FAP Protein Overview: Sequence, Structure, Function and Protein Interaction

FAP Protein Overview

The APC gene encodes a multidomain protein that plays a major role in tumor suppression by antagonizing the WNT (see WNT1; 164820) signaling pathway. Inappropriate activation of this pathway through loss of APC function contributes to cancer progression, as in familial adenomatous polyposis (FAP; 175100). APC also has a role in cell migration, adhesion, chromosome segregation, spindle assembly, apoptosis, and neuronal differentiation (Hanson and Miller, 2005). The APC protein is an integral part of the beta-catenin (CTNNB1; 116806) signaling pathway.

FAP protein family

Belongs to the peptidase S9B family.

FAP protein name

Recommended name
Prolyl endopeptidase FAP
Short name
FAPalpha||SIMP||Seprase||APCE
Aliases
DPPIV, seprase
Alternative name
Gelatine degradation protease FAP Integral membrane serine protease Post-proline cleaving enzyme Serine integral membrane protease Surface-expressed protease Antiplasmin-cleaving enzyme FAP, soluble form

FAP Gene family protein

FAP Protein Sequence

Species Human FAP protein
Length 760
Mass (Da) 87713
Sequence Human FAP protein sequence
Species Mouse FAP protein
Length 761
Mass (Da) 87945
Sequence Mouse FAP protein sequence
Species
Length
Mass (Da)
Sequence

FAP Protein Molecular Weight & PI

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) [Contains: Antiplasmin-cleaving enzyme FAP, soluble form (EC 3.4.14.5) (EC 3.4.21.-) (EC 3.4.21.26) (APCE) ] Homo sapiens (Human).

The parameters have been computed for the following feature

FT CHAIN 1-760 Prolyl endopeptidase FAP. {ECO:0000305}.

Molecular weight (Da)

87712.56

Theoretical pI

6.21

FAP Protein Structure

Crystal Structure Of Human Fibroblast Activation Protein alpha
Deposited
2005-03-21   Released:  2005-04-12
Deposition Author(s)
Aertgeerts, K., Levin, I., Shi, L., Prasad, G.S., Zhang, Y., Kraus, M.L., Salakian, S., Snell, G.P., Sridhar, V., Wijnands, R., Tennant, M.G.
Organism(s)
Homo sapiens
Expression System
Spodoptera frugiperda
Experimental Data Snapshot
Method
X-RAY DIFFRACTION
Resolution
2.6000 Å
R-Value Free
0.283
R-Value Work
0.223
1Z68 From PDB

Human FAP protein Secondary structure

FAP Protein Interaction

Recombinant FAP Protein Feature

FAP Protein, Human, Recombinant (ECD, His Tag)

High Purity
> 95 % as determined by SDS-PAGE
Low Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
High Activity
Measured by its ability to convert the substrate benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin (Z-GP-AMC) to Z-Gly-Pro and 7-amino-4-methylcoumarin (AMC). The specific activity is >1200 pmol/min/μg

Recombinant FAP protein citations

Title
A tumor-targeted activatable phthalocyanine-tetrapeptide-doxorubicin conjugate for synergistic chemo-photodynamic therapy
Year
2017
Author
Ke, MR;Chen, SF;Peng, XH;Zheng, QF;Zheng, BY;Yeh, CK;Huang, JD;
Journal
Eur J Med Chem
Title
A tumor-targeted activatable phthalocyanine-tetrapeptide-doxorubicin conjugate for synergistic chemo-photodynamic therapy
Year
2017
Author
Ke, MR;Chen, SF;Peng, XH;Zheng, QF;Zheng, BY;Yeh, CK;Huang, JD;
Journal
Eur J Med Chem
Title
Targeting cancer-associated fibroblasts by dual-responsive lipid-albumin nanoparticles to enhance drug perfusion for pancreatic tumor therapy
Year
2020
Author
Yu, Q;Qiu, Y;Li, J;Tang, X;Wang, X;Cun, X;Xu, S;Liu, Y;Li, M;Zhang, Z;He, Q;
Journal
J Control Release

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