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Gene_locus Report for: human-FAP

Name Class
human-FAPName Homo sapiens (Human) fibroblast activation protein alpha FAPalpha, integral membrane serine protease seprase FAPA, FAP, SEPR
SpeciesHomo sapiens
Organismman
Gene_nameFAPA
FAP
SEPRASE
BlockX
FamilyDPP4N_Peptidase_S9
Database (13)
Paper (12)
CommentFibroblast activation protein (FAP). However, FAP is not expressed in normal fibroblasts, normal or malignant epithelial cells, or the stroma of benign epithelial tumors. FAP is a cell membrane-bound serine peptidase overexpressed on the surface of cancer-associated fibroblasts. Serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenascin, laminin, fibronectin, fibrin or casein. FAP can hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro. Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY cleavage product proangiogenic FAP enhances tumor growth progression), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB). Promotes glioma cell invasion through the brain parenchyma by degrading the proteoglycan brevican. Acts as a tumor suppressor in melanocytic cells through regulation of cell proliferation and survival in a serine protease activity-independent manner
Proteinhuman-FAP
Peptidehuman-FAP
Structure6Y0F
1Z68
Inhibitor (11)
SubstrateZ-Gly-Pro-AMC
Tree_nodeDPP4N_Peptidase_S9170601
Peptidase_S9281115
Structure299322
OldTremblQ99998
Q86Z29

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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