Species living in extremely cold environments resist the freezing conditions through antifreeze proteins (Afps). Apart from being essential proteins for various organisms living in sub-zero temperatures, Afpshave numerous applications in different industries. They possess very small resemblance to each other and cannot be easily identified using simple search algorithms such as BLAST and PSI-BLAST. Diverse AFPs found in fishes (Type I, II, III, IV and antifreeze glycoproteins (AFGPs)), are sub-types and show low sequence and structural similarity, making their accurate prediction challenging. Although several machine-learning methods have been proposed for the classification of AFPs, prediction methods that have greater reliability are required. In this paper, we propose a novel machine-learning-based approach for the prediction of AFP sequences using latent space learning through a deep auto-encoder method. For latent space pruning, we use the output of the auto-encoder with a deep neural network classifier to learn the non-linear mapping of the protein sequence descriptor and class label. The proposed method outperformed the existing methods, yielding excellent results in comparison. A comprehensive ablation study is performed, and the proposed method is evaluated in terms of widely used performance measures. In particular, the proposed method demonstrated a high Matthews correlation coefficient of 0.52, F-score of 0.49, and Youden's index of 0.81 on an independent test dataset, thereby outperforming the existing methods for Afp prediction.In Antarctic fish, a survival mechanism that prevented them from freezing in seawater at sub-zero temperatures was observed, which led to the discovery of antifreeze proteins (AFP) 1 . AFPs have been identified as a crucial substance for resisting a freezing environment in various species including plants, bacteria, fungi, insects, and animals 2 . Ice exists in different geometric shapes due to the varying arrangements of oxygen atoms; therefore, the structural and sequential arrangements of AFPs largely vary to accommodate this heterogeneity of ice molecules 3 . Ice also exhibits the property of recrystallization, by which small ice crystals bind to the water molecules, thus becoming a large ice lattice, causing severe damage to the cell membrane, which, in some cases, may be lethal 4 . AFPs are commonly categorized into glycoproteins (AFGPs) and non-glycoproteins (AFPs) 5 . They protect the organisms using two mechanisms: (i) thermal hysteresis (TH), by which the freezing point of water is depressed to a few degrees by the adsorption-inhibition effect without altering the melting point 6 ; (ii) ice crystal inhibition, by which the AFP sites bind to the surfaces of ice and inhibit their growth to become a larger ice lattice, developing either small harmless ice crystals or forming a needle-shaped lattice, thus diminishing the recrystallization property of ice 2 .AFPs are indispensable in organisms such as fish 7 , fungi 8 , bacteria 9 , plants 10 , and insects 11 . Furthermo...