SEC11

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0004252 serine-type endopeptidase activity	IEA GO_REF:0000002	MODIFY	Summary: SEC11 is a serine-family peptidase, but the InterPro signal peptidase motifs support the more informative signal peptidase activity. Reason: The active-site analysis of Sec11 identified Ser-44 together with His-83 and two Asp residues as important for signal peptidase activity. Because the gene already has direct signal peptidase activity evidence, this broad endopeptidase row should be refined to that specific activity. Proposed replacements: signal peptidase activity Supporting Evidence: PMID:10206957 Instead, a serine, histidine, and two aspartic acids are important for signal peptidase activity by the Sec11p subunit of the yeast signal peptidase complex.
GO:0005515 protein binding	IPI PMID:10206957 The catalytic mechanism of endoplasmic reticulum signal pept...	REMOVE	Summary: Sec11 physically associates with Spc3 in the signal peptidase complex, but the generic protein binding term is not an informative molecular function. Reason: The reported Sec11-Spc3 association is best captured by the accepted signal peptidase complex cellular-component rows. GO:0005515 does not describe the catalytic signal peptidase activity and should not be used as a stand-alone function for this complex subunit. Supporting Evidence: PMID:9148931 The signal peptidase complex in yeast consists of four subunits.
GO:0005515 protein binding	IPI PMID:16093310 Large-scale identification of yeast integral membrane protei...	REMOVE	Summary: The split-ubiquitin interaction screen produced a generic Sec11-Spc1 binding assertion, but complex membership is the biologically informative interpretation. Reason: The interaction is consistent with Spc1 being a noncatalytic signal peptidase complex subunit, yet protein binding is too generic to keep as a molecular-function annotation for SEC11. Supporting Evidence: PMID:8910564 These results indicate that although both Spc1p and Spc2p are noncatalytic, they are functionally distinct.
GO:0005515 protein binding	IPI PMID:37968396 The social and structural architecture of the yeast protein ...	REMOVE	Summary: The AP-MS interactome row is another generic Sec11-Spc3 binding assertion; it does not add a specific molecular activity. Reason: Independent high-throughput interaction evidence can reinforce the placement of Sec11 in the ER signal peptidase complex, but GO:0005515 is not informative for the catalytic SPC subunit and is redundant with accepted signal peptidase complex rows. Supporting Evidence: PMID:37968396 Here we develop a sensitive high-throughput method using highly reproducible affinity enrichment coupled to mass spectrometry combined with a quantitative two-dimensional analysis strategy to comprehensively map the interactome of Saccharomyces cerevisiae.
GO:0005515 protein binding	IPI PMID:9148931 The yeast SPC22/23 homolog Spc3p is essential for signal pep...	REMOVE	Summary: Spc1 is a noncatalytic signal peptidase complex subunit, so generic protein binding should be removed rather than retained as a function. Reason: Spc1 contributes to the ER signal peptidase complex, and that complex-membership statement is more specific and already accepted. The generic protein binding row does not express SEC11's signal peptidase activity. Supporting Evidence: PMID:9148931 In eucaryotic cells signal sequences of secretory and membrane proteins are cleaved by the signal peptidase complex during their transport into the lumen of the endoplasmic reticulum.
GO:0005515 protein binding	IPI PMID:9148931 The yeast SPC22/23 homolog Spc3p is essential for signal pep...	REMOVE	Summary: Spc3 is the second essential yeast SPC subunit, but Sec11-Spc3 binding is complex membership rather than a useful stand-alone activity. Reason: The Sec11-Spc3 association is part of the signal peptidase complex architecture. Keeping GO:0005515 would obscure the specific catalytic activity that Sec11 carries out in that complex. Supporting Evidence: PMID:42586426 Both Sec11 and Sec11ΔCTS were coimmunoprecipitated with Spc3 (Fig. 2C, left panel), indicating that Sec11 associates with Spc3 regardless of the presence of the CTS.
GO:0005783 endoplasmic reticulum	IDA PMID:11058593 Signal peptidase and oligosaccharyltransferase interact in a...	MODIFY	Summary: SEC11 functions in the ER, but as an integral component of the ER membrane signal peptidase complex. Reason: Signal peptide cleavage by Sec11 occurs at the endoplasmic reticulum during precursor maturation, and direct solubilization/localization studies support the more precise ER membrane term. Proposed replacements: endoplasmic reticulum membrane Supporting Evidence: PMID:2644273 The membrane association of yeast signal peptidase is resistant to carbonate extraction, indicating that it is an integral membrane protein.
