P58IPK is a DNAJC3-family cochaperone with tetratricopeptide repeats, an N-terminal signal peptide, and a C-terminal J domain. It assists protein folding in the endoplasmic reticulum through chaperone and unfolded-client interactions. Its secretory targeting is compatible with an ER-lumen cochaperone, while stable ER-membrane attachment is not established.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005783 endoplasmic reticulum | IBA GO_REF:0000033 | ACCEPT | Summary: ER localization is consistent with signal-peptide and cochaperone architecture. Reason: An N-terminal signal peptide and DNAJC3-family J/TPR architecture support the phylogenetically curated ER annotation. Supporting Evidence: file:DROME/P58IPK/P58IPK-uniprot.txt DR InterPro; IPR051727; DnaJ_C3_Co-chaperones. file:DROME/P58IPK/P58IPK-uniprot.txt DR InterPro; IPR001623; DnaJ_domain. file:DROME/P58IPK/P58IPK-uniprot.txt FT SIGNAL 1..36 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/P58IPK/P58IPK-uniprot.txt FT DOMAIN 396..463 FT /note="J" FT /evidence="ECO:0000259|PROSITE:PS50076" |
| GO:0005783 endoplasmic reticulum | IEA GO_REF:0000044 | ACCEPT | Summary: Broad ER localization is biologically supported independently of the automated location mapping. Reason: The signal peptide and DNAJC3 architecture support ER targeting. The ARBA sentence in UniProt is not treated as experimental localization evidence. Supporting Evidence: file:DROME/P58IPK/P58IPK-uniprot.txt DR InterPro; IPR051727; DnaJ_C3_Co-chaperones. file:DROME/P58IPK/P58IPK-uniprot.txt DR InterPro; IPR001623; DnaJ_domain. file:DROME/P58IPK/P58IPK-uniprot.txt FT SIGNAL 1..36 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/P58IPK/P58IPK-uniprot.txt FT DOMAIN 396..463 FT /note="J" FT /evidence="ECO:0000259|PROSITE:PS50076" |
| GO:0012505 endomembrane system | HDA PMID:19317464 Mapping organelle proteins and protein complexes in Drosophi... | KEEP AS NON CORE | Summary: The broad endomembrane-proteomics assignment is consistent with ER biology. Reason: PMID:19317464 is a proteomic localization study; the exact source is abstract-only in the cache. The assignment is retained as compatible high-throughput evidence and does not establish membrane insertion. Supporting Evidence: file:DROME/P58IPK/P58IPK-uniprot.txt DR InterPro; IPR051727; DnaJ_C3_Co-chaperones. file:DROME/P58IPK/P58IPK-uniprot.txt DR InterPro; IPR001623; DnaJ_domain. file:DROME/P58IPK/P58IPK-uniprot.txt FT SIGNAL 1..36 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/P58IPK/P58IPK-uniprot.txt FT DOMAIN 396..463 FT /note="J" FT /evidence="ECO:0000259|PROSITE:PS50076" |
| GO:0034975 protein folding in endoplasmic reticulum | IBA GO_REF:0000033 | ACCEPT | Summary: ER protein folding is the coherent cochaperone role. Reason: The signal peptide, TPR-repeat substrate-binding architecture, and J domain support the existing IBA role in ER protein folding. Supporting Evidence: file:DROME/P58IPK/P58IPK-uniprot.txt DR InterPro; IPR051727; DnaJ_C3_Co-chaperones. file:DROME/P58IPK/P58IPK-uniprot.txt DR InterPro; IPR001623; DnaJ_domain. file:DROME/P58IPK/P58IPK-uniprot.txt FT SIGNAL 1..36 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/P58IPK/P58IPK-uniprot.txt FT DOMAIN 396..463 FT /note="J" FT /evidence="ECO:0000259|PROSITE:PS50076" |
| GO:0051087 protein-folding chaperone binding | IBA GO_REF:0000033 | ACCEPT | Summary: Chaperone interaction is supported by the J-domain cochaperone architecture. Reason: The DNAJC3-family protein contains a J domain at residues 396-463 and TPR repeats. This supports the existing phylogenetic inference of protein-folding-chaperone interaction without calling the protein an ATPase. Supporting Evidence: file:DROME/P58IPK/P58IPK-uniprot.txt DR InterPro; IPR051727; DnaJ_C3_Co-chaperones. file:DROME/P58IPK/P58IPK-uniprot.txt DR InterPro; IPR001623; DnaJ_domain. file:DROME/P58IPK/P58IPK-uniprot.txt FT SIGNAL 1..36 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/P58IPK/P58IPK-uniprot.txt FT DOMAIN 396..463 FT /note="J" FT /evidence="ECO:0000259|PROSITE:PS50076" |
| GO:0051787 misfolded protein binding | IBA GO_REF:0000033 | ACCEPT | Summary: Client binding is consistent with DNAJC3-family cochaperone function. Reason: The TPR/J architecture supports the existing IBA misfolded-protein-binding inference; binding and delivery to a chaperone are distinct from independent ATP-driven folding. Supporting Evidence: file:DROME/P58IPK/P58IPK-uniprot.txt DR InterPro; IPR051727; DnaJ_C3_Co-chaperones. file:DROME/P58IPK/P58IPK-uniprot.txt DR InterPro; IPR001623; DnaJ_domain. file:DROME/P58IPK/P58IPK-uniprot.txt FT SIGNAL 1..36 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/P58IPK/P58IPK-uniprot.txt FT DOMAIN 396..463 FT /note="J" FT /evidence="ECO:0000259|PROSITE:PS50076" |
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