Calmodulin - Rattus norvegicus (Rat)

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P62161 (CALM_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 92. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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⁺, AND MASS SPECTROMETRY. 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 By similarity. Interacts with RRAD. Interacts with USP6; the interaction is calcium dependent By similarity. Interacts with CDK5RAP2. Interacts with SCN5A By similarity. Ref.10
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.
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
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	spindle pole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium channel regulator activity Non-traceable author statement. Source: RGD calcium-dependent protein binding Inferred from physical interaction. Source: RGD phosphatidylinositol 3-kinase binding Inferred from physical interaction. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EGFR	P00533	6	EBI-397530,EBI-297353	From a different organism.
GRB7	Q14451	9	EBI-397530,EBI-970191	From a different organism.
Hmox2	P23711	2	EBI-397530,EBI-2910092
Kcnn2	P70604	2	EBI-397530,EBI-1031103

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.7

Chain

2 – 149

148

Calmodulin

PRO_0000198227

Regions

Domain

8 – 43

EF-hand 1

Domain

44 – 79

EF-hand 2

Domain

81 – 116

EF-hand 3

Domain

117 – 149

EF-hand 4

Calcium binding

Calcium binding

Calcium binding

Calcium binding

Amino acid modifications

Modified residue

N-acetylalanine Ref.7 Ref.11

Modified residue

N6-acetyllysine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

Phosphothreonine; by CaMK4 Ref.9

Modified residue

N6-acetyllysine By similarity

Modified residue

100

Phosphotyrosine By similarity

Modified residue

116

N6,N6,N6-trimethyllysine Ref.7

Modified residue

139

Phosphotyrosine By similarity

Cross-link

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

Secondary structure

149

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P62161 [UniParc].

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

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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Rat calmodulin cDNA." Sherbany A.A., Parent A.S., Brosius J. DNA 6:267-272(1987) [PubMed: 2885164] [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: 3035194] [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: 3037336] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Structural organization of multiple rat calmodulin genes." Nojima H. J. Mol. Biol. 208:269-282(1989) [PubMed: 2527998] [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: 1315919] [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: 15489334] [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: 201628] [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, 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: 12392717] [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: 18056528] [Abstract] Cited for: INTERACTION WITH RRAD.
[11]	Lubec G., Chen W.-Q. Submitted (FEB-2007) to UniProtKB Cited for: ACETYLATION AT ALA-2, 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: 3990807] [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: 3145979] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+	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.

IPI

IPI00231955.

PIR

MCRT. S03206.

RefSeq

NP_036650.1. NM_012518.3.
NP_059022.1. NM_017326.1.
NP_114175.1. NM_031969.2.

UniGene

Rn.216430.
Rn.2892.
Rn.4166.
Rn.5968.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G4Y	X-ray	1.60	R	2-149	[»]
1NIW	X-ray	2.05	A/C/E/G	2-149	[»]
1QX5	X-ray	2.54	B/D/I/J/K/R/T/Y	2-148	[»]
1QX7	X-ray	3.09	A/B/I/M/R	2-148	[»]
2HQW	X-ray	1.90	A	2-149	[»]
2PQ3	X-ray	1.30	A	2-77	[»]
2YGG	X-ray	2.23	B	1-149	[»]
3B32	X-ray	1.60	A	2-76	[»]
3BXK	X-ray	2.55	A/C	2-149	[»]
3BXL	X-ray	2.30	A	2-149	[»]
3CLN	X-ray	2.20	A	2-149	[»]
3EK4	X-ray	2.65	A	3-149	[»]
3EK7	X-ray	1.85	A	3-149	[»]
3EK8	X-ray	2.80	A	3-149	[»]
3EKH	X-ray	2.00	A	3-149	[»]
3EKJ	X-ray	2.80	A	3-149	[»]
3EVR	X-ray	2.00	A	3-148	[»]
3EVU	X-ray	1.75	A	3-148	[»]
3EVV	X-ray	2.60	A	3-148	[»]
3IFK	X-ray	2.03	A/B	2-91	[»]

ProteinModelPortal

P62161.

SMR

P62161. Positions 2-148.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29528N.

IntAct

P62161. 9 interactions.

MINT

MINT-268601.

STRING

P62161.

PTM databases

PhosphoSite

P62161.

Proteomic databases

PRIDE

P62161.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000022603; ENSRNOP00000022603; ENSRNOG00000016770.
ENSRNOT00000064679; ENSRNOP00000063822; ENSRNOG00000004060.

GeneID

24242.
24244.
50663.

KEGG

rno:24242.
rno:24244.
rno:50663.

UCSC

M16659. rat.

Organism-specific databases

CTD

801.
805.
808.

RGD

2257. Calm1.
2258. Calm2.
2259. Calm3.

Phylogenomic databases

eggNOG

maNOG12102.

GeneTree

ENSGT00560000076590.

HOVERGEN

HBG012180.

InParanoid

P62161.

OrthoDB

EOG4001KK.

PhylomeDB

P62161.

Gene expression databases

ArrayExpress

P62161.

Genevestigator

P62161.

GermOnline

ENSRNOG00000004060. Rattus norvegicus.
ENSRNOG00000016770. Rattus norvegicus.

Family and domain databases

InterPro

IPR018248. EF-hand.
IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca-bd.
IPR001125. Recoverin.
[Graphical view]

Gene3D

G3DSA:1.10.238.10. EF-Hand_type. 2 hits.

K02183.

Pfam

PF00036. efhand. 4 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

NextBio

602729.

Entry information

Entry name

CALM_RAT

Accession

Primary (citable) accession number: P62161
Secondary accession number(s): P02593

Q61380

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents