Collagen is a protein originated from animal tissues and widely used in various industries, such as food, biomedical, pharmaceutical and in the photography sector. The main sources of collagen are the by-products of cattle and pigs, which are associated with the risk of contagious diseases and restrictions on the consumption of pigs by some religions, these factors have led researchers and users of collagen to find different sources of extraction. Thus, the aim of this study was to isolate and characterize pepsin-soluble collagen from rabbit meat, skin and ear, regarding its physical-chemical and functional properties. The analysis was carried out in a completely randomized design (CRD), with three treatments (skin, ears and meat). Each analysis was carried out with three replications. Collagen extracts from meat, skin and ears showed yields of 9.0, 24.4 and 23.8% and mainly high protein content 80.7, 95.5 and 94.5% on a dry basis, respectively. FTIR spectra displayed the characteristic peaks of amide A, B, I, II and III and SDS-PAGE analysis showed high molecular weight bands and those collagens mainly consist of type I collagen; in addition, collagens showed greater solubility at acidic pH, as found in other collagen research. Foaming was only seen at collagen concentrations of 0.25 and 0.5%, whereas at 1.0%, the consistency was creamy with no foaming. Positively, at lower concentrations, foam is obtained. The emulsifying activity index for the meat, skin and ears was 44.7, 46.6 and 48.2 m2/g, respectively; the results were superior to other sources, such as gelatin from the skin and bones of cattle and even marine species skins. Based on the results, rabbit meat, skin and ears proved to be a viable source for collagen extraction as an alternative to bovine and porcine collagen, adding value to the by-products of rabbit production.