PN placement:ER proteostasis|Protein transport|SEC61 channel accessory protein ; PN-node mapping: group "SEC61 channel accessory protein"=no_mapping (broad category); parent class "Protein transport"=mapped/ok GO:0015031 protein transport; branch=no_mapping.
Consistency: Deep research ↔ review YAML ↔ PN annotation consistent. All describe SERP1/RAMP4 as a stress-induced, Sec61-translocon-associated single-pass ER membrane protein that stabilizes nascent membrane/secretory substrates during ER stress and facilitates post-stress N-glycosylation; 2024 cryo-EM (PMID:38896445) places RAMP4 in the Sec61 lateral gate. No contradictions. The PN group is deliberately left unmapped (heterogeneous "SEC61 accessory" members), which fits.
PN story / NEW pressure: PN asserts no specific role beyond the unmapped accessory-protein grouping. SERP1's substantive functions — GO:0030968 ER unfolded protein response (IBA, CORE) and translocon-associated ER membrane localization — are already captured in GOA/review. No defensible NEW GO term is needed; review proposes none. Already captured.
Mapping strategy: Concern — the parent class node projects GO:0015031 protein transport as new_to_goa. SERP1 is a translocon-associated substrate stabilizer/chaperone, not a transport carrier; it does not itself transport proteins. GO:0015031 over-reaches (TOMM20/HSPA8/RAB7A precedent: rejected as broader/unsupported). The group-level no_mapping decision is appropriate; the class-level GO:0015031 should not propagate to SERP1.
Evidence alignment: Good overlap on the defining paper (PMID:10601334) and translocon structure (PMID:38896445). Review extends with antiviral/ER-stress papers (DENV-2 PMID:31461934; hepatic injury PMID:35419615; translocon reviews) not enumerated in the terse PN row. Review also flags PMID:23264731 as a wrong-gene (MTR120) mis-attribution → REMOVE for GO:0005881 cytoplasmic microtubule.
Verdict: Consistent and well-curated. Recommend NOT propagating class-level GO:0015031 protein transport to SERP1 (over-reach); UPR + ER-membrane already captured.