FAP 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, vibronectin, tenascin, laminin, fibronectin, fibrin or casein. Have also 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. Belongs to the peptidase S9B family. Expressed in adipose tissue. Expressed in the dermal fibroblasts in the fetal skin. Expressed in the granulation tissue of healing wounds and on reactive stromal fibroblast in epithelial cancers. Expressed in activated fibroblast-like synoviocytes from inflamed synovial tissues. Expressed in activated hepatic stellate cells (HSC) and myofibroblasts from cirrhotic liver, but not detected in normal liver. Expressed in glioma cells (at protein level). Expressed in glioblastomas and glioma cells. Isoform 1 and isoform 2 are expressed in melanoma, carcinoma and fibroblast cell lines. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: EC 3.4.14.5; EC 3.4.21.26; Membrane protein, integral; Protease
Chromosomal Location of Human Ortholog: 2q24.2
Cellular Component:  apical part of cell; basal part of cell; cell surface; cytoplasm; extracellular space; integral component of membrane; invadopodium membrane; lamellipodium; lamellipodium membrane; plasma membrane; ruffle membrane
Molecular Function:  dipeptidyl-peptidase activity; endopeptidase activity; integrin binding; metalloendopeptidase activity; peptidase activity; protease binding; protein binding; protein dimerization activity; protein homodimerization activity; serine-type endopeptidase activity; serine-type peptidase activity
Biological Process:  angiogenesis; cell adhesion; endothelial cell migration; melanocyte apoptotic process; melanocyte proliferation; mitotic cell cycle arrest; negative regulation of cell proliferation involved in contact inhibition; negative regulation of extracellular matrix disassembly; negative regulation of extracellular matrix organization; positive regulation of cell cycle arrest; positive regulation of execution phase of apoptosis; proteolysis; proteolysis involved in cellular protein catabolic process; regulation of collagen catabolic process; regulation of fibrinolysis
Reference #:  Q12884 (UniProtKB)
Alt. Names/Synonyms: 170 kDa melanoma membrane-bound gelatinase; Antiplasmin-cleaving enzyme FAP, soluble form; APCE; Dipeptidyl peptidase FAP; DKFZp686G13158; DPPIV; FAP; FAPA; FAPalpha; Fibroblast activation protein alpha; fibroblast activation protein, alpha; fibroblast activation protein, alpha subunit; Gelatine degradation protease FAP; Integral membrane serine protease; Post-proline cleaving enzyme; Prolyl endopeptidase FAP; SEPR; Seprase; Serine integral membrane protease; SIMP; Surface-expressed protease
Gene Symbols: FAP
Molecular weight: 87,713 Da
Basal Isoelectric point: 6.21  Predict pI for various phosphorylation states
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
Select Structure to View Below

FAP

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  cBioPortal  |  Wikipedia  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene