Sequence, Organization, and Expression of the Human FEM1B Gene

• Published in: Biochemical and biophysical research communications 2000-01, Vol.267 (1), p.317-320
• Main Authors: Ventura-Holman, Tereza, Maher, Joseph F.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Brain - metabolism; Caenorhabditis elegans; Caenorhabditis elegans - genetics; Caenorhabditis elegans Proteins; Carrier Proteins; Cell Cycle Proteins - biosynthesis; Cell Cycle Proteins - chemistry; Cell Cycle Proteins - genetics; Cloning, Molecular; Conserved Sequence; Exons; FEM-1 protein; Fem1a gene; Fem1b gene; Humans; Introns; Mice; Molecular Sequence Data; Recombinant Proteins - biosynthesis; Recombinant Proteins - chemistry; Sequence Alignment; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.1999.1942

The FEM-1 protein of Caenorhabditis elegans functions within the nematode sex-determination pathway. Two mouse homologs, encoded by the Fem1a and Fem1b genes, have been reported. We report here the characterization of a novel human gene, designated FEM1B, that is highly homologous to the mouse Fem1b gene. FEM1B encodes a protein, designated FEM1β, that shows >99% amino acid identity to the corresponding mouse Fem1b protein, including 100% amino acid identity in the N-terminal ANK repeat domain. FEM1β represents the first characterized human member of the FEM-1 protein family. The human and mouse genes show conservation of coding sequence and its intron/exon organization, flanking untranslated and genomic sequences, and expression pattern in adult tissues. These findings suggest that there may be evolutionary conservation of regulation and function between the mouse and human FEM1B genes.