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P62161 (CALM_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. 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:Calm1
Synonyms:Calm, Cam, Cam1
AND
Name:Calm2
Synonyms:Cam2, Camb
AND
Name:Calm3
Synonyms:Cam3, Camc
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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, MYO1C, TTN/titin and SRY. Interacts with MYO10 and MYO5A. 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 By similarity. Interacts with RRAD. Interacts with ORAI1; this may play a role in the regulation of ORAI1-mediated calcium transport. Ref.10 Ref.14

Subcellular location

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 By similarity.

Phosphorylation results in a decreased activity.

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_processactivation of adenylate cyclase activity

Inferred from direct assay PubMed 19305019. Source: RGD

calcium-mediated signaling

Inferred from mutant phenotype PubMed 20717650. Source: RGD

detection of calcium ion

Inferred from electronic annotation. Source: Ensembl

positive regulation of cyclic-nucleotide phosphodiesterase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric-oxide synthase activity

Inferred from direct assay PubMed 20529840. Source: RGD

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 high voltage-gated calcium channel activity

Inferred from mutant phenotype PubMed 18322004. Source: RGD

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

Inferred from electronic annotation. Source: Ensembl

regulation of ryanodine-sensitive calcium-release channel activity

Inferred from direct assay PubMed 15628869. Source: RGD

regulation of store-operated calcium channel activity

Inferred by curator Ref.14. Source: RGD

response to amphetamine

Inferred from expression pattern PubMed 10854758. Source: RGD

response to corticosterone

Inferred from expression pattern PubMed 16503919. Source: RGD

   Cellular_componentcalcium channel complex

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 21912933PubMed 7492944. Source: RGD

cytosol

Traceable author statement. Source: Reactome

growth cone

Inferred from direct assay PubMed 7492944. Source: RGD

neuron projection

Inferred from direct assay PubMed 7492944. Source: RGD

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 7492944. Source: RGD

plasma membrane

Inferred from direct assay PubMed 21912933. Source: RGD

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_functionadenylate cyclase binding

Inferred from direct assay PubMed 19305019. Source: RGD

calcium channel regulator activity

Non-traceable author statement PubMed 12032157. Source: RGD

calcium ion binding

Inferred from direct assay PubMed 15628869Ref.14. Source: RGD

calcium-dependent protein binding

Inferred from physical interaction PubMed 12032157PubMed 21855531. Source: RGD

enzyme regulator activity

Inferred from mutant phenotype PubMed 20717650. Source: RGD

ion channel binding

Inferred from direct assay PubMed 15628869Ref.14. Source: RGD

nitric-oxide synthase binding

Inferred from direct assay PubMed 20529840. Source: RGD

nitric-oxide synthase regulator activity

Inferred from direct assay PubMed 20529840. Source: RGD

phosphatidylinositol 3-kinase binding

Inferred from physical interaction PubMed 17492691. Source: RGD

protein N-terminus binding

Inferred from mutant phenotype PubMed 19292454. Source: RGD

protein binding

Inferred from physical interaction PubMed 12021391Ref.10. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction PubMed 21855531. Source: RGD

protein phosphatase activator activity

Inferred from electronic annotation. Source: Ensembl

type 3 metabotropic glutamate receptor binding

Inferred from physical interaction PubMed 21855531. Source: RGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EGFRP005336EBI-397530,EBI-297353From a different organism.
GRB7Q144519EBI-397530,EBI-970191From a different organism.
Hmox2P237112EBI-397530,EBI-2910092
Kcnn2P706042EBI-397530,EBI-1031103
Kcnq2O889434EBI-397530,EBI-7900557
SEC61A1P383774EBI-397530,EBI-8517797From a different organism.
THOP1P528882EBI-397530,EBI-372399From a different organism.
Thop1P241552EBI-397530,EBI-6372841

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 149148Calmodulin
PRO_0000198227

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.7 Ref.11
Modified residue221N6-acetyllysine; alternate By similarity
Modified residue451Phosphothreonine; by CaMK4 Ref.9
Modified residue951N6-acetyllysine By similarity
Modified residue1001Phosphotyrosine By similarity
Modified residue1021Phosphoserine By similarity
Modified residue1161N6,N6,N6-trimethyllysine Ref.7
Modified residue1391Phosphotyrosine By similarity
Cross-link22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P62161 [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]"Rat calmodulin cDNA."
Sherbany A.A., Parent A.S., Brosius J.
DNA 6:267-272(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Structure of a gene for rat calmodulin."
Nojima H., Hirofumi S.
J. Mol. Biol. 193:439-445(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"Multiple calmodulin mRNA species are derived from two distinct genes."
Nojima H., Kishi K., Sokabe H.
Mol. Cell. Biol. 7:1873-1880(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Structural organization of multiple rat calmodulin genes."
Nojima H.
J. Mol. Biol. 208:269-282(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: SHR.
[5]"Molecular cloning of calmodulin mRNA species which are preferentially expressed in neurons in the rat brain."
Ni B., Rush S., Gurd J.W., Brown I.R.
Brain Res. Mol. Brain Res. 13:7-17(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Brain.
[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].
Tissue: Pituitary.
[7]"Sequence homology of the Ca2+-dependent regulator of cyclic nucleotide phosphodiesterase from rat testis with other Ca2+-binding proteins."
Dedman J.R., Jackson R.L., Schreiber W.E., Means A.R.
J. Biol. Chem. 253:343-346(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-149, ACETYLATION AT ALA-2, METHYLATION AT LYS-116.
Tissue: Testis.
[8]Lubec G., Chen W.-Q., Kang S.U., Lubec S.
Submitted (SEP-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 15-31; 79-87 AND 92-107, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain and Hippocampus.
[9]"Phosphorylation of calmodulin by Ca2+/calmodulin-dependent protein kinase IV."
Ishida A., Kameshita I., Okuno S., Kitani T., Fujisawa H.
Arch. Biochem. Biophys. 407:72-82(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-45.
[10]"Rad GTPase deficiency leads to cardiac hypertrophy."
Chang L., Zhang J., Tseng Y.-H., Xie C.-Q., Ilany J., Bruning J.C., Sun Z., Zhu X., Cui T., Youker K.A., Yang Q., Day S.M., Kahn C.R., Chen Y.E.
Circulation 116:2976-2983(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RRAD.
[11]Lubec G., Chen W.-Q.
Submitted (FEB-2007) to UniProtKB
Cited for: ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"Three-dimensional structure of calmodulin."
Babu Y.S., Sack J.S., Greenhough T.J., Bugg C.E., Means A.R., Cook W.J.
Nature 315:37-40(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[13]"Structure of calmodulin refined at 2.2-A resolution."
Babu Y.S., Bugg C.E., Cook W.J.
J. Mol. Biol. 204:191-204(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[14]"Crystal structure of calmodulin binding domain of orai1 in complex with Ca2+ calmodulin displays a unique binding mode."
Liu Y., Zheng X., Mueller G.A., Sobhany M., DeRose E.F., Zhang Y., London R.E., Birnbaumer L.
J. Biol. Chem. 287:43030-43041(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ORAI1, INTERACTION WITH ORAI1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M16659 mRNA. Translation: AAA40864.1.
X13817 mRNA. Translation: CAA32050.1.
M19312 mRNA. Translation: AAA40862.1.
M17069 mRNA. Translation: AAA40863.1.
X13933 mRNA. Translation: CAA32120.1.
X13931, X13932, X05117 Genomic DNA. Translation: CAA32119.1.
X13833, X13834, X13835 Genomic DNA. Translation: CAA32062.1.
X14265 Genomic DNA. Translation: CAA32478.1.
AF178845 mRNA. Translation: AAD55398.1.
BC058485 mRNA. Translation: AAH58485.1.
BC063187 mRNA. Translation: AAH63187.1.
PIRMCRT. S03206.
RefSeqNP_036650.1. NM_012518.3.
NP_059022.1. NM_017326.2.
NP_114175.1. NM_031969.2.
UniGeneRn.216430.
Rn.2892.
Rn.4166.
Rn.5968.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G4YX-ray1.60R2-149[»]
1NIWX-ray2.05A/C/E/G2-149[»]
1QX5X-ray2.54B/D/I/J/K/R/T/Y2-149[»]
1QX7X-ray3.09A/B/I/M/R2-149[»]
2HQWX-ray1.90A2-149[»]
2MGUNMR-A2-149[»]
2PQ3X-ray1.30A2-77[»]
2YGGX-ray2.23B1-149[»]
3B32X-ray1.60A2-76[»]
3BXKX-ray2.55A/C2-149[»]
3BXLX-ray2.30A2-149[»]
3CLNX-ray2.20A2-149[»]
3EK4X-ray2.65A3-149[»]
3EK7X-ray1.85A3-149[»]
3EK8X-ray2.80A3-149[»]
3EKHX-ray2.00A3-149[»]
3EKJX-ray2.80A3-149[»]
3EVRX-ray2.00A3-148[»]
3EVUX-ray1.75A3-148[»]
3EVVX-ray2.60A3-148[»]
3IFKX-ray2.03A/B2-91[»]
3SG2X-ray2.00A3-149[»]
3SG3X-ray2.10A3-149[»]
3SG4X-ray2.40A3-149[»]
3SG5X-ray1.90A3-149[»]
3SG6X-ray1.70A3-149[»]
3SG7X-ray1.90A3-149[»]
3SJQX-ray1.90A/B1-149[»]
3WLCX-ray2.49A3-149[»]
3WLDX-ray2.70A3-149[»]
4EHQX-ray1.90A2-149[»]
4G27X-ray1.65R1-149[»]
4G28X-ray1.63R1-149[»]
4I2YX-ray2.20A/B3-149[»]
4IL1X-ray3.00A/B/C/D1-149[»]
4J9YX-ray1.51R1-149[»]
4J9ZX-ray1.66R1-149[»]
ProteinModelPortalP62161.
SMRP62161. Positions 1-149.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246428. 24 interactions.
DIPDIP-29528N.
IntActP62161. 14 interactions.
MINTMINT-268601.
STRING10116.ENSRNOP00000022603.

