Summary: Fibronectin type III domain
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Fibronectin type III domain Edit Wikipedia article
|The tenth type III domain of fibronectin|
The Fibronectin type III domain is an evolutionary conserved protein domain that is widely found in animal proteins. The fibronectin protein in which this domain was first identified contains 16 copies of this domain. The domain is about 100 amino acids long and possesses a beta sandwich structure. Fibronectin domains are found in a wide variety of extracellular proteins. They are widely distributed in animal species, but also found more sporadically in yeast, plant and bacterial proteins.
 Human proteins containing this domain
ABI3BP; ANKFN1; ASTN2; AXL; BOC; BZRAP1; C20orf75; CDON; CHL1; CMYA5; CNTFR; CNTN1; CNTN2; CNTN3; CNTN4; CNTN5; CNTN6; COL12A1; COL14A1; COL20A1; COL7A1; CRLF1; CRLF3; CSF2RB; CSF3R; DCC; DSCAM; DSCAML1; EBI3; EGFLAM; EPHA1; EPHA10; EPHA2; EPHA3; EPHA4; EPHA5; EPHA6; EPHA7; EPHA8; EPHB1; EPHB2; EPHB3; EPHB4; EPHB6; EPOR; FANK1; FLRT1; FLRT2; FLRT3; FN1; FNDC1; FNDC3A; FNDC3B; FNDC4; FNDC5; FNDC7; FNDC8; FSD1; FSD1L; FSD2; GHR; HCFC1; HCFC2; HUGO; IFNGR2; IGF1R; IGSF22; IGSF9; IGSF9B; IL11RA; IL12B; IL12RB1; IL12RB2; IL20RB; IL23R; IL27RA; IL31RA; IL6R; IL6ST; IL7R; INSR; INSRR; ITGB4; Il6ST; KAL1; KALRN; L1CAM; LEPR; LIFR; LRFN2; LRFN3; LRFN4; LRFN5; LRIT1; LRRN1; LRRN3; MERTK; MID1; MID2; MPL; MYBPC1; MYBPC2; MYBPC3; MYBPH; MYBPHL; MYLK; MYOM1; MYOM2; MYOM3; NCAM1; NCAM2; NEO1; NFASC; NOPE; NPHS1; NRCAM; OBSCN; OBSL1; OSMR; PHYHIP; PHYHIPL; PRLR; PRODH2; PTPRB; PTPRC; PTPRD; PTPRF; PTPRG; PTPRH; PTPRJ; PTPRK; PTPRM; PTPRO; PTPRS; PTPRT; PTPRU; PTPRZ1; PTPsigma; PUNC; RIMBP2; ROBO1; ROBO2; ROBO3; ROBO4; ROS1; SDK1; SDK2; SNED1; SORL1; SPEG; TEK; TIE1; TNC; TNN; TNR; TNXB; TRIM36; TRIM42; TRIM46; TRIM67; TRIM9; TTN; TYRO3; UMODL1; USH2A; VASN; VWA1; dJ34F7.1; fmi;
 See also
- Monobody, an engineered antibody mimetic based on the structure of the fibronectin type III domain
- Bazan, J. F. (1990). "Structural design and molecular evolution of a cytokine receptor superfamily". Proceedings of the National Academy of Sciences of the United States of America 87 (18): 6934–6938. PMC 54656. PMID 2169613. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=54656.
- Little, E.; Bork, P.; Doolittle, R. F. (1994). "Tracing the spread of fibronectin type III domains in bacterial glycohydrolases". Journal of molecular evolution 39 (6): 631–643. PMID 7528812.
- Kornblihtt, A. R.; Umezawa, K.; Vibe-Pedersen, K.; Baralle, F. E. (1985). "Primary structure of human fibronectin: Differential splicing may generate at least 10 polypeptides from a single gene". The EMBO journal 4 (7): 1755–1759. PMC 554414. PMID 2992939. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=554414.
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Fibronectin type III domain Provide feedback
No Pfam abstract.
Kornblihtt AR, Umezawa K, Vibe-Pedersen K, Baralle FE; , EMBO J 1985;4:1755-1759.: Primary structure of human fibronectin: differential splicing may generate at least 10 polypeptides from a single gene. PUBMED:2992939 EPMC:2992939
Internal database links
|Similarity to PfamA using HHSearch:||Tissue_fac Interfer-bind|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR003961
Fibronectins are multi-domain glycoproteins found in a soluble form in plasma, and in an insoluble form in loose connective tissue and basement membranes [PUBMED:3780752]. They contain multiple copies of 3 repeat regions (types I, II and III), which bind to a variety of substances including heparin, collagen, DNA, actin, fibrin and fibronectin receptors on cell surfaces. The wide variety of these substances means that fibronectins are involved in a number of important functions: e.g., wound healing; cell adhesion; blood coagulation; cell differentiation and migration; maintenance of the cellular cytoskeleton; and tumour metastasis [PUBMED:3031656]. The role of fibronectin in cell differentiation is demonstrated by the marked reduction in the expression of its gene when neoplastic transformation occurs. Cell attachment has been found to be mediated by the binding of the tetrapeptide RGDS to integrins on the cell surface [PUBMED:2466295], although related sequences can also display cell adhesion activity.
Plasma fibronectin occurs as a dimer of 2 different subunits, linked together by 2 disulphide bonds near the C terminus. The difference in the 2 chains occurs in the type III repeat region and is caused by alternative splicing of the mRNA from one gene [PUBMED:3780752]. The observation that, in a given protein, an individual repeat of one of the 3 types (e.g., the first FnIII repeat) shows much less similarity to its subsequent tandem repeats within that protein than to its equivalent repeat between fibronectins from other species, has suggested that the repeating structure of fibronectin arose at an early stage of evolution. It also seems to suggest that the structure is subject to high selective pressure [PUBMED:6317187].
The fibronectin type III repeat region is an approximately 100 amino acid domain, different tandem repeats of which contain binding sites for DNA, heparin and the cell surface [PUBMED:3780752]. The superfamily of sequences believed to contain FnIII repeats represents 45 different families, the majority of which are involved in cell surface binding in some manner, or are receptor protein tyrosine kinases, or cytokine receptors.
|Molecular function||protein binding (GO:0005515)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
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Curation and family details
|Number in seed:||106|
|Number in full:||58087|
|Average length of the domain:||84.30 aa|
|Average identity of full alignment:||20 %|
|Average coverage of the sequence by the domain:||23.88 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||16|
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There are 10 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the fn3 domain has been found. There are 274 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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