[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Brain; PubMed=2885164 [NCBI, ExPASy, EBI, Israel, Japan] Sherbany A.A., Parent A.S., Brosius J.; "Rat calmodulin cDNA."; DNA 6:267-272(1987).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Brain; DOI=10.1016/0022-2836(87)90258-0; PubMed=3035194 [NCBI, ExPASy, EBI, Israel, Japan] Nojima H., Hirofumi S.; "Structure of a gene for rat calmodulin."; J. Mol. Biol. 193:439-445(1987).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=3037336 [NCBI, ExPASy, EBI, Israel, Japan] Nojima H., Kishi K., Sokabe H.; "Multiple calmodulin mRNA species are derived from two distinct genes."; Mol. Cell. Biol. 7:1873-1880(1987).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=SHR; DOI=10.1016/0022-2836(89)90388-4; PubMed=2527998 [NCBI, ExPASy, EBI, Israel, Japan] Nojima H.; "Structural organization of multiple rat calmodulin genes."; J. Mol. Biol. 208:269-282(1989).
[5]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Wistar; TISSUE=Brain; DOI=10.1016/0169-328X(92)90039-E; PubMed=1315919 [NCBI, ExPASy, EBI, Israel, Japan] Ni B., Rush S., Gurd J.W., Brown I.R.; "Molecular cloning of calmodulin mRNA species which are preferentially expressed in neurons in the rat brain."; Brain Res. Mol. Brain Res. 13:7-17(1992).
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Pituitary; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[7]	PROTEIN SEQUENCE OF 2-149, ACETYLATION AT ALA-2, AND METHYLATION AT LYS-116. TISSUE=Testis; PubMed=201628 [NCBI, ExPASy, EBI, Israel, Japan] Dedman J.R., Jackson R.L., Schreiber W.E., Means A.R.; "Sequence homology of the Ca2+-dependent regulator of cyclic nucleotide phosphodiesterase from rat testis with other Ca2+-binding proteins."; J. Biol. Chem. 253:343-346(1978).
[8]	PROTEIN SEQUENCE OF 15-31; 79-87 AND 92-107, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus; Lubec G., Chen W.-Q., Kang S.U., Lubec S.; Submitted (SEP-2007) to UniProtKB.
[9]	PHOSPHORYLATION AT THR-45. DOI=10.1016/S0003-9861(02)00514-3; PubMed=12392717 [NCBI, ExPASy, EBI, Israel, Japan] Ishida A., Kameshita I., Okuno S., Kitani T., Fujisawa H.; "Phosphorylation of calmodulin by Ca2+/calmodulin-dependent protein kinase IV."; Arch. Biochem. Biophys. 407:72-82(2002).
[10]	ACETYLATION AT ALA-2, AND MASS SPECTROMETRY. Lubec G., Chen W.-Q.; Submitted (FEB-2007) to UniProtKB.
[11]	X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). DOI=10.1038/315037a0; PubMed=3990807 [NCBI, ExPASy, EBI, Israel, Japan] Babu Y.S., Sack J.S., Greenhough T.J., Bugg C.E., Means A.R., Cook W.J.; "Three-dimensional structure of calmodulin."; Nature 315:37-40(1985).
[12]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). DOI=10.1016/0022-2836(88)90608-0; PubMed=3145979 [NCBI, ExPASy, EBI, Israel, Japan] Babu Y.S., Bugg C.E., Cook W.J.; "Structure of calmodulin refined at 2.2-A resolution."; J. Mol. Biol. 204:191-204(1988).

Comments

FUNCTION: Calmodulin mediates the control of a large number of enzymes and other proteins by Ca(2+), AND MASS SPECTROMETRY. Among the enzymes to be stimulated by the calmodulin-Ca(2+) 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: Interacts with CEP97, CEP110, TTN/titin and SRY (By similarity).
INTERACTION:
P00533:EGFR (xeno); NbExp=2; IntAct=EBI-397530, EBI-297353;
P04626:ERBB2 (xeno); NbExp=1; IntAct=EBI-397530, EBI-641062;
Q14451:GRB7 (xeno); NbExp=1; IntAct=EBI-397530, EBI-1257061;
P70604:Kcnn2; NbExp=1; IntAct=EBI-397530, EBI-1031103;
SUBCELLULAR LOCATION: Spindle. Note=Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules (By similarity).
PTM: Ubiquitination results in a strongly decreased activity (By similarity).
PTM: Phosphorylation results in a decreased activity.
MISCELLANEOUS: This protein has four functional calcium-binding sites.
SIMILARITY: Belongs to the calmodulin family.
SIMILARITY: Contains 4 EF-hand domains.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M16659; AAA40864.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X13817; CAA32050.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M19312; AAA40862.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M17069; AAA40863.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X13933; CAA32120.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X13931; CAA32119.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X13932; CAA32119.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X05117; CAA32119.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X13833; CAA32062.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X13834; CAA32062.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X13835; CAA32062.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X14265; CAA32478.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF178845; AAD55398.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC058485; AAH58485.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC063187; AAH63187.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S03206; MCRT.