GO:0005787 signal peptidase complex	IBA GO_REF:0000033	ACCEPT	Summary: PTN000086750 places ER signal peptidase complex membership in the eukaryotic SEC11 clade, and S. cerevisiae SEC11 is a directly characterized member of that clade. Reason: PAINT's Eukaryota node is consistent with biochemical evidence that yeast Sec11 is the 18-kDa catalytic chain in the four-subunit ER signal peptidase complex; SEC11 itself is an experimental seed for this IBA, which marks direct descendant support rather than circularity. Supporting Evidence: PMID:1846444 Partially purified yeast microsomal signal peptidase appears to be a complex of four polypeptides of 13, 18, 20, and 25 kDa. The 18-kDa chain is the product of the Sec11 gene, which is necessary for signal peptidase activity.
GO:0005787 signal peptidase complex	IDA PMID:1846444 Yeast signal peptidase contains a glycoprotein and the Sec11...	ACCEPT	Summary: Purification of yeast microsomal signal peptidase identified Sec11 as the 18-kDa subunit of a four-polypeptide complex. Reason: The paper directly characterized the yeast enzyme as a membrane complex and assigned the 18-kDa subunit to Sec11, matching GO:0005787. Supporting Evidence: PMID:1846444 Partially purified yeast microsomal signal peptidase appears to be a complex of four polypeptides of 13, 18, 20, and 25 kDa. The 18-kDa chain is the product of the Sec11 gene, which is necessary for signal peptidase activity.
GO:0005787 signal peptidase complex	IDA PMID:8910564 Structurally related Spc1p and Spc2p of yeast signal peptida...	ACCEPT	Summary: Genetic analysis of Spc1 and Spc2 was performed in the established context of the Sec11-containing yeast signal peptidase complex. Reason: Spc1 and Spc2 are noncatalytic partners in yeast SPC, and the SEC11 genetic interactions reported in this study reinforce Sec11's assignment to that complex. Supporting Evidence: PMID:8910564 These results indicate that although both Spc1p and Spc2p are noncatalytic, they are functionally distinct. PMID:1846444 Partially purified yeast microsomal signal peptidase appears to be a complex of four polypeptides of 13, 18, 20, and 25 kDa. The 18-kDa chain is the product of the Sec11 gene, which is necessary for signal peptidase activity.
GO:0005787 signal peptidase complex	IEA GO_REF:0000117	ACCEPT	Summary: The ARBA complex prediction agrees with direct yeast biochemical and phylogenetic evidence for SEC11. Reason: SEC11 is experimentally established as a component of the yeast signal peptidase complex, so the electronic ARBA row asserts the correct cellular component. Supporting Evidence: PMID:1846444 Partially purified yeast microsomal signal peptidase appears to be a complex of four polypeptides of 13, 18, 20, and 25 kDa.
GO:0005787 signal peptidase complex	IPI PMID:9148931 The yeast SPC22/23 homolog Spc3p is essential for signal pep...	ACCEPT	Summary: Sec11 and Spc3 are essential subunits of the four-subunit yeast signal peptidase complex. Reason: The Spc3 purification and depletion study places Sec11 in the yeast SPC and shows that Spc3 is also required for in-vitro and in-vivo signal peptidase activity. Supporting Evidence: PMID:9148931 We have purified and analyzed the fourth subunit of yeast signal peptidase, Spc3p. The protein is essential for viability of yeast cells.
GO:0005789 endoplasmic reticulum membrane	EXP PMID:10206957 The catalytic mechanism of endoplasmic reticulum signal pept...	ACCEPT	Summary: Sec11 is the catalytic subunit of the ER membrane signal peptidase complex. Reason: Mutational analysis of Sec11 catalytic residues assayed the ER signal peptidase complex, and independent biochemical extraction showed that yeast signal peptidase is membrane integral. Supporting Evidence: PMID:2644273 The membrane association of yeast signal peptidase is resistant to carbonate extraction, indicating that it is an integral membrane protein.
GO:0005789 endoplasmic reticulum membrane	EXP PMID:2644273 Solubilization and characterization of yeast signal peptidas...	ACCEPT	Summary: Detergent solubilization and carbonate extraction established yeast signal peptidase as an integral membrane enzyme. Reason: Sec11 is the catalytic subunit of that yeast signal peptidase complex, so ER membrane is the correct functional cellular component. Supporting Evidence: PMID:2644273 The membrane association of yeast signal peptidase is resistant to carbonate extraction, indicating that it is an integral membrane protein.
GO:0005789 endoplasmic reticulum membrane	IEA GO_REF:0000044	ACCEPT	Summary: The UniProt subcellular-location mapping to ER membrane is correct for the Sec11 catalytic subunit. Reason: Multiple biochemical studies put Sec11 in the ER-associated, integral membrane signal peptidase complex. Supporting Evidence: PMID:2644273 The enzyme can be solubilized in nonionic detergent (0.5% Nikkol) without added salt, but salt increased the efficiency of solubilization.
GO:0005789 endoplasmic reticulum membrane	NAS PMID:9148931 The yeast SPC22/23 homolog Spc3p is essential for signal pep...	ACCEPT	Summary: Yeast SPC cleaves signal sequences during protein transport into the ER lumen, placing Sec11 at the ER membrane. Reason: Sec11 belongs to the yeast SPC; the complex is an ER membrane enzyme acting on precursors as they enter the ER lumen. Supporting Evidence: PMID:9148931 In eucaryotic cells signal sequences of secretory and membrane proteins are cleaved by the signal peptidase complex during their transport into the lumen of the endoplasmic reticulum.
GO:0008233 peptidase activity	IBA GO_REF:0000033	MODIFY	Summary: The root PAINT peptidase assertion is true for SEC11 but less specific than the experimentally supported signal peptidase activity. Reason: PTN000086749 captures a conserved peptidase function across the PTHR10806 root, spanning bacterial, archaeal, and eukaryotic type-I signal peptidases. For yeast SEC11, the specific inherited and experimentally verified activity is cleavage of signal peptides, so this row should be narrowed to GO:0009003. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000086749 SUPPORTS TRANSFER The root node supports a broad peptidase assertion across PTHR10806; S. cerevisiae SEC11 should carry the more specific signal peptidase activity term. Proposed replacements: signal peptidase activity Supporting Evidence: PMID:10206957 Instead, a serine, histidine, and two aspartic acids are important for signal peptidase activity by the Sec11p subunit of the yeast signal peptidase complex.
GO:0008233 peptidase activity	IEA GO_REF:0000002	MODIFY	Summary: The S26B family mapping is a correct but broad peptidase assertion. Reason: Sec11 is a peptidase S26B-family enzyme whose characterized molecular activity is signal peptidase activity; the broader InterPro2GO row should be refined rather than retained alongside GO:0009003. Proposed replacements: signal peptidase activity Supporting Evidence: PMID:10206957 Instead, a serine, histidine, and two aspartic acids are important for signal peptidase activity by the Sec11p subunit of the yeast signal peptidase complex.
GO:0008233 peptidase activity	IMP PMID:10206957 The catalytic mechanism of endoplasmic reticulum signal pept...	MODIFY	Summary: Sec11 catalytic-site mutants affect signal peptidase activity, not an unspecified protease activity. Reason: The mutagenesis paper identifies residues required for the signal peptidase reaction carried out by the Sec11 subunit; GO:0009003 is the specific term supported by the data. Proposed replacements: signal peptidase activity Supporting Evidence: PMID:10206957 Instead, a serine, histidine, and two aspartic acids are important for signal peptidase activity by the Sec11p subunit of the yeast signal peptidase complex.
GO:0009003 signal peptidase activity	EXP PMID:10206957 The catalytic mechanism of endoplasmic reticulum signal pept...	ACCEPT	Summary: Sec11 is the catalytic signal peptidase subunit and its active-site residues are required for SPC proteolysis. Reason: Directed mutagenesis of Ser-44, His-83, Asp-103, and Asp-109 established that Sec11 itself supplies residues required for the ER signal peptidase reaction. Supporting Evidence: PMID:10206957 Instead, a serine, histidine, and two aspartic acids are important for signal peptidase activity by the Sec11p subunit of the yeast signal peptidase complex.
GO:0009003 signal peptidase activity	IEA GO_REF:0000120	ACCEPT	Summary: The combined automated EC-based assertion matches the experimentally characterized activity of yeast Sec11. Reason: SEC11 directly enables EC 3.4.21.89-type signal peptidase activity in the ER signal peptidase complex. Supporting Evidence: PMID:10206957 Instead, a serine, histidine, and two aspartic acids are important for signal peptidase activity by the Sec11p subunit of the yeast signal peptidase complex.
GO:0016020 membrane	IEA GO_REF:0000002	MODIFY	Summary: Sec11 is membrane associated, but the specific functional site is the ER membrane. Reason: The generic InterPro2GO membrane row is correct for a type-I signal peptidase, but yeast biochemical evidence places the Sec11-containing complex in the endoplasmic reticulum membrane. Proposed replacements: endoplasmic reticulum membrane Supporting Evidence: PMID:2644273 The membrane association of yeast signal peptidase is resistant to carbonate extraction, indicating that it is an integral membrane protein.
