FAP — Fibroblast activation protein alpha
FAP belongs to a gene co-expression module in 2 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.
FAP's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Endothelial | Endothelial Membrane Transport Endothelial cell development | AQP1, CDH24, CEBPG, CLIC5, LSM6, OIT3, OSTF1, RAVER2 +9 more | View in SCUBA |
| Fibroblasts | Activated Myofibroblast State Wound healing | BGN, BMP1, CPXM1, CTHRC1, EGFL6, KIAA0930, MASP1, OLFML2B +7 more | View in SCUBA |
About the gene
| Synonyms | DPPIV |
|---|---|
| Chromosome | 2: 162170684-162245151 |
| Predicted location | Intracellular, Secreted |
| Essential gene | No |
| Protein class | Cancer-related genes, Enzymes, Plasma proteins, Predicted intracellular proteins, Predicted secreted proteins |
| Molecular function | Hydrolase, Protease, Serine protease |
| Biological process | Angiogenesis, Apoptosis, Cell adhesion |
Function
Cell surface glycoprotein 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, vitronectin, tenascin, laminin, fibronectin, fibrin or casein. Also has dipeptidyl peptidase activity, exhibiting the ability to 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), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB). The plasma membrane form, in association with either DPP4, PLAUR or integrins, is involved in the pericellular proteolysis of the extracellular matrix (ECM), and hence promotes cell adhesion, migration and invasion through the ECM. Plays a role in tissue remodeling during development and wound healing. Participates in the cell invasiveness towards the ECM in malignant melanoma cancers. Enhances tumor growth progression by increasing angiogenesis, collagen fiber degradation and apoptosis and by reducing antitumor response of the immune system. 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.
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.