Using Stropharia rugosoannulata as the raw material, the albumin and glutelin were extracted by using modified Osborne method. Subsequently, the sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), scanning electron microscope (SEM) and fourier transform infrared spectroscopy (FTIR) were performed, and the physicochemical and functional properties were analyzed and compared. The results showed that the protein content of the S. rugosoannulata fruiting bodies was 30.98%, the extraction rates of albumin and glutelin were 39.74% and 13.42%, respectively. Albumin exhibited a molecular weight distribution ranging from 17 to 75 kDa, whereas glutelin possessed a broader distribution (17~180 kDa). Albumin presented a smooth and porous surface, while glutelin displayed a loose structure with laminations and fissures. Both albumin and glutelin displayed characteristic protein absorption peaks at amide Ⅰ and Ⅱ bands. The two proteins differed significantly in the contents of free sulfhydryl groups and disulfide bonds as albumin contained more free sulfhydryl groups than glutelin but less disulfide bonds. Glutelin showed no phase transition from 40 ℃ to 180 ℃, indicating its high thermal stability, while albumin underwent thermal transition at 150.02 ℃. Compared with soy protein isolate (SPI), albumin and glutelin exhibited relatively low solubility, but they presented distinct trends with variations in temperature and pH. Albumin possessed rheological properties similar to those of SPI, while glutelin exhibited weak gel properties. Albumin and glutelin showed significantly lower water-holding and oil-holding capacity than SPI, but glutelin exhibited favorable foaming and emulsifying properties, with several characteristics superior to or comparable with SPI. In conclusion, the glutelin from S. rugosoannulata boasts broader application fields and prospects, and can be applied to develop emulsion and gel-based food products.