| IED ID | IndEnz0002008827 |
| Enzyme Type ID | protease008827 |
| Protein Name |
Signal peptide peptidase-like 2B SPP-like 2B SPPL2b EC 3.4.23.- |
| Gene Name | Sppl2b |
| Organism | Rattus norvegicus (Rat) |
| 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 Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MAAARLAASLLLLAAQVACEFGVLRVVPQSGGTRGRDYCILYNPQWAHLPHDLNKVSLLKLRDLSTTQLCSHLDVPVEDFTNQIALVARGNCTFYEKVRLAQGSGAHGLLIVSKERLVPPRGNKTQYEEISIPVALLSHRDLQDIFRRFGHEVMVALYAPSEPVMDYNMVIIFIMAVGTVALGGYWAGSHDVKKYMKHKRDDVPEKQEDEAVDVTPVMICVFVVMCCFMLVLLYYFYDRLVYVIIGIFCLASSTGLYSCLAPCVRKLPFCTCRVPDNNLPYFHKRPQARMLLLALFCVTVSVVWGVFRNEDQWAWVLQDTLGIAFCLYMLRTIRLPTFKACTLLLLVLFVYDIFFVFITPYLTKSGNSIMVEVATGPSNSSTHEKLPMVLKVPRLNTSPLSLCDRPFSLLGFGDILVPGLLVAYCHRFDIQVQSSRIYFVACTIAYGLGLLVTFVALVLMRHGQPALLYLVPCTLLTSCTVALWRREMGAFWTGSGFADAPQTPWAAPQGPVPPKDVDASLSEQPRGEELAQSPLATEEAGATDPAKDPDSPVAGPLSPSNGDQVQPIPVVTPGTSA |
| Enzyme Length | 577 |
| Uniprot Accession Number | Q5PQL3 |
| Absorption | |
| Active Site | ACT_SITE 352; /evidence=ECO:0000250|UniProtKB:P49810; ACT_SITE 414; /evidence=ECO:0000250|UniProtKB:P49810 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.23.- |
| Enzyme Function | FUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane. Functions in ITM2B and TNF processing. Catalyzes the intramembrane cleavage of the anchored fragment of shed TNF-alpha (TNF), which promotes the release of the intracellular domain (ICD) for signaling to the nucleus. May play a role in the regulation of innate and adaptive immunity. {ECO:0000250|UniProtKB:Q8TCT7}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (1); Domain (1); Glycosylation (1); Motif (1); Region (1); Signal peptide (1); Topological domain (10); Transmembrane (9) |
| Keywords | Cell membrane;Endosome;Glycoprotein;Golgi apparatus;Hydrolase;Lysosome;Membrane;Protease;Reference proteome;Signal;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q3TD49}; Multi-pass membrane protein {ECO:0000305}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8TCT7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TCT7}. Lysosome membrane {ECO:0000250|UniProtKB:Q8TCT7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TCT7}. Endosome membrane {ECO:0000250|UniProtKB:Q8TCT7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TCT7}. Membrane {ECO:0000250|UniProtKB:Q8TCT7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TCT7}; Lumenal side {ECO:0000250|UniProtKB:Q8TCT7}. Note=targeted through the entire secretory pathway to endosomes/lysosomes. {ECO:0000250|UniProtKB:Q8TCT7}. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000250|UniProtKB:Q8TCT7}. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000250|UniProtKB:Q8TCT7 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 465..467; /note=PAL |
| Gene Encoded By | |
| Mass | 63,737 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |