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UniProtKB/Swiss-Prot entry P62157

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CALM_BOVIN
Primary accession number P62157
Secondary accession numbers P02593 P70667 P99014 Q08D84 Q2KJE6 Q61379 Q61380
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 59)
Name and origin of the protein
Protein name Calmodulin
Synonym CaM
Gene name
Name: CALM
Synonyms: CAM
From
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1002/mrd.10292; PubMed=12658628 [NCBI, ExPASy, EBI, Israel, Japan]
Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H., Takahashi T., Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y., Tsujimoto G., Izaike Y., Todoroki J., Hashizume K.;
"Characterization of gene expression profiles in early bovine pregnancy using a custom cDNA microarray.";
Mol. Reprod. Dev. 65:9-18(2003).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus, and Hereford;
TISSUE=Fetal pons, Ileum, and Uterus;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[3]
 PROTEIN SEQUENCE OF 2-149.
TISSUE=Uterus;
Grand R.J.A., Perry S.V.;
"The amino acid sequence of the troponin C-like protein (modulator protein) from bovine uterus.";
FEBS Lett. 92:137-142(1978).
[4]
 PROTEIN SEQUENCE OF 2-149.
TISSUE=Brain;
Kasai H., Kato Y., Isobe T., Kawasaki H., Okuyama T.;
"Determination of the complete amino acid sequence of calmodulin (phenylalanine-rich acidic protein II) from bovine brain.";
Biomed. Res. 1:248-264(1980).
[5]
 PROTEIN SEQUENCE OF 2-149, ACETYLATION AT ALA-2, AND METHYLATION AT LYS-116.
TISSUE=Brain;
PubMed=7356670 [NCBI, ExPASy, EBI, Israel, Japan]
Watterson D.M., Sharief F., Vanaman T.C.;
"The complete amino acid sequence of the Ca2+-dependent modulator protein (calmodulin) of bovine brain.";
J. Biol. Chem. 255:962-975(1980).
[6]
 PROTEIN SEQUENCE OF 2-28, AND UBIQUITINATION AT LYS-22.
PubMed=9716384 [NCBI, ExPASy, EBI, Israel, Japan]
Laub M., Steppuhn J.A., Blueggel M., Immler D., Meyer H.E., Jennissen H.P.;
"Modulation of calmodulin function by ubiquitin-calmodulin ligase and identification of the responsible ubiquitylation site in vertebrate calmodulin.";
Eur. J. Biochem. 255:422-431(1998).
[7]
 PROTEIN SEQUENCE OF 39-61.
PubMed=3058479 [NCBI, ExPASy, EBI, Israel, Japan]
Pribilla I., Krueger H., Buchner K., Otto H., Schiebler W., Tripier D., Hucho F.;
"Heat-resistant inhibitors of protein kinase C from bovine brain.";
Eur. J. Biochem. 177:657-664(1988).
[8]
 METHYLATION AT LYS-116.
Weise C.;
Unpublished observations (OCT-2002).
[9]
 3D-STRUCTURE MODELING OF TRIMETHYLATED CALMODULIN.
DOI=10.1002/prot.340030102; PubMed=3375233 [NCBI, ExPASy, EBI, Israel, Japan]
Strynadka N.C.J., James M.N.G.;
"Two trifluoperazine-binding sites on calmodulin predicted from comparative molecular modeling with troponin-C.";
Proteins 3:1-17(1988).
[10]
 STRUCTURE BY NMR OF 1-75.
DOI=10.1021/bi971022+; PubMed=9305950 [NCBI, ExPASy, EBI, Israel, Japan]
Bentrop D., Bertini I., Cremonini M.A., Forsen S., Luchinat C., Malmendal A.;
"Solution structure of the paramagnetic complex of the N-terminal domain of calmodulin with two Ce3+ ions by 1H NMR.";
Biochemistry 36:11605-11618(1997).
[11]
 STRUCTURE BY NMR OF 77-149.
DOI=10.1016/0014-5793(93)80839-M; PubMed=8262263 [NCBI, ExPASy, EBI, Israel, Japan]
Finn B.E., Drakenberg T., Forsen S.;
"The structure of apo-calmodulin. A 1H NMR examination of the carboxy-terminal domain.";
FEBS Lett. 336:368-374(1993).
[12]
 X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=1519061 [NCBI, ExPASy, EBI, Israel, Japan]
Meador W.E., Means A.R., Quiocho F.A.;
"Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex.";
Science 257:1251-1255(1992).
[13]
 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-148.
PubMed=8259515 [NCBI, ExPASy, EBI, Israel, Japan]
Meador W.E., Means A.R., Quiocho F.A.;
"Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures.";
Science 262:1718-1721(1993).
[14]
 X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 6-148 GLU-85 DEL.
