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InterPro: IPR013032 EGF-like region, conserved site
Protein matches
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UniProtKB Matches: 6878 proteins |
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Accession
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IPR013032 EGF-like_reg_CS |
Secondary
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IPR000561
,
IPR006209
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Type
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Conserved_site |
Signatures
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InterPro Relationships
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Found in
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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
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InterPro annotation
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Entry Details in BioMart
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Abstract
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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.
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Structural links
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Database links
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Example proteins
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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 |
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| IPR013091 |
EGF calcium-binding |
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| IPR001254 |
Peptidase S1/S6, chymotrypsin/Hap |
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| IPR000800 |
Notch domain |
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| IPR000859 |
CUB |
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| IPR006210 |
EGF-like |
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| IPR008297 |
Notch |
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| IPR017871 |
ABC transporter, conserved site |
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| IPR009003 |
Serine/cysteine peptidase, trypsin-like |
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| IPR011656 |
Notch, NODP domain |
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| IPR016060 |
Complement control module |
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| IPR013032 |
EGF-like region, conserved site |
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| IPR018114 |
Peptidase S1/S6, chymotrypsin/Hap, active site |
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| IPR002110 |
Ankyrin repeat |
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| IPR018097 |
EGF-like calcium-binding, conserved site |
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| IPR001881 |
EGF-like calcium-binding |
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| IPR016317 |
Pro-epidermal growth factor |
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| IPR003593 |
ATPase, AAA+ type, core |
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| IPR010660 |
Notch, NOD domain |
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| IPR003439 |
ABC transporter-like |
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| IPR020683 |
Ankyrin repeat-containing domain |
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| IPR011042 |
Six-bladed beta-propeller, TolB-like |
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| IPR000033 |
Low-density lipoprotein receptor, class B (YWTD) repeat |
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| IPR001438 |
EGF-like, type 2 |
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| IPR000152 |
EGF-type aspartate/asparagine hydroxylation site |
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| IPR000742 |
EGF-like, type 3 |
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| IPR001336 |
EGF, type 1 |
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| IPR000436 |
Sushi/SCR/CCP |
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| IPR001314 |
Peptidase S1A, chymotrypsin |
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ModBase |
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SWISS-MODEL |
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PDB Chain |
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CATH Domain |
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SCOP Domain |
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Additional Reading
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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
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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
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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
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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
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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
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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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