RefSeq

NP_036650.1; -.
NP_059022.1; -.
NP_114175.1; -.

UniGene

Rn.216430

3D structure databases

PDB

1G4Y; X-ray; 1.60 A; R=1-149.	[ExPASy / RCSB / EBI]
1NIW; X-ray; 2.05 A; A/C/E/G=1-149.	[ExPASy / RCSB / EBI]
1QX5; X-ray; 2.54 A; B/D/I/J/K/R/T/Y=1-149.	[ExPASy / RCSB / EBI]
1QX7; X-ray; 3.09 A; A/B/I/M/R=1-149.	[ExPASy / RCSB / EBI]
2HQW; X-ray; 1.90 A; A=2-149.	[ExPASy / RCSB / EBI]
2PQ3; X-ray; 1.30 A; A=2-77.	[ExPASy / RCSB / EBI]
3B32; X-ray; 1.60 A; A=2-76.	[ExPASy / RCSB / EBI]
3CLN; X-ray; 2.20 A; A=2-149.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1G4Y; -.
1NIW; -.
1QX5; -.
1QX7; -.
2HQW; -.
2PQ3; -.
3B32; -.
3CLN; -.

ModBase

P62161.

Protein-protein interaction databases

IntAct

P62161; -.

PTM databases

PhosphoSite

P62161; -.

Organism-specific databases

RGD

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

GeneLynx

Calm1; Rattus norvegicus.

Gene expression databases

ArrayExpress

P62161; -.

GermOnline

ENSRNOG00000004060; Rattus norvegicus.
ENSRNOG00000016770; Rattus norvegicus.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR011992; EF-Hand_type.
IPR002048; EF_hand_Ca_bd.
IPR001125; Recoverin.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.238.10; EF-Hand_type; 1.

Pfam

PF00036; efhand; 4.
Pfam graphical view of domain structure.

PRINTS

PR00450; RECOVERIN.

ProDom

PD000012; EF-hand; 2.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00054; EFh; 4.
SMART graphical view of domain structure.

PROSITE

PS00018; EF_HAND_1; 4.
PS50222; EF_HAND_2; 4.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P62161.

Genome annotation databases

Ensembl

ENSRNOG00000004060; Rattus norvegicus. [Contig view]
ENSRNOG00000016770; Rattus norvegicus. [Contig view]

GeneID

24242; -.
24244; -.
50663; -.

KEGG

rno:24242; -.
rno:24244; -.
rno:50663; -.

Phylogenomic databases

HOVERGEN

P62161; -.

Other

P62161; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Calcium; Direct protein sequencing; Methylation; Phosphoprotein; Repeat; Ubl conjugation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 149`	`148`	`Calmodulin.`	`PRO_0000198227`
`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.`
`CA_BIND`	`21 32`	`12`	`1.`
`CA_BIND`	`57 68`	`12`	`2.`
`CA_BIND`	`94 105`	`12`	`3.`
`CA_BIND`	`130 141`	`12`	`4.`
`MOD_RES`	`2 2`		`N-acetylalanine.`
`MOD_RES`	`45 45`		`Phosphothreonine; by CaMK4.`
`MOD_RES`	`100 100`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`116 116`		`N6,N6,N6-trimethyllysine.`
`CROSSLNK`	`22 22`		`Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) (By similarity).`
`HELIX`	`7 19`	`13`
`STRAND`	`24 29`	`6`
`HELIX`	`30 32`	`3`
`HELIX`	`33 39`	`7`
`HELIX`	`46 56`	`11`
`STRAND`	`61 65`	`5`
`HELIX`	`66 76`	`11`
`HELIX`	`83 91`	`9`
`STRAND`	`97 102`	`6`
`HELIX`	`103 110`	`8`
`HELIX`	`119 129`	`11`
`STRAND`	`133 138`	`6`
`HELIX`	`139 147`	`9`

Sequence information

Length: 149 AA [This is the length of the unprocessed precursor]

Molecular weight: 16838 Da [This is the MW of the unprocessed precursor]

CRC64: 6B4BC3FCDE10727B [This is a checksum on the sequence]

        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

P62161 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools