Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
Combined Automated Annotation using Multiple IEA Methods
PDZ-domain-directed basolateral targeting of the peripheral membrane protein FRMPD2 in epithelial cells
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FRMPD2 is a basolateral membrane scaffold protein in epithelial cells whose localization requires the FERM domain (phosphatidylinositol binding) and PDZ2 domain (p0071 binding). Knockdown impairs tight junction formation.
"FRMPD2 is localized in a polarized fashion in epithelial cells at the basolateral membrane and partially colocalizes with the tight-junction marker protein Zonula-occludens-1. Downregulation of FRMPD2 protein in Caco-2 cells is associated with an impairment of tight junction formation"
Lrit1, a Retinal Transmembrane Protein, Regulates Selective Synapse Formation in Cone Photoreceptor Cells and Visual Acuity
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Frmpd2 is a photoreceptor scaffold protein that interacts with LRIT1 via its PDZ3 domain. The Frmpd2-Lrit1-mGluR6 axis regulates selective synapse formation between cone photoreceptors and cone ON-bipolar cells.
"Lrit1 interacts with Frmpd2, a photoreceptor scaffold protein, and with mGluR6, an ON-bipolar cell-specific glutamate receptor...the Frmpd2-Lrit1-mGluR6 axis regulates selective synapse formation in cone photoreceptors and is essential for normal visual function"
The second PDZ domain of scaffold protein Frmpd2 binds to GluN2A of NMDA receptors
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The PDZ2 domain of mouse Frmpd2 directly binds GluN2A and GluN2B C-termini, with higher affinity for GluN2A. Crystal structure solved at 1.80 A.
"the second PDZ (PDZ2) domain but not the first or third PDZ domain of Frmpd2 binds to the C-terminus of GluN2A and GluN2B, two subunits of NMDA receptors...the interaction of Frmpd2 to GluN2A subunit is more strongly than that to GluN2B subunit"
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Frmpd2 localizes to the postsynaptic membrane and is involved in NMDAR-mediated synaptic excitatory transmission.
"the Frmpd2 is specifically expressed at postsynaptic membrane...the scaffold protein Frmpd2 is probably involved in synaptic NMDA receptors-mediated neural excitatory and neurotoxicity in a PDZ2 domain-dependent manner"
RNAi screening identifies mediators of NOD2 signaling: Implications for spatial specificity of MDP recognition
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FRMPD2 spatially assembles the NOD2-RIPK2 signalosome at the basolateral membrane, restricting innate immune responses to the basolateral compartment. Crohn disease-associated NOD2 mutations impair FRMPD2 interaction.
"FRMPD2 interacts with NOD2 via leucine-rich repeats and forms a complex with the membrane-associated protein ERBB2IP...FRMPD2 spatially assembles the NOD2-signaling complex, hereby restricting NOD2-mediated immune responses to the basolateral compartment of polarized intestinal epithelial cells"
UniProt entry for mouse Frmpd2
Frmpd2 deep research (falcon provider)
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Comprehensive literature review confirming Frmpd2 functions as a multi-context scaffold protein with roles in NMDAR anchoring (hippocampus), photoreceptor synapse organization (retina), epithelial polarity/tight junctions, and NOD2 innate immune signaling. Epilepsy relevance noted from bioRxiv preprint.