NCU04637 encodes a fungal Rvs167-family endocytic adaptor with an N-terminal BAR domain and a C-terminal SH3 domain. Comparative evidence supports lipid binding and association with cortical actin patches, where Rvs proteins help organize endocytic membrane invaginations and vesicle scission. The detailed localization dynamics and interaction partners of the Neurospora protein remain to be established.
Summary: Rvs167-family placement and BAR/SH3 architecture support a cytoplasmic protein acting at the cytoplasmic face of endocytic membranes.
Reason: Rvs167-family placement and BAR/SH3 architecture support a cytoplasmic protein acting at the cytoplasmic face of endocytic membranes. Characterized fungal Rvs proteins associate with cortical actin patches, a more precise localization than cytoplasm.
Supporting Evidence:
file:NEUCR/NCU04637/NCU04637-uniprot.txt
DR PANTHER; PTHR47174:SF1; REDUCED VIABILITY UPON STARVATION PROTEIN 167; 1.
Rvs161 consists solely of a BAR domain, whereas Rvs167 is composed of a BAR domain followed by a region rich in glycine, proline, and alanine (GPA), and an SH3 (Src-homology 3) domain at its C-terminus
Summary: The Rvs167 subfamily assignment, N-terminal BAR and C-terminal SH3 domains support conserved endocytic function.
Reason: The Rvs167 subfamily assignment, N-terminal BAR and C-terminal SH3 domains support conserved endocytic function. Genetic and biochemical studies of fungal Rvs proteins establish membrane association and a role in endocytic scission.
Supporting Evidence:
file:NEUCR/NCU04637/NCU04637-uniprot.txt
DR PANTHER; PTHR47174:SF1; REDUCED VIABILITY UPON STARVATION PROTEIN 167; 1.
Rvs161 consists solely of a BAR domain, whereas Rvs167 is composed of a BAR domain followed by a region rich in glycine, proline, and alanine (GPA), and an SH3 (Src-homology 3) domain at its C-terminus
Summary: The Rvs167 subfamily assignment, N-terminal BAR and C-terminal SH3 domains support conserved endocytic function.
Reason: The Rvs167 subfamily assignment, N-terminal BAR and C-terminal SH3 domains support conserved endocytic function. Genetic and biochemical studies of fungal Rvs proteins establish membrane association and a role in endocytic scission.
Supporting Evidence:
file:NEUCR/NCU04637/NCU04637-uniprot.txt
DR PANTHER; PTHR47174:SF1; REDUCED VIABILITY UPON STARVATION PROTEIN 167; 1.
Rvs161 consists solely of a BAR domain, whereas Rvs167 is composed of a BAR domain followed by a region rich in glycine, proline, and alanine (GPA), and an SH3 (Src-homology 3) domain at its C-terminus
Summary: Purified Rvs161–Rvs167 binds liposomes, and the target retains the BAR domain and Rvs167-specific architecture.
Reason: Purified Rvs161–Rvs167 binds liposomes, and the target retains the BAR domain and Rvs167-specific architecture. Lipid binding is therefore a defensible conserved property; no particular lipid species is asserted.
Supporting Evidence:
file:NEUCR/NCU04637/NCU04637-uniprot.txt
DR PANTHER; PTHR47174:SF1; REDUCED VIABILITY UPON STARVATION PROTEIN 167; 1.
Rvs161 consists solely of a BAR domain, whereas Rvs167 is composed of a BAR domain followed by a region rich in glycine, proline, and alanine (GPA), and an SH3 (Src-homology 3) domain at its C-terminus
Summary: Rvs167-family proteins act at cortical actin patches during endocytosis.
Reason: Rvs167-family proteins act at cortical actin patches during endocytosis. Target family placement and intact BAR/SH3 architecture support the curated ancestral localization inference.
Supporting Evidence:
file:NEUCR/NCU04637/NCU04637-uniprot.txt
DR PANTHER; PTHR47174:SF1; REDUCED VIABILITY UPON STARVATION PROTEIN 167; 1.
Rvs161 consists solely of a BAR domain, whereas Rvs167 is composed of a BAR domain followed by a region rich in glycine, proline, and alanine (GPA), and an SH3 (Src-homology 3) domain at its C-terminus
Summary: Rvs167-family proteins act at cortical actin patches during endocytosis.
Reason: Rvs167-family proteins act at cortical actin patches during endocytosis. Target family placement and intact BAR/SH3 architecture support the curated ancestral localization inference.
Supporting Evidence:
file:NEUCR/NCU04637/NCU04637-uniprot.txt
DR PANTHER; PTHR47174:SF1; REDUCED VIABILITY UPON STARVATION PROTEIN 167; 1.
Rvs161 consists solely of a BAR domain, whereas Rvs167 is composed of a BAR domain followed by a region rich in glycine, proline, and alanine (GPA), and an SH3 (Src-homology 3) domain at its C-terminus
Summary: Rvs167-family proteins act at cortical actin patches during endocytosis.
Reason: Rvs167-family proteins act at cortical actin patches during endocytosis. Target family placement and intact BAR/SH3 architecture support the curated ancestral localization inference.
Supporting Evidence:
file:NEUCR/NCU04637/NCU04637-uniprot.txt
DR PANTHER; PTHR47174:SF1; REDUCED VIABILITY UPON STARVATION PROTEIN 167; 1.
Rvs161 consists solely of a BAR domain, whereas Rvs167 is composed of a BAR domain followed by a region rich in glycine, proline, and alanine (GPA), and an SH3 (Src-homology 3) domain at its C-terminus
Summary: The medial cortex annotation describes a particular spatial distribution.
Reason: The medial cortex annotation describes a particular spatial distribution. Conserved cortical endocytosis is supported, but the relevant ancestral localization pattern has not been established in Neurospora hyphae; family membership alone does not locate the protein specifically at the cell middle.
Supporting Evidence:
file:NEUCR/NCU04637/NCU04637-uniprot.txt
DR PANTHER; PTHR47174:SF1; REDUCED VIABILITY UPON STARVATION PROTEIN 167; 1.
Rvs161 consists solely of a BAR domain, whereas Rvs167 is composed of a BAR domain followed by a region rich in glycine, proline, and alanine (GPA), and an SH3 (Src-homology 3) domain at its C-terminus
Summary: Mating projection tip localization may be conserved for particular Rvs proteins, but the transfer to this filamentous fungal protein requires evidence about its sexual structures and localization.
Reason: Mating projection tip localization may be conserved for particular Rvs proteins, but the transfer to this filamentous fungal protein requires evidence about its sexual structures and localization. The conserved endocytic role does not determine that exact spatial context.
Supporting Evidence:
file:NEUCR/NCU04637/NCU04637-uniprot.txt
DR PANTHER; PTHR47174:SF1; REDUCED VIABILITY UPON STARVATION PROTEIN 167; 1.
Rvs161 consists solely of a BAR domain, whereas Rvs167 is composed of a BAR domain followed by a region rich in glycine, proