id: B7FXQ8 gene_symbol: B7FXQ8 taxon: id: NCBITaxon:556484 label: Phaeodactylum tricornutum status: COMPLETE description: >- The small heat-shock protein HSP20A of Phaeodactylum tricornutum has architecture supporting oligomerization, unfolded-protein binding, and a protective chaperone role. Specific heat, salt, and peroxide responses remain unresolved. source_documents: - genes/PHATC/B7FXQ8/B7FXQ8-uniprot.txt - genes/PHATC/B7FXQ8/B7FXQ8-goa.tsv - publications/PMID_29983375.md - genes/PHATC/B7FXQ8/B7FXQ8-hypotheses/prediction-salt-and-peroxide-stress/openscientist.md predictions: - source_method: ProtNLM2 source_version: UniProt 2024_06 pilot predicted_term: id: GO:0009651 label: response to salt stress predicted_term_type: GO_BP review: assessment: UNC confidence_score: 1 summary: >- The target has an alpha-crystallin/Hsp20 domain and is assigned to the small heat-shock protein family. Characterized sHSPs bind unfolded proteins and form regulated oligomers (PMID:29983375), but those properties do not establish a salt-triggered response in this diatom protein. The inspected evidence contains no target expression or functional assay under salt stress. Response to salt stress is absent from the cached annotations and remains uncertain. supported_by: - reference_id: file:PHATC/B7FXQ8/B7FXQ8-uniprot.txt supporting_text: >- ID B7FXQ8_PHATC Unreviewed; 163 AA. ... DR InterPro; IPR002068; A-crystallin/Hsp20_dom. ... DR InterPro; IPR008978; HSP20-like_chaperone. ... DR InterPro; IPR031107; Small_HSP. ... FT DOMAIN 47..155 ... FT /note="SHSP" - reference_id: PMID:29983375 supporting_text: >- Small heat-shock proteins (sHSPs) are molecular chaperones that bind partially and globally unfolded states of their client proteins. ... the archaeal Hsp16.5, which forms ordered and symmetric 24-subunit oligomers - reference_id: file:PHATC/B7FXQ8/B7FXQ8-hypotheses/prediction-salt-and-peroxide-stress/openscientist.md supporting_text: >- the salt and peroxide predictions are outliers even relative to the family's own conservative InterPro2GO mapping - source_method: ProtNLM2 source_version: UniProt 2024_06 pilot predicted_term: id: GO:0051259 label: protein complex oligomerization predicted_term_type: GO_BP review: assessment: COR confidence_score: 2 summary: >- The 163-residue target has the small heat-shock protein architecture, including the alpha-crystallin domain. Structural and functional experiments on sHSPs establish conserved oligomer assembly and plasticity (PMID:29983375), supporting transfer of broad protein oligomerization to this family member. This inference does not prescribe a particular oligomer size. The process is absent from the cached annotations. supported_by: - reference_id: file:PHATC/B7FXQ8/B7FXQ8-uniprot.txt supporting_text: >- ID B7FXQ8_PHATC Unreviewed; 163 AA. ... DR InterPro; IPR002068; A-crystallin/Hsp20_dom. ... DR InterPro; IPR008978; HSP20-like_chaperone. ... DR InterPro; IPR031107; Small_HSP. ... FT DOMAIN 47..155 ... FT /note="SHSP" - reference_id: PMID:29983375 supporting_text: >- Small heat-shock proteins (sHSPs) are molecular chaperones that bind partially and globally unfolded states of their client proteins. ... the archaeal Hsp16.5, which forms ordered and symmetric 24-subunit oligomers - source_method: ProtNLM2 source_version: UniProt 2024_06 pilot predicted_term: id: GO:0006457 label: protein folding predicted_term_type: GO_BP review: assessment: COR confidence_score: 2 summary: >- The alpha-crystallin/Hsp20 domain and small-HSP family assignment support a holdase chaperone role. Characterized sHSPs bind nonnative clients and protect them from aggregation (PMID:29983375), allowing subsequent recovery of folding with other chaperones. The broad protein-folding process can encompass this assistance; it does not imply that the protein itself catalyzes ATP-dependent refolding. There is no more specific existing GOA/UniProt annotation against which to call this prediction less precise. supported_by: - reference_id: file:PHATC/B7FXQ8/B7FXQ8-uniprot.txt supporting_text: >- ID B7FXQ8_PHATC Unreviewed; 163 AA. ... DR InterPro; IPR002068; A-crystallin/Hsp20_dom. ... DR InterPro; IPR008978; HSP20-like_chaperone. ... DR InterPro; IPR031107; Small_HSP. ... FT DOMAIN 47..155 ... FT /note="SHSP" - reference_id: PMID:29983375 supporting_text: >- Small heat-shock proteins (sHSPs) are molecular