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InterPro: IPR008957 Fibronectin, type III-like fold

Protein matchesHelp
UniProtKB
Matches:
8664 proteins
AccessionHelp IPR008957 Fibronectin_typ-III-like_fold
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Children IPR003961 Fibronectin, type III
IPR019482 Interleukin-12, beta subunit, central domain
Found in IPR001187 Tissue factor
IPR006987 Poxvirus interferon gamma receptor
IPR008355 Interferon gamma receptor alpha subunit
IPR015713 Interleukin-20 receptor, alpha subunit
IPR015725 Myosin light chain kinase
IPR015726 Serine/threonine protein kinase, striated muscle-specific
IPR015775 Tyrosine-protein kinase, receptor Axl-related
IPR015781 Tyrosine-protein kinase, angiopoietin receptor
IPR016246 Tyrosine-protein kinase, insulin-like receptor
IPR016257 Tyrosine-protein kinase, ephrin receptor
IPR016354 Tissue factor/coagulation factor III
IPR019472 Interleukin-10-like receptor, alpha subunit
IPR020424 Interleukin-12, beta subunit, central region
IPR020682 Obscurin/Myosin light chain kinase
IPR020694 Tyrosine-protein kinase, ephrin receptor, subgroup
IPR020696 Tyrosine-protein kinase, receptor Tie-1
IPR020704 Tyrosine-protein kinase, receptor TYRO3, Zebrafish
IPR020705 Tyrosine-protein kinase, receptor MER
IPR020710 Tyrosine-protein kinase, insulin receptor
IPR020712 Tyrosine-protein kinase, insulin-related receptor
IPR020713 Tyrosine-protein kinase, insulin-like receptor, Drosphila
IPR020714 Tyrosine-protein kinase, insulin-like growth factor receptor
IPR020738 Tyrosine-protein kinase, receptor ROS/Sevenless
IPR020741 Tyrosine-protein kinase, receptor TYRO3
IPR020766 Tyrosine-protein kinase, ephrin A10 receptor
IPR020767 Tyrosine-protein kinase, ephrin B6 receptor
IPR020768 Tyrosine-protein kinase, ephrin A receptor
IPR020769 Tyrosine-protein kinase, ephrin B receptor
IPR020770 Tyrosine-protein kinase, ephrin A1/A2 receptor
IPR020772 Tyrosine-protein kinase, receptor Daf-2
Contains IPR003528 Long hematopoietin receptor, single chain, conserved site
IPR003529 Long hematopoietin receptor, gp130 family 2, conserved site
IPR003530 Long hematopoietin receptor, soluble alpha chain, conserved site
IPR003531 Short hematopoietin receptor, family 1, conserved site
IPR003532 Short hematopoietin receptor, family 2, conserved site
IPR010457 Immunoglobulin C2-set-like, ligand-binding
IPR015152 Erythropoietin receptor, ligand binding
IPR015319 Interleukin-4 receptor alpha chain, N-terminal
IPR015321 Interleukin-6 receptor alpha chain, binding
IPR015373 Interferon alpha/beta receptor, beta chain
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Fibronectin is composed of three repeating structural motifs, of which one is the fibronectin III (FnIII) module. The three modules form a linear sequence of multiple tandem copies connected by short linker peptides. The secondary structure of the FnIII10 module, which is the only fibronectin module to possess an integrin binding RGD motif, consists of two beta-sheets containing the antiparallel beta-strands ABE and DCFG, respectively, which fold up to form a beta-sandwich. The RGD sequence is located in the loop connecting the beta-strands [1].

Structural linksHelp
PDB - click here

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR008957 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
A2CG49 Kalirin

O01761 Muscle M-line assembly protein unc-89

O14522 Receptor-type tyrosine-protein phosphatase T

P20241 Neuroglian

Q12114 Chitin biosynthesis protein CHS5

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR013783 Immunoglobulin-like fold
IPR001251 Cellular retinaldehyde-binding/triple function, C-terminal
IPR000998 MAM
IPR017441 Protein kinase, ATP binding site
IPR017442 Serine/threonine-protein kinase-like domain
IPR013098 Immunoglobulin I-set
IPR007850 RCSD
IPR016130 Protein-tyrosine phosphatase, active site
IPR011009 Protein kinase-like domain
IPR008957 Fibronectin, type III-like fold
IPR018159 Spectrin/alpha-actinin
IPR000719 Protein kinase, catalytic domain
IPR002290 Serine/threonine-protein kinase domain
IPR001357 BRCT
IPR000242 Protein-tyrosine phosphatase, receptor/non-receptor type
IPR011511 Variant SH3
IPR003961 Fibronectin, type III
IPR002017 Spectrin repeat
IPR011993 Pleckstrin homology-type
IPR007110 Immunoglobulin-like
IPR003598 Immunoglobulin subtype 2
IPR003599 Immunoglobulin subtype
IPR001849 Pleckstrin homology
IPR000219 Dbl homology (DH) domain
IPR000387 Dual-specific/protein-tyrosine phosphatase, conserved region
IPR001452 Src homology-3 domain
IPR013151 Immunoglobulin
IPR008271 Serine/threonine-protein kinase, active site
IPR009134 Tyrosine-protein kinase, vascular endothelial growth factor receptor (VEGFR), N-terminal
ModBase
SWISS-MODEL
PDB Chain
CATH Domain
SCOP Domain

PublicationsHelp
1. Krammer A, Lu H, Isralewitz B, Schulten K, Vogel V.
Forced unfolding of the fibronectin type III module reveals a tensile molecular recognition switch.
Proc. Natl. Acad. Sci. U.S.A. 96 1351-6 1999 [PubMed: 9990027]
http://dx.doi.org/10.1073/pnas.96.4.1351

Additional ReadingHelp
Lupardus PJ, Garcia KC.
The structure of interleukin-23 reveals the molecular basis of p40 subunit sharing with interleukin-12.
J. Mol. Biol. 382 2008 931-41 [PubMed: 18680750]
http://dx.doi.org/10.1016/j.jmb.2008.07.051
Beyer BM, Ingram R, Ramanathan L, Reichert P, Le HV, Madison V, Orth P.
Crystal structures of the pro-inflammatory cytokine interleukin-23 and its complex with a high-affinity neutralizing antibody.
J. Mol. Biol. 382 2008 942-55 [PubMed: 18708069]
http://dx.doi.org/10.1016/j.jmb.2008.08.001
Carafoli F, Saffell JL, Hohenester E.
Structure of the tandem fibronectin type 3 domains of neural cell adhesion molecule.
J. Mol. Biol. 377 2008 524-34 [PubMed: 18261743]
http://dx.doi.org/10.1016/j.jmb.2008.01.030
Svensson LA, Bondensgaard K, Norskov-Lauritsen L, Christensen L, Becker P, Andersen MD, Maltesen MJ, Rand KD, Breinholt J.
Crystal structure of a prolactin receptor antagonist bound to the extracellular domain of the prolactin receptor.
J. Biol. Chem. 283 2008 19085-94 [PubMed: 18467331]
http://dx.doi.org/10.1074/jbc.M801202200
LaPorte SL, Juo ZS, Vaclavikova J, Colf LA, Qi X, Heller NM, Keegan AD, Garcia KC.
Molecular and structural basis of cytokine receptor pleiotropy in the interleukin-4/13 system.
Cell 132 2008 259-72 [PubMed: 18243101]
http://dx.doi.org/10.1016/j.cell.2007.12.030
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InterPro 23.1