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InterPro: IPR000742 EGF-like, type 3

Protein matches Help

UniProtKB

Matches:

6742 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR000742 EGF_3

Type

Domain

Signatures Help

Database	ID	Name	Proteins
PROSITE profile	PS50026	EGF_3	6742
Signatures in BioMart

InterPro Relationships Help

Children

IPR001336 EGF, type 1
IPR001881 EGF-like calcium-binding

Found in

IPR014394 Coagulation factor XII/hepatocyte growth factor activator
IPR015447 Neurexin
IPR015781 Tyrosine-protein kinase, angiopoietin receptor
IPR016348 L-selectin
IPR017047 Teratocarcinoma-derived growth factor Cripto
IPR017369 SPAN protein/blastula protease 10
IPR017436 Cripto related protein 3
IPR020696 Tyrosine-protein kinase, receptor Tie-1

Contains

IPR000152 EGF-type aspartate/asparagine hydroxylation site
IPR001438 EGF-like, type 2
IPR013032 EGF-like region, conserved site
IPR013111 EGF, extracellular
IPR018097 EGF-like calcium-binding, conserved site

InterPro annotation

Entry Details in BioMart

Abstract

A sequence of about thirty to forty amino-acid residues long found in the sequence of epidermal growth factor (EGF) has been shown [1, 2, 3, 4, 5, 6] to be present, in a more or less conserved form, in a large number of other, mostly animal proteins. The functional significance of EGF domains in what appear to be unrelated proteins is not yet clear. However, a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase). The EGF domain includes six cysteine residues which have been shown (in EGF) to be involved in disulphide bonds. The main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet. Subdomains between the conserved cysteines vary in length.

Structural links Help

PDB - click here

SCOP: b.29.1.4 , d.169.1.1 , g.12.1.1 , g.23.1.1 , g.27.1.1 , g.3.11.1 , g.3.11.5 , g.3.18.1 , g.32.1.1 , j.45.1.1

CATH: 2.10.25.10 , 2.10.70.10 , 2.60.120.200 , 3.10.100.10 , 3.90.290.10 , 4.10.740.10

Database links Help

PROSITE doc: PDOC00021

Interactions Help

This domain has been experimentally proven to be involved in Protein:Protein interactions.
Representative data is shown with the following example proteins:

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000742

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O14944 Proepiregulin

P01132 Pro-epidermal growth factor

P07207 Neurogenic locus Notch protein

P14585 Protein lin-12

Q39191 Wall-associated receptor kinase 1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013091	EGF calcium-binding
IPR000800	Notch domain
IPR017442	Serine/threonine-protein kinase-like domain
IPR006210	EGF-like
IPR008297	Notch
IPR011009	Protein kinase-like domain
IPR011656	Notch, NODP domain
IPR000719	Protein kinase, catalytic domain
IPR013032	EGF-like region, conserved site
IPR002110	Ankyrin repeat
IPR018097	EGF-like calcium-binding, conserved site
IPR001881	EGF-like calcium-binding
IPR016317	Pro-epidermal growth factor
IPR010660	Notch, NOD domain
IPR020683	Ankyrin repeat-containing domain
IPR000033	Low-density lipoprotein receptor, class B (YWTD) repeat
IPR011042	Six-bladed beta-propeller, TolB-like
IPR008271	Serine/threonine-protein kinase, active site
IPR001438	EGF-like, type 2
IPR000152	EGF-type aspartate/asparagine hydroxylation site
IPR000742	EGF-like, type 3
IPR001336	EGF, type 1
	ModBase
	SWISS-MODEL
	PDB Chain
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Davis CG. The many faces of epidermal growth factor repeats. New Biol. 2 410-9 1990 [PubMed: 2288911]
2.	Blomquist MC, Hunt LT, Barker WC. Vaccinia virus 19-kilodalton protein: relationship to several mammalian proteins, including two growth factors. Proc. Natl. Acad. Sci. U.S.A. 81 7363-7 1984 [PubMed: 6334307] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=6334307&action=stream&blobtype=pdf
3.	Hommel U, Harvey TS, Driscoll PC, Campbell ID. Human epidermal growth factor. High resolution solution structure and comparison with human transforming growth factor alpha. J. Mol. Biol. 227 271-82 1992 [PubMed: 1522591] http://dx.doi.org/10.1016/0022-2836(92)90697-I
4.	Doolittle RF, Feng DF, Johnson MS. Computer-based characterization of epidermal growth factor precursor. Nature 307 558-60 1984 [PubMed: 6607417] http://dx.doi.org/10.1038/307558a0
5.	Appella E, Weber IT, Blasi F. Structure and function of epidermal growth factor-like regions in proteins. FEBS Lett. 231 1-4 1988 [PubMed: 3282918] http://dx.doi.org/10.1016/0014-5793(88)80690-2
6.	Sorkin A. Internalization of the epidermal growth factor receptor: role in signalling. Biochem. Soc. Trans. 29 480-4 2001 [PubMed: 11498013] http://www.biochemsoctrans.org/bst/029/bst0290480.htm

Additional Reading Open in usermanual
	Tamkun JW, DeSimone DW, Fonda D, Patel RS, Buck C, Horwitz AF, Hynes RO. Structure of integrin, a glycoprotein involved in the transmembrane linkage between fibronectin and actin. Cell 46 1986 271-82 [PubMed: 3487386] http://dx.doi.org/10.1016/0092-8674(86)90744-0
	Huai Q, Zhou A, Lin L, Mazar AP, Parry GC, Callahan J, Shaw DE, Furie B, Furie BC, Huang M. Crystal structures of two human vitronectin, urokinase and urokinase receptor complexes. Nat. Struct. Mol. Biol. 15 2008 422-3 [PubMed: 18376415] http://dx.doi.org/10.1038/nsmb.1404
	Kwon HJ, Lagace TA, McNutt MC, Horton JD, Deisenhofer J. Molecular basis for LDL receptor recognition by PCSK9. Proc. Natl. Acad. Sci. U.S.A. 105 2008 1820-5 [PubMed: 18250299] http://dx.doi.org/10.1073/pnas.0712064105
	Lee YK, Parks DJ, Lu T, Thieu TV, Markotan T, Pan W, McComsey DF, Milkiewicz KL, Crysler CS, Ninan N, Abad MC, Giardino EC, Maryanoff BE, Damiano BP, Player MR. 7-fluoroindazoles as potent and selective inhibitors of factor Xa. J. Med. Chem. 51 2008 282-97 [PubMed: 18159923] http://dx.doi.org/10.1021/jm701217r
	Qiao JX, Cheney DL, Alexander RS, Smallwood AM, King SR, He K, Rendina AR, Luettgen JM, Knabb RM, Wexler RR, Lam PY. Achieving structural diversity using the perpendicular conformation of alpha-substituted phenylcyclopropanes to mimic the bioactive conformation of ortho-substituted biphenyl P4 moieties: discovery of novel, highly potent inhibitors of Factor Xa. Bioorg. Med. Chem. Lett. 18 2008 4118-23 [PubMed: 18550370] http://dx.doi.org/10.1016/j.bmcl.2008.05.095
	Bruckner K, Perez L, Clausen H, Cohen S. Glycosyltransferase activity of Fringe modulates Notch-Delta interactions. Nature 406 2000 411-5 [PubMed: 10935637] http://dx.doi.org/10.1038/35019075
	Corte JR, Fang T, Pinto DJ, Han W, Hu Z, Jiang XJ, Li YL, Gauuan JF, Hadden M, Orton D, Rendina AR, Luettgen JM, Wong PC, He K, Morin PE, Chang CH, Cheney DL, Knabb RM, Wexler RR, Lam PY. Structure-activity relationships of anthranilamide-based factor Xa inhibitors containing piperidinone and pyridinone P4 moieties. Bioorg. Med. Chem. Lett. 18 2008 2845-9 [PubMed: 18424044] http://dx.doi.org/10.1016/j.bmcl.2008.03.092

InterPro 24.0