| IED ID | IndEnz0002009372 |
| Enzyme Type ID | protease009372 |
| Protein Name |
Signal peptidase complex catalytic subunit SEC11 EC 3.4.21.89 Secretory protein 11 Signal peptidase I |
| Gene Name | SEC11 YIR022W |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MNLRFELQKLLNVCFLFASAYMFWQGLAIATNSASPIVVVLSGSMEPAFQRGDILFLWNRNTFNQVGDVVVYEVEGKQIPIVHRVLRQHNNHADKQFLLTKGDNNAGNDISLYANKKIYLNKSKEIVGTVKGYFPQLGYITIWISENKYAKFALLGMLGLSALLGGE |
| Enzyme Length | 167 |
| Uniprot Accession Number | P15367 |
| Absorption | |
| Active Site | ACT_SITE 44; /note=Charge relay system; /evidence=ECO:0000305|PubMed:10206957; ACT_SITE 83; /note=Charge relay system; /evidence=ECO:0000305|PubMed:10206957; ACT_SITE 109; /note=Charge relay system; /evidence=ECO:0000305|PubMed:10206957 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.; EC=3.4.21.89; Evidence={ECO:0000269|PubMed:10206957}; |
| DNA Binding | |
| EC Number | 3.4.21.89 |
| Enzyme 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 (PubMed:2644273, PubMed:7615509, PubMed:10206957, PubMed:11058593). Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids (By similarity). {ECO:0000250|UniProtKB:P67812, ECO:0000269|PubMed:10206957, ECO:0000269|PubMed:11058593, ECO:0000269|PubMed:2644273, ECO:0000269|PubMed:7615509}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Glycosylation (1); Mutagenesis (9); Region (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) |
| Keywords | Endoplasmic reticulum;Glycoprotein;Hydrolase;Membrane;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix |
| Interact With | P46965; Q12133 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10206957, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:2644273}; Single-pass type II membrane protein {ECO:0000269|PubMed:10206957, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:2644273}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:10206957}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10921929; 11283351; 12559573; 14559916; 15055575; 15300682; 16093310; 16510493; 16554755; 19536198; 2022624; 21918511; 22533807; 23396477; 25079602; 6996832; 8910564; |
| Motif | |
| Gene Encoded By | |
| Mass | 18,762 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.89; |