GO:0045047 protein targeting to ER	IMP PMID:3283143 SEC11 is required for signal peptide processing and yeast ce...	MODIFY	Summary: The classic sec11 phenotype is failed signal-peptide removal after ER entry, so the direct SEC11 process is protein maturation. Reason: The invertase and acid phosphatase precursors in sec11 mutant cells were core glycosylated, indicating ER entry had occurred; what remained defective was signal-peptide cleavage. GO:0016485 is the live protein-processing term for this proteolytic SPC reaction. Proposed replacements: protein processing Supporting Evidence: PMID:3283143 At 37 degrees C, the restrictive growth temperature, sec11 cells accumulate core-glycosylated forms of invertase and acid phosphatase, each retaining an intact signal peptide.
GO:0051604 protein maturation	IBA GO_REF:0000033	MODIFY	Summary: PTN000086750 correctly propagates the eukaryotic SPC maturation role to SEC11 but can be refined to protein processing. Reason: Cleaving N-terminal signal peptides is a direct protein-maturation step for ER-translocated precursors. The eukaryotic PAINT node is consistent with SEC11's direct experimental evidence; GO:0016485 protein processing is the live process term for this proteolytic SPC reaction. 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 PMID:10206957 Instead, a serine, histidine, and two aspartic acids are important for signal peptidase activity by the Sec11p subunit of the yeast signal peptidase complex.
GO:0051604 protein maturation	IDA PMID:10206957 The catalytic mechanism of endoplasmic reticulum signal pept...	MODIFY	Summary: Sec11 catalytic residues are required for the signal-peptide cleavage step of precursor maturation. Reason: The catalytic-site analysis directly ties Sec11 to signal peptide removal by the ER signal peptidase complex, which is an N-terminal protein maturation event; GO:0016485 protein processing is the live process term for this proteolytic cleavage. Proposed replacements: protein processing Supporting Evidence: PMID:10206957 Instead, a serine, histidine, and two aspartic acids are important for signal peptidase activity by the Sec11p subunit of the yeast signal peptidase complex.
GO:0051604 protein maturation	IEA GO_REF:0000002	MODIFY	Summary: The S26B-family InterPro process mapping fits SEC11 because signal peptide cleavage matures ER-translocated precursors. Reason: The existing direct experimental rows show that yeast Sec11 performs signal peptidase cleavage; GO:0016485 protein processing is the live process term for this proteolytic SPC reaction. Proposed replacements: protein processing Supporting Evidence: PMID:3283143 sec11 mutant cells are uniquely defective in signal peptide processing of at least two different secretory proteins.
GO:0051604 protein maturation	IMP PMID:10206957 The catalytic mechanism of endoplasmic reticulum signal pept...	MODIFY	Summary: Sec11 mutants impair signal peptide cleavage, the core maturation step carried out by SPC. Reason: Perturbing Sec11 catalytic residues compromises the same signal peptidase activity established biochemically for the ER SPC, and GO:0016485 protein processing is the live process term for this cleavage. Proposed replacements: protein processing Supporting Evidence: PMID:10206957 Instead, a serine, histidine, and two aspartic acids are important for signal peptidase activity by the Sec11p subunit of the yeast signal peptidase complex.
GO:0051604 protein maturation	IMP PMID:3283143 SEC11 is required for signal peptide processing and yeast ce...	MODIFY	Summary: The sec11 mutant accumulates ER-entered glycoprotein precursors retaining intact signal peptides. Reason: The temperature-sensitive sec11 phenotype directly demonstrates a block in signal-peptide removal from secretory precursors, which is the protein processing reaction catalyzed by SPC. Proposed replacements: protein processing Supporting Evidence: PMID:3283143 At 37 degrees C, the restrictive growth temperature, sec11 cells accumulate core-glycosylated forms of invertase and acid phosphatase, each retaining an intact signal peptide.

Gene Description

Existing Annotations Review

Core Functions

Cleaves N-terminal signal peptides from nascent secretory and membrane-protein precursors as the catalytic SEC11 subunit of the ER signal peptidase complex.

References

Deep Research

SGD

SGD gene description for SEC11 (yeast)

📚 Additional Documentation

Notes

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