FAP
entrez
2191
canonical
uniprot
Q12884
canonical
ensembl
ENSG00000078098
resolver
ensp
ENSP00000188790
resolver
ensp
ENSP00000411391
resolver
ensp
ENSP00000781559
resolver
enst
ENST00000443424
resolver
genesymbol
FAP
resolver
hgnc
HGNC:3590
resolver
uniprot
B4DLR2
resolver
uniprot
F6V7M8
resolver
uniprot
O00199
resolver
uniprot
Q53TP5
resolver
uniprot
Q86Z29
resolver
uniprot
Q99998
resolver
uniprot
Q9UID4
resolver
uniprot_entry
B4DLR2_HUMAN
resolver
uniprot_entry
F6V7M8_HUMAN
resolver
uniprot_entry
SEPR_HUMAN
resolver
uniprot_sec
O00199
resolver
uniprot_sec
Q53TP5
resolver
uniprot_sec
Q86Z29
resolver
uniprot_sec
Q99998
resolver
uniprot_sec
Q9UID4
resolver
activity_regulation
ACTIVITY REGULATION: Gelatinase activity is inhibited by serine-protease inhibitors, such as phenylmethylsulfonyl fluoride (PMSF), 4-(2-aminoethyl)-benzenesulfonyl fluoride hydrochloride (AEBSF), 4-amidino phenylsulfonyl fluoride (APSF) and diisopropyl fluorophosphate (DFP), N-ethylmaleimide (NEM) and phenylmethylsulfonyl fluoride (PMSF). Dipeptidyl peptidase activity is inhibited by 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), diisopropylfluorophosphate (DFP). Prolyl endopeptidase activity is inhibited by the boronic acid peptide Ac-Gly-BoroPro, Ac-Gly-Pro-chloromethyl ketone and Thr-Ser-Gly-chloromethyl ketone. {ECO:0000269|PubMed:10593948, ECO:0000269|PubMed:16410248, ECO:0000269|PubMed:16480718, ECO:0000269|PubMed:17381073, ECO:0000269|PubMed:2172980, ECO:0000269|PubMed:9065413}.
uniprot
proteins
amino_acid_sequence
MKTWVKIVFGVATSAVLALLVMCIVLRPSRVHNSEENTMRALTLKDILNGTFSYKTFFPNWISGQEYLHQSADNNIVLYNIETGQSYTILSNRTMKSVNASNYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLSNGEFVRGNELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITFNGRENKIFNGIPDWVYEEEMLATKYALWWSPNGKFLAYAEFNDTDIPVIAYSYYGDEQYPRTINIPYPKAGAKNPVVRIFIIDTTYPAYVGPQEVPVPAMIASSDYYFSWLTWVTDERVCLQWLKRVQNVSVLSICDFREDWQTWDCPKTQEHIEESRTGWAGGFFVSTPVFSYDAISYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAINIFRVTQDSLFYSSNEFEEYPGRRNIYRISIGSYPPSKKCVTCHLRKERCQYYTASFSDYAKYYALVCYGPGIPISTLHDGRTDQEIKILEENKELENALKNIQLPKEEIKKLEVDEITLWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVRSVFAVNWISYLASKEGMVIALVDGRGTAFQGDKLLYAVYRKLGVYEVEDQITAVRKFIEMGFIDEKRIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASVYTERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGLSGLSTNHLYTHMTHFLKQCFSLSD
uniprot
proteins
ec_number
3.4.14.5
uniprot
proteins
ec_number
3.4.21.-
uniprot
proteins
ec_number
3.4.21.26
uniprot
proteins
function
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 (PubMed:14751930, PubMed:16223769, PubMed:16410248, PubMed:16480718, PubMed:17381073, PubMed:18095711, PubMed:21288888, PubMed:24371721). Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vitronectin, tenascin, laminin, fibronectin, fibrin or casein (PubMed:10347120, PubMed:10455171, PubMed:12376466, PubMed:16223769, PubMed:16651416, PubMed:18095711, PubMed:2172980, PubMed:7923219, PubMed:9065413). 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 (PubMed:10347120, PubMed:10593948, PubMed:16175601, PubMed:16223769, PubMed:16410248, PubMed:16651416, PubMed:17381073, PubMed:21314817, PubMed:24371721, PubMed:24717288). Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB) (PubMed:21314817). 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. {ECO:0000250|UniProtKB:P97321, ECO:0000269|PubMed:10347120, ECO:0000269|PubMed:10455171, ECO:0000269|PubMed:10593948, ECO:0000269|PubMed:12376466, ECO:0000269|PubMed:14751930, ECO:0000269|PubMed:16175601, ECO:0000269|PubMed:16223769, ECO:0000269|PubMed:16410248, ECO:0000269|PubMed:16480718, ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:17105646, ECO:0000269|PubMed:17381073, ECO:0000269|PubMed:18095711, ECO:0000269|PubMed:20707604, ECO:0000269|PubMed:21288888, ECO:0000269|PubMed:21314817, ECO:0000269|PubMed:2172980, ECO:0000269|PubMed:24371721, ECO:0000269|PubMed:24717288, ECO:0000269|PubMed:7923219, ECO:0000269|PubMed:9065413}.
uniprot
proteins
mass_dalton
87713
uniprot
proteins
mutagenesis
MUTAGEN 123; /note="R->A,M,E: Reduces dipeptidyl peptidase and endopeptidase activities."; /evidence="ECO:0000269|PubMed:17381073"; MUTAGEN 203; /note="E->A,D,Q: Reduces dipeptidyl peptidase and endopeptidase activities. Does not inhibit cell adhesion, migration and invasion. Inhibits dipeptidyl peptidase and endopeptidase activities; when associated with A-204."; /evidence="ECO:0000269|PubMed:16175601, ECO:0000269|PubMed:17381073"; MUTAGEN 204; /note="E->A,D,Q: Reduces dipeptidyl peptidase and endopeptidase activities. Does not inhibit cell adhesion, migration and invasion. Inhibits dipeptidyl peptidase and endopeptidase activities; when associated with A-203."; /evidence="ECO:0000269|PubMed:16175601, ECO:0000269|PubMed:17381073"; MUTAGEN 624; /note="S->A: Reduces dipeptidyl peptidase and gelatinolytic activities. Does not inhibit cell adhesion, migration and invasion."; /evidence="ECO:0000269|PubMed:10593948, ECO:0000269|PubMed:16175601"; MUTAGEN 656; /note="Y->F: Reduces dipeptidyl peptidase and endopeptidase activities."; /evidence="ECO:0000269|PubMed:17381073"; MUTAGEN 657; /note="A->D,N: Inhibits endopeptidase activity. Increases dipeptidyl peptidase activity."; /evidence="ECO:0000269|PubMed:17381073"; MUTAGEN 657; /note="A->F,V: Reduces dipeptidyl peptidase and endopeptidase activities."; /evidence="ECO:0000269|PubMed:17381073"; MUTAGEN 657; /note="A->Q: Inhibits endopeptidase activity. No change in dipeptidyl peptidase activity."; /evidence="ECO:0000269|PubMed:17381073"; MUTAGEN 657; /note="A->S,T: Strongly reduces endopeptidase activity. No change in dipeptidyl peptidase activity."; /evidence="ECO:0000269|PubMed:17381073"; MUTAGEN 704; /note="N->A: Reduces dipeptidyl peptidase and endopeptidase activities."; /evidence="ECO:0000269|PubMed:17381073
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:15809306, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:7911242, ECO:0000269|PubMed:9065413}.; PTM: The N-terminus may be blocked.
uniprot
proteins
protein_family
Peptidase S9B family
uniprot
proteins
pubmed
10347120
uniprot
proteins
pubmed
10455171
uniprot
proteins
pubmed
10593948
uniprot
proteins
pubmed
10644713
uniprot
proteins
pubmed
12376466
uniprot
proteins
pubmed
14751930
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15809306
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16175601
uniprot
proteins
pubmed
16223769
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16410248
uniprot
proteins
pubmed
16480718
uniprot
proteins
pubmed
16651416
uniprot
proteins
pubmed
17105646
uniprot
proteins
pubmed
17381073
uniprot
proteins
pubmed
18095711
uniprot
proteins
pubmed
18262497
uniprot
proteins
pubmed
20707604
uniprot
proteins
pubmed
21288888
uniprot
proteins
pubmed
21314817
uniprot
proteins
pubmed
2172980
uniprot
proteins
pubmed
24371721
uniprot
proteins
pubmed
24717288
uniprot
proteins
pubmed
7519584
uniprot
proteins
pubmed
7911242
uniprot
proteins
pubmed
7923219
uniprot
proteins
pubmed
9065413
uniprot
proteins
pubmed
9247085
uniprot
proteins
sequence_length
760
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Prolyl endopeptidase FAP]: Cell surface {ECO:0000269|PubMed:10593948, ECO:0000269|PubMed:16175601, ECO:0000269|PubMed:17105646, ECO:0000269|PubMed:24717288, ECO:0000269|PubMed:7911242}. Cell membrane {ECO:0000269|PubMed:12376466, ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:9065413, ECO:0000303|PubMed:10455171}; Single-pass type II membrane protein {ECO:0000255}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:9065413}; Single-pass type II membrane protein {ECO:0000255}. Cell projection, invadopodium membrane {ECO:0000269|PubMed:12376466, ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:7923219, ECO:0000269|PubMed:9065413, ECO:0000303|PubMed:10455171}; Single-pass type II membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000303|PubMed:10455171}; Single-pass type II membrane protein {ECO:0000255}. Membrane {ECO:0000269|PubMed:2172980}; Single-pass type II membrane protein {ECO:0000255}. Note=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. Colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. Anchored and enriched preferentially by integrin alpha-3/beta-1 at invadopodia, plasma membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. Localized at plasma and ruffle membranes in a collagen-independent manner. Colocalized with PLAUR preferentially at the cell surface of invadopodia membranes in a cytoskeleton-, integrin- and vitronectin-dependent manner. Concentrated at invadopodia membranes, specialized protrusions of the ventral plasma membrane in a fibrobectin-dependent manner. Colocalizes with extracellular components (ECM), such as collagen fibers and fibronectin. {ECO:0000269|PubMed:10593948, ECO:0000269|PubMed:12376466, ECO:0000269|PubMed:16175601, ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:17105646, ECO:0000269|PubMed:2172980, ECO:0000269|PubMed:24717288, ECO:0000269|PubMed:7911242, ECO:0000269|PubMed:7923219, ECO:0000269|PubMed:9065413, ECO:0000303|PubMed:10455171}.; SUBCELLULAR LOCATION: [Antiplasmin-cleaving enzyme FAP, soluble form]: Secreted {ECO:0000269|PubMed:14751930, ECO:0000269|PubMed:16223769, ECO:0000269|PubMed:24371721}. Note=Found in blood plasma and serum. {ECO:0000269|PubMed:14751930, ECO:0000269|PubMed:16223769, ECO:0000269|PubMed:24371721}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000303|PubMed:10644713}.
uniprot
proteins
transmembrane_region
TRANSMEM 5..25; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins