CAMLG (P49069) curation notes

Identity

Core function: GET/TRC insertase receptor for tail-anchored (TA) proteins

CAML, together with WRB/GET1, forms the mammalian ER membrane receptor for the cytosolic ATPase TRC40/GET3, which delivers newly synthesized tail-anchored membrane proteins for post-translational insertion into the ER membrane. CAML is the mammal-specific subunit (not homologous to yeast Get2); WRB is the Get1 orthologue.

Reactome: R-HSA-9609523 "Insertion of tail-anchored proteins into the endoplasmic reticulum membrane".

GET complex membership and reciprocal stability with WRB

CAML and WRB depend on each other for stability/correct topology.
- PMID:32187542
- PMID:31417168
- GO terms: GET complex (GO:0043529) part_of — well supported (IDA PMID:32910895, IPI PMID:23041287). Protein stabilization (GO:0050821) is supported in the WRB/CAML context (PMID:32187542) but note PMID:20553626 also annotated stabilization in the unrelated RNF122 context.

Secondary / historical functions

Calcium signaling (original discovery)

CAML was originally cloned as a cyclophilin-B-binding protein that induces calcium influx in T cells and activates NF-AT/IL-2 transcription. This is the historical basis of the "defense response" (GO:0006952) and "signal transduction" (GO:0007165) TAS annotations from PMID:7522304. Plausible but largely supplanted by the well-established GET insertase role; treat as non-core/contextual.
- PMID:7522304

B cell homeostasis

By-similarity/ISS: "Essential for the survival of peripheral follicular B cells" (UniProt). Mouse phenotype; CAML interacts with TACI/TNFRSF13B (PMID:9311921 — not cached). Non-core for the human gene's molecular function.

EGFR recycling

CAML-deficient cells have defective EGFR recycling; CAML associates with the EGFR kinase domain ligand-dependently (PMID:12919676). This is the basis of Ensembl IEA "receptor recycling" and "epidermal growth factor receptor signaling pathway" terms (not in the current existing_annotations list except via interactome IPI). Context-dependent; potentially confounded by the general role of CAML in membrane protein biogenesis.

The negative regulation of (protein) ubiquitination / proteasomal catabolism / protein stabilization and ubiquitin-protein-ligase-binding annotations all derive from one yeast-two-hybrid + co-IP study of the RING E3 RNF122, in which CAML stabilizes RNF122 (and is not its substrate). These are narrow, single-study, context-specific findings, not the core GET function.
- PMID:20553626
- PMID:20553626

Over-annotations / non-informative

Localization

Well supported: ER membrane / ER (multiple EXP/IDA: PMID:23041287, PMID:31417168, PMID:12919676). Core.

Summary of action plan

Falcon deep research synthesis (2026-06-21)

Falcon deep research has now completed (file:human/CAMLG/CAMLG-deep-research-falcon.md,
25 citations). It strongly corroborates the GET/TRC insertase-receptor core above and
adds substrate-specificity and disease-mechanism detail; no change to the core call.

Net: no change to calls — CAMLG is the mammal-specific ER GET-pathway insertase
receptor subunit (with WRB) for tail-anchored proteins; the new client/disease
detail strengthens that core and its proteostasis relevance.