149.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29154N.
STRING9031.ENSGALP00000037503.

Chemistry

BindingDBP62149.

Proteomic databases

PaxDbP62149.
PRIDEP62149.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG5126.
HOVERGENHBG012180.
InParanoidP62149.
OMANEVDEMI.
OrthoDBEOG7F7WBV.
TreeFamTF300912.

Gene expression databases

ArrayExpressP62149.

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

EvolutionaryTraceP62149.

Entry information

Entry nameCALM_CHICK
AccessionPrimary (citable) accession number: P62149
Secondary accession number(s): P02593 expand/collapse secondary AC list , P70667, P99014, Q5ZIQ6, Q61379, Q61380
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 99 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