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  2. Calmodulin - Wikipedia

    en.wikipedia.org/wiki/Calmodulin

    Calmodulin is a small, highly conserved protein that is 148 amino acids long (16.7 kDa). The protein has two approximately symmetrical globular domains (the N- and C- domains) each containing a pair of EF hand motifs [5] separated by a flexible linker region for a total of four Ca 2+ binding sites, two in each globular domain. [6]

  3. Troponin C type 1 - Wikipedia

    en.wikipedia.org/wiki/Troponin_C_type_1

    7134 21924 Ensembl ENSG00000114854 ENSMUSG00000091898 UniProt P63316 P19123 RefSeq (mRNA) NM_003280 NM_009393 RefSeq (protein) NP_003271 NP_033419 Location (UCSC) Chr 3: 52.45 – 52.45 Mb Chr 14: 30.93 – 30.93 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Troponin C, also known as TN-C or TnC, is a protein that resides in the troponin complex on actin thin filaments of striated ...

  4. Calcium-binding protein - Wikipedia

    en.wikipedia.org/wiki/Calcium-binding_protein

    Calcium-binding proteins can be either intracellular and extracellular. Those that are intracellular can contain or lack a structural EF-hand domain. Extracellular calcium-binding proteins are classified into six groups. [2] Since Ca (2+) is an important second messenger, it can act as an activator or inhibitor in gene transcription.

  5. Calcium signaling - Wikipedia

    en.wikipedia.org/wiki/Calcium_signaling

    Shows Ca 2+ release from the endoplasmic reticulum through phospholipase C (PLC) pathway.. Calcium signaling is the use of calcium ions (Ca 2+) to communicate and drive intracellular processes often as a step in signal transduction.

  6. Cell adhesion molecule - Wikipedia

    en.wikipedia.org/wiki/Cell_adhesion_molecule

    Thus, rise in extracellular Ca2+ ions may serve to prime the integrin heterodimer. The release of intracellular Ca2+ have been shown to be important for integrin inside-out activation. [16] However, extracellular Ca2+ binding may exert different effects depending on the type of integrin and the cation concentration. [17]

  7. Voltage-gated calcium channel - Wikipedia

    en.wikipedia.org/wiki/Voltage-gated_calcium_channel

    The α 1 subunit forms the Ca 2+ selective pore, which contains voltage-sensing machinery and the drug/toxin-binding sites. A total of ten α 1 subunits that have been identified in humans: [1] α 1 subunit contains 4 homologous domains (labeled I–IV), each containing 6 transmembrane helices (S1–S6). This arrangement is analogous to a homo ...

  8. Calmodulin 1 - Wikipedia

    en.wikipedia.org/wiki/Calmodulin_1

    Calmodulin 1 is a protein in humans that is encoded by the CALM1 gene. [3] Calmodulin [4] plays a role in calcium signal transduction pathways by regulating control of ion channels, enzymes, aquaporins, and other proteins. It functions as a calcium-binding protein that has been grouped into the EF-hand motif found in eukaryotic cells ...

  9. Calcium metabolism - Wikipedia

    en.wikipedia.org/wiki/Calcium_metabolism

    Calcium is the most abundant mineral in the human body. [3] The average adult body contains in total approximately 1 kg, 99% in the skeleton in the form of calcium phosphate salts. [ 3 ] The extracellular fluid (ECF) contains approximately 22 mmol, of which about 9 mmol is in the plasma . [ 4 ]