Pig epidermal growth factor precursor contains segments that are highly conserved among species
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Pig epidermal growth factor precursor contains segments that are highly conserved among species. / Jørgensen, P E; Jensen, L.G.; Sørensen, B S; Poulsen, Steen Seier; Nexø, Ebba.
In: Scandinavian Journal of Clinical & Laboratory Investigation, Vol. 58, No. 4, 07.1998, p. 287-98.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Pig epidermal growth factor precursor contains segments that are highly conserved among species
AU - Jørgensen, P E
AU - Jensen, L.G.
AU - Sørensen, B S
AU - Poulsen, Steen Seier
AU - Nexø, Ebba
PY - 1998/7
Y1 - 1998/7
N2 - The 53-aa polypeptide epidermal growth factor (EGF) is synthesized as a 1200-aa precursor. The non-EGF part of the precursor is very long compared with EGF, and can therefore be expected to have a biological role of its own. We have sequenced cDNA of the pig EGF precursor and compared a 668-aa segment with that of the human, the rat and the mouse EGF precursors, in order to identify highly conserved domains. The examined part of the precursor contains EGF itself and six so-called EGF-like modules. The overall amino acid identity among the four species is 64%. However, the amino acid identity differed from around 30% in some segments to around 70% in others. The highest amino acid identity, 71%, was observed for a 345-aa segment that contains three EGF-like modules and which is homologous to a part of the low-density lipoprotein receptor (LDL receptor). The amino acid identities are 64% for EGF itself, and 50-67% for the remaining three EGF-like modules. The segment of the LDL receptor that is homologous to a part of the EGF precursor is important for the function of the LDL receptor, and EGF-like modules seem to be involved in protein-protein interactions in a number of proteins. In conclusion, some segments of the EGF precursor are remarkably well conserved among species and it is tempting to speculate that they have a biological function.
AB - The 53-aa polypeptide epidermal growth factor (EGF) is synthesized as a 1200-aa precursor. The non-EGF part of the precursor is very long compared with EGF, and can therefore be expected to have a biological role of its own. We have sequenced cDNA of the pig EGF precursor and compared a 668-aa segment with that of the human, the rat and the mouse EGF precursors, in order to identify highly conserved domains. The examined part of the precursor contains EGF itself and six so-called EGF-like modules. The overall amino acid identity among the four species is 64%. However, the amino acid identity differed from around 30% in some segments to around 70% in others. The highest amino acid identity, 71%, was observed for a 345-aa segment that contains three EGF-like modules and which is homologous to a part of the low-density lipoprotein receptor (LDL receptor). The amino acid identities are 64% for EGF itself, and 50-67% for the remaining three EGF-like modules. The segment of the LDL receptor that is homologous to a part of the EGF precursor is important for the function of the LDL receptor, and EGF-like modules seem to be involved in protein-protein interactions in a number of proteins. In conclusion, some segments of the EGF precursor are remarkably well conserved among species and it is tempting to speculate that they have a biological function.
KW - Amino Acid Sequence
KW - Animals
KW - Base Sequence
KW - DNA, Complementary
KW - Epidermal Growth Factor
KW - Female
KW - Humans
KW - Mice
KW - Molecular Sequence Data
KW - Protein Precursors
KW - Rats
KW - Receptors, LDL
KW - Species Specificity
KW - Swine
M3 - Journal article
C2 - 9741816
VL - 58
SP - 287
EP - 298
JO - Scandinavian Journal of Clinical & Laboratory Investigation
JF - Scandinavian Journal of Clinical & Laboratory Investigation
SN - 0036-5513
IS - 4
ER -
ID: 47486662