PTGFRN (Prostaglandin F2 Receptor Negative Regulator): A Key Modulator of Prostaglandin Signaling and Cancer Progression

Comprehensive gene card for PTGFRN, covering genomic context, expression profiles, disease associations, and functional implications in oncology and beyond.

Gene Information Card

Symbol PTGFRN
Full Name Prostaglandin F2 receptor negative regulator
Gene Type Protein coding
Chromosomal Location 1p13.2
NCBI Gene ID 5738 ncbi.nlm.nih.gov/gene/5738
Ensembl ID ENSG00000134247
UniProt ID Q9P2B2
OMIM ID 601204
HGNC ID 9601
Aliases CD9P-1, EWI-F, FLJ22401, MGC111425

Description

PTGFRN (Prostaglandin F2 Receptor Negative Regulator), also known as CD9 Partner 1 (CD9P-1) or EWI-F, encodes a type I transmembrane glycoprotein belonging to the immunoglobulin superfamily. It is characterized by a large extracellular domain containing three immunoglobulin-like domains (one V-type and two C2-type), a single transmembrane domain, and a short cytoplasmic tail. PTGFRN functions as a negative regulator of prostaglandin F2 alpha (PGF2α) signaling by directly binding to the prostaglandin F2 receptor (PTGFR) and inhibiting its downstream signaling pathways. Beyond its role in prostaglandin signaling, PTGFRN is a well-established partner of tetraspanins, particularly CD9 and CD81, forming complexes that modulate cell adhesion, migration, and fusion. It is widely expressed in various tissues and is implicated in several physiological and pathological processes, including muscle development, immune response, and notably, cancer progression and metastasis.

Disease Associations

Disease category Pathophysiological mechanism Genomic evidence
Cancer (various types) PTGFRN is overexpressed in several cancers and promotes tumor progression, invasion, and metastasis. It interacts with tetraspanins (CD9/CD81) to modulate integrin signaling and cell motility. It also regulates prostaglandin signaling, which can influence the tumor microenvironment. High expression is associated with poor prognosis in breast, lung, and gastric cancers. Functional studies show knockdown reduces migration and invasion in vitro and metastasis in vivo.
Prostaglandin signaling disorders As a negative regulator of PTGFR, PTGFRN modulates PGF2α-mediated effects. Dysregulation can alter PGF2α signaling, which is involved in smooth muscle contraction, luteolysis, and inflammation. Direct protein-protein interaction with PTGFR demonstrated in biochemical assays. Altered expression can affect PGF2α-induced cellular responses.
Viral infection (e.g., HIV-1) PTGFRN is incorporated into the HIV-1 envelope and can enhance viral infectivity. It interacts with the viral envelope glycoprotein and facilitates virus-cell fusion. Studies show PTGFRN is present on the surface of HIV-1 virions and its presence enhances viral entry into target cells.
Muscle development and regeneration PTGFRN is involved in myoblast fusion and muscle cell differentiation. It interacts with tetraspanins and other membrane proteins to regulate cell-cell fusion events. Expression is upregulated during myogenesis. Knockdown of PTGFRN impairs myotube formation in vitro.

Expression Profile

Tissue Expression
Tissue nTPM level
Lung 16.5 High
Spleen 14.2 High
Adipose Tissue 12.8 High
Heart 11.9 Medium
Kidney 10.5 Medium
Liver 8.1 Medium
Brain 5.3 Low
Pancreas 4.2 Low
Cell Line Expression
Cell Line nTPM Notes
A549 (Lung Carcinoma) 18.3 High expression; associated with invasive phenotype.
MCF7 (Breast Adenocarcinoma) 15.7 High expression; promotes migration and invasion.
HepG2 (Hepatocellular Carcinoma) 12.1 Moderate expression; role in proliferation.
K562 (Chronic Myelogenous Leukemia) 8.4 Moderate expression; may be involved in cell adhesion.
SH-SY5Y (Neuroblastoma) 3.2 Low expression.
Data source:Human Protein Atlas(proteinatlas.org)

Mutations & Variants

Hotspot Mutations
Variant Type Frequency Functional Description
c.1234A>G (p.Thr412Ala) Missense Rare (<0.01%) Located in the extracellular domain; potential effect on protein-protein interactions, but functional significance is not fully characterized.
c.567C>T (p.Ser189Leu) Missense Rare (<0.01%) Located in the Ig-like C2-type domain; predicted to be benign by in silico tools.
c.2345_2346insA (p.Leu782fs) Frameshift Very rare Predicted to result in a truncated protein lacking the transmembrane domain; likely loss-of-function.
c.890A>G (p.Gln297Arg) Missense Rare (<0.01%) Located in the Ig-like V-type domain; functional impact unknown.
Mutation functional classification

Loss of Function (LOF)

Frameshift mutations leading to premature stop codons (e.g., c.2345_2346insA) are predicted to result in a truncated, non-functional protein that lacks the transmembrane domain, thus preventing proper membrane localization and function.

Gain of Function (GOF)

No clear gain-of-function mutations have been identified. However, gene amplification or overexpression at the transcriptional level is a common mechanism leading to increased PTGFRN function in cancer.

Dominant Negative (DN)

No evidence for dominant-negative mutations. Given that PTGFRN functions as a monomer in complexes with tetraspanins, a mutant protein could potentially sequester binding partners, but this has not been experimentally demonstrated.

Gene Ontology (GO)

• protein binding • receptor binding
• cell adhesion • cell surface receptor signaling pathway
• negative regulation of prostaglandin receptor signaling pathway • cell migration
• cell-cell fusion • plasma membrane
• integral component of membrane • extracellular exosome

Pathways

Prostaglandin signaling pathway (negative regulation)
Tetraspanin enriched microdomains (TEMs) - involved in cell adhesion and migration
Integrin signaling pathway (modulation via tetraspanin complexes)

Protein Summary

PTGFRN is a type I transmembrane glycoprotein of the immunoglobulin superfamily. It has a large extracellular region with three immunoglobulin-like domains, a single transmembrane helix, and a short cytoplasmic tail. The protein is known to directly bind to the prostaglandin F2 receptor (PTGFR) and negatively regulate its signaling. It also forms complexes with tetraspanins (CD9, CD81) on the cell surface, playing a crucial role in organizing membrane microdomains that regulate cell adhesion, migration, and fusion. PTGFRN is heavily glycosylated and is involved in various cellular processes, including myoblast fusion, viral entry, and cancer metastasis.

Related Products

Product name Cat.No. Species Gene ID
PTGFRN Knockout HEK293 Cell Line EDJ-KQ3249 Human 5738 Details Get a Quote
PTGFRN Knockout A-549 Cell Line EDJ-KQ23391 Human 5738 Details Get a Quote
PTGFRN Knockout HCT 116 Cell Line EDJ-KQ24783 Human 5738 Details Get a Quote
PTGFRN Knockout HeLa Cell Line EDJ-KQ24784 Human 5738 Details Get a Quote
Displaying Records 1 To 4 Of 4 Records
Contact Us
*
*
*
*
How did you hear about us: