| Identification |
|---|
| HMDB Protein ID
| HMDBP13508 |
| Secondary Accession Numbers
| None |
| Name
| Secapin |
| Synonyms
|
- AcSecapin-1
|
| Gene Name
| Not Available |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Not Available |
| Specific Function
| Serine protease inhibitor which exhibits antifibrinolytic, antielastolytic and antimicrobial activities (PubMed:27208884). Displays antimicrobial activity against bacteria and fungi (PubMed:27208884). Likely functions in the innate immune response to microbial infection and possibly in the venom, as an antifibrinolytic agent (PubMed:27208884). The recombinant form inhibits trypsin (IC(50)=80.02 nM, Ki=127.25 nM), chymotrypsin (IC(50)=393.78 nM, Ki=432.59 nM), the microbial serine proteases subtilisin A (IC(50)=379.20 nM, Ki=492.77 nM) and proteinase K (IC(50)=189.43 nM, Ki=271.76 nM), plasmin (IC(50)=457.98 nM, Ki=502.91 nM), human elastase (IC(50)=347.81 nM, Ki=469.90 nM) and porcine elastase (IC(50)=94.70 nM, Ki=125.62 nM) (PubMed:27208884). Does not inhibit thrombin (PubMed:27208884). Binds to human plasmin and inhibits the plasmin-mediated degradation of fibrin to fibrin degradation products (PubMed:27208884). Also binds to bacterial and fungal surfaces and exhibits antimicrobial activity against the Gram-positive bacteria B.thuringiensis (MIC=4.21 uM) and P.larvae (MIC=11.13 uM), the Gram-negative bacterium E.coli (MIC=6.50 uM), and the fungus B.bassiana (IC(50)=2.57 uM) (PubMed:27208884). The synthetic peptide also exhibits antimicrobial activity against the Gram-positive bacterium P.larvae (MIC=41.12 uM), the Gram-negative bacterium P.aeruginosa (MIC=65.75 uM), and the fungus B.bassiana (IC(50)=44.27 uM) (Ref.2). In vitro it does not induce an inflammatory response and has no cytotoxic activity against mouse embryo cells (Ref.2). |
| Pathways
|
Not Available
|
| Reactions
| Not Available |
| GO Classification
|
| Cellular Component |
| extracellular region |
|
| Cellular Location
|
Not Available
|
| Gene Properties |
|---|
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| Not Available |
| Gene Sequence
|
Not Available
|
| Protein Properties |
|---|
| Number of Residues
| Not Available |
| Molecular Weight
| 13569.57 |
| Theoretical pI
| Not Available |
| Pfam Domain Function
|
|
| Signals
|
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| A0A0K1YW63 |
| UniProtKB/Swiss-Prot Entry Name
| SECP_APICE |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Lee KS, Kim BY, Yoon HJ, Choi YS, Jin BR: Secapin, a bee venom peptide, exhibits anti-fibrinolytic, anti-elastolytic, and anti-microbial activities. Dev Comp Immunol. 2016 Oct;63:27-35. doi: 10.1016/j.dci.2016.05.011. Epub 2016 May 18. [PubMed:27208884 ]
|
