Venom Protein Card


Accession: Pre00072    Venom serine protease Bi-VSP   [Bombus ignitus]

Basic info
Organism Bombus ignitus
Taxonomy Insecta > Hymenoptera > Apidae > Bombus > Bombus ignitus
Protein Description Venom serine protease Bi-VSP
Mass Weight 39460.81 Da
Isoelectric Point 6.26
Expression Highly expressed in venom gland
Annotation
Function Multifunctional venom serine protease. In insects, it acts as an arthropod prophenoloxidase-activating factor, thereby triggering the phenoloxidase cascade. When injected into larvae, it induces a lethal melanization response in target insects by modulating the innate immune response. In mammals, it converts fibrinogen into fibrin, activates prothrombin, and also degrades fibrin. In mammal, it may act in a cooperative manner with the serine protease inhibitor Bi-KTI (AC G3LH89) to promote the spread of bee venom under anti-bleeding conditions.
Pfam
PF12032 CLIP
Features
Feature key Position Length
Signal Peptide 1..26 26
Propeptide 27..113 87
Chain 114..360 247
Cross-Reference
NCBI Nucleotide FJ159442.1
NCBI Protein ACI01044.1
UniProt B5U2W0
Sequence
ATGACGGGCTCCAAGATGCTGTTCGCATGTTTGGCGTTAATTGCTTTCCTGCATCCATTAGTTCACGTGGCGTCAGCTCAAGAATGTACCACACCGAACAATAAAGCAGGCAAGTGTCTCGGCATCAGAGTATGTAAACCGCTGCTGGAAATGCTGCAGACTCAGGGCCATGCAGCTGCCGATTTCCTGAGGCAATCAGTGTGTAAATACGAGAATAATAATCCGATCGTTTGTTGTCCGAACGAAGAAAGCAGGGAGGACAGAGGAATTTTGGTAGGAAACGAGTATGAGCCTTTGCGTCCACCACACTGTGGTTTTAGCAACGTCTCTCACACCAGGGTGGTCGGTGGTAAGCCAGCTGTACTTGGTGCTTGGCCATGGATTGCTGCATTAGGTTTTCGTTATCCCCGAAACCCAGCTCTTGAACCACTATGGAAGTGCGGAGGTTCCCTGATATCGTCTAGGCATGTTTTAACTGCAGCACATTGTGCAGAAATCAATGAATTGTACGTGGTTCGTATCGGTGACTTAAATCTAGTACGAAATGACGACGGAGCACATCCTGTTCAAATAGAAATCGAATCTAAAATAATACATCCTGATTATATTTCCGGAGTAACCAAACATGATATCGCCATTCTTAAATTGGTGGAGGAGGTGCCATTTTCGGAGTACGTATATCCCATTTGTCTTCCCGTAGAGGATAACCTTCGAAATAACAATTTCGAGCGCTATTACCCCTTCGTTGCTGGATGGGGATCACTAGCACATCATGGACCAGGTAGTGACGATTTAATGGAAGTACAAGTGCCAGTGATTAGCAACACCGAATGCAAGAACTCTTATGCCAGATTTGCTGCTGCACATGTTACCGATACTGTATTATGCGCCGGATACACTCAAGGCGGAAAGGATGCTTGTCAAGGTGACAGCGGAGGACCACTGATGCTACCAAAGAAATTCACCTTCTATCAAATAGGTGTTGTGTCTTATGGTCATAAGTGCGCCGCAGCTGGATATCCCGGCGTTTACACTAGGGTCACGTCGTACCTCGACGACTTTATTCTCCCAGCGATGCAATAA
MTGSKMLFACLALIAFLHPLVHVASAQECTTPNNKAGKCLGIRVCKPLLEMLQTQGHAAADFLRQSVCKYENNNPIVCCPNEESREDRGILVGNEYEPLRPPHCGFSNVSHTRVVGGKPAVLGAWPWIAALGFRYPRNPALEPLWKCGGSLISSRHVLTAAHCAEINELYVVRIGDLNLVRNDDGAHPVQIEIESKIIHPDYISGVTKHDIAILKLVEEVPFSEYVYPICLPVEDNLRNNNFERYYPFVAGWGSLAHHGPGSDDLMEVQVPVISNTECKNSYARFAAAHVTDTVLCAGYTQGGKDACQGDSGGPLMLPKKFTFYQIGVVSYGHKCAAAGYPGVYTRVTSYLDDFILPAMQ

3D Structure
Publication
1. Choo Y.M., Lee K.S., Yoon H.J., Kim B.Y., Sohn M.R., Roh J.Y., Je Y.H., Kim N.J., Kim I., Woo S.D., Sohn H.D., Jin B.R.;
"Dual function of a bee venom serine protease: prophenoloxidase-activating factor in arthropods and fibrin(ogen)olytic enzyme in mammals.";
PLoS ONE 5:E10393-E10393(2010).
2. Choo Y.M., Lee K.S., Yoon H.J., Qiu Y., Wan H., Sohn M.R., Sohn H.D., Jin B.R.;
"Antifibrinolytic role of a bee venom serine protease inhibitor that acts as a plasmin inhibitor.";
PLoS ONE 7:E32269-E32269(2012).