To elucidate the molecular characteristics and homology of the parvalbumin (PV) gene from Trachinotus ovatus, the full-length cDNA sequence was obtained by gene cloning, and systematic analyses were conducted using bioinformatics approaches. The results showed that the open reading frame of the PV gene was 330 bp in length, encoding 110 amino acids, with a predicted molecular mass of 12.1 kDa and a theoretical isoelectric point (PI) of 4.94. The PV was found to be hydrophilic and thermostable, predominantly composed of typical α-helical structures, belonging to the EF-hand protein family, with potential modification regions and Ca²⁺-binding sites. Sequence alignment revealed that the PV shared 100% homology with the PV sequence of T. anak, indicating a high degree of conservation. This study enriches the database of fish allergens and provides theoretical support for further elucidating their allergenic mechanism and developing hypoallergenic aquatic product processing technologies.