Abstract: C-type lectin is the main member of the lectin family, which has abundant diversity in invertebrates. Their unique biological functions are widely applied in many fields, such as biology, medicine and so on. In this study, a novel C-type lectin RPCL was cloned from Ridgeia piscesae, a tube worm collected from the deep-sea hydrothermal region at Juan de Fuca Ridge in the northeast Pacific Ocean. The similarity between this gene and the reported lectins is very low, and the predicted 3D structure was quite different from the known lectins, suggesting that it may have some special properties. Furthermore, the heterologous recombinant expression of MRPCL was successfully achieved, and a large amount of soluble proteins were obtained through purification and renaturation. It will facilitate the further study on the function of RPCL.