# DNAJC22 (Q8N4W6) research notes

Poorly characterized **polytopic membrane** protein of the HSP40/DnaJ co-chaperone
family; liver-enriched.

## Architecture
- N-terminal TM2-type region, multiple predicted transmembrane helices, and a
  C-terminal **J-domain** (the module that engages and stimulates HSP70 chaperones).
  [UniProt Q8N4W6]

## Functional inference
- Drosophila ortholog **Wurst** is a transmembrane J-domain protein that recruits
  clathrin and Hsc70 to the apical membrane to drive clathrin-mediated endocytosis
  (e.g. tracheal/airway liquid clearance), suggesting a related membrane
  co-chaperone/endocytic role for DNAJC22. Direct functional data for the human
  protein are lacking.

## Curation calls
- Core MF: predicted membrane-anchored HSP40 co-chaperone (GO:0031072 heat shock
  protein binding), family/domain-level inference only.
- Bare `protein binding` to MEOX2 (high-throughput) marked over-annotated.