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SIGLEC14 (sialic acid binding Ig-like lectin 14)
Siglec-14 is a sialic acid-recognizing activatory receptor found on certain immune cells types that is undergoing concerted evolution with the gene for Siglec-5 (an inhibitory receptor) via ongoing gene conversion of exons encoding amino-terminal V-set lg-like domains. The result is that the two molecules have similar binding properties for sialic acids. However surprisingly, a critical arginine residue required for sialic acid recognition has been mutated in the corresponding molecules from the chimpanzee, gorilla and orangutan. It appears that this may be the ancestral condition, and that the human molecules have restored the arginine residue required for sialic acid recognition. It is unclear what the evolutionary significance of this adjustment is, and further studies are needed.
Types of Human-Specific Changes in SIGLEC14:
Functional Differences in protein coding sequences
Partial Pseudogenization in the Human population
Angata, T., Hayakawa, T., Yamanaka, M., Varki, A., and Nakamura, M. 2006. Discovery of Siglec-14, a novel sialic acid receptor undergoing concerted evolution with Siglec-5 in primates. FASEB J. 20:1964-1973.
Carlin, A.F., Chang, Y.C., Areschoug, T., Lindahl, G., Hurtado-Ziola, N., King, C.C., Varki, A., and Nizet, V. 2009. Group B Streptococcus suppression of phagocyte functions by protein-mediated engagement of human Siglec-5. J Exp Med. 206:1691-1699.

