Domain

Anthrax toxin receptor, extracellular (IPR008400)

Short name: Anthrax_toxin_rcpt_extracel

Domain relationships

None.

Description

Anthrax is an acute disease in humans and animals, which is caused by the bacterium Bacillus anthracis. While the disease can be lethal, there are effective vaccines against anthrax, and some forms of the disease respond well to antibiotic treatment.

The anthrax toxin consists of the proteins protective antigen (PA), lethal factor (LF) and oedema factor (EF). The first step of toxin entry into host cells is the recognition by PA of a receptor on the surface of the target cell. The subsequent cleavage of receptor-bound PA enables EF and LF to bind and form a heptameric PA63 pre-pore, which triggers endocytosis. PA has been shown to bind to two cellular receptors, termed anthrax toxin receptor 1 and 2. Both bind to PA with high affinity and are capable of mediating toxicity [PMID: 15243628, PMID: 15079089], and both are type 1 membrane proteins that include an approximately 200-aa extracellular von Willebrand factor A (VWA) domain with a metal ion-dependent adhesion site (MIDAS) motif [PMID: 15079089].

This region is found in the putatively extracellular N-terminal half of the anthrax receptor. It is probably part of the Ig superfamily and most closely related to IPR002909.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0004872 receptor activity

Cellular Component

GO:0016021 integral component of membrane

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
Pfam