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InterPro: IPR008957 Fibronectin, type III-like fold
Protein matches
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UniProtKB Matches: 8664 proteins |
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Accession
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IPR008957 Fibronectin_typ-III-like_fold |
Type
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Domain |
Signatures
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InterPro Relationships
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Children
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IPR003961 Fibronectin, type III
IPR019482 Interleukin-12, beta subunit, central domain
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Found in
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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
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Contains
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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
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InterPro annotation
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Entry Details in BioMart
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Abstract
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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].
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Structural links
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Example proteins
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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 |
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| IPR001251 |
Cellular retinaldehyde-binding/triple function, C-terminal |
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| IPR000998 |
MAM |
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| IPR017441 |
Protein kinase, ATP binding site |
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| IPR017442 |
Serine/threonine-protein kinase-like domain |
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| IPR013098 |
Immunoglobulin I-set |
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| IPR007850 |
RCSD |
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| IPR016130 |
Protein-tyrosine phosphatase, active site |
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| IPR011009 |
Protein kinase-like domain |
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| IPR008957 |
Fibronectin, type III-like fold |
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| IPR018159 |
Spectrin/alpha-actinin |
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| IPR000719 |
Protein kinase, catalytic domain |
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| IPR002290 |
Serine/threonine-protein kinase domain |
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| IPR001357 |
BRCT |
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| IPR000242 |
Protein-tyrosine phosphatase, receptor/non-receptor type |
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| IPR011511 |
Variant SH3 |
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| IPR003961 |
Fibronectin, type III |
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| IPR002017 |
Spectrin repeat |
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| IPR011993 |
Pleckstrin homology-type |
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| IPR007110 |
Immunoglobulin-like |
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| IPR003598 |
Immunoglobulin subtype 2 |
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| IPR003599 |
Immunoglobulin subtype |
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| IPR001849 |
Pleckstrin homology |
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| IPR000219 |
Dbl homology (DH) domain |
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| IPR000387 |
Dual-specific/protein-tyrosine phosphatase, conserved region |
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| IPR001452 |
Src homology-3 domain |
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| IPR013151 |
Immunoglobulin |
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| IPR008271 |
Serine/threonine-protein kinase, active site |
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| IPR009134 |
Tyrosine-protein kinase, vascular endothelial growth factor receptor (VEGFR), N-terminal |
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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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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
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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
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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
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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
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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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