TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*1.A.75.1.1









Piezo1 (FAM38a) mechanosensitive ion channel. Has a C-terminal DUF3595 (pfam 12166) domain (Coste et al., 2010).  Fam38A expression may cause increased cell migration and metastasis in lung tumours (McHugh et al. 2012). Imporatnt for gastrointestinal tract function (Alcaino et al. 2017). A high-resolution cryo-electron microscopy structure of the mouse Piezo1 trimer has been determined (Saotome et al. 2017). The detergent-solubilized complex adopts a three-blade propeller shape with a curved transmembrane region containing at least 26 transmembrane helices per protomer. The flexible propeller blades can adopt distinct conformations, and consist of a series of four-TMS bundles termed 'Piezo repeats'. Carboxy-terminal domains line the central ion pore, and the channel is closed by constrictions in the cytosol. A kinked helical beam and anchor domain link the Piezo repeats to the pore, and are poised to control gating allosterically (Saotome et al. 2017). The Piezo1 pore remains fully open if only one subunit is activated, for example by binding the agonist, Yoda1 (Lacroix et al. 2018). The channel mediates uterine artery shear stress mechanotransduction and vasldilation during pregnancy (John et al. 2018).

Eukaryota
Metazoa
Piezo1 of Homo sapiens (Q92508)
*1.A.75.1.2









Piezo2 (FAM38b) is the major transducer of mechanical force for touch sensation in mice (Ranade et al. 2014). It is a rapidly adapting mechanically activated ion channel expressed in a subset of sensory neurons of the dorsal root ganglion and in cutaneous mechanoreceptors called Merkel cell neurite complexes.  Ranade et al. 2014 showed that touch and pain are mediated by distinct receptors. Piezo2 mediates alloknesis (pathological sensations including itch of dry skin (Feng et al. 2018).

Eukaryota
Metazoa
Piezo2 of Homo sapiens (Q9H5I5)
*1.A.75.1.3









Piezo mechanosensitive ion channel (Kim et al., 2012)

Eukaryota
Metazoa
Piezo (CG8486) of Drosophila melanogaster (Q9VLS3)
*1.A.75.1.4









Hypothetical protein, HP (2462 aas)

Eukaryota
Viridiplantae
HP of Arabinodopsis thaliana (F4IN58)
*1.A.75.1.5









Cholesterol uptake-associated protein, ChUP-1 homologue of 2544 aas and >40 TMSs.

Eukaryota
Intramacronucleata
HP of Paramecium tetraurelia (A0EF36)
*1.A.75.1.6









Hypothetical protein, HP (2724 aas)

Eukaryota
Kinetoplastida
HP of Trypanosoma cruzi (Q4E330)
*1.A.75.1.7









Piezo homologue 

Eukaryota
Metazoa
Piezo homologue of Ascaris suum (F1KQU6)
*1.A.75.1.8









Mechanosensitive piezo channel protein, isoform a, of 2438 aas.  The C-terminal extracellular domain (before the last TMS) has a β-sandwich fold (Kamajaya et al. 2014).

Eukaryota
Metazoa
Piezo of Caenorhabditis elegans
*1.A.75.1.9









Piezo channel of 2013 aas and about 21 TMSs.

Eukaryota
Metazoa
Piezo of Schistosoma mansoni (Blood fluke)
*1.A.75.1.10









Piezo channel of 2470 aas

Eukaryota
Intramacronucleata
Piezo of Paramecium tetraurelia
*1.A.75.1.11









Piezo channel of 2598 aas.

Eukaryota
Kinetoplastida
Piezo of Trypanosoma cruzi
*1.A.75.1.12









Uncharacterized piezo-like channel protein of 1864 aas and ~15 TMSs.

Eukaryota
Kinetoplastida
Putative piezo protein of Leishmania donovani
*1.A.75.1.13









Uncharacterized piezo channel homologue of 1931 aas and 31 putative TMSs.

Eukaryota
Kinetoplastida
UP of Bodo saltans
*1.A.75.1.14









Piezo1 (Fam38a) of 2547 aas and 38 TMSs. The three-bladed propeller-like electron cryo-microscopic structure and its mechanotransduction components are known (Zhao et al. 2018). There are nine repeat units consisting of four transmembrane helices, each of which is termed a transmembrane helical unit (THU). These assemble into a highly curved blade-like structure. The last transmembrane helix encloses a hydrophobic pore, followed by three intracellular fenestration sites and side portals that contain pore-property-determining residues. The central region forms a 90 Å-long intracellular beam-like structure, which undergoes a lever-like motion to connect the THUs to the pore via the interfaces of the C-terminal domain, the anchor-resembling domain and the outer helix. Deleting extracellular loops in the distal THUs or mutating single residues in the beam impairs the mechanical activation of Piezo1. Thus, Piezo1 possesses a 38-transmembrane-helix topology with mechanotransduction components that enable a lever-like mechanogating mechanism (Zhao et al. 2018). The Piezo1 pore remains fully open if only one of the three subunits is activate, for example by binding the agonist, Yoda1 (Lacroix et al. 2018).

Eukaryota
Metazoa
Piezo1 of Mus musculus
*1.A.75.1.15









Piezo-type mechanosensitive ion channel component 2of 1818 aas and 31 putative TMSs.

Eukaryota
Viridiplantae
Piezo of Glycine soja
*1.A.75.1.16









Uncharacterized protein of 2321 aas and ~35 TMSs.

Eukaryota
Postciliodesmatophora
UP of Stentor coeruleus
*1.A.75.1.17









Piezo homologue of 3315 aas and ~48 TMSs.

Eukaryota
Chromerida
Piezo of Vitrella brassicaformis
*1.A.75.1.18









Piezo homologue of 2620 aas and ~47 TMSs.

Eukaryota
Kinetoplastida
Piezo of Leptomonas pyrrhocoris
*1.A.75.1.19









Fibronectin, type IIIof 2452 aas and ~41 TMSs.

Eukaryota
Viridiplantae
Piezo homologue of Ostreococcus tauri
*1.A.75.1.20









Piezo homologue of 2888 aas and ~40 TMSs.

Eukaryota
Intramacronucleata
Piezo of Pseudocohnilembus persalinus
*1.A.75.1.21









Piezo homologue of 2401 aas and ~ 38 TMSs.

Eukaryota
Entamoebidae
Piezo of Entamoeba histolytica