## DNAJC3
- **UniProt:** Q13217 (p58IPK/ERdj6/PRKRI) · **batch:** proteostasis-batch-2026-06-07b · **review status:** COMPLETE
- **PN placement:** `ER proteostasis|Chaperone|HSP70 system|J-domain containing HSP70 cochaperone` (branch ER) ; **PN-node mapping:** type=mapped, scope=ok_for_propagation_to_go, GO:0030544 Hsp70 protein binding (parents no_mapping)
- **Consistency:** Consistent on the chaperone axis, but the PN node captures only half the gene. Notes/YAML describe a dual-function ER J-protein: (1) TPR+J-domain co-chaperone binding BiP (HSPA5)/HSC70 (HSPA8), stimulating their ATPase and binding misfolded substrates via the TPR groove (GO:0051087, GO:0051787 ACCEPT/core); and (2) a stress-inducible inhibitor of the eIF2-alpha kinases PKR/PERK/GCN2 (GO:0004860 protein kinase inhibitor activity, GO:0019901 protein kinase binding ACCEPT/core). The PN "J-domain HSP70 cochaperone" type correctly captures axis (1); the kinase-inhibition axis is outside this node (legitimately, since it is not an HSP70 function).
- **PN story / NEW pressure:** PN's HSP70-binding assertion is fully captured (GO:0051087 ACCEPT/core, plus misfolded protein binding). PN-projected GO:0030544 (verified real, child of GO:0051087) is a defensible narrower specialization — DNAJC3 binds HSPA8/BiP directly via its J domain. No NEW proteostasis GO term needed; the second (kinase-inhibitor) function is already richly annotated. Verdict: already captured.
- **Mapping strategy:** GO:0030544 mapping appropriate; DNAJC3 has direct chaperone-binding evidence so the type-level propagation does not over-reach. The node legitimately omits the eIF2-alpha-kinase-inhibition function, which is not HSP70-system biology.
- **Evidence alignment:** Review core PMIDs (8576172 PKR inhibition; 25466870 disease/BiP co-chaperone; 8666242/12601012 p58IPK) are dual-function focused; PN frames only the cochaperone half. Complementary, not contradictory.
- **Verdict:** CONSISTENT — GO:0030544 sound for the cochaperone axis; PN node intentionally scopes out the (well-captured) eIF2-alpha-kinase-inhibitor function.