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The ion channel viral protein U, Vpu of 81 aas and 1 TMS. Vpu(1-32), forms a helix bundle with characteristic open states. Different amilorides inhibit channel activity (Römer et al. 2004). The mutation A18H converts a non-specific channel to a selective proton channel that is sensitive to rimantadine (Sharma et al., 2011).  Vpu forms stable pentamers (Padhi et al. 2013).  The mechanism of Vpu, a weakly conducting cation-selective channel that assists in detachment of the virion from infected cells, has been proposed (Padhi et al. 2014).  Interactions of Vpu with host cellular constituents have been reviewed (González 2015). Vpu forms large homo aggregates of 16 or 32 subunits (Lin et al. 2016). Vpu is involved in the enhancement of virion release via formation of an ion channel. Cyclohexamethylene amiloride (Hma) inhibits ion channel activity. A putative binding site for Hma blockers in a pentameric model bundle built of parallel aligned helices of the first 32 residues of Vpu was found near Ser-23. Hma orientates along the channel axis with its alkyl ring pointing inside the pore, which leads to a blockage of the pore (Lemaitre et al. 2004).

Accession Number:P05919
Protein Name:Vpu
Molecular Weight:9111.00
Species:Human immunodeficiency virus type 1 (HXB2 isolate) (HIV-1) [11706]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Host membrane1 / Single-pass type I membrane protein2
Substrate ion

Cross database links:

Pfam: PF00558   

Gene Ontology

GO:0005829 C:cytosol
GO:0005789 C:endoplasmic reticulum membrane
GO:0033644 C:host cell membrane
GO:0016021 C:integral to membrane
GO:0005216 F:ion channel activity
GO:0006915 P:apoptosis
GO:0019059 P:initiation of viral infection
GO:0044419 P:interspecies interaction between organisms
GO:0006811 P:ion transport
GO:0019047 P:provirus integration
GO:0019076 P:release of virus from host

References (2)

[1] “Complete nucleotide sequences of functional clones of the AIDS virus.”  Ratner   3040055
[2] “The Vpu protein of human immunodeficiency virus type 1 forms cation-selective ion channels.”  Ewart   8794357

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