chaperones that bind partially and globally unfolded states of their client proteins. ... the archaeal Hsp16.5, which forms ordered and symmetric 24-subunit oligomers - source_method: ProtNLM2 source_version: UniProt 2024_06 pilot predicted_term: id: GO:0009408 label: response to heat predicted_term_type: GO_BP review: assessment: UNC confidence_score: 1 summary: >- The target has an alpha-crystallin/Hsp20 domain consistent with a small-HSP chaperone. Experiments on other small HSPs establish oligomer plasticity and binding to unfolded clients (PMID:29983375), but do not establish this diatom protein's involvement in a heat-triggered response. The heat-shock family name alone does not identify the stimulus controlling this member. Response to heat is absent from the cached annotations and remains uncertain without target-specific thermal-response evidence or a justified transfer from a characterized close relative. supported_by: - reference_id: file:PHATC/B7FXQ8/B7FXQ8-uniprot.txt supporting_text: >- ID B7FXQ8_PHATC Unreviewed; 163 AA. ... DR InterPro; IPR002068; A-crystallin/Hsp20_dom. ... DR InterPro; IPR008978; HSP20-like_chaperone. ... DR InterPro; IPR031107; Small_HSP. ... FT DOMAIN 47..155 ... FT /note="SHSP" - reference_id: PMID:29983375 supporting_text: >- Small heat-shock proteins (sHSPs) are molecular chaperones that bind partially and globally unfolded states of their client proteins. ... the archaeal Hsp16.5, which forms ordered and symmetric 24-subunit oligomers - source_method: ProtNLM2 source_version: UniProt 2024_06 pilot predicted_term: id: GO:0042542 label: response to hydrogen peroxide predicted_term_type: GO_BP review: assessment: UNC confidence_score: 1 summary: >- The small-HSP architecture supports a chaperone function, but it does not establish involvement in a response specifically triggered by hydrogen peroxide. General protection of unfolded proteins and evidence for stress responses in other sHSPs do not determine the target's peroxide response. No relevant target or close-ortholog expression, perturbation, or protection experiment is established in the inspected sources. The predicted process is absent from the cached annotations and remains uncertain. supported_by: - reference_id: file:PHATC/B7FXQ8/B7FXQ8-uniprot.txt supporting_text: >- ID B7FXQ8_PHATC Unreviewed; 163 AA. ... DR InterPro; IPR002068; A-crystallin/Hsp20_dom. ... DR InterPro; IPR008978; HSP20-like_chaperone. ... DR InterPro; IPR031107; Small_HSP. ... FT DOMAIN 47..155 ... FT /note="SHSP" - reference_id: file:PHATC/B7FXQ8/B7FXQ8-hypotheses/prediction-salt-and-peroxide-stress/openscientist.md supporting_text: >- the salt and peroxide predictions are outliers even relative to the family's own conservative InterPro2GO mapping - source_method: ProtNLM2 source_version: UniProt 2024_06 pilot predicted_term: id: GO:0051082 label: unfolded protein binding predicted_term_type: GO_MF review: assessment: COR confidence_score: 2 summary: >- The target has the characteristic alpha-crystallin/Hsp20 domain of small heat-shock proteins. Client-binding experiments on characterized sHSPs demonstrate recognition of partially or globally unfolded proteins (PMID:29983375), providing a mechanistic basis for transferring broad unfolded-protein binding. This does not establish a particular client or ATP-dependent foldase activity. The molecular function is absent from the cached annotations. supported_by: - reference_id: file:PHATC/B7FXQ8/B7FXQ8-uniprot.txt supporting_text: >- ID B7FXQ8_PHATC Unreviewed; 163 AA. ... DR InterPro; IPR002068; A-crystallin/Hsp20_dom. ... DR InterPro; IPR008978; HSP20-like_chaperone. ... DR InterPro; IPR031107; Small_HSP. ... FT DOMAIN 47..155 ... FT /note="SHSP" - reference_id: PMID:29983375 supporting_text: >- Small heat-shock proteins (sHSPs) are molecular chaperones that bind partially and globally unfolded states of their client proteins. ... the archaeal Hsp16.5, which forms ordered and symmetric 24-subunit oligomers references: - id: file:PHATC/B7FXQ8/B7FXQ8-uniprot.txt title: B7FXQ8-uniprot.txt - id: PMID:29983375 title: Engineering of a Polydisperse Small Heat-Shock Protein Reveals Conserved Motifs of Oligomer Plasticity. - id: file:PHATC/B7FXQ8/B7FXQ8-hypotheses/prediction-salt-and-peroxide-stress/openscientist.md title: 'OpenScientist focused report: B7FXQ8 salt and peroxide ProtNLM terms'