Additional names and abbreviations: | calmodulin: calmodulin (CaM); modulator protein |
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Isoforms: | isoform 1 (the main isoform, and the only isoform found in most species) plant isoform 2 (isoform found only in some plants) plant isoform 4 (isoform found only in some plants) plant isoform 6 (isoform found only in some plants) |
Yeast Protein Database Entries: | CMD1 |
Basic Chemical and Physical
Information: |
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Number of amino acids: | isoform 1: 147 (Fagus sylvatica, Saccharomyces cerevisiae, Kluyveromyces lactis) - 162 (Chlamydomonas reinhardtii) plant isoform 2: 148 (all species) plant isoform 4: 148 (all species) plant isoform 6: 148 (all species) View a list of all sources stored in the database |
Molecular weight: | isoform 1: 16.063 kD (Kluyveromyces lactis) - 18.165 kD (Chlamydomonas reinhardtii) plant isoform 2: 16.688 kD (Arabidopsis thaliana) - 16.806 kD (Petunia hybrida) plant isoform 4: 16.704 kD (all species) plant isoform 6: 16.702 kD (all species) View a list of all sources stored in the database |
pI: | isoform 1: calculated pI (Homo sapiens) = 3.9 (InfoCard) |
Number of functional calcium binding sites: | isoform 1, vertebrates: 4 (InfoCard) |
Macroscopic calcium binding constants: | isoform 1, Bos taurus, low salt: K1 = 1 x 107; K2 = 3.98 x 107; K3 = 3.16 x 106; K4 = 2.5 x 106 (measured by: competitive chelator pH: 7.5 temperature: 25 degrees Celsius buffer: 0.002 M Tris-HCl ) (InfoCard) isoform 1, Bos taurus, medium salt: K1 = 1.58 x 106; K2 = 2.5 x 107; K3 = 1 x 106; K4 = 1 x 106 (measured by: competitive chelator pH: 7.5 temperature: 25 degrees Celsius salt: 10 mM KCl buffer: 0.002 M Tris-HCl ) (InfoCard) isoform 1, Bos taurus, medium salt: K1 = 6.30 x 105; K2 = 1 x 107; K3 = 2.50 x 105; K4 = 5.00 x 105 (measured by: competitive chelator pH: 7.5 temperature: 25 degrees Celsius salt: 25 mM KCl buffer: 0.002 M Tris-HCl ) (InfoCard) isoform 1, Bos taurus, medium salt: K1 = 2.50 x 105; K2 = 5 x 106; K3 = 3.98 x 104; K4 = 3.16 x 105 (measured by: competitive chelator pH: 7.5 temperature: 25 degrees Celsius salt: 50 mM KCl buffer: 0.002 M Tris-HCl ) (InfoCard) isoform 1, Bos taurus, medium salt: K1 = 7.90 x 104; K2 = 3.98 x 106; K3 = 2.50 x 104; K4 = 3.98 x 105 (measured by: competitive chelator pH: 7.5 temperature: 25 degrees Celsius salt: 100 mM KCl buffer: 0.002 M Tris-HCl ) (InfoCard) isoform 1, Bos taurus, high salt: K1 = 5.00 x 104; K2 = 1.58 x 106; K3 = 1.00 x 104; K4 = 2.00 x 105 (measured by: competitive chelator pH: 7.5 temperature: 25 degrees Celsius salt: 150 mM KCl buffer: 0.002 M Tris-HCl ) (InfoCard) |
Other metal binding constants: | not yet available in the data library |
Protein stability: | not yet available in the data library |
Post-translational modifications: | isoform 1, flowering plants: trimethylation at Lys115 (InfoCard) isoform 1, mammals: phosphorylation (made by: casein kinase II effect: Alters the ability of calmodulin to activate selected target enzymes. No apprent effect on calicium binding to calmodulin. ) (InfoCard) isoform 1, mammals: phosphorylation (made by: insulin receptor kinase effect: Alters the ability of calmodulin to activate selected target enzymes. No apprent effect on calicium binding to calmodulin. ) (InfoCard) isoform 1, vertebrates: trimethylation at Lys115 (InfoCard) isoform 1, Rattus norvegicus: phosphorylation (made by: insulin receptor kinase) (InfoCard) |
Basic Biological
Information: |
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Source organisms: | isoform 1: eukaryotes plant isoform 2: Arabidopsis thaliana, Petunia hybrida plant isoform 4: Arabidopsis thaliana plant isoform 6: Arabidopsis thaliana View an annotated list of all sources stored in the database |
Tissues: | isoform 1, eukaryotes: all tissues and cells (InfoCard) |
Subcellular localization: | not yet available in the data library |
Regulation: | not yet available in the data library |
Genomic Information: |
