FAP report

I. Expression across cell types

II. Expression across tissues

sc-RNAseq data

Insufficient scRNA-seq data for expression of FAP at tissue level.

III. Associated gene sets

GO_0001525Biological processangiogenesis
GO_0051917Biological processregulation of fibrinolysis
GO_1902362Biological processmelanocyte apoptotic process
GO_0007155Biological processcell adhesion
GO_0060244Biological processnegative regulation of cell proliferation involved in contact inhibition
GO_0043542Biological processendothelial cell migration
GO_0006508Biological processproteolysis
GO_0010710Biological processregulation of collagen catabolic process
GO_0051603Biological processproteolysis involved in protein catabolic process
GO_1903054Biological processnegative regulation of extracellular matrix organization
GO_0097325Biological processmelanocyte proliferation
GO_0010716Biological processnegative regulation of extracellular matrix disassembly
GO_1900119Biological processpositive regulation of execution phase of apoptosis
GO_0051726Biological processregulation of cell cycle
GO_0032587Cellular componentruffle membrane
GO_0045178Cellular componentbasal part of cell
GO_0005615Cellular componentextracellular space
GO_0005886Cellular componentplasma membrane
GO_0016020Cellular componentmembrane
GO_0005925Cellular componentfocal adhesion
GO_0009986Cellular componentcell surface
GO_0031258Cellular componentlamellipodium membrane
GO_0005737Cellular componentcytoplasm
GO_1905368Cellular componentpeptidase complex
GO_0030027Cellular componentlamellipodium
GO_0045177Cellular componentapical part of cell
GO_0042803Molecular functionprotein homodimerization activity
GO_0008233Molecular functionpeptidase activity
GO_0008239Molecular functiondipeptidyl-peptidase activity
GO_0004175Molecular functionendopeptidase activity
GO_0042802Molecular functionidentical protein binding
GO_0005178Molecular functionintegrin binding
GO_0002020Molecular functionprotease binding
GO_0008236Molecular functionserine-type peptidase activity
GO_0005515Molecular functionprotein binding
GO_0004252Molecular functionserine-type endopeptidase activity

IV. Literature review

[source]
Gene nameFAP
Protein nameFibroblast activation protein alpha
Prolyl endopeptidase FAP (EC 3.4.21.26) (170 kDa melanoma membrane-bound gelatinase) (Dipeptidyl peptidase FAP) (EC 3.4.14.5) (Fibroblast activation protein alpha) (FAPalpha) (Gelatine degradation protease FAP) (EC 3.4.21.-) (Integral membrane serine protease) (Post-proline cleaving enzyme) (Serine integral membrane protease) (SIMP) (Surface-expressed protease) (Seprase) [Cleaved into: Antiplasmin-cleaving enzyme FAP, soluble form (APCE) (EC 3.4.14.5) (EC 3.4.21.-) (EC 3.4.21.26)]
Fibroblast activation protein alpha (cDNA FLJ60298, highly similar to Seprase)
Synonyms
DescriptionFUNCTION: 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. .

AccessionsH0YG61
H7C4D9
B4DLR2
C9J131
ENST00000447386.5
ENST00000188790.9 [Q12884-1]
Q12884
F8WF29
ENST00000422436.5
ENST00000443424.5
ENST00000462608.5
ENST00000450031.2