Endothelin-converting enzyme 2; also known as ECE-2; is a metalloprotease that possesses many properties consistent with it being a neuropeptide-processing enzyme. Endothelin-converting enzymes (ECEs) are the key enzymes in the endothelin (ET) biosynthesis that catalyze the conversion of big ET; the biologically inactive precursor of mature ET. Two enzymes; termed ECE-1 and ECE-2; have been molecularly identified. ECE-2 is found primarily in neural tissues; with high levels of expression in midbrain; cerebellum; hypothalamus; frontal cortex and spinal cord and moderate levels in hippocampus and striatum. ECE-2 is strongly down-regulated in inferior parietal lobe from Alzheimer disease patients (at protein level). ECE-2 converts big endothelin-1 to endothelin-1. It is involved in the processing of various neuroendocrine peptides; including neurotensin; angiotensin I; substance P; proenkephalin-derived peptides; and prodynorphin-derived peptides. ECE-2 may limit beta-amyloid peptide accumulation in brain. It may also have methyltransferase activity. A comparison of residues around the cleavage site revealed that ECE-2 exhibits a unique cleavage site selectivity that is related to but distinct from that of ECE-1.
This antimicrobial gene is one of several chemokine genes clustered on the q-arm of chromosome 17. Chemokines form a superfamily of secreted proteins involved in immunoregulatory and inflammatory processes. The superfamily is divided into four subfamilies based on the arrangement of the N-terminal cysteine residues of the mature peptide. This chemokine, a member of the CC subfamily, displays chemotactic activity for eosinophils, but not mononuclear cells or neutrophils. This eosinophil-specific chemokine is thought to be involved in eosinophilic inflammatory diseases such as atopic dermatitis, allergic rhinitis, asthma and parasitic infections.
Human delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase(ECH1) is a member of the hydratase/isomerase superfamily and contains a C-terminal peroxisomal targeting sequence and localizes to peroxisomes. ECH1 shows high sequence similarity to enoyl-CoA hydratases of several species, particularly within a conserved domain characteristic of these proteins. The rat orthologlocalizes to the matrix of both the peroxisome and mitochondria.It can isomerize 3-trans, 5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA, indicating that it is a delta3,5-delta2,4-dienoyl-CoA isomerase. ECH1 plays an important role in the auxiliary step of the fatty acid beta-oxidation pathway.
Tumor necrosis factor receptor superfamily member EDAR is a Single-pass type I membrane protein. Edar was expressed reiteratively in signaling centers regulating key steps in morphogenesis. activin signaling from mesenchyme induces the expression of the TNF receptor edar in the epithelial signaling centers; thus making them responsive to Wnt-induced ectodysplasin from the nearby ectoderm. This is the first demonstration of integration of the Wnt; activin; and TNF signaling pathways. Defects in EDAR are a cause of ectodermal dysplasia anhidrotic (EDA); also known ectodermal dysplasia hypohidrotic autosomal recessive (HED). Ectodermal dysplasia defines a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. EDA is characterized by sparse hair (atrichosis or hypotrichosis); abnormal or missing teeth and the inability to sweat due to the absence of sweat glands.
EDEM2, also known as C20orf31, belongs to a family of proteins involved in ER-associated degradation (ERAD) of glycoproteins. In the endoplasmic reticulum (ER), misfolded proteins are retrotranslocated to the cytosol and degraded by the proteasome. Early in this pathway, a proposed lumenal ER lectin, EDEM, recognizes misfolded glycoproteins in the ER, disengages the nascent molecules from the folding pathway, and facilitates their targeting for disposal. In humans there are a total of three EDEM homologs. The amino acid sequences of these proteins are different from other lectins but are closely related to the Class I mannosidases (family 47 glycosidases). EDEM2 is one of the EDEM homologs. Overexpression of EDEM2 accelerates the degradation of misfolded alpha1-antitrypsin, indicating that the protein is involved in ERAD.
Endothelial Differentiation-Related Factor 1 (EDF1) is a 148 amino acid transcriptional coactivator that contains 1 HTH cro/C1-type DNA-binding domain. It has been postulated that the protein functions as a bridging molecule that interconnects regulatory proteins and the basal transcriptional machinery, thereby modulating the transcription of genes involved in endothelial differentiation. When endothelial cells are induced to differentiate in vitro, EDF1 is downregulated, leading to inhibition of cell growth and cell polarization. EDF1 binds calmodulin thorough its IQ domain and regulates nitric oxide synthase activity through calmodulin sequestration in the cytoplasm. Though ubiquitously expressed, EDF1 is most abundant in adult liver, heart, adipose tissues, intestine and pancreas. In fetal tissues, EDF1 is most abundant in kidney. There are two isoforms of EDF1 that are produced as a result of alternative splicing events.
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