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GenBank entries: | View a list of GenBank entries
stored in the database |
Gene length: | not yet available in the data library |
Gene structure: | not yet available in the data library |
Promoter: | not yet available in the data library |
Gene copies: | isoform 1, Homo sapiens: 3 gene copies (code for an indentical protein) (InfoCard) |
Alleles: | no alleles are currently stored in the data library |
Chromosomal localization: | isoform 1, Homo sapiens, expressed (GenBank code U12022): q24-q31 region of chromosome 14 (CALM1) (InfoCard) isoform 1, Homo sapiens, expressed (GenBank code U94728): p21.1-21.3 region of chromosome 2 (CALM2) (InfoCard) isoform 1, Homo sapiens, expressed (GenBank code X52606): q13.2-13.3 region of chromosome 19 (CALM3) (InfoCard) |
|-helixI-|--loop1----|helixII| En**nn**nX*Y*ZG#Ix**zn**nn*n HUMAN : ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAEL SPOMBE : MTTRNLTDEQIAEFREAFSLFDRDQDGNITSNELGVVMRSLGQSPTAAEL SCEREV : MSSNLTEEQIAEFKEAFALFDKDNNGSISSSELATVMRSLGLSPSEAEV |helixIII|--loop2----|helixIV| |-helixV-|-loop3 En**nn**nX*Y*ZG#Ix**zn**nn*n En**nn**nX*Y*ZG HUMAN : ELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNG SPOMBE : ELQDMINEVDADGNGTIDFTEFLTMMARKMKDTDNEEEVREAFKVFDKDGNG SCEREV : EVNDLMNEIDVDGNHQIEFSEFLALMSRQLKSNDSEQELLEAFKVFDKNGDG -----|helixVI| |helixVII|--loop4----|helixVIII| #Ix**zn**nn*n En**nn**nX*Y*ZG#Ix**zn**nn*n HUMAN : YISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK SPOMBE : YITVEELTHVLTSLGERLSQEEVADMIREADTDGDGVINYEEFSRVISSK SCEREV : LISAAELKHVLTSIGEKLTDAEVDDMLREVSDGSGEI-NIQQFAALLSKSequence alignment for the entire calmodulin subfamilyLoop 4 of SCEREV calmodulin does not bind calcium
General information:
Biological roles:
Disease states:
Target molecules:
Calcium-coordination: |
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isoform 1, all vertebrates: |
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Nature of the conformational
changes: |
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Conformational change between apo and four calcium ions bound states of isoform 1: |
The conformational change is a reorganization of existing secondary structural elements in each domain. Upon calcium-binding, the bottoms of helices I and II swing apart, while the tops pinch together; a similar change is observed for helices III and IV. The interface between helcies II and IV is completely disrupted, as the two helices move apart along their entire lengths. The interfaces beteen helices I and IV and between helices II and III are not much affected by calcium-binding. (InfoCard) |
Conformational change between four calcium ions bound and four calcium ions and target peptide bound states of isoform 1: |
Target peptide binding to calcium-loaded calmodulin effects mainly the quarternary structure: the structure of the two domains is not changed. In the absence of peptide, the two domains do not interact to a large extent, and the linekr between the two domains is flexible. Peptide binding causes calmodulin to compact, as the two domains wrap around the target peptide, with CaM-C interacting with the N-terminal portion of one face of the peptide and CaM-N interacting with the C-terminal portion of the other face. The flexible nature of the tether between the two domains allows calmodulin to bind to peptides of varying length. (InfoCard) |
Secondary structure: (as reported in the PDB file and its accompanying reference) |
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isoform 1, all vertebrates, four calcium ions bound state: |
Helices: N-terminal domain: helix 1: 5 - 19, helix 2: 29 - 37, helix 3: 45 - 55, helix 4: 65 - 75, C-terminal domain: helix 5: 82 - 92, helix 6: 102 - 111, helix 7: 118 - 128, helix 8: 138 - 146 Beta strands: N-terminal domain: strand 1: 27 - 29, strand 2: 63 - 65, C-terminal domain: strand 3: 100 - 102, strand 4: 136 - 138 (pdb code 1CLL: InfoCard) |
isoform 1, all vertebrates, apo state: |
