title: Androgens affect the processing of secretory protein precursors in the guinea pig seminal vesicle. II. Identification of conserved sites for protein processing.
abstract: The guinea pig seminal vesicle epithelium is an androgen-dependent tissue that synthesizes and secretes four major secretory proteins (SVP-1, SVP-2, SVP-3, and SVP-4). Sequencing of near full-length cDNA clones corresponding to the two most abundant mRNAs produced by the seminal vesicle reveals that all four secretory proteins are cleaved from two secretory protein precursors. Amino acid sequences from purified SVP-2 match the central region of the predicted amino acid sequences from the smaller cDNA clone, GP2 (581 nucleotides). Similar analysis demonstrates that the predicted amino acid sequence from the longer cDNA clone, GP1 (1368 nucleotides), codes for the related proteins SVP-3 and SVP-4 as well as SVP-1. The 43.2 kilodalton polyprotein precursor coded by GP1 contains two different sets of 24 amino acid tandemly repeated sequences. The two secretory protein precursors have extensive regions of peptide sequence homology, particularly in regions where protein processing must occur to produce the mature secretory proteins. Analysis of the predicted secondary structure of the two precursor polypeptides revealed a strong correlation between structural features and sites of protein processing.
authors.affiliation: Department of Biochemistry and Molecular Biology, Mayo Clinic/Foundation, Rochester, Minnesota 55905.
authors.forename: J E
authors.initials: JE
authors.lastname: Hagstrom
authors.forename: S
authors.initials: S
authors.lastname: Harvey
authors.forename: B
authors.initials: B
authors.lastname: Madden
authors.forename: D
authors.initials: D
authors.lastname: McCormick
authors.forename: E D
authors.initials: ED
authors.lastname: Wieben
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D004247:DNA / Q000235:genetics; D005796:Genes; D006168:Guinea Pigs; D008297:Male; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000378:metabolism; D029584:Prostatic Secretory Proteins; D014176:Protein Biosynthesis; D011498:Protein Precursors / Q000378:metabolism*; D011499:Protein Processing, Post-Translational / Q000187:drug effects; D011506:Proteins / Q000235:genetics; D012333:RNA, Messenger / Q000235:genetics; D012091:Repetitive Sequences, Nucleic Acid; D029589:Seminal Plasma Proteins; D012669:Seminal Vesicles / Q000166:cytology / Q000187:drug effects* / Q000378:metabolism; D012689:Sequence Homology, Nucleic Acid; D013329:Structure-Activity Relationship; D013739:Testosterone / Q000494:pharmacology*
chemical_list: D029584:Prostatic Secretory Proteins; D011498:Protein Precursors; D011506:Proteins; D012333:RNA, Messenger; D029589:Seminal Plasma Proteins; C043076:beta-microseminoprotein; D013739:Testosterone; D004247:DNA; D010447:Peptide Hydrolases