pam-1 encodes a metalloprotease that is the C. elegans puromycin-sensitive aminopeptidase (PSA) ortholog; in the one-cell embryo, PAM-1 is required for timely exit from meiosis II proper centrosome positioning, proper localization of polarity and cell fate determinants, and formation of the anteroposterior axis; genetic studies indicate that cyb-3, which encodes a B-type cyclin, is required for pam-1(lf) meiotic exit defects, suggesting that CYB-3 activity is regulated by PAM-1, directly or indirectly, in the early embryo; a pam-1::gfp reporter fusion is expressed in embryos, larvae, and adults; in larvae and adults, expression is particularly notable in the posterior intestine and amphid sensory neurons; in males, expression is also seen in neurons in the developing and mature male tail; in vitro, PAM-1 exhibits metal-dependent aminopeptidase activity, hydrolyzing the N-terminal amino acid from various peptide substrates.
Enables metalloaminopeptidase activity. Involved in several processes, including exit from meiosis; first cell cycle pseudocleavage; and regulation of reproductive process. Located in condensed chromosome; cytoplasm; and mitotic spindle pole. Expressed in amphid process; intestine; male-specific anatomical entity; nerve ring; and tail neurons. Is an ortholog of human NPEPPS (aminopeptidase puromycin sensitive).
Map position created from combination of previous interpolated map position (based on known location of sequence) and allele information. Therefore this is not a genetic map position based on recombination frequencies or genetic experiments. This was done on advice of the CGC.