This article is missing information about consensus cystine repeat, difulfide bond position (residues, inter/intra?).(March 2019) |
EGF-like domain | |||||||||
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Identifiers | |||||||||
Symbol | EGF | ||||||||
Pfam | PF00008 | ||||||||
Pfam clan | CL0001 | ||||||||
ECOD | 389.1.1 | ||||||||
InterPro | IPR000742 | ||||||||
PROSITE | PDOC00021 | ||||||||
SCOP2 | 1apo / SCOPe / SUPFAM | ||||||||
CDD | cd00053 | ||||||||
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EGF-like domain, extracellular | |||||||||
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Identifiers | |||||||||
Symbol | EGF_2 | ||||||||
Pfam | PF07974 | ||||||||
Pfam clan | CL0001 | ||||||||
InterPro | IPR013111 | ||||||||
CDD | cd00054 | ||||||||
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The EGF-like domain is an evolutionary conserved protein domain, which derives its name from the epidermal growth factor where it was first described. It comprises about 30 to 40 amino-acid residues and has been found in a large number of mostly animal proteins.[2][3] Most occurrences of the EGF-like domain are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted. An exception to this is the prostaglandin-endoperoxide synthase. The EGF-like domain includes 6 cysteine residues which in the epidermal growth factor have been shown to form 3 disulfide bonds. The structures of 4-disulfide EGF-domains have been solved from the laminin and integrin proteins. The main structure of EGF-like domains is a two-stranded β-sheet followed by a loop to a short C-terminal, two-stranded β-sheet. These two β-sheets are usually denoted as the major (N-terminal) and minor (C-terminal) sheets.[4] EGF-like domains frequently occur in numerous tandem copies in proteins: these repeats typically fold together to form a single, linear solenoid domain block as a functional unit.