Search results for HGFAC

Showing 5 results out of 5

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Species

Types

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Species

Types

Compartments

Reaction types

Search properties

Protein (2 results from a total of 2)

Identifier: R-HSA-1641473
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: HGFAC: Q04756
Identifier: R-HSA-6800283
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: Q04756

Complex (1 results from a total of 1)

Identifier: R-HSA-6800311
Species: Homo sapiens
Compartment: extracellular region

Reaction (1 results from a total of 1)

Identifier: R-HSA-6800299
Species: Homo sapiens
Compartment: extracellular region, plasma membrane
HGF is a pleiotropic factor and activates hepatocyte growth factor receptor (MET), a proto-oncogenic receptor tyrosine kinase. HGF is secreted into the extracellular matrix as an inactive single chain precursor (pro-HGF (32-728)) and requires cleavage at Arg494–Val495 to form the biologically active alpha-beta heterodimer. Hepatocyte growth factor activator (HGFAC, commonly known as HGFA) is a serine protease that converts HGF into its active form (Shia et al. 2005). The Kunitz-type protease inhibitor 1 (SPINT1, aka HAI1) is an inhibitor of HGFAC activity (Shia et al. 2005).

Pathway (1 results from a total of 1)

Identifier: R-HSA-6806942
Species: Homo sapiens
Hepatocyte growth factor (HGF), the ligand for MET receptor tyrosine kinase (RTK), is secreted into the extracellular matrix (ECM) as an inactive single chain precursor (pro-HGF). The biologically active HGF is the heterodimer of alpha and beta chains that are produced via proteolytic cleavage of pro-HGF by the plasma membrane bound serine protease Hepsin (HPN) (Kirchhofer et al. 2005, Owen et al. 2010) or the ECM-associated serine protease Hepatocyte growth factor activator (HGFAC, commonly known as HGFA) (Shia et al. 2005). HGF binds to the extracellular SEMA and PSI domains of MET RTK, inducing a conformational change that enables MET dimerization or oligomerization (Kirchhofer et al. 2004, Stamos et al. 2004, Hays and Watowich 2004, Gherardi et al. 2006). MET dimers trans-autophosphorylate on tyrosine residues in the activation loop, leading to increased kinase activity, and on tyrosine residues at the cytoplasmic tail that serve as docking sites for adapter proteins involved in MET signal transduction (Ferracini et al. 1991, Longati et al. 1994, Rodrigues and Park 1994, Ponzetto et al. 1994).
CD44v6 was implicated as a MET co-receptor, but its role has been disputed (Orian-Rousseau et al. 2002, Dortet et al. 2010, Olaku et al. 2011, Hasenauer et al. 2013, Elliot et al. 2014).
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