TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*1.A.68.1.1









The viral small hydrophobic protein (V-SHP; hRSV-SH) of 64 aas with 1 TMS,  It forms a pentameric ion conducting pore in the membrane (Surya and Torres 2015) that transports monovalent cations (Hyser and Estes 2015). The SH protein has two protonatable His residues in its transmembrane domain that are oriented facing the lumen of the channel.  Their protonation may serve as a pH sensor, to promote electrostatic repulsion and reduced oligomer stability at low pH (Surya and Torres 2015).  Pyronin B can reduce SH channel activity, and its likely binding site on the SH protein channel has been identified. Black lipid membrane experiments confirmed that protonation of both histidine residues reduces stability and channel activity (Li et al. 2014).  Water transport was observed with histidine residues of five chains (His22 and His51) playing a key role in pore permeability (Araujo et al. 2016).

Viruses
Mononegavirales
SH protein of human respiratory syncytial virus (P04852)
*1.A.68.1.2









BSV small hydrophobic (SH) protein of 81 aas (Karger et al. 2001).

Viruses
Mononegavirales
SH of bovine respiratory syncytial virus
*1.A.68.1.3









Small hydrophobic viroporin protein (SH), also called small protein 1A, of 65 aas and 1 TMS. Forms a proton-selective ion channel, playing a role in budding and /or virus entry. May also play a role in counteracting host innate immunity (Russell et al. 2015).  The SH protein is stable in its pentameric membrane-integrated form. Simulations also showed the presence of water molecules within the bilayer by density distribution, thus confirming that the SH protein is a viroporin (Araujo et al. 2016).

Viruses
Mononegavirales
Viroporin SH of human respiratory syncytial virus B