Summary: Fibronectin type I domain
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This is the Wikipedia entry entitled "Fibronectin type I domain". More...
Fibronectin type I domain Edit Wikipedia article
| Fibronectin, type I | |||||||||
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| Identifiers | |||||||||
| Symbol | Fibrnctn1 | ||||||||
| Pfam | PF00039 | ||||||||
| InterPro | IPR000083 | ||||||||
| SMART | SM00058 | ||||||||
| PROSITE | PDOC00965 | ||||||||
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Fibronectin, type I repeats are one of the three repeats found in the fibronectin protein. Fibronectin is a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Type I domain (FN1) is approximately 40 residues in length. Four conserved cysteines are involved in disulfide bonds. The 3D structure of the FN1 domain has been determined.[1][2][3] It consists of two antiparallel beta-sheets, first a double-stranded one, that is linked by a disulfide bond to a triple-stranded beta-sheet. The second conserved disulfide bridge links the C-terminal adjacent strands of the domain.
In human tissue plasminogen activator chain A the FN1 domain together with the following epidermal growth factor (EGF)-like domain are involved in fibrin-binding.[4] It has been suggested that these two modules form a single structural and functional unit.[3] The two domains keep their specific tertiary structure, but interact intimately to bury a hydrophobic core; the inter-module linker makes up the third strand of the EGF-module's major beta-sheet.
[edit] Human proteins containing this domain
[edit] References
- ^ Campbell ID, Baron M, Norman D, Willis A (1990). "Structure of the fibronectin type 1 module". Nature 345 (6276): 642â646. doi:10.1038/345642a0. PMID 2112232.
- ^ Driscoll PC, Harvey TS, Campbell ID, Baron M, Dudgeon TJ, Downing AK, Smith BO (1992). "Solution structure of the fibrin binding finger domain of tissue-type plasminogen activator determined by 1H nuclear magnetic resonance". J. Mol. Biol. 225 (3): 821â833. doi:10.1016/0022-2836(92)90403-7. PMID 1602484.
- ^ a b Driscoll PC, Campbell ID, Dudgeon TJ, Downing AK, Smith BO (1995). "The solution structure and backbone dynamics of the fibronectin type I and epidermal growth factor-like pair of modules of tissue-type plasminogen activator". Structure 3 (8): 823â833. doi:10.1016/S0969-2126(01)00217-9. PMID 7582899.
- ^ Bennett WF, Paoni NF, Keyt BA, Botstein D, Presta L, Wurm FM, Zoller MJ, Jones AJ (1991). "High resolution analysis of functional determinants on human tissue-type plasminogen activator". J. Biol. Chem. 266 (8): 5191â5201. PMID 1900516.
This article incorporates text from the public domain Pfam and InterPro IPR000083
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
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No Pfam abstract.
Literature references
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Baron M, Norman D, Willis A, Campbell ID; , Nature 1990;345:642-646.: Structure of the fibronectin type 1 module. PUBMED:2112232 EPMC:2112232
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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
External database links
| HOMSTRAD: | FN1 |
| PANDIT: | PF00039 |
| PRINTS: | PR00012 |
| Pseudofam: | PF00039 |
| SCOP: | 1tpm |
| SYSTERS: | fn1 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR000083
Fibronectin type I repeats are one of the three repeats found in the fibronectin protein. Fibronectin is a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Type I domain (FN1) is approximately 40 residues in length. Four conserved cysteines are involved in disulphide bonds. The 3D structure of the FN1 domain has been determined [PUBMED:2112232, PUBMED:1602484, PUBMED:7582899]. It consists of two antiparallel beta-sheets, first a double-stranded one, that is linked by a disulphide bond to a triple-stranded beta-sheet. The second conserved disulphide bridge links the C-terminal adjacent strands of the domain.
In human tissue plasminogen activator chain A the FN1 domain together with the following epidermal growth factor (EGF)-like domain are involved in fibrin-binding [PUBMED:1900516]. It has been suggested that these two modules form a single structural and functional unit [PUBMED:7582899]. The two domains keep their specific tertiary structure, but interact intimately to bury a hydrophobic core; the inter-module linker makes up the third strand of the EGF-module's major beta-sheet.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Cellular component | extracellular region (GO:0005576) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
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| Seed (20) |
Full (1772) |
Representative proteomes | NCBI (1849) |
Meta (0) |
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| RP15 (20) |
RP35 (53) |
RP55 (138) |
RP75 (393) |
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| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
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| Seed (20) |
Full (1772) |
Representative proteomes | NCBI (1849) |
Meta (0) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (20) |
RP35 (53) |
RP55 (138) |
RP75 (393) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Swissprot_feature_table |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Sonnhammer ELL |
| Number in seed: | 20 |
| Number in full: | 1772 |
| Average length of the domain: | 38.10 aa |
| Average identity of full alignment: | 42 % |
| Average coverage of the sequence by the domain: | 17.20 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 39 | ||||||||||||
| Family (HMM) version: | 13 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Structures
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 fn1 domain has been found. There are 70 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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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence