FAP

Prolyl endopeptidase FAP. UniProt annotates extracellular residues 26–760.

Molecule screening

The FAP campaign screened 24 molecules and repeated five selections. All five passed the recorded docking and pose checks.

View campaign results

RNA expression by cell type

Percentage of cells with detected FAP RNA in the public colon adenocarcinoma cell groups.

Fibroblasts26.1%

Endothelial cells18.4%

Adipocytes6.2%

Tumor cells1.7%

Macrophages (group B)0.4%

CD4 T cells0.2%

Granulocytes0.2%

Macrophages (group A)0.2%

Regulatory T cells0.2%

B cells0.1%

CD8 T cells0.1%

Dendritic cells0.0%

Natural killer cells0.0%

RNA detection · Cancer Surfaceome Atlas, Table S6, row 58. Source study · Measurements (JSON)

Inspect the molecular structure

Published reference structure

FAP with linagliptin

Deposited structure 6Y0F. The deposited asymmetric unit contains four FAP copies and linagliptin.

PDB entry: 6Y0F
Target ID: T-ENSG00000078098

FAP · chains A, B, C, D (ribbon)
Linagliptin · carbon in ochre; oxygen red; nitrogen blue (sticks)

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Sequence & binding sites

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Sequence annotations and source records

Canonical sequence and topology

Target ID: T-ENSG00000078098
UniProt accession: Q12884
Sequence state: available
Canonical sequence: Yes
Length in amino acids: 760
Sequence SHA-256: fc502b7363283bca3ea0e276ed1d65d0ae8d5064519a226a06f9c77059235b6f

View and select the full canonical sequence

Canonical amino-acid sequence

MKTWVKIVFGVATSAVLALLVMCIVLRPSRVHNSEENTMRALTLKDILNGTFSYKTFFPNWISGQEYLHQSADNNIVLYNIETGQSYTILSNRTMKSVNASNYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLSNGEFVRGNELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITFNGRENKIFNGIPDWVYEEEMLATKYALWWSPNGKFLAYAEFNDTDIPVIAYSYYGDEQYPRTINIPYPKAGAKNPVVRIFIIDTTYPAYVGPQEVPVPAMIASSDYYFSWLTWVTDERVCLQWLKRVQNVSVLSICDFREDWQTWDCPKTQEHIEESRTGWAGGFFVSTPVFSYDAISYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAINIFRVTQDSLFYSSNEFEEYPGRRNIYRISIGSYPPSKKCVTCHLRKERCQYYTASFSDYAKYYALVCYGPGIPISTLHDGRTDQEIKILEENKELENALKNIQLPKEEIKKLEVDEITLWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVRSVFAVNWISYLASKEGMVIALVDGRGTAFQGDKLLYAVYRKLGVYEVEDQITAVRKFIEMGFIDEKRIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASVYTERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGLSGLSTNHLYTHMTHFLKQCFSLSD

Sequence positions 1–760

Gray shows the full canonical sequence. Colored spans mark the listed intervals.

Membrane-spanning segments

5–25 (Helical; Signal-anchor for type II membrane protein)

Source-annotated domains

1–4 (Cytoplasmic); 26–760 (Extracellular)

Source-annotated extracellular intervals

26–760

UniProt annotates the following extracellular intervals.

One-based positions include both interval endpoints.
Start	End	Length	Sequence and source
26	760	735	Sequence and source Basis reviewed-uniprot-topological-domain Evidence class source-annotated-topology Sequence SHA-256 8a73e2ecfae3560153da161736dc9f14bd86bbfa1301bf3bb006ea38a2e844ac Amino-acid sequence for this intervalLRPSRVHNSEENTMRALTLKDILNGTFSYKTFFPNWISGQEYLHQSADNNIVLYNIETGQSYTILSNRTMKSVNASNYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLSNGEFVRGNELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITFNGRENKIFNGIPDWVYEEEMLATKYALWWSPNGKFLAYAEFNDTDIPVIAYSYYGDEQYPRTINIPYPKAGAKNPVVRIFIIDTTYPAYVGPQEVPVPAMIASSDYYFSWLTWVTDERVCLQWLKRVQNVSVLSICDFREDWQTWDCPKTQEHIEESRTGWAGGFFVSTPVFSYDAISYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAINIFRVTQDSLFYSSNEFEEYPGRRNIYRISIGSYPPSKKCVTCHLRKERCQYYTASFSDYAKYYALVCYGPGIPISTLHDGRTDQEIKILEENKELENALKNIQLPKEEIKKLEVDEITLWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVRSVFAVNWISYLASKEGMVIALVDGRGTAFQGDKLLYAVYRKLGVYEVEDQITAVRKFIEMGFIDEKRIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASVYTERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGLSGLSTNHLYTHMTHFLKQCFSLSD

Sequence and topology sources

Source role: canonical-sequence
Source: alphafold-db-canonical-uniprot-field
Extracted field: uniprotSequence
Source row accession: Not recorded

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Open sequence source

Source role: reviewed-topology
Source: UniProt reviewed human surface-field snapshot
Extracted field: Not recorded
Source row accession: Q12884

Download source snapshot (gzip)

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}.
transmembrane: TRANSMEM 5..25; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255"
topological_domain: TOPO_DOM 1..4; /note="Cytoplasmic"; /evidence="ECO:0000255, ECO:0000303|PubMed:14751930"; TOPO_DOM 26..760; /note="Extracellular"; /evidence="ECO:0000255, ECO:0000303|PubMed:14751930"
signal_peptide: Not recorded
lipidation: Not recorded

Download all canonical target sequences (FASTA)

Protein identity and location

Protein: Prolyl endopeptidase FAP
Protein location: Transmembrane protein
Canonical sequence: Q12884 · 760 amino acids
Extracellular region: UniProt annotates extracellular residues 26–760.

More structures and generated models

Structure snapshots

Published reference structure

FAP with a SUMO-I3 VHH fusion

Deposited structure 9DVR. FAP dimer bound by two SUMO-I3 VHH molecules.

PDB entry: 9DVR
Target ID: T-ENSG00000078098

FAP soluble ectodomain dimer · chains A, B (ribbon)
SUMO-I3 VHH fusion · chains G, H (ribbon)

Download PNG · Download settings · Source coordinates (CIF)

Expression in normal tissues

RNA specificity: Tissue enhanced
RNA distribution: Detected in many
RNA tissue-specific nTPM: endometrium 1: 29.4
Protein specificity: Group enriched
Protein distribution: Detected in some
Immunohistochemistry reliability: Uncertain
Protein tissue-specific intensity: blood vessel: 187,180.7; skin: 538,235.3
Tissue cell-type enrichment: Adipose subcutaneous - Adipose progenitor cells, Adipose visceral - Adipose progenitor cells, Minor Salivary Gland - Macrophages, Prostate - Fibroblasts, Skeletal muscle - Fibroblasts, Testis - Early spermatids, Thyroid gland - Fibroblasts

Human Protein Atlas: FAP

Known molecule interactions

Known Molecule Interactions linked to FAP.
Molecule	Stable ID	Category	Reference or intention	Claim
Linagliptin	RF020	Reference ligand	source	source-backed known interaction

Molecule screening results

The FAP campaign screened 24 molecules and repeated five selections. All five passed the recorded docking and pose checks.

Compare molecules, poses, and repeated runs →

Structures

Structures records linked to FAP.
Name	Stable ID	Action	Format	Status	Claim
9DVR	S-RCSB-9DVR	Not recorded	Not recorded	not recorded	verified deposited experimental structure
6Y0F	S-RCSB-6Y0F	Not recorded	Not recorded	not recorded	verified deposited experimental structure

Sources and downloads

UniProt protein record Target measurements (JSON)Sequence annotations (JSON)Target sequences (FASTA)

FAP · ENSG00000078098 · Q12884