Shelling A N, Butler R, Jones T, Laval S, Boyle J M, Ganesan T S
ICRF Laboratories, Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, United Kingdom.
Genomics. 1995 Jan 20;25(2):584-7. doi: 10.1016/0888-7543(95)80065-t.
A protein receptor tyrosine kinase (EDDR1) has been isolated from a complementary DNA library of SKOV-3, an epithelial ovarian cancer cell line. The primary structure of the predicted amino acid sequence of the protein shows a novel N-terminal region that has homology to a factor VIII-like domain. The C-terminal catalytic domain has all of the canonical sequence motifs of a receptor tyrosine kinase with homology to the TRK-2H protein (49%), which suggests that it is a type II receptor. It is expressed in epithelial cells of several tissues. To determine the chromosomal localization of the gene, somatic cell hybrids were analyzed by PCR amplification using oligonucleotide primers specific for EDDR1. Segregation was observed to a hybrid containing human chromosome 6. Cosmids for EDDR1 were isolated from a human chromosome 6 cosmid library and were shown by fluorescence in situ hybridization to map to 6q16.
一种蛋白质受体酪氨酸激酶（EDDR1）已从上皮性卵巢癌细胞系SKOV-3的互补DNA文库中分离出来。该蛋白质预测氨基酸序列的一级结构显示出一个新的N端区域，该区域与因子VIII样结构域具有同源性。C端催化结构域具有受体酪氨酸激酶的所有典型序列基序，与TRK-2H蛋白具有同源性（49%），这表明它是一种II型受体。它在多种组织的上皮细胞中表达。为了确定该基因的染色体定位，使用针对EDDR1的寡核苷酸引物通过PCR扩增分析体细胞杂种。观察到该基因分离到一个含有人类6号染色体的杂种中。从人类6号染色体粘粒文库中分离出EDDR1的粘粒，并通过荧光原位杂交显示其定位于6q16。
