2pn5

Structural highlights

Function

TEPR1_ANOGA Plays an essential role in the innate immune response against bacteria, fungi and protozoa infection (PubMed:15006349). After proteolytic cleavage, the protein C-terminus binds covalently through a thioester bond to the pathogen surface resulting in pathogen clearance either by melanization or lysis (PubMed:15006349, PubMed:19286136). Initiate the recruitment and activation of a cascade of proteases, mostly of CLIP-domain serine proteases, which leads to the proteolytic cleavage of the prophenoloxidase (PPO) into active phenoloxidase (PO), the rate-limiting enzyme in melanin biosynthesis (By similarity). In response to parasite P.berghei-mediated infection, binds to and mediates killing of ookinetes, as they egress from midgut epithelial cells into the basal labyrinth, by both lysis and melanization (PubMed:15006349, PubMed:19286136). During bacterial infection, binds to both Gram-positive and Gram-negative bacteria but only promotes phagocytosis of Gram-negative bacteria (By similarity). Promotes the accumulation of SPCLIP1 onto the surface of P.berghei ookinetes and bacterium E.coli which leads to the melanization of the pathogen (By similarity). Recruits CLIPA2 to bacteria surface (By similarity). In response to bacterial infection, required for periostial hemocyte aggregation, but not for the aggregation of sessile hemocytes in non-periostial regions (By similarity). During the late stage of fungus B.bassiana-mediated infection, required for the initiation of hyphae melanization by binding to the surface of hyphae and recruiting prophenoloxidase PPO to them (By similarity). Plays a role in male fertility by binding to defective sperm cells and promoting their removal during spermatogenesis (PubMed:26394016).[UniProtKB:C9XI63]^{[1] [2] [3]} Binds to and mediates killing of parasite P.bergei ookinetes by lysis and melanization.^[4] Binds covalently through a thioester bond to the pathogen surface resulting in pathogen clearance.[UniProtKB:Q9GYW4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

1. ↑ Blandin S, Shiao SH, Moita LF, Janse CJ, Waters AP, Kafatos FC, Levashina EA. Complement-like protein TEP1 is a determinant of vectorial capacity in the malaria vector Anopheles gambiae. Cell. 2004 Mar 5;116(5):661-70. doi: 10.1016/s0092-8674(04)00173-4. PMID:15006349 doi:http://dx.doi.org/10.1016/s0092-8674(04)00173-4
2. ↑ Fraiture M, Baxter RH, Steinert S, Chelliah Y, Frolet C, Quispe-Tintaya W, Hoffmann JA, Blandin SA, Levashina EA. Two mosquito LRR proteins function as complement control factors in the TEP1-mediated killing of Plasmodium. Cell Host Microbe. 2009 Mar 19;5(3):273-84. doi: 10.1016/j.chom.2009.01.005. PMID:19286136 doi:http://dx.doi.org/10.1016/j.chom.2009.01.005
3. ↑ Pompon J, Levashina EA. A New Role of the Mosquito Complement-like Cascade in Male Fertility in Anopheles gambiae. PLoS Biol. 2015 Sep 22;13(9):e1002255. doi: 10.1371/journal.pbio.1002255., eCollection 2015. PMID:26394016 doi:http://dx.doi.org/10.1371/journal.pbio.1002255
4. ↑ Blandin S, Shiao SH, Moita LF, Janse CJ, Waters AP, Kafatos FC, Levashina EA. Complement-like protein TEP1 is a determinant of vectorial capacity in the malaria vector Anopheles gambiae. Cell. 2004 Mar 5;116(5):661-70. doi: 10.1016/s0092-8674(04)00173-4. PMID:15006349 doi:http://dx.doi.org/10.1016/s0092-8674(04)00173-4
5. ↑ Baxter RH, Chang CI, Chelliah Y, Blandin S, Levashina EA, Deisenhofer J. Structural basis for conserved complement factor-like function in the antimalarial protein TEP1. Proc Natl Acad Sci U S A. 2007 Jul 10;104(28):11615-20. Epub 2007 Jul 2. PMID:17606907