SEC11

Summary: The S26 InterPro signatures correctly identify SEC11 as a serine peptidase; GO:0004252 captures the Sec11 catalytic mechanism while GO:0009003 captures the signal-peptide substrate class.

Reason: Candida SEC11 is an S26B signal peptidase with the conserved signal-peptidase catalytic subunit architecture. GO:0009003 signal peptidase activity is a sibling of GO:0004252 under endopeptidase activity, not a child, and the serine-type term records the conserved Sec11 active-site mechanism independently of the substrate-specific signal peptidase rows.

Summary: The ER localization transferred from S. cerevisiae SEC11 is sound but should be refined to the ER membrane.

Reason: SEC11 is a single-pass component of the ER signal peptidase complex. The broader endoplasmic-reticulum location is true, but GOA already carries the more precise endoplasmic reticulum membrane term from UniProt SubCell and orthology to S. cerevisiae.

Proposed replacements: endoplasmic reticulum membrane

Summary: The PTN000086750 IBA correctly places eukaryotic SEC11 proteins in the ER signal peptidase complex.

Reason: Candida Q5A869 is in the fungal SEC11 subfamily of PTHR10806, and the PTN000086750 PAINT node is scoped to Eukaryota for the signal peptidase complex annotation. This is the expected complex for the catalytic SEC11 subunit.

Summary: The automated UniProt assertion to signal peptidase complex agrees with the eukaryotic PAINT node and the reviewed UniProt family assignment.

Reason: Although ARBA alone would not be strong support, the term is independently corroborated by PAINT node PTN000086750 and by orthology to S. cerevisiae SEC11, so retaining signal peptidase complex membership is appropriate.

Summary: UniProt's ER membrane SubCell mapping is the expected location for a SEC11 signal peptidase complex subunit.

Reason: The signal peptidase complex is embedded in the ER membrane; the Candida SEC11 UniProt record likewise describes Q5A869 as an ER membrane type-II membrane protein by similarity.

Summary: The manually transferred ER membrane location from S. cerevisiae SEC11 is sound.

Reason: Candida SEC11 and S. cerevisiae SEC11 are in the same fungal SEC11 PANTHER subfamily, and the curated Q5A869 record describes the Candida protein as a single-pass ER membrane protein by similarity to S. cerevisiae.

Summary: Root biological process ND annotation: when it was made, no biological process had been curated for this gene product from literature.

Reason: ACCEPT under the ND acceptance rule (projects/NO_DATA.md). The evidence this review cites for the biological process is inferred (from orthologs, family membership or sequence features) or comes from other species; none of it is literature on this gene product in this species. This was judged from the review's own content during the NO_DATA re-action pass, not from a new literature search. Earlier action: TOO_GENERAL. PMID:32102426 is a review of Candida secretory pathways that describes signal peptidase in general terms.

Summary: The PTN000086749 root IBA is correct for the SEC11 family but intentionally generic.

Reason: PTN000086749 was placed at the PTHR10806 root and therefore asserts only the broad peptidase activity shared across the family. Candida SEC11 is specifically an ER signal peptidase, so refine the broad parent to GO:0009003 signal peptidase activity.

Proposed replacements: signal peptidase activity

Summary: The automated peptidase annotation is true but should be refined to signal peptidase activity.

Reason: IPR001733 is the peptidase S26B signature carried by signal peptidase catalytic subunits. For Candida SEC11, the informative molecular-function assertion is GO:0009003 signal peptidase activity rather than its broad peptidase parent.

Proposed replacements: signal peptidase activity

Summary: GO:0009003 is the exact molecular function for Candida SEC11's inferred EC 3.4.21.89 activity.

Reason: The EC 3.4.21.89 assignment, fungal SEC11 PANTHER subfamily placement, and conserved ER signal peptidase complex biology all support signal peptidase activity for Q5A869.

Summary: The manually transferred signal peptidase activity from S. cerevisiae SEC11 is sound.

Reason: Candida SEC11 is the S. cerevisiae-like fungal PTHR10806:SF6 catalytic SPC subunit. The Q5A869 reviewed record carries EC 3.4.21.89 and catalytic-site features by similarity to S. cerevisiae SEC11, and no Candida-specific loss or divergence is evident.

Summary: SEC11 is a membrane protein, but the specific supported location is the ER membrane.

Reason: The InterPro-to-GO membrane mapping is true for the S26B signal-peptidase domain architecture but too general for a eukaryotic SEC11 subunit. The Q5A869 UniProt record and GOA's UniProt SubCell row support endoplasmic reticulum membrane.

Proposed replacements: endoplasmic reticulum membrane

Summary: SEC11 cleaves signal peptides after ER targeting and translocation; it is not the targeting machinery.

Reason: GO:0045047 covers directing proteins toward the ER via their targeting signals. SEC11 functions downstream in the ER signal peptidase complex, where it cleaves the signal peptide after the nascent chain has been targeted to and translocated into the ER.

Summary: The PTN000086750 IBA to protein maturation appropriately captures SEC11-catalyzed signal peptide removal in eukaryotes but should be refined to the live protein processing term for SPC proteolysis.

Reason: Signal peptide cleavage converts secretory-pathway preproteins toward their mature forms. PAINT places GO:0051604 at the same eukaryote-scoped PTN000086750 node as signal peptidase complex membership, so the row reflects conserved eukaryotic SPC function rather than a bacterial or off-branch transfer. GO:0051604 is nevertheless broader than the signal-peptide cleavage step; after obsoletion of GO:0006465 signal peptide processing, GO:0016485 protein processing is the live process-level term for this SPC reaction.

Proposed replacements: protein processing

Summary: The automated protein maturation row agrees with the eukaryotic PAINT assertion and the known SPC maturation step but is too broad for the specific proteolytic processing reaction.

Reason: Signal peptide cleavage is a protein-maturation event for preproteins entering the secretory pathway. Although the row is automated, it is corroborated by the PTN000086750 IBA and by the 2020 Candida secretory-pathway synthesis. GO:0016485 protein processing is the live process term for the signal-peptide proteolysis carried out by SEC11.

Proposed replacements: protein processing