| IED ID | IndEnz0002001953 |
| Enzyme Type ID | protease001953 |
| Protein Name |
Signal peptidase complex catalytic subunit SEC11C EC 3.4.21.89 Microsomal signal peptidase 21 kDa subunit SPase 21 kDa subunit SEC11 homolog C SEC11-like protein 3 SPC21 |
| Gene Name | SEC11C SEC11L3 SPC21 |
| Organism | Canis lupus familiaris (Dog) (Canis familiaris) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Carnivora Caniformia Canidae (dog coyote wolf fox) Canis Canis lupus (Gray wolf) Canis lupus familiaris (Dog) (Canis familiaris) |
| Enzyme Sequence | MVRAGAVGTHLPASGLDIFGDLRKMNKRQLYYQVLNFAMIVSSALMIWKGLIVLTGSESPIVVVLSGSMEPAFHRGDLLFLTNFREDPIRAGEIVVFKVEGRDIPIVHRVIKVHEKDNGDIKFLTKGDNNEVDDRGLYKEGQNWLEKKDVVGRARGFLPYVGMVTIIMNDYPKFKYALLAVMGAYVLLKRES |
| Enzyme Length | 192 |
| Uniprot Accession Number | P13679 |
| Absorption | |
| Active Site | ACT_SITE 68; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q9BY50; ACT_SITE 108; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q9BY50; ACT_SITE 134; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q9BY50 |
| 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:14559916, ECO:0000269|PubMed:3511473}; |
| 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:3511473, PubMed:8444896, PubMed:14559916). 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:14559916, ECO:0000269|PubMed:3511473, ECO:0000269|PubMed:8444896}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Initiator methionine (1); Region (1); Topological domain (2); Transmembrane (1) |
| Keywords | Direct protein sequencing;Endoplasmic reticulum;Hydrolase;Membrane;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:3511473, ECO:0000269|PubMed:8444896}; Single-pass type II membrane protein {ECO:0000269|PubMed:8444896}. |
| Modified Residue | |
| Post Translational Modification | PTM: May undergo processing at the N-terminus. {ECO:0000250|UniProtKB:Q9BY50}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 21,600 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |