Target Atlas

Computational Target Profile

ANO5

IDG Tbio

A dark anoctamin (TMEM16E) tied to limb-girdle muscular dystrophy, characterised without an experimental structure.

ANO5 (TMEM16E) belongs to the anoctamin family, but unlike its channel relatives it is reported to act in plasma-membrane repair and lipid scrambling rather than as a chloride channel. Recessive loss-of-function mutations cause limb-girdle muscular dystrophy (LGMD2L / LGMDR12) and Miyoshi myopathy, while a dominant gain-of-function variant causes gnathodiaphyseal dysplasia — yet it has no experimental structure in the PDB and a thin functional literature. We resolve the canonical 913-residue sequence into an eight-helix topology, a residue-level pore / interface hypothesis, post-translational features and a construct / validation plan, all computed with Orbion's Astra suite from sequence alone.

UniProt Q75V66 ·AFDB AF-Q75V66-F1 ·913 aa·Anoctamin (TMEM16) family·PDB: none
At a Glance
Fold
Eight predicted transmembrane helices; a multi-pass anoctamin / TMEM16-family membrane protein.
Pore-Lining Surface
AstraBIND pore / interface hypothesis (confidence 0.654, medium) around TM6 — a residue-level starting point for mutagenesis; no validated ligand.
Structural Anchors
N-glycosylation at six predicted sites, including N335 (UniProt).
Flexible Regions
Elevated predicted disorder at the N-terminus (1–64) and C-tail (883–910) — the cytoplasmic termini and natural truncation boundaries.
Clean Signal
Aggregation-prone segment flagged (max 0.528).
Prediction Confidence
8–12 TM Helices
0.97
Multi-Pass Membrane
0.97
Transporter Class
0.99
Binding Pocket
0.65

Model-reported confidence for the headline calls (amber = the load-bearing prediction the rest of the profile builds on). These are model-estimated probabilities that rank and gate each call — not calibrated rates of experimental success.

The Gap

Why This Target Is Still Dark

Most tractable membrane-protein families have been structurally explored. ANO5 has not: an IDG Tbio anoctamin with no experimental structure in the PDB and only a handful of functional studies. UniProt notes a role in annexin-dependent plasma-membrane repair and, pointedly, that it does not show the calcium-activated chloride-channel activity of some family members — so even its molecular function is unsettled. What is firm is the disease link: recessive loss-of-function ANO5 variants underlie limb-girdle muscular dystrophy (LGMD2L / LGMDR12) and Miyoshi myopathy, while a dominant gain-of-function variant causes gnathodiaphyseal dysplasia.

That combination — a solid disease association with near-zero structural information — is where prediction earns its keep: everything below is computed from the canonical 913-residue sequence, with no experimental ANO5 structure used as input.

Architecture & Topology

How the Sequence Is Organised

extracellularintracellularTM1TM2TM3TM4TM5TM6TM7TM8NC
Pocket-Lining HelixTransmembrane Helix Disordered Loop
Predicted Membrane Topology · Pocket-Lining Helices in Amber · Disordered Loops Dashed · N/C Termini In Situ
ElementResiduesNote
Transmembrane Helices8 predictedBoundaries: 300–320; 381–401; 463–483; 512–532; 558–578; 680–700; 733–753; 835–855.
Per-Residue Disorder
N-TermC-Tail00.511400800913
Disordered Regions Shaded in Amber · Dashed Line = 0.5 Call Threshold · the Natural Truncation Boundaries for Construct Design

The Predicted Pocket

The Predicted Pore-Lining Surface

For this genuine orphan, AstraBIND has no ligand-bound relative to retrieve from — so these residues are a structure-based cavity prediction, not a retrieval-grounded pocket, and the score reflects cavity geometry rather than a known binding site. Treat them as an exploratory starting point for mutagenesis only; the topology, disorder and modification maps above are the higher-confidence outputs for this target. No validated ligand; not a proven druggable site.

Site: Predicted pore / gating interface

Pocket-Lining Residues
TM6701
Loop / Surface704, 706, 708

Post-Translational & Structural Features

Specific, Testable Residues

  • N-glycosylation at six predicted sites (N335, N366, N380, N768, N778, N791) — extracellular-loop modifications (UniProt).
  • Aggregation-prone segment flagged (AstraUNFOLD amyloid max 0.528) — worth screening in construct design.

Recommended Experimental Follow-Up

An Orphan Sequence, Turned Into a Ranked Plan

Each prediction is paired with the experiment that would test it and the readout to watch for.

PredictionExperimentReadout
Predicted Pore / Interface Residues (TM6)Alanine scan at the predicted TM6 residues + membrane-repair / scrambling assayFunctional change — tests the predicted site
Disordered Termini (1–64; 883–910)N- and C-terminal truncationImproved expression / thermostability for cryo-EM
Predicted Anoctamin / Scramblase FunctionLipid-scrambling / membrane-repair assayConfirm the predicted functional class

Scope & Limitations

What This Is — and Isn't

  • Prediction, not experiment. These are computational hypotheses to prioritise experiments — not a structure or an assay. Nothing here is wet-lab validated.
  • The pocket is predicted; the ligand is not named. AstraBIND is retrieval-based; the honest output is a residue-level hypothesis, not a proven druggable site or a validated binder.
  • Thin biology. ANO5's molecular function is unsettled — it is reported in plasma-membrane repair and lipid scrambling rather than as a chloride channel — and the disease rationale rests chiefly on LGMD2L and gnathodiaphyseal-dysplasia genetics. Treat mechanism as a hypothesis.

All predictions were generated with Orbion's Astra suite from the canonical ANO5 sequence (UniProt Q75V66), using AlphaFold-derived structural features. Reported values are model outputs; model internals are out of scope.

References

  1. [1]UniProt Consortium. UniProtKB entry Q75V66 (ANO5, human). uniprot.org.
  2. [2]Pharos (Illuminating the Druggable Genome). ANO5 target record — Tbio. pharos.nih.gov.
  3. [3]Penttilä S et al. Eight new mutations and the expanding phenotype variability in muscular dystrophy caused by ANO5. (2012). https://doi.org/10.1212/wnl.0b013e31824c4682
  4. [4]Savarese M et al. Next generation sequencing on patients with LGMD and nonspecific myopathies: Findings associated with ANO5 mutations. (2015). https://doi.org/10.1016/j.nmd.2015.03.011
  5. [5]Di Zanni E et al. Gain of function of TMEM16E/ANO5 scrambling activity caused by a mutation associated with gnathodiaphyseal dysplasia. (2018). https://doi.org/10.1007/s00018-017-2704-9

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