1.C.4.8.1 Cellular endolysosome-modulating aerolysin-like pore-forming protein, ALP1, of 156 aas (Wang et al. 2020). The protein shows sequence similarity in its N-terminal half with family 1.C.73 members and in its C-terminal half with family 1.C.4 members. βγ-CAT is a complex of an ALP (BmALP1) and a trefoil factor (BmTFF3) in
the firebelly toad (Bombina maxima). It is a
secreted endogenous pore-forming protein that modulates the biochemical
properties of endolysosomes by inducing pore formation. BmALP3, a paralog of BmALP1 that lacks membrane pore-forming capacity, like BmALP1, has a conserved cysteine in
its C-terminal regions. BmALP3 is readily oxidized to a disulfide
bond-linked homodimer, and this homodimer can oxidize BmALP1 via
disulfide bond exchange, resulting in the dissociation of βγ-CAT
subunits and elimination of its biological activity. BmALP3 senses environmental oxygen tension in vivo,
leading to modulation of βγ-CAT activity. This C-terminal cysteine site is well conserved in numerous vertebrate
ALPs, suggesting that it is a regulatory ALP (BmALP3)
that modulates the activity on the active ALP (BmALP1) in a
redox-dependent manner (Wang et al. 2020). An aerolysin-like pore-forming protein complex targets viral envelope to inactivate herpes simplex virus type 1 (Liu et al. 2021).
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Accession Number: | 6LH8_A |
Protein Name: | A Chain A, aerolysin-like protein |
Length: | 157 |
Molecular Weight: | |
Species: | Bombina maxima [161274] |
Substrate |
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1: MSASVTVLWD KEIEGSNEVV KVDEMVASNI SNVKVEFYLK ERHFDRTITH NITLPRATEV
61: PIGTEIQLEP KHRLNGNTEP ITFTYGSLES YTELSEDKVT MPEFVEPKTK LIVILTRNEN
121: ITSAPVEISV GDIKETATYI CQSQSGINAE VNTEPL