# DNAJC25 (Q9H1X3) research notes

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

## Architecture
- N-terminal signal-anchor/transmembrane segment followed by a **J-domain** (HPD
  tripeptide), plus additional predicted transmembrane helices. [UniProt Q9H1X3]

## Functional inference
- By phylogenetic inference within its family, predicted to act at the ER membrane as
  a co-chaperone assisting HSP70-dependent protein folding/quality control. No direct
  experimental functional data exist for the human protein.

## Curation calls
- Core MF: predicted membrane-anchored HSP40 co-chaperone (GO:0031072 heat shock
  protein binding), family/domain-level inference only.
- Localization annotations accepted/kept non-core per UniProt; no foldase claim made.