The glycoprotein (G) is one of the structural proteins on the surface of infectious haematopoietic necrosis virus (IHNV) and has important functions. In this study, the open reading frame of the glycoprotein gene was amplified by reverse transcriptase-PCR (RT-PCR) from isolate IHNV-Sn1203 and cloned into the pET27b(+) vector. The structure and characteristics of the glycoprotein gene were analyzed using bioinformatics software. The results showed that the G gene was 1 527 bp, encoding a 508 amino acid protein, Isolate IHNV-Sn1203 shared closer identity with strains isolated from South Korea, and the homology of at nucleotide and amino acid level of the G gene were 96.68% and 97.05%, respectively. The molecular weight was 56.55 kD and the isoelectric point was 6.15. The glycoprotein was rich inserine, tyrosine, and contained 28 potential phosphorylation sites. According to the protein structure prediction, the glycoprotein may have four N-glycosylationsites and seven O-glycosylation sites. The glycoprotein is hydrophilic, with an N-terminal signal peptide and a transmembrane region from amino acid 483 to 508. The glycoprotein was estimated to be highly antigenic. Phylogenetic analysis showed that isolate IHNV-Sn1203 was in the same branch as isolates from Japan and South Korea, belonging to the JRt genotype. This study established a foundation for research into the genetic background, pathogenesis, and molecular epidemiology of IHNV.