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Molecular Cloning and Sequence Analysis of Two Porcine Seminal Proteins, PSP-I and PSP-II: New Members of the Spermadhesin Family

1993; Mary Ann Liebert, Inc.; Volume: 12; Issue: 7 Linguagem: Inglês

10.1089/dna.1993.12.605

1557-7430

Simon C.M. Kwok, Dongfang Yang, Guoli Dai, Michael J. Soares, Shiuan Chen, John P. McMurtry,

Forensic and Genetic Research

Two full-length cDNAs encoding porcine seminal proteins, PSP-I and PSP-II, have been isolated from a porcine seminal vesicle cDNA library. Nucleotide sequence analysis of the 706-bp PSP-I cDNA predicts a precursor protein of 133 amino acid residues, which includes a 21-residue signal peptide and a 112-residue secreted protein. On the other hand, the complete sequence of the 686-bp PSP-II cDNA reveals a coding sequence for a 21-residue signal peptide and a 116-residue secreted protein. The predicted amino acid sequences agree very well with those determined by conventional amino acid sequence analysis. Alignment of the two cDNA sequences shows an overall 66% sequence homology throughout their entire length. However, the sequence homology is much higher in the 3′ untranslated region (72%) than in the coding region (61%). This suggests that these two genes evolved by duplication and divergence from a common ancestral gene. They share about 50% amino acid sequence homology and a similar overall structure with three members of the spermadhesin family.