Chemistry

BindingDBP62161.

PTM databases

PhosphoSiteP62161.

Proteomic databases

PaxDbP62161.
PRIDEP62161.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000022603; ENSRNOP00000022603; ENSRNOG00000016770.
ENSRNOT00000064679; ENSRNOP00000063822; ENSRNOG00000004060.
GeneID24242.
24244.
50663.
KEGGrno:24242.
rno:24244.
rno:50663.
UCSCRGD:2257. rat.

Organism-specific databases

CTD801.
805.
808.
RGD2257. Calm1.
2258. Calm2.
2259. Calm3.

Phylogenomic databases

eggNOGCOG5126.
GeneTreeENSGT00690000101867.
HOGENOMHOG000233018.
HOVERGENHBG012180.
InParanoidP62161.
KOK02183.
OMATEQISEF.
OrthoDBEOG7F7WBV.
TreeFamTF300912.

Enzyme and pathway databases

ReactomeREACT_206767. Disease.
REACT_212996. Signal Transduction.
REACT_224525. Neuronal System.
REACT_225304. Organelle biogenesis and maintenance.
REACT_227097. Immune System.

Gene expression databases

GenevestigatorP62161.

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.
[Graphical view]
PfamPF13499. EF-hand_7. 2 hits.
[Graphical view]
SMARTSM00054. EFh. 4 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP62161.
NextBio602729.
PROP62161.

Entry information

Entry nameCALM_RAT
AccessionPrimary (citable) accession number: P62161
Secondary accession number(s): P02593 expand/collapse secondary AC list , P70667, P99014, Q61379, Q61380
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 120 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