C7GLT4 · SEC11_YEAS2
- ProteinSignal peptidase complex catalytic subunit SEC11
- GeneSEC11
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids167 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
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 (By similarity).
Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids (By similarity).
Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids (By similarity).
Catalytic activity
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 44 | Charge relay system | ||||
Sequence: S | ||||||
Active site | 83 | Charge relay system | ||||
Sequence: H | ||||||
Active site | 109 | Charge relay system | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | signal peptidase complex | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | signal peptide processing |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSignal peptidase complex catalytic subunit SEC11
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionC7GLT4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-9 | Cytoplasmic | ||||
Sequence: MNLRFELQK | ||||||
Transmembrane | 10-30 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: LLNVCFLFASAYMFWQGLAIA | ||||||
Topological domain | 31-167 | Lumenal | ||||
Sequence: TNSASPIVVVLSGSMEPAFQRGDILFLWNRNTFNQVGDVVVYEVEGKQIPIVHRVLRQHNNHADKQFLLTKGDNNAGNDISLYANKKIYLNKSKEIVGTVKGYFPQLGYITIWISENKYAKFALLGMLGLSALLGGE |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000412356 | 1-167 | Signal peptidase complex catalytic subunit SEC11 | |||
Sequence: MNLRFELQKLLNVCFLFASAYMFWQGLAIATNSASPIVVVLSGSMEPAFQRGDILFLWNRNTFNQVGDVVVYEVEGKQIPIVHRVLRQHNNHADKQFLLTKGDNNAGNDISLYANKKIYLNKSKEIVGTVKGYFPQLGYITIWISENKYAKFALLGMLGLSALLGGE | ||||||
Glycosylation | 121 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Interaction
Subunit
Component of the signal peptidase complex (SPC) composed of a catalytic subunit SEC11 and three accessory subunits SPC1, SPC2 and SPC3 (By similarity).
The complex induces a local thinning of the ER membrane which is used to measure the length of the signal peptide (SP) h-region of protein substrates. This ensures the selectivity of the complex towards h-regions shorter than 18-20 amino acids (By similarity).
SPC associates with the translocon complex (By similarity).
The complex induces a local thinning of the ER membrane which is used to measure the length of the signal peptide (SP) h-region of protein substrates. This ensures the selectivity of the complex towards h-regions shorter than 18-20 amino acids (By similarity).
SPC associates with the translocon complex (By similarity).
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 153-164 | C-terminal short (CTS) helix | ||||
Sequence: ALLGMLGLSALL |
Domain
The C-terminal short (CTS) helix is essential for catalytic activity. It may be accommodated as a transmembrane helix in the thinned membrane environment of the complex, similarly to the signal peptide in the complex substrates.
Sequence similarities
Belongs to the peptidase S26B family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length167
- Mass (Da)18,762
- Last updated2009-10-13 v1
- ChecksumFC877232D6888DF3