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- Table of Contents
Facts about Prolyl endopeptidase FAP.
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 (PubMed:10347120, PubMed:10593948, PubMed:16175601, PubMed:16223769, PubMed:16651416, PubMed:16410248, PubMed:17381073, PubMed:21314817, PubMed:24371721, PubMed:24717288). Natural neuropeptide hormones such as dipeptidyl peptidase would be the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB) (PubMed:21314817).
Human | |
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Gene Name: | FAP |
Uniprot: | Q12884 |
Entrez: | 2191 |
Belongs to: |
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peptidase S9B family |
170 kDa melanoma membrane-bound gelatinase; DKFZp686G13158; DPPIV; EC 3.4.21.-; FAP; FAPA; Fibroblast Activation Protein alpha; fibroblast activation protein, alpha; Integral membrane serine protease; Seprase; vibronectin
Mass (kDA):
87.713 kDA
Human | |
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Location: | 2q24.2 |
Sequence: | 2; NC_000002.12 (162170684..162243472, complement) |
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.
[Prolyl endopeptidase FAP]: Cell surface. Cell membrane; Single-pass type II membrane protein. Cell projection, lamellipodium membrane; Single-pass type II membrane protein. Cell projection, invadopodium membrane; Single-pass type II membrane protein. Cell projection, ruffle membrane; Single-pass type II membrane protein. Membrane; Single-pass type II membrane protein. Localized on cell surface with lamellipodia and invadopodia membranes and on shed vesicles. Colocalized with DPP4 at invadopodia and lamellipodia membranes of migratory activated endothelial cells in collagenous matrix. Colocali
PMID: 7911242 by Scanlan M.J., et al. Molecular cloning of fibroblast activation protein alpha, a member of the serine protease family selectively expressed in stromal fibroblasts of epithelial cancers.
PMID: 9247085 by Goldstein L.A., et al. Molecular cloning of seprase: a serine integral membrane protease from human melanoma.
*More publications can be found for each product on its corresponding product page