spp-4 encodes an antimicrobial peptide that belongs to the SPP-protein family, called caenopores, with structural similarity to saposin-like proteins (SAPLIPs), the amoebapores and the mammalian NK-lysin and granulysin; caenopores are part of the worm's innate immune system and interact with and eliminate bacteria via membrane pore-forming activity; C. elegans has at least 33 putative SPP proteins; phylogenetic analysis indicates that spp-4 is most similar to spp-2, spp-5 and spp-6.
Enriched in hypodermis; intestine; male-specific anatomical entity; muscle cell; and neurons based on tiling array; RNA-seq; single-cell RNA-seq; and microarray studies. Is affected by several genes including daf-16; daf-2; and dpy-10 based on microarray and RNA-seq studies. Is affected by twenty-four chemicals including Heme; methylmercuric chloride; and bisphenol S based on microarray and RNA-seq studies. Is predicted to encode a protein with the following domains: Saposin B type, region 2; Saposin B type domain; Saposin-like; Phosphorylation site; and Saposin-like type B, region 2.
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.