Target type: biologicalprocess
The proteolytic removal of a signal peptide from a protein during or after transport to a specific location in the cell. [GOC:mah, ISBN:0815316194]
Signal peptide processing is a crucial step in the biosynthesis and targeting of proteins destined for secretion or localization to specific organelles. It involves the removal of the N-terminal signal peptide, a short amino acid sequence that directs the nascent polypeptide chain to the secretory pathway.
The process begins with the translation of mRNA on ribosomes in the cytoplasm. As the signal peptide emerges from the ribosome, it is recognized by a signal recognition particle (SRP), a ribonucleoprotein complex that binds to both the signal peptide and the ribosome. The SRP-ribosome complex then interacts with the SRP receptor on the endoplasmic reticulum (ER) membrane. This interaction facilitates the docking of the ribosome to the ER membrane, where protein translocation occurs.
Once the ribosome is anchored to the ER membrane, the nascent polypeptide chain enters the ER lumen through a protein translocator channel. The signal peptide leads the way, initiating the transfer of the polypeptide across the membrane.
As the polypeptide chain enters the ER lumen, a protease called signal peptidase cleaves off the signal peptide. This cleavage event is typically highly specific and occurs within the ER lumen. The signal peptide is then degraded, while the mature protein folds and undergoes further modifications within the ER.
The removal of the signal peptide is essential for several reasons. First, it allows the protein to fold properly in the ER lumen. Second, it removes the targeting signal, ensuring that the protein is not incorrectly transported to other cellular compartments. Finally, it prevents the protein from being prematurely secreted from the cell.
Signal peptide processing is a highly conserved process that plays a fundamental role in cellular function. It ensures that proteins destined for secretion or localization to specific organelles are correctly synthesized, folded, and targeted to their final destinations.'
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| Protein | Definition | Taxonomy |
|---|---|---|
| Signal peptidase I | A signal peptidase I that is encoded in the genome of Escherichia coli K-12. [PRO:DNx, UniProtKB:P00803] | Escherichia coli K-12 |
| Signal peptidase I | A signal peptidase I that is encoded in the genome of Escherichia coli K-12. [PRO:DNx, UniProtKB:P00803] | Escherichia coli K-12 |
| Furin | A furin that is encoded in the genome of human. [PRO:CNA, UniProtKB:P09958] | Homo sapiens (human) |
| Furin | A furin that is encoded in the genome of human. [PRO:CNA, UniProtKB:P09958] | Homo sapiens (human) |
| Compound | Definition | Classes | Roles |
|---|---|---|---|
| diminazene | diminazene : A triazene derivative that is triazene in which each of the terminal nitrogens is substituted by a 4-carbamimidoylphenyl group. Diminazene: An effective trypanocidal agent. | carboxamidine; triazene derivative | antiparasitic agent; trypanocidal drug |
| camostat | camostat : A benzoate ester resulting from the formal condensation of the carboxy group of 4-guanidinobenzoic acid with the hydroxy group of 2-(dimethylamino)-2-oxoethyl (4-hydroxyphenyl)acetate. It is a potent inhibitor of the human transmembrane protease serine 2 (TMPRSS2) and its mesylate salt is currently under investigation for its effectiveness in COVID-19 patients. | benzoate ester; carboxylic ester; diester; guanidines; tertiary carboxamide | anti-inflammatory agent; anticoronaviral agent; antifibrinolytic drug; antihypertensive agent; antineoplastic agent; antiviral agent; serine protease inhibitor |
| n,n-(4-xylylidene)bisaminoguanidine | N,N-(4-xylylidene)bisaminoguanidine: RN in Chemline for di-HCl: 7044-24-8; RN for unspecified HCl: 62580-72-7 N,N'-(p-xylylidene)bis(aminoguanidine) : A guanidine derivative comprised of two carbamimidamido (guanidino) groups, each linked via one of their amino nitrogens to the imino nitrogens of 1,4-phenylenedimethanimine. | ||
| 5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine | 5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine: structure in first source halicin : A member of the class of thiadiazoles that is 1,3,4-thiadiazol-2-amine which is substituted by a (5-nitro-1,3-thiazol-2-yl)sulfanediyl group at position 5. It is a c-Jun N-terminal kinase inhibitor (IC50 = 0.7uM) and exhibits antibacterial properties. | 1,3-thiazoles; C-nitro compound; organic sulfide; primary amino compound; thiadiazoles | antibacterial agent; c-Jun N-terminal kinase inhibitor |
| arylomycin a-c16 |