RESUMO
BACKGROUND: Renal cancer is one of the common malignant tumors of the urinary system, seriously threatening human being’s health. The current discoveries, however, are far enough for efficient and secure treatment of renal cancer. AIMS: The aim was to explore the mechanism of matrix metalloproteinase‑7 (MMP‑7) protein in renal carcinoma cell metastasis by bioinformatics analysis. MATERIALS AND METHODS: Bioinformatics methods were used to analyze the composition of amino acids, as well as transmembrane structure, coiled coils, subcellular localization, signal peptide, functions and structures at all levels. RESULTS AND CONCLUSIONS: It showed that the gene MMP‑7 totally had 1131 bp. A peptide chain containing 267 amino acids was encoded in the coding region. Based on random coil, α helix, and further super‑helix, it had formed a stable neutral hydrophilic protein. The subcellular location analysis indicated that the protein was located outside the cell. The mature peptide started from the 18th amino acid, and its front‑end was the sequence of the signal peptide, belonging to the secreted protein. Analysis of the functional domain showed that this protein had two functional domains, the PG binding domain, and the zinc finger binding domain. Moreover, the protein, which was cross‑linked with it, was also one related to cancer cell proliferation and metastasis. To sum up, MMP‑7 is a stable neutral hydrophilic secreted protein, and it may play a vital role in the invasion and metastasis of cancer cells.