[Kramer JM] zmp for Zinc MetalloProtease. cg115 is deletion derivative of pk205tci, no apparent phenotype. Overexpression of zmp-1 leads to abnormality, degradation of extracellular matrix components. cDNAs map to C28H8/EGAP1. Encodes predicted protein related to matrix metalloproteases.
zmp-1 encodes a zinc matrix metalloproteinase that enables anchor cell (AC) invasion during postembryonic vulval development; ZMP-1's proteinase activity has been confirmed in vitro; N-terminus to C-terminus, ZMP-1 is predicted to have a signal sequence, peptidoglycan-binding domain, a central matrix protease domain, a coiled-coil domain, and four hemopexin domains; ZMP-1 is expressed in AC during larval development, vulD and vulE in larvae and adults, and vulA in young adults onward; ZMP-1 is expressed in AC at the time it invades the basement membrane (L3 larval stage), and is localized to puncta often concentrated at the invasive basolateral membrane; ZMP-1::GFP diffuses from AC to utse cytoplasm upon fusion of these cells; ZMP-1 expression in AC requires EGL-43 (perhaps directly), and FOS-1A (indirectly); transcription of zmp-1 in AC, vulA, and vulE is driven by physically distinct sites in the zmp-1 5' flanking sequence; other regulators of ZMP-1 expression in other cell types include COG-1, EGL-38, LIN-11, LIN-29, and NHR-67; zmp-1(cg115) and zmp-1(RNAi) animals have no grossly obvious phenotypes, but null zmp-1(cg115) mutations enhance a subtle defect of AC invasion seen with null cdh-3(pk87) or him-4(rh319) mutations.
Enables metallopeptidase activity. Involved in basement membrane disassembly. Located in cell surface. Expressed in several structures, including P6.paal; P6.paar; P6.papl; gonad; and vulval cell. Human ortholog(s) of this gene implicated in prostate cancer and transitional cell carcinoma. Is an ortholog of human MMP15 (matrix metallopeptidase 15) and MMP24 (matrix metallopeptidase 24).