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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]
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.
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 ...
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.
The integrins contain multiple divalent cation binding sites in the extracellular domain [14]). The integrin cation binding sites can be occupied by Ca2+ or by Mn2+ ions. Cations are necessary but not sufficient for integrins to convert from the inactive bent conformation into the active extended conformation.
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 ...
Calcineurin is a heterodimer of a 61-kD calmodulin-binding catalytic subunit, calcineurin A and a 19-kD Ca 2+-binding regulatory subunit, calcineurin B.There are three isozymes of the catalytic subunit, each encoded by a separate gene (PPP3CA, PPP3CB, and PPP3CC) and two isoforms of the regulatory, also encoded by separate genes (PPP3R1, PPP3R2).
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 ...