SMART: Pfam domain fn1

The domain within your query sequence starts at position 199 and ends at position 234; the E-value for the fn1 domain shown below is 7.7e-11.

CFDETRYEYFEVGDHWARVSEGHVEQCGCMEGQARC

fn1

PFAM accession number:	PF00039
Interpro abstract (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.
GO component:	extracellular region (GO:0005576)

PFAM accession number:

PF00039

Interpro abstract (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.

GO component:

extracellular region (GO:0005576)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry fn1