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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).

Accession Number:P04852
Protein Name:Small hydrophobic protein
Molecular Weight:7536.00
Species:Human respiratory syncytial virus A (strain A2) [11259]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Virion membrane1 / Single-pass type II membrane protein2
Substrate monovalent cations

Cross database links:

Pfam: PF03579   

Gene Ontology

GO:0048222 C:glycoprotein network
GO:0020002 C:host cell plasma membrane
GO:0016021 C:integral to membrane
GO:0055036 C:virion membrane
GO:0015992 P:proton transport

References (9)

[1] “The 1A protein gene of human respiratory syncytial virus: nucleotide sequence of the mRNA and a related polycistronic transcript.”  Collins   3879976
[2] “A cold-passaged, attenuated strain of human respiratory syncytial virus contains mutations in the F and L genes.”  Connors   7747420
[3] “Acquisition of the ts phenotype by a chemically mutagenized cold-passaged human respiratory syncytial virus vaccine candidate results from the acquisition of a single mutation in the polymerase (L) gene.”  Crowe J.E.   9035372
[4] “The 1A protein of respiratory syncytial virus is an integral membrane protein present as multiple, structurally distinct species.”  Olmsted   2649692
[5] “The small hydrophobic (SH) protein accumulates within lipid-raft structures of the Golgi complex during respiratory syncytial virus infection.”  Rixon   15105532
[6] “The respiratory syncytial virus small hydrophobic protein is phosphorylated via a mitogen-activated protein kinase p38-dependent tyrosine kinase activity during virus infection.”  Rixon   15659757
[7] “Function of the respiratory syncytial virus small hydrophobic protein.”  Fuentes   17494063
[8] “The RSV F and G glycoproteins interact to form a complex on the surface of infected cells.”  Low   18036342
[9] “Structure and ion channel activity of the human respiratory syncytial virus (hRSV) small hydrophobic protein transmembrane domain.”  Gan   18369195

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FASTA formatted sequence
61:	RVNT