PubMed=8341712 [NCBI, ExPASy, EBI, Israel, Japan]
Raghunathan S., Chandross R.J., Cheng B.P., Persechini A., Sobottka S.E., Kretsinger R.H.;
"The linker of des-Glu84-calmodulin is bent.";
Proc. Natl. Acad. Sci. U.S.A. 90:6869-6873(1993).
[15]
 X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
DOI=10.1021/bi00255a006; PubMed=7803388 [NCBI, ExPASy, EBI, Israel, Japan]
Cook W.J., Walter L.J., Walter M.R.;
"Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex.";
Biochemistry 33:15259-15265(1994).
[16]
 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 4-149.
DOI=10.1038/nsb1194-795; PubMed=7634090 [NCBI, ExPASy, EBI, Israel, Japan]
Vandonselaar M., Hickie R.A., Quail J.W., Delbaere L.T.;
"Trifluoperazine-induced conformational change in Ca(2+)-calmodulin.";
Nat. Struct. Biol. 1:795-801(1994).
[17]
 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-147.
DOI=10.1016/S0969-2126(97)00308-0; PubMed=9438860 [NCBI, ExPASy, EBI, Israel, Japan]
Wall M.E., Clarage J.B., Phillips G.N.;
"Motions of calmodulin characterized using both Bragg and diffuse X-ray scattering.";
Structure 5:1599-1612(1997).
[18]
 X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 79-149.
DOI=10.1107/S090744490100347X; PubMed=11320306 [NCBI, ExPASy, EBI, Israel, Japan]
Olsson L.L., Sjolin L.;
"Structure of Escherichia coli fragment TR2C from calmodulin to 1.7 A resolution.";
Acta Crystallogr. D 57:664-669(2001).
Comments
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
AB099053; BAC56543.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC105380; AAI05381.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC120080; AAI20081.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC123890; AAI23891.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A90719; MCBO.
RefSeq NP_001039714.1; -.
UniGene Bt.12896
3D structure databases
PDB
1A29; X-ray; 2.74 A; A=1-149.[ExPASy / RCSB / EBI]
1AK8; NMR; -; A=1-76.[ExPASy / RCSB / EBI]
1CDM; X-ray; 2.00 A; A=5-148.[ExPASy / RCSB / EBI]
1CM1; X-ray; 2.00 A; A=2-149.[ExPASy / RCSB / EBI]
1CM4; X-ray; 2.00 A; A/C/E/G=2-149.[ExPASy / RCSB / EBI]
1CMF; NMR; -; A=77-149.[ExPASy / RCSB / EBI]
1CMG; NMR; -; A=77-149.[ExPASy / RCSB / EBI]
1DEG; X-ray; 2.90 A; A=6-148.[ExPASy / RCSB / EBI]
1FW4; X-ray; 1.70 A; A=79-149.[ExPASy / RCSB / EBI]
1LIN; X-ray; 2.00 A; A=1-149.[ExPASy / RCSB / EBI]
1PRW; X-ray; 1.70 A; A=1-149.[ExPASy / RCSB / EBI]
1QIV; X-ray; 2.64 A; A=1-149.[ExPASy / RCSB / EBI]
1QIW; X-ray; 2.30 A; A/B=1-149.[ExPASy / RCSB / EBI]
1XA5; X-ray; 2.12 A; A=1-149.[ExPASy / RCSB / EBI]
2CLN; Model; -; A=1-149.[ExPASy / RCSB / EBI]
2FOT; X-ray; 2.45 A; A=2-149.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A29; -.
1AK8; -.
1CDM; -.
1CM1; -.
1CM4; -.
1CMF; -.
1CMG; -.
1DEG; -.
1FW4; -.
1LIN; -.
1PRW; -.
1QIV; -.
1QIW; -.
1XA5; -.
2CLN; -.
2FOT; -.
ModBase P62157.
Protein-protein interaction databases
IntAct P62157; -.
Ontologies
GO
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from InterPro).
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).
ProtoNet P62157.
Genome annotation databases
Ensembl ENSBTAG00000014583; Bos taurus. [Contig view]
GeneID 520277; -.
KEGG bta:520277; -.
Phylogenomic databases
HOVERGEN P62157; -.
Other
LinkHub P62157; -.
UniRef 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
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   149  148     Calmodulin. PRO_0000198222
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 (By similarity). 
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). 
HELIX   7    20  14      
STRAND   25    28  4      
HELIX   30    39  10      
HELIX   46    54  9      
STRAND   61    65  5      
HELIX   66    73  8      
HELIX   86    93  8      
STRAND   98   101  4      
HELIX   103   112  10      
HELIX   119   129  11      
STRAND   134   138  5      
HELIX   139   146  8      
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
P62157 in FASTA format

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