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InterPro: IPR013032 EGF-like region, conserved site

Protein matchesHelp
UniProtKB
Matches:
6878 proteins
AccessionHelp IPR013032 EGF-like_reg_CS
SecondaryHelp IPR000561 , IPR006209
TypeHelp Conserved_site
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR000742 EGF-like, type 3
IPR001169 Integrin beta subunit, C-terminal
IPR001336 EGF, type 1
IPR001438 EGF-like, type 2
IPR001491 Thrombomodulin
IPR001881 EGF-like calcium-binding
IPR002049 EGF-like, laminin
IPR006210 EGF-like
IPR008297 Notch
IPR010423 Plasmodium ookinete surface Pvs28
IPR011170 Growth factor, vaccinia C11R type
IPR011398 Fibrillin
IPR012012 Integrin beta subunit, subgroup
IPR012013 Integrin beta-4 subunit
IPR012111 Hemolectin/hemocytin
IPR012224 Peptidase S1A, coagulation factor VII/IX/X/C/Z
IPR013091 EGF calcium-binding
IPR013111 EGF, extracellular
IPR014394 Coagulation factor XII/hepatocyte growth factor activator
IPR015149 Thrombomodulin-like, EGF-like
IPR015435 Integrin beta-3 subunit, C-terminal
IPR015437 Integrin beta-7 subunit, C-terminal
IPR015440 Integrin beta-nu subunit, C-terminal
IPR015442 Integrin beta-8 subunit-like, C-terminal
IPR015446 Bone morphogenetic protein 1/tolloid-like protein
IPR015455 Thrombospondin, type 2
IPR015497 Epidermal growth factor receptor ligand
IPR015781 Tyrosine-protein kinase, angiopoietin receptor
IPR015812 Integrin beta subunit
IPR016316 Complement component C1q/Thrombomodulin
IPR016317 Pro-epidermal growth factor
IPR016348 L-selectin
IPR017047 Teratocarcinoma-derived growth factor Cripto
IPR017048 Fibulin-1
IPR017050 Peptidase M12A, astacin, nematode
IPR017369 SPAN protein/blastula protease 10
IPR017430 Glycoside hydrolase, family 56, Hyaluronidase
IPR020696 Tyrosine-protein kinase, receptor Tie-1
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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] to be present, in a more or less conserved form, in a large number of other, mostly animal proteins. The list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied. 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 linksHelp
PDB - click here
Database linksHelp
PDBe-motif: PS00022 , PS01186
PROSITE doc: PDOC00021

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR013032 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O00187 Mannan-binding lectin serine protease 2

P01132 Pro-epidermal growth factor

P07207 Neurogenic locus Notch protein

P14585 Protein lin-12

P25371 Probable ATP-dependent permease

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR013525 ABC-2 type transporter
IPR013091 EGF calcium-binding
IPR001254 Peptidase S1/S6, chymotrypsin/Hap
IPR000800 Notch domain
IPR000859 CUB
IPR006210 EGF-like
IPR008297 Notch
IPR017871 ABC transporter, conserved site
IPR009003 Serine/cysteine peptidase, trypsin-like
IPR011656 Notch, NODP domain
IPR016060 Complement control module
IPR013032 EGF-like region, conserved site
IPR018114 Peptidase S1/S6, chymotrypsin/Hap, active site
IPR002110 Ankyrin repeat
IPR018097 EGF-like calcium-binding, conserved site
IPR001881 EGF-like calcium-binding
IPR016317 Pro-epidermal growth factor
IPR003593 ATPase, AAA+ type, core
IPR010660 Notch, NOD domain
IPR003439 ABC transporter-like
IPR020683 Ankyrin repeat-containing domain
IPR011042 Six-bladed beta-propeller, TolB-like
IPR000033 Low-density lipoprotein receptor, class B (YWTD) repeat
IPR001438 EGF-like, type 2
IPR000152 EGF-type aspartate/asparagine hydroxylation site
IPR000742 EGF-like, type 3
IPR001336 EGF, type 1
IPR000436 Sushi/SCR/CCP
IPR001314 Peptidase S1A, chymotrypsin
ModBase
SWISS-MODEL
PDB Chain
CATH Domain
SCOP Domain

PublicationsHelp
1. Campbell ID, Bork P.
Epidermal growth factor-like modules.
Curr. Opin. Struct. Biol. 3 385-92 1993
2. 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
3. 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
4. Davis CG.
The many faces of epidermal growth factor repeats.
New Biol. 2 410-9 1990 [PubMed: 2288911]
5. 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

Additional ReadingHelp
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
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
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
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
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InterPro 24.0