Helices: N-terminal domain: helix 1: 6 - 19, helix 2: 29 - 38, helix 3: 45 - 55, helix 4: 65 - 75, C-terminal domain: helix 5: 82 - 91, helix 6: 102 - 111, helix 7: 118 - 127, helix 8: 139 - 146 Beta strands: N-terminal domain: strand 1: 26 - 28, strand 2: 62 - 64 (pdb code 1CFC: InfoCard) |
Additional structural information: | |
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Available structures: (follow the links from the PDB code to the retrieve the PDB files) |
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Apo Structures: |
1CMF: isoform 1, Bos taurus, C-terminal domain, pH 6 NMR solution structure, 20 models (InfoCard) 1CFC: isoform 1, Xenopus laevis, full length protein, pH 6.3 NMR solution structure, 25 models, 27.7 restraints per residue (InfoCard) 1DMO: isoform 1, Xenopus laevis, full length protein, pH 7.5 NMR solution structure, 30 models, 18.02 restraints per residue (InfoCard) |
Calcium Loaded Structures: |
1CMG: isoform 1, Bos taurus, C-terminal domain, pH 6 NMR solution structure, 20 models 2 Ca ions bound (InfoCard) 1TRC: isoform 1, Bos taurus, C-terminal domain, Crystal structure, 3.6 angstrom resolution, R-value = 25.7 2 Ca ions bound (InfoCard) 1OSA: isoform 1, Paramecium tetraurelia, full length protein, Crystal structure, 1.68 angstrom resolution, R-value = 19.4 4 Ca ions bound (InfoCard) 1CLM: isoform 1, Paramecium tetraurelia, full length protein, Crystal structure, 1.8 angstrom resolution, R-value = 21 4 Ca ions bound (InfoCard) 4CLN: isoform 1, Drosophila melanogaster, full length protein, Crystal structure, 2.2 angstrom resolution, R-value = 19.7 4 Ca ions bound (InfoCard) 1CLL: isoform 1, Homo sapiens, full length protein, pH 5 Crystal structure, 1.7 angstrom resolution, R-value = 21.6 4 Ca ions bound (InfoCard) 3CLN: isoform 1, Rattus norvegicus, full length protein, pH 5.6 Crystal structure, 2.2 angstrom resolution, R-value = 17.5 4 Ca ions bound (InfoCard) |
Other Metal Bound Structures: |
1AK8: isoform 1, Bos taurus, N-terminal domain, NMR solution structure, 23 models, 13.15 restraints per residue 2 Ce ions bound (InfoCard) |
Target Peptide Bound Structures: |
2BBN: isoform 1, Drosophila melanogaster, full length protein, pH 6.8 NMR solution structure, 24 models, 10.82 restraints per residue 4 Ca ions bound , bound to 1 equivalentsof the following portion of skeletal muscle myosin light chain kinase: peptide derived from the calmodulin binding domain of the skeletal muscle myosin light chain kinase (InfoCard) 1CDL: isoform 1, Bos taurus, full length protein, pH 4.6 Crystal structure, 2.4 angstrom resolution, R-value = 22 4 Ca ions bound , bound to 1 equivalentsof the following portion of smooth muscle myosin light chain kinase: peptide derived from the calmodulin binding domain of the smooth muscle myosin light chain kinase (InfoCard) 1CDM: isoform 1, Bos taurus, full length protein, Crystal structure, 2 angstrom resolution, R-value = 20.8 4 Ca ions bound , bound to 1 equivalentsof the following portion of calcium/calmodulin-dependent protein kinase II: peptide derived from the calmodulin binding domain (InfoCard) |
Drug Bound Structures: |
1CTR: isoform 1, Bos taurus, full length protein, pH 5.8 Crystal structure, 2.45 angstrom resolution, R-value = 22.2 4 Ca ions bound , bound to 1 equivalentsof the following portion of trifluoperazine: complete molecule (InfoCard) 1LIN: isoform 1, Bos taurus, full length protein, pH 5.5 Crystal structure, 2 angstrom resolution, R-value = 22 4 Ca ions bound , bound to 4 equivalentsof the following portion of trifluoperazine: complete molecule (InfoCard) 1A29: isoform 1, Bos taurus, full length protein, pH 5.6 Crystal structure, 2.74 angstrom resolution, R-value = 19.7, R-free = 26.5 4 Ca ions bound , bound to 2 equivalentsof the following portion of trifluoperazine: complete molecule (InfoCard) |
Mutant Structures: |
1AHR: isoform 1, Gallus gallus, full length protein, pH 4.25 Crystal structure, 1.8 angstrom resolution, R-value = 21.1 4 Ca ions bound Mutations: T79 deleted + D80 deleted (InfoCard) |