Open AccessHuman epidermal growth factor precursor: cDNA sequence, expressionin vitroand gene organization
Author(s) -
Graeme I. Bell,
Noel M. Fong,
Michelle M. Stempien,
M. A. Wormsted,
Daniel Caput,
Lailing Ku,
Mickey S. Urdea,
Leslie B. Rall,
Ray Sánchez-Pescador
Publication year - 1986
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/14.21.8427
Subject(s) - biology , epidermal growth factor , exon , complementary dna , exon shuffling , microbiology and biotechnology , tandem exon duplication , gene , intron , peptide sequence , gene duplication , nucleic acid sequence , snap23 , genetics , hspa2 , cell culture
Complementary DNA clones encoding the human kidney epidermal growth factor (EGF) precursor have been isolated and sequenced. They predict the sequence of a 1,207 amino acid protein which contains EGF flanked by polypeptide segments of 970 and 184 residues at its NH2- and COOH-termini, respectively. The structural organization of the human EGF precursor is similar to that previously described for the mouse protein and there is 66% identity between the two sequences. Transfection of COS-7 cells with the human EGF precursor cDNA linked to the SV40 early promoter indicate that it can be synthesized as a membrane protein with its NH2-terminus external to the cell surface. The human EGF precursor gene is approximately 110 kilobase pairs and has 24 exons. Its exon-intron organization revealed that various domains of the EGF precursor are encoded by individual exons. Moreover, 15 of the 24 exons encode protein segments that are homologous to sequences in other proteins. Exon duplication and shuffling appear to have played an important role in determining the present structure of this protein.