Sec11 is the conserved fungal catalytic subunit of the signal peptidase complex, an endoplasmic-reticulum membrane protease in the peptidase S26B family. In the ER signal peptidase complex, Sec11 cleaves hydrophobic N-terminal signal peptides from newly translocated secretory and membrane protein precursors, producing mature proteins that continue through the secretory pathway.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004252 serine-type endopeptidase activity | IEA GO_REF:0000002 | ACCEPT | Summary: Sec11 is a serine peptidase-family signal peptidase; this InterPro-derived term captures a mechanistic property that complements the accepted signal peptidase activity rows. Reason: The S26/SPase signatures and UniProt catalytic-site features support a serine signal peptidase fold. GO:0009003 signal peptidase activity is a sibling of GO:0004252 under endopeptidase activity, not a child, so the two terms capture orthogonal aspects of Sec11 catalysis: the signal peptide substrate class and the Ser/His/Asp active-site mechanism. Supporting Evidence: file:genes/EMENI/sec11/sec11-uniprot.txt InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS file:genes/EMENI/sec11/sec11-uniprot.txt InterPro; IPR019533; Peptidase_S26 |
| GO:0005783 endoplasmic reticulum | IEA GO_REF:0000107 | TOO GENERAL | Summary: Sec11 is an ER-membrane signal peptidase complex subunit; the ER location is true but broader than the accepted ER membrane location. Reason: UniProt places Q5B8K4 in the endoplasmic reticulum membrane by similarity to S. cerevisiae Sec11, and PANTHER places the gene in the same fungal SEC11 subfamily as the S. cerevisiae donor used by the EnsemblFungi transfer. GO:0005783 is broader than the accepted endoplasmic reticulum membrane rows, which capture the Sec11 functional location more precisely. Supporting Evidence: file:genes/EMENI/sec11/sec11-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0005787 signal peptidase complex | IBA GO_REF:0000033 | ACCEPT | Summary: The PANTHER Eukaryota node supports conserved membership in the ER signal peptidase complex. Reason: PAINT places signal peptidase complex at PTN000086750, scoped to Eukaryota, rather than at the PTHR10806 root. Q5B8K4 sits in the fungal SEC11 subfamily, and no Aspergillus-specific loss or divergence argues against retaining the conserved eukaryotic complex-membership assertion. Supporting Evidence: file:interpro/panther/PTHR10806/PTHR10806-paint.tsv PTHR10806 PTN000086750 GO:0005787 C IBD false SGD:S000001461|UniProtKB:P13679|UniProtKB:P67811|UniProtKB:P67812|UniProtKB:Q9BY50 taxon:2759 20250902 file:genes/EMENI/sec11/sec11-uniprot.txt SUBUNIT: Component of the signal peptidase complex |
| GO:0005787 signal peptidase complex | IEA GO_REF:0000107 | ACCEPT | Summary: Transfer of signal peptidase complex membership from S. cerevisiae SEC11 to the A. nidulans ortholog is exact. Reason: The EnsemblFungi transfer from S. cerevisiae points to the same conserved fungal SEC11 subfamily represented by Q5B8K4 and P15367 in PTHR10806:SF6; complex membership is also independently supported by the Eukaryota PAINT node PTN000086750. Supporting Evidence: file:genes/EMENI/sec11/sec11-uniprot.txt PANTHER; PTHR10806:SF6; SIGNAL PEPTIDASE COMPLEX CATALYTIC SUBUNIT SEC11 file:interpro/panther/PTHR10806/PTHR10806-paint.tsv PTHR10806 PTN000086750 GO:0005787 C IBD false |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Sec11 is an integral ER membrane component of the signal peptidase complex. Reason: The UniProt subcellular-location mapping is consistent with the reviewed Q5B8K4 flat-file annotation, which places Sec11 in the endoplasmic reticulum membrane as a single-pass type II membrane protein. Supporting Evidence: file:genes/EMENI/sec11/sec11-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane file:genes/EMENI/sec11/sec11-uniprot.txt TRANSMEM 19..39 |
| GO:0005789 endoplasmic reticulum membrane | ISS GO_REF:0000024 | ACCEPT | Summary: The manually transferred ER-membrane location from yeast Sec11 is biologically appropriate for A. nidulans Sec11. Reason: Q5B8K4 is in the same fungal SEC11 PANTHER subfamily as S. cerevisiae Sec11, and its UniProt flat file describes the same single-pass ER membrane topology. No species-specific evidence suggests a different compartment. Supporting Evidence: file:genes/EMENI/sec11/sec11-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane file:interpro/panther/PTHR10806/PTHR10806-entries.csv P15367,Signal peptidase complex catalytic subunit SEC11,protein,559292,Saccharomyces cerevisiae |
| GO:0008233 peptidase activity | IBA GO_REF:0000033 | TOO GENERAL | Summary: The root PAINT peptidase assignment is true for the family but too broad for this eukaryotic Sec11 member. Reason: PTN000086749 places generic peptidase activity at the root of PTHR10806, spanning bacterial, archaeal, and eukaryotic type I signal peptidases. For Q5B8K4, the accepted signal peptidase activity rows state the exact conserved Sec11 catalytic function, so GO:0008233 is an uninformative ancestor rather than an incorrect IBA. Supporting Evidence: file:interpro/panther/PTHR10806/PTHR10806-paint.tsv PTHR10806 PTN000086749 GO:0008233 F IBD false SGD:S000001461|UniProtKB:P13679|UniProtKB:P67811|UniProtKB:P67812|UniProtKB:Q8IE14|UniProtKB:Q9BY50 file:genes/EMENI/sec11/sec11-uniprot.txt CATALYTIC ACTIVITY: Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.; EC=3.4.21.89 |
| GO:0008233 peptidase activity | IEA GO_REF:0000120 | TOO GENERAL | Summary: The combined IEA peptidase call is directionally correct but broader than the accepted signal peptidase activity rows. Reason: The Peptidase_S26B family, yeast orthology, and UniProt record all support a signal peptidase, not merely an unspecified peptidase. Because GO:0009003 is already accepted in this review, retaining GO:0008233 would not add useful functional resolution. Supporting Evidence: file:genes/EMENI/sec11/sec11-uniprot.txt InterPro; IPR001733; Peptidase_S26B file:genes/EMENI/sec11/sec11-uniprot.txt SIMILARITY: Belongs to the peptidase S26B family. |
| GO:0009003 signal peptidase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Signal peptidase activity is the exact catalytic activity of the Sec11-containing ER signal peptidase complex. Reason: The EC-based IEA is corroborated by UniProt similarity to yeast Sec11 and human SEC11A, PTHR10806 family membership, and structural work showing that Sec11 is the conserved catalytic subunit of the eukaryotic signal peptidase complex. Supporting Evidence: file:genes/EMENI/sec11/sec11-uniprot.txt Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum PMID:42586426 Sec11, the catalytic subunit of the SPC, contains an N-terminal transmembrane domain and a C-terminal hydrophobic region. |
| GO:0009003 signal peptidase activity | ISS GO_REF:0000024 | ACCEPT | Summary: Yeast-to-A. nidulans transfer of signal peptidase activity is exact for the conserved fungal catalytic subunit. Reason: S. cerevisiae SEC11 and A. nidulans Sec11 are in the same PTHR10806:SF6 subfamily, and the Q5B8K4 flat file identifies the conserved signal peptidase I catalytic reaction by similarity to yeast SEC11. The ISS row therefore transfers the same molecular activity rather than a species-specific downstream phenotype. Supporting Evidence: file:genes/EMENI/sec11/sec11-uniprot.txt CATALYTIC ACTIVITY: Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.; EC=3.4.21.89 file:interpro/panther/PTHR10806/PTHR10806-entries.csv Q5B8K4,Signal peptidase complex catalytic subunit sec11,protein,227321,Emericella nidulans |
| GO:0016020 membrane | IEA GO_REF:0000002 | TOO GENERAL | Summary: Sec11 is a membrane protein, but the existing ER membrane rows provide the correct compartmental specificity. Reason: Peptidase S26B/SPase I signatures and the Q5B8K4 topology support a membrane signal peptidase. GO:0016020 is nevertheless only a broad ancestor of the accepted endoplasmic reticulum membrane annotations. Supporting Evidence: file:genes/EMENI/sec11/sec11-uniprot.txt Single-pass type II membrane protein |
| GO:0045047 protein targeting to ER | IEA GO_REF:0000107 | REMOVE | Summary: Sec11 processes signal peptides after ER targeting; it is not known to direct proteins to the ER. Reason: GO:0045047 describes the direction of proteins toward the ER. Sec11 acts in the ER membrane signal peptidase complex after nascent chains have already been targeted and translocated by the SRP/Sec61 or Sec62/Sec63-dependent machinery. The A. nidulans overexpression study grouped AN10354 with ER translocation candidates but only assayed secretion after AN10354 overexpression, so the automatic transfer of the targeting process from yeast is not supported for this catalytic peptidase subunit. Supporting Evidence: PMID:42586426 First, these sequences target nascent chains to the ER membrane by interacting with the signal recognition particle (SRP), which delivers the ribosome-nascent chain complex to the Sec61 translocon. Upon targeting, signal sequences trigger the opening of the Sec61 protein-conducting channel by binding at its lateral gate. Subsequently, they ensure proper folding and localization of nascent chains through timely processing by the signal peptidase complex (SPC). PMID:28955462 Sec63 (AN0834) and the ortholog of S. cerevisiae SEC11 (AN10354) were overexpressed (generating strains NID1600 and NID1608, respectively). |
| GO:0051604 protein maturation | IBA GO_REF:0000033 | MODIFY | Summary: PAINT supports the conserved eukaryotic role of Sec11 in maturing nascent proteins by signal peptide cleavage, but the GOA term is broader than the live process term for the SPC reaction. Reason: PTN000086750 places protein maturation at Eukaryota for PTHR10806. That scope is appropriate for A. nidulans Sec11 because eukaryotic Sec11 matures secretory precursors as part of the ER signal peptidase complex; the node is separate from the root-level generic peptidase call and is not transferring a lineage-specific phenotype. 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 SPC proteolysis. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000086750 SUPPORTS TRANSFER PTN000086750 correctly supports a eukaryotic Sec11 protein-maturation process, but the gene-level row can be refined to the live protein processing term for SPC-catalyzed signal peptide cleavage. Proposed replacements: protein processing Supporting Evidence: file:interpro/panther/PTHR10806/PTHR10806-paint.tsv PTHR10806 PTN000086750 GO:0051604 P IBD false SGD:S000001461|UniProtKB:P67812|UniProtKB:Q9BY50 taxon:2759 20260528 PMID:42586426 Following targeting, these sequences are cleaved by the heterotetrameric signal peptidase complex (SPC). |
| GO:0051604 protein maturation | IEA GO_REF:0000120 | MODIFY | Summary: The combined automated protein maturation annotation matches the conserved Sec11 signal peptide-processing role but is one level broader than the live SPC process term. Reason: S26B family membership and the yeast Sec11 orthology both point to cleavage of signal peptides from newly translocated proteins, a direct protein-maturation step in the ER signal peptidase complex. GO:0016485 protein processing is the live process term for that proteolytic cleavage after obsoletion of GO:0006465 signal peptide processing. Proposed replacements: protein processing Supporting Evidence: file:genes/EMENI/sec11/sec11-uniprot.txt Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum PMID:42586426 Following targeting, these sequences are cleaved by the heterotetrameric signal peptidase complex (SPC). |
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