CELE_F02A9.6, emb-33, F02A9.6

glp-1 encodes an N-glycosylated transmembrane protein that, along with LIN-12, comprises one of two C. elegans members of the LIN-12/Notch family of receptors; from the N- to the C-terminus, GLP-1 is characterized by ten extracellular EGF-like repeats, three LIN-12/Notch repeats, a CC-linker, a transmembrane domain, a RAM domain, six intracellular ankyrin repeats, and a PEST sequence; in C. elegans, GLP-1 activity is required for cell fate specification in germline and somatic tissues; in the germline, GLP-1, acting as a receptor for the DSL family ligand LAG-2, is essential for mitotic proliferation of germ cells and maintenance of germline stem cells; in somatic tissues, maternally provided GLP-1, acting as a receptor for the DSL family ligand APX-1, is required for inductive interactions that specify the fates of certain embryonic blastomeres; GLP-1 is also required for some later embryonic cell fate decisions, and in these decisions its activity is functionally redundant with that of LIN-12; GLP-1 expression is regulated temporally and spatially via translational control, as GLP-1 mRNA, present ubiquitously in the germline and embryo, yields detectable protein solely in lateral, interior, and endomembranes of distal, mitotic germ cells, and then predominantly in the AB blastomere and its descendants in the early embryo; proper spatial translation of glp-1 mRNA in the embryo is dependent upon genes such as the par genes, that are required for normal anterior-posterior asymmetry in the early embryo; signaling through GLP-1 controls the activity of the downstream Notch pathway components LAG-3 and LAG-1, the latter being predicted to function as part of a transcriptional feedback mechanism that positively regulates GLP-1 expression; signaling through the DNA-binding protein LAG-1 is believed to involve a direct interaction between LAG-1 and the GLP-1 RAM and ankyrin domains

CELE_C12D8.11, rop1, C12D8.11

rop-1 encodes an RNAi-binding protein that is orthologous to the vertebrate 60-kDa Ro autoantigen that is the protein component of the Ro ribonucleoprotein (RNP) complex; ROP-1 binds the single C. elegans Ro RNP RNA component, YRN-1 (Y RNA) in vivo and although loss of rop-1 activity via mutation results in no obvious visible phenotypes, it does result in a dramatic decrease in YRN-1 levels, indicating that ROP-1 is necessary for maintaining normal levels of the Ro RNP Y RNA; in addition, rop-1 mutations also result in a statistically significant increase in mutant 5S rRNA molecules found in ribosomal RNA preparations, suggesting that ROP-1 may play a role in quality control of 5S rRNA processing; rop-1 mRNA is detectable during all stages of development, and rop-1 promoter fusions appear to be expressed in all cell types, except the germline.