| Aspect | Key finding | Evidence type | Study (author, year, journal) | Quantitative/statistical detail (if any) | URL/DOI (if present in paper metadata) | Citation ID to use |
|---|---|---|---|---|---|---|
| identity/domain | HSP-12.3 is the C. elegans small heat shock protein encoded by F38E11.1 (Ce12.3), belonging to the Hsp12/sHSP family and retaining the conserved α-crystallin domain with very short N-terminus and little or no C-terminal tail. | Sequence/structural annotation; comparative family analysis | Krause, 2013, unknown journal; Ramsay, 2012, unknown journal | Family proteins are ~12.2–12.6 kDa; α-crystallin core described as ~80–100 aa. | N/A | (pqac-00000002, pqac-00000003) |
| oligomerization | Unlike many sHSPs that form large multimers, HSP-12.3 is reported to assemble as a tetramer, and HSP-12.2/HSP-12.3 can form heterotetramers. | In vitro biochemistry / oligomerization analysis | Krause, 2013, unknown journal; Ramsay, 2012, unknown journal | Tetrameric organization reported for Hsp12 members except Hsp12.6 in recombinant preparations. | N/A | (pqac-00000002, pqac-00000001) |
| in vitro chaperone activity | Recombinant HSP-12.3 did not prevent aggregation of thermally unfolding citrate synthase in standard assays, so no conventional in vitro chaperone activity was detected. | In vitro chaperone assay | Ramsay, 2012, unknown journal | Negative assay reported at 43°C with citrate synthase aggregation assay. | N/A | (pqac-00000006, pqac-00000007) |
| regulation/pathways | hsp-12.3 is repeatedly described as a DAF-16/FOXO-associated insulin-signaling target, being upregulated when daf-2/IIS is reduced and downregulated when daf-16 activity is reduced; hpk-1 loss also reduces hsp-12.3 expression. | Transcriptomics / genetics | Ramsay, 2012, unknown journal; Berber et al., 2016, Scientific Reports | No gene-specific fold-change reported in extracted text; HPK-1 loss reduced post-stress survival by ~25% overall, while hsp-12.3 was among genes reduced in hpk-1(-). | https://doi.org/10.1038/srep19582 | (pqac-00000000, pqac-00000008, pqac-00000009) |
| hypoxia/HIF-1 | In 2024 whole-genome hypoxia profiling, hsp-12.3 was listed among stress-response genes positively regulated by HIF-1 under short-term hypoxia, but the supplied excerpt did not give an hsp-12.3-specific fold change or direct-target ChIP evidence. | RNA-seq / hypoxia transcriptomics | Feng, Qu & Powell-Coffman, 2024, PLOS ONE | Stress-response category significance Bonferroni/FDR = 7.88E-03; no per-gene hsp-12.3 value in provided text. | https://doi.org/10.1371/journal.pone.0295094 | (pqac-00000010) |
| proteostasis/sequestration | In the evolutionary sequestration study, HSP-12.3 was classified as sequestrase-negative and lacked sequence features associated with sequestrase-positive sHSPs, arguing against a major role in inclusion-forming sequestration. | Comparative functional assay / sequence-feature analysis | Shrivastava et al., 2022, Journal of Cell Biology | Sequestrase-positive sHSPs had longer NTEs on average (39 vs 25 aa) and longer CTEs (21 vs 6 aa); Hsp-12.3 was in the “none” group for sequestrase activity. | https://doi.org/10.1083/jcb.202202149 | (pqac-00000011, pqac-00000012) |
| expression with age | HSP-12.3 protein abundance increases with age and is among age-increasing proteins that rise even more strongly in long-lived daf-2 mutants. | Deep quantitative proteomics | Narayan et al., 2016, Cell Systems | 55 proteins increased with age; 25% (14/55) increased to a much greater extent in daf-2(e1370), including HSP-12.3; >9,300 proteins were reproducibly identified per replicate. | https://doi.org/10.1016/j.cels.2016.06.011 | (pqac-00000013) |
| localization/tissue expression | Direct HSP-12.3 localization evidence is limited; cross-reactive antibody data suggest expression patterns similar to Hsp12-family proteins, while Hsp12.6 family staining in adults is restricted to vulval cells and spermatheca, so localization for HSP-12.3 remains inferred rather than definitive. | Immunostaining / family-level expression analysis | Krause, 2013, unknown journal | Hsp12.6 peaks in L1 and in adults localizes to vulval cells and spermatheca; explicit HSP-12.3 localization was not shown in the excerpt. | N/A | (pqac-00000002, pqac-00000004) |
| phenotypes/functional tests | hsp-12.3 RNAi did not measurably alter lifespan in several tested genetic backgrounds, but the result is considered inconclusive because RNAi specificity was not verified and redundancy with hsp-12.2/heterotetramerization could mask function. | Genetics / RNAi lifespan testing | Ramsay, 2012, unknown journal | No lifespan effect seen in N2, phsp-12.6::HSP-12.6::DSRED2, hsf-1(sy441), or daf-16(mu86) backgrounds in the reported experiments. | N/A | (pqac-00000000, pqac-00000001) |


*Table: This table compiles the most relevant evidence found for C. elegans hsp-12.3/F38E11.1, organized by annotation-relevant aspects such as domain identity, regulation, localization, and functional testing. It is useful as a quick evidence map distinguishing direct findings from family-level inference and highlighting where data remain limited.*