Valdenaire O, Rohrbacher E, Mattei M G
F. Hoffmann-La Roche Ltd., Pharma Division, Basel, Switzerland.
J Biol Chem. 1995 Dec 15;270(50):29794-8. doi: 10.1074/jbc.270.50.29794.
The two human endothelin-converting enzyme (ECE-1) isoforms, which differ by their N-terminal region, are encoded by a single gene. The gene is composed of 19 exons that span more than 68 kilobases and has been mapped to the 1p36 band of the human genome. The two isoform mRNAs display different tissue distributions. Their precursors are transcribed from two distinct start sites, upstream from exon 1 and exon 3, respectively. Sequence analysis of the two putative promoters revealed the presence of motifs characteristic for several transcription factors. Comparison of the ECE-1 gene structure with those of other zinc metalloproteases, as well as a phylogenetic study, confirm the existence of a metalloprotease subfamily composed of ECE-1, ECE-2, neutral endopeptidase, Kell blood group protein, and two bacterial enzymes.
两种人内皮素转化酶（ECE-1）同工型，其N端区域不同，由单个基因编码。该基因由19个外显子组成，跨越超过68千碱基，已被定位到人类基因组的1p36带。两种同工型mRNA表现出不同的组织分布。它们的前体分别从外显子1和外显子3上游的两个不同起始位点转录。对两个假定启动子的序列分析揭示了几种转录因子特有的基序的存在。将ECE-1基因结构与其他锌金属蛋白酶的结构进行比较，以及系统发育研究，证实了由ECE-1、ECE-2、中性内肽酶、凯尔血型蛋白和两种细菌酶组成的金属蛋白酶亚家族的存在。
