3 Ontology Annotations
| GO Term | Gene Name |
|---|---|
| GO:0050825 | IPR000104 |
| GO:0042309 | IPR000104 |
| GO:0050826 | IPR000104 |
| Type: | Family | Name: | Antifreeze protein, type I |
| Description: | Marine teleosts from polar oceans can be protected from freezing in icy sea-water by serum antifreeze proteins (AFPs) or glycoproteins (AFGPs) []:these function by binding to, and preventing the growth of, ice crystals within the fish and depressing the non-equilibrium freezing point to below that of the melting point.Despite functional similarity, antifreeze proteins are structurally diverse and include glycosylated and at least 3 non-glycosylated forms: the AFGP of nototheniids and cods are polymers of atripeptide repeat, Ala-Ala-Thr, with a disaccharide attached to the threonine residue; type I AFPs are foundin flounder and sculpin; type II AFPs of sea-raven, smelt and herring are Cys-rich proteins; and type III AFPs, found in eel pouts, are rich inbeta-structure. Non-homologous antifreeze proteins have also been identified in insects and plants [].Type I AFPs are Ala-rich, amphiphilic, alpha-helical proteins []. The ice-binding sites of all AFPs are relatively flat and hydrophobic and have an uninterupted section of alanines running the length of the approximately 16.5A helix repeat. Basedon the energy-minimised structure [], a model has been proposed todescribe the binding of the protein to ice crystals, whereby the protein binds to an ice nucleation structure, in a zipper-like fashion, viahydrogen bonding of the methyl-group of threonine side chains (with an 11-residue period) to oxygen atoms in the ice lattice. The growth of ice crystals is thusstopped, or retarded, and the freezing point depressed. The high lysince content of these peptides may serve to promote the solubility of these proteins. | Short Name: | Antifreeze_1 |
| GO Term | Gene Name |
|---|---|
| GO:0050825 | IPR000104 |
| GO:0042309 | IPR000104 |
| GO:0050826 | IPR000104 |
