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1.C.113.  The Hemolysin III (Hly III) Family

The Hly III family (SwissProt family UPF0073) consists of proteins of 200-250 residues with 7 putative TMSs. They are from bacteria and eukaryotes (both plants and animals). One is a characterized hemolysin from Bacillus cereus. Another is a protein induced during differentiation of monocytes to macrophage in humans.

Bacillus cereus hemolysin III activity has been tested in crude extracts, and from Escherichia coli carrying the hly-III gene (Baida and Kuzmin 1996). It was concluded that hemolysin III is a pore-forming hemolysin with functional pore diameter of about 3-3.5 nm. Hemolysis occurs in at least three steps: (i) the temperature-dependent binding of the Hly-III monomers to the erythrocyte membrane; (ii) the temperature-dependent formation of the transmembrane oligomeric pore, and (iii) the temperature-independent erythrocyte lysis.

One homologue is a receptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism (Tanabe et al. 2015, Yamauchi et al. 2003). Required for normal glucose and fat homeostasis and for maintaining normal body weight. ADIPOQ-binding activates a signaling cascade that leads to increased AMPK activity, and ultimately to increased fatty acid oxidation, increased glucose uptake and decreased gluconeogenesis. This receptor has high affinity for globular adiponectin and low affinity for full-length adiponectin.  The relationship between this receptor and the hemolysins is not clear, but they are definitely homologous with the same general topology.

References associated with 1.C.113 family:

Baida, G.E. and N.P. Kuzmin. (1995). Cloning and primary structure of a new hemolysin gene from Bacillus cereus. Biochim. Biophys. Acta. 1264: 151-154. 7495855
Baida, G.E. and N.P. Kuzmin. (1996). Mechanism of action of hemolysin III from Bacillus cereus. Biochim. Biophys. Acta. 1284: 122-124. 8962879
Góñez, L.J., G. Naselli, I. Banakh, H. Niwa, and L.C. Harrison. (2008). Pancreatic expression and mitochondrial localization of the progestin-adipoQ receptor PAQR10. Mol Med 14: 697-704. 18769639
Hafiane, A., K. Gasbarrino, and S.S. Daskalopoulou. (2019). Adiponectin and cholesterol efflux. Metabolism 153953. [Epub: Ahead of Print] 31377319
Lee, Y., A. Nakano, S. Nakamura, K. Sakai, M. Tanaka, K. Sanematsu, N. Shigemura, and T. Matsui. (2021). In vitro and in silico characterization of adiponectin-receptor agonist dipeptides. NPJ Sci Food 5: 29. 34772952
Miller, E.N., L.R. Jarboe, L.P. Yomano, S.W. York, K.T. Shanmugam, and L.O. Ingram. (2009). Silencing of NADPH-dependent oxidoreductase genes (yqhD and dkgA) in furfural-resistant ethanologenic Escherichia coli. Appl. Environ. Microbiol. 75: 4315-4323. 19429550
Pang, Y., J. Dong, and P. Thomas. (2013). Characterization, neurosteroid binding and brain distribution of human membrane progesterone receptors δ and {epsilon} (mPRδ and mPR{epsilon}) and mPRδ involvement in neurosteroid inhibition of apoptosis. Endocrinology 154: 283-295. 23161870
Petersen, S.L., K.A. Intlekofer, P.J. Moura-Conlon, D.N. Brewer, J. Del Pino Sans, and J.A. Lopez. (2013). Nonclassical progesterone signalling molecules in the nervous system. J Neuroendocrinol 25: 991-1001. 23763432
Rehli, M., S.W. Krause, L. Schwarzfischer, M. Kreutz, and R. Andreesen. (1995). Molecular cloning of a novel macrophage maturation-associated transcript encoding a protein with several potential transmembrane domains. Biochem. Biophys. Res. Commun. 217: 661-667. 7503749
Tanabe, H., Y. Fujii, M. Okada-Iwabu, M. Iwabu, Y. Nakamura, T. Hosaka, K. Motoyama, M. Ikeda, M. Wakiyama, T. Terada, N. Ohsawa, M. Hato, S. Ogasawara, T. Hino, T. Murata, S. Iwata, K. Hirata, Y. Kawano, M. Yamamoto, T. Kimura-Someya, M. Shirouzu, T. Yamauchi, T. Kadowaki, and S. Yokoyama. (2015). Crystal structures of the human adiponectin receptors. Nature 520: 312-316. 25855295
Vasiliauskaité-Brooks, I., R. Sounier, P. Rochaix, G. Bellot, M. Fortier, F. Hoh, L. De Colibus, C. Bechara, E.M. Saied, C. Arenz, C. Leyrat, and S. Granier. (2017). Structural insights into adiponectin receptors suggest ceramidase activity. Nature. [Epub: Ahead of Print] 28329765
Wunderlich, J. (2022). Updated List of Transport Proteins in. Front Cell Infect Microbiol 12: 926541. 35811673
Yamauchi, T., J. Kamon, Y. Ito, A. Tsuchida, T. Yokomizo, S. Kita, T. Sugiyama, M. Miyagishi, K. Hara, M. Tsunoda, K. Murakami, T. Ohteki, S. Uchida, S. Takekawa, H. Waki, N.H. Tsuno, Y. Shibata, Y. Terauchi, P. Froguel, K. Tobe, S. Koyasu, K. Taira, T. Kitamura, T. Shimizu, R. Nagai, and T. Kadowaki. (2003). Cloning of adiponectin receptors that mediate antidiabetic metabolic effects. Nature 423: 762-769. 12802337