Fap fibroblast activation protein [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Fapprovided by MGI
Official Full Name: fibroblast activation proteinprovided by MGI
Primary source: MGI:MGI:109608
See related: Ensembl:ENSMUSG00000000392 AllianceGenome:MGI:109608
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: SIMP
Summary: This gene belongs to the serine protease family. The encoded protein is an inducible cell-surface bound glycoprotein specifically expressed in tumor-associated fibroblasts and pericytes of epithelial tumors and has protease and gelatinase activity. The protein plays a role in remodeling of the extracellular matrix (ECM) and may affect tumorigenesis and tissue repair. Alternately spliced transcript variants of this gene are described in the literature (PMID 9139873), but the full-length sequence of these variants is not available. [provided by RefSeq, Apr 2013]
Expression: Biased expression in limb E14.5 (RPKM 7.4), mammary gland adult (RPKM 2.8) and 9 other tissues See more
Orthologs: human all
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Genomic context

Location:: 2 C1.3; 2 35.85 cM

Exon count:: 26

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	2	NC_000068.8 (62331280..62404365, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	2	NC_000068.7 (62500936..62575509, complement)

Chromosome 2 - NC_000068.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Mechanical stiffness promotes skin fibrosis through FAPalpha-AKT signaling pathway.
Title: Mechanical stiffness promotes skin fibrosis through FAPα-AKT signaling pathway.
FAP expression in adipose tissue macrophages promotes obesity and metabolic inflammation.
Title: FAP expression in adipose tissue macrophages promotes obesity and metabolic inflammation.
Stereotactic ablative radiotherapy and FAPalpha-based cancer vaccine suppresses metastatic tumor growth in 4T1 mouse breast cancer.
Title: Stereotactic ablative radiotherapy and FAPα-based cancer vaccine suppresses metastatic tumor growth in 4T1 mouse breast cancer.
Dendritic cells infected with recombinant adenoviral vector encoding mouse fibroblast activation protein-alpha and human livin alpha exert an antitumor effect against Lewis lung carcinoma in mice.
Title: Dendritic cells infected with recombinant adenoviral vector encoding mouse fibroblast activation protein-α and human livin α exert an antitumor effect against Lewis lung carcinoma in mice.
FAP-targeted CAR-T suppresses MDSCs recruitment to improve the antitumor efficacy of claudin18.2-targeted CAR-T against pancreatic cancer.
Title: FAP-targeted CAR-T suppresses MDSCs recruitment to improve the antitumor efficacy of claudin18.2-targeted CAR-T against pancreatic cancer.
Inhibition of Fap Promotes Cardiac Repair by Stabilizing BNP.
Title: Inhibition of Fap Promotes Cardiac Repair by Stabilizing BNP.
Targeting FAPalpha-expressing hepatic stellate cells overcomes resistance to antiangiogenics in colorectal cancer liver metastasis models.
Title: Targeting FAPα-expressing hepatic stellate cells overcomes resistance to antiangiogenics in colorectal cancer liver metastasis models.
Design, Synthesis and Preclinical Assessment of (99m)Tc-iFAP for In Vivo Fibroblast Activation Protein (FAP) Imaging.
Title: Design, Synthesis and Preclinical Assessment of (99m)Tc-iFAP for In Vivo Fibroblast Activation Protein (FAP) Imaging.
Deletion of fibroblast activation protein provides atheroprotection.
Title: Deletion of fibroblast activation protein provides atheroprotection.
Genetic ablation of fibroblast activation protein alpha attenuates left ventricular dilation after myocardial infarction.
Title: Genetic ablation of fibroblast activation protein alpha attenuates left ventricular dilation after myocardial infarction.

Submit: New GeneRIF Correction See all GeneRIFs (36)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (6)
Targeted (4) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

Fap (e-PCR), detects polymorphism
- UniSTS:257072

Fap (e-PCR), detects polymorphism
- UniSTS:257073

Fap (e-PCR), detects polymorphism
- UniSTS:143070

Y10007 (e-PCR)
- UniSTS:158968

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables dipeptidyl-peptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables dipeptidyl-peptidase activity	ISO Inferred from Sequence Orthology more info
enables dipeptidyl-peptidase activity	ISS Inferred from Sequence or Structural Similarity more info
enables endopeptidase activity	ISO Inferred from Sequence Orthology more info
enables identical protein binding	ISO Inferred from Sequence Orthology more info
enables integrin binding	IEA Inferred from Electronic Annotation more info
enables integrin binding	ISO Inferred from Sequence Orthology more info
enables peptidase activity	IDA Inferred from Direct Assay more info	PubMed
enables peptidase activity	ISO Inferred from Sequence Orthology more info
enables protease binding	IEA Inferred from Electronic Annotation more info
enables protease binding	ISO Inferred from Sequence Orthology more info
enables protein homodimerization activity	ISO Inferred from Sequence Orthology more info
enables protein homodimerization activity	ISS Inferred from Sequence or Structural Similarity more info
enables serine-type endopeptidase activity	ISO Inferred from Sequence Orthology more info
enables serine-type endopeptidase activity	ISS Inferred from Sequence or Structural Similarity more info
enables serine-type peptidase activity	ISO Inferred from Sequence Orthology more info
enables serine-type peptidase activity	ISS Inferred from Sequence or Structural Similarity more info

Process	Evidence Code	Pubs
involved_in angiogenesis	IEA Inferred from Electronic Annotation more info
involved_in cell adhesion	IEA Inferred from Electronic Annotation more info
involved_in endothelial cell migration	ISO Inferred from Sequence Orthology more info
involved_in endothelial cell migration	ISS Inferred from Sequence or Structural Similarity more info
involved_in melanocyte apoptotic process	IDA Inferred from Direct Assay more info	PubMed
involved_in melanocyte proliferation	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of cell proliferation involved in contact inhibition	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of extracellular matrix disassembly	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of extracellular matrix disassembly	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of extracellular matrix organization	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of extracellular matrix organization	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of execution phase of apoptosis	IDA Inferred from Direct Assay more info	PubMed
involved_in proteolysis	IBA Inferred from Biological aspect of Ancestor more info
involved_in proteolysis	ISO Inferred from Sequence Orthology more info
involved_in proteolysis	ISS Inferred from Sequence or Structural Similarity more info
involved_in proteolysis involved in protein catabolic process	ISO Inferred from Sequence Orthology more info
involved_in proteolysis involved in protein catabolic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in regulation of cell cycle	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of collagen catabolic process	ISO Inferred from Sequence Orthology more info
involved_in regulation of collagen catabolic process	ISS Inferred from Sequence or Structural Similarity more info

Component	Evidence Code	Pubs
located_in anchoring junction	IEA Inferred from Electronic Annotation more info
located_in apical part of cell	IDA Inferred from Direct Assay more info	PubMed
located_in basal part of cell	IDA Inferred from Direct Assay more info	PubMed
located_in cell surface	IDA Inferred from Direct Assay more info	PubMed
located_in extracellular space	IEA Inferred from Electronic Annotation more info
located_in extracellular space	ISO Inferred from Sequence Orthology more info
located_in lamellipodium	ISO Inferred from Sequence Orthology more info
located_in lamellipodium membrane	IEA Inferred from Electronic Annotation more info
part_of peptidase complex	IEA Inferred from Electronic Annotation more info
part_of peptidase complex	ISO Inferred from Sequence Orthology more info
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	ISS Inferred from Sequence or Structural Similarity more info
located_in ruffle membrane	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: prolyl endopeptidase FAP

Names: FAPalpha; dipeptidyl peptidase FAP; fibroblast activation protein alpha; gelatine degradation protease FAP; integral membrane serine protease; post-proline cleaving enzyme; seprase; serine integral membrane protease; surface-expressed protease

NP_032012.1

EC 3.4.14.5

EC 3.4.21.26

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_007986.3 → NP_032012.1 prolyl endopeptidase FAP

See identical proteins and their annotated locations for NP_032012.1

Status: REVIEWED

Source sequence(s)

AL928576

Consensus CDS

CCDS16067.1

UniProtKB/Swiss-Prot

P97321

UniProtKB/TrEMBL

A0A172Q394, G3UXR2

Related

ENSMUSP00000099793.4, ENSMUST00000102732.10

Conserved Domains (3) summary

pfam00326
Location:553 → 757

Peptidase_S9; Prolyl oligopeptidase family

pfam00930
Location:106 → 473

DPPIV_N; Dipeptidyl peptidase IV (DPP IV) N-terminal region

pfam18811
Location:37 → 57

DPPIV_rep; Dipeptidyl peptidase IV (DPP IV) low complexity region