Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
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SwissProt keyword-derived (SPKW) annotations present in the Sept 2025 goa_uniprot_gcrp snapshot but removed from the current GOA release after GOA retired the keyword2GO pipeline for cellular organisms.
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The retired SPKW annotations for NFP - protein tyrosine kinase activity (from the Tyrosine-protein kinase keyword) and defense response (from the Plant defense keyword) - were both correctly removed; the first is biologically wrong (pseudokinase; Ser/Thr not Tyr) and the second is redundant with more specific curated defense terms.
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
The NFP locus of Medicago truncatula controls an early step of Nod factor signal transduction upstream of a rapid calcium flux and root hair deformation.
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The nfp mutant fails every assayed Nod factor response (no calcium flux, no calcium spiking, no early nodulin expression, no root hair deformation), placing NFP at the most upstream, nodulation-specific step of Nod factor signal transduction.
"The nfp mutant thus shows no rapid calcium flux, the earliest detectable Nod factor response of wild-type plants, and no root hair deformation. The nfp mutant is also deficient in Nod factor-induced calcium spiking and early nodulin gene expression."
LysM domains of Medicago truncatula NFP protein involved in Nod factor perception. Glycosylation state, molecular modeling and docking of chitooligosaccharides and Nod factors.
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The three tandem LysM domains of the NFP ectodomain are predicted to bind the rhizobial lipo-chitooligosaccharide Nod factor; NFP is highly N-glycosylated.
"A convergent model can be proposed where the sulfated, O-acetylated lipo-chitooligosaccharidic Nod factor of S. meliloti binds in similar orientation to the three LysM domains of M. truncatula NFP."
The Medicago truncatula lysin [corrected] motif-receptor-like kinase gene family includes NFP and new nodule-expressed genes.
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NFP is a LysM-RLK whose intracellular kinase domain is a pseudokinase - it deviates from conserved catalytic kinase sequences and shows no autophosphorylation activity, implying it must associate with an active kinase.
"Consistent with deviations from conserved kinase domain sequences, NFP did not show autophosphorylation activity, suggesting that NFP needs to associate with an active kinase or has unusual functional characteristics different from classical kinases."
Contribution of NFP LysM domains to the recognition of Nod factors during the Medicago truncatula/Sinorhizobium meliloti symbiosis.
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The NFP LysM2 domain, and specifically a single leucine residue (Leu154), are important for rhizobial infection, demonstrating that LysM domain residues are functionally required for Nod factor recognition.
"we have demonstrated the importance of the NFP LysM2 domain for rhizobial infection and we have pinpointed the importance of a single leucine residue of LysM2 in that step of the symbiosis."
Epidermal and cortical roles of NFP and DMI3 in coordinating early steps of nodulation in Medicago truncatula.
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Epidermal NFP is sufficient to induce cortical cell divisions leading to nodule primordium formation, establishing NFP's role in nodule organogenesis.
"Epidermal NFP is sufficient to induce cortical cell divisions leading to nodule primordia formation."
NFP, a LysM protein controlling Nod factor perception, also intervenes in Medicago truncatula resistance to pathogens.
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NFP positively contributes to M. truncatula immunity: nfp mutants are more susceptible to the oomycete Aphanomyces euteiches and the fungus Colletotrichum trifolii, and NFP overexpression increases resistance.
"nfp, but not lyk3, mutants were significantly more susceptible than wildtype plants to A. euteiches, whereas NFP overexpression increased resistance."
Nod factor receptors form heteromeric complexes and are essential for intracellular infection in medicago nodules.
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NFP and the active LysM-RLK LYK3 form heteromeric receptor complexes at the cell periphery (plasma membrane) in M. truncatula nodules; NFP is also observed in the vacuolar lumen of cells undergoing receptor breakdown.
"our Förster resonance energy transfer-fluorescence lifetime imaging microscopy analysis indicates that NFP and LYK3 form heteromeric complexes at the cell periphery in M. truncatula nodules."
The small GTPase ROP10 of Medicago truncatula is required for both tip growth of root hairs and nod factor-induced root hair deformation.
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The intracellular kinase domain of NFP interacts with the small GTPase ROP10 in a GTP-dependent manner; this interaction is required for root hair deformation during rhizobial infection.
"ROP10 interacted with the kinase domain of the NF receptor NFP in a GTP-dependent manner."
Deep research report (falcon / Edison Scientific) on Medicago truncatula NFP (UniProt Q0GXS4)
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Independently confirms that NFP has a nonclassical/aberrant intracellular kinase domain lacking key conserved kinase motifs (P-loop/DFG-related features and an activation-loop segment) and shows no detectable autophosphorylation in vitro, supporting interpretation of NFP as a pseudokinase / non-catalytic signalling subunit - corroborating the REMOVE decisions on the catalytic kinase-activity annotations.
"lacking key conserved motifs (including P-loop/DFG-related features and an activation-loop segment), and ... was observed in vitro, supporting interpretation of NFP as a likely ... or signaling subunit that requires an active kinase partner"
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Confirms NFP is a plasma-membrane LysM receptor-like kinase whose three tandem extracellular LysM domains mediate recognition of rhizobial Nod factors (lipo-chitooligosaccharides), and that NFP acts at the earliest step of Nod factor signalling, genetically upstream of DMI1/DMI2/DMI3 and NSP1/NSP2, controlling both rhizobial infection and nodule organogenesis.
"acts at the ... earliest stages of Nod factor signaling ... and is genetically placed ... upstream of DMI1/DMI2/DMI3 and NSP1/NSP2 ... Arrighi et al. further argue that NFP functions throughout infection and may control partly distinct pathways for ... symbiotic infection ... and ... nodule organogenesis"
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Confirms NFP's role at the symbiosis-immunity interface: NFP/NFR-type receptors can trigger defense-like outputs, and recent work links the NFP kinase domain to the immune co-receptor MtSOBIR1 - consistent with the review's treatment of NFP's defense role as a real but secondary, non-core function.
"NFP/NFR-type receptors lie at a ... symbiosis–immunity interface ... Recent work connects NFP to ... a known immunity coreceptor"
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Adds recent (2023-2024) mechanistic context not in the original review: NFP can functionally associate with multiple LysM-RLK partners (MtLYK2, MtLYK3, MtLYK2bis) whose kinase-active cytoplasmic domains can trans-phosphorylate the NFP cytoplasmic domain, extending the single-partner NFP-LYK3 heteromer model toward a multi-partner receptor-complex landscape.
"cytoplasmic domains of MtLYK2/3/2bis display kinase activity, and kinase-active versions can induce mobility shifts/retardation consistent with ... trans-phosphorylation of the MtNFP cytoplasmic domain"
UniProtKB entry Q0GXS4 (NFP_MEDTR), Serine/threonine receptor-like kinase NFP
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The UniProt curated subcellular location places NFP at the cell membrane and, on the basis of PMID:25351493, in the vacuole lumen of nodule cells undergoing breakdown of the Nod factor receptors - the source of the GO_REF:0000044 subcellular-location IEA to vacuolar lumen.
"SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. Vacuole lumen. Note=Removed from the plasma membrane upon the release of rhizobia into the host cytoplasm. Vacuolar localization is observed in cells undergoing breakdown of the receptors."