P62161 (CALM_RAT) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › 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+. 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. Interacts with MYO10. Interacts with RRAD. 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 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 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	activation of adenylate cyclase activity Inferred from direct assay PubMed 19305019. Source: RGD calcium-mediated signaling Inferred from mutant phenotype PubMed 20717650. Source: RGD positive regulation of nitric-oxide synthase activity Inferred from direct assay PubMed 20529840. Source: RGD regulation of high voltage-gated calcium channel activity Inferred from mutant phenotype PubMed 18322004. Source: RGD 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 PubMed 23109337. Source: RGD response to amphetamine Inferred from expression pattern PubMed 10854758. Source: RGD response to corticosterone stimulus Inferred from expression pattern PubMed 16503919. Source: RGD
Cellular_component	cytosol Traceable author statement. Source: Reactome growth cone Inferred from direct assay PubMed 7492944. Source: RGD nucleoplasm Traceable author statement. Source: Reactome plasma membrane Inferred from direct assay PubMed 21912933. Source: RGD spindle pole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	adenylate 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 15628869PubMed 23109337. Source: RGD ion channel binding Inferred from direct assay PubMed 15628869PubMed 23109337. 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 protein N-terminus binding Inferred from mutant phenotype PubMed 19292454. 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
Thop1	P24155	2	EBI-397530,EBI-6372841

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 149

148

Calmodulin

PRO_0000198227

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.7 Ref.11

Modified residue

22

1

N6-acetyllysine By similarity

Modified residue

45

1

Phosphothreonine; by CaMK4 Ref.9

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.7

Modified residue

139

1

Phosphotyrosine By similarity

Cross-link

22

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

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

149

Helix Strand Turn

Details...

Helix

7 – 19

13

Beta strand

24 – 29

6

Helix

30 – 32

3

Helix

33 – 39

7

Helix

46 – 56

11

Beta strand

61 – 65

5

Helix

66 – 76

11

Turn

79 – 81

3

Helix

83 – 91

9

Beta strand

97 – 102

6

Helix

103 – 110

8

Helix

113 – 115

3

Helix

119 – 129

11

Beta strand

133 – 138

6

Helix

139 – 147

9

Sequences

	Sequence		Length	Mass (Da)
	P62161 [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]	"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, 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, 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).
+	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_017326.2.
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	[»]
3SG2	X-ray	2.00	A	3-149	[»]
3SG3	X-ray	2.10	A	3-149	[»]
3SG4	X-ray	2.40	A	3-149	[»]
3SG5	X-ray	1.90	A	3-149	[»]
3SG6	X-ray	1.70	A	3-149	[»]
3SG7	X-ray	1.90	A	3-149	[»]
3SJQ	X-ray	1.90	A/B	1-149	[»]
4EHQ	X-ray	1.90	A	2-149	[»]
4G27	X-ray	1.65	R	1-149	[»]
4G28	X-ray	1.63	R	1-149	[»]
4J9Y	X-ray	1.51	R	1-149	[»]
4J9Z	X-ray	1.66	R	1-149	[»]

ProteinModelPortal

P62161.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29528N.

IntAct

P62161. 10 interactions.

MINT

MINT-268601.

STRING

10116.ENSRNOP00000022603.

PTM databases

PhosphoSite

P62161.

Proteomic databases

PaxDb

P62161.

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

RGD:2257. rat.

Organism-specific databases

CTD

801.
805.
808.

RGD

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

Phylogenomic databases

eggNOG

COG5126.

GeneTree

ENSGT00690000101867.

HOGENOM

HOG000233018.

HOVERGEN

HBG012180.

InParanoid

P62161.

KO

K02183.

OrthoDB

EOG4001KK.

Enzyme and pathway databases

Reactome

REACT_109781. Immune System.
REACT_110573. Disease.
REACT_111984. Signal Transduction.
REACT_78038. Neuronal System.

Gene expression databases

ArrayExpress

P62161.

Genevestigator

P62161.

GermOnline

ENSRNOG00000004060. Rattus norvegicus.
ENSRNOG00000016770. Rattus norvegicus.

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

P62161.

EvolutionaryTrace

P62161.

NextBio

602729.

Entry information

Entry name

CALM_RAT

Accession

Primary (citable) accession number: P62161
Secondary accession number(s): P02593 , P70667, P99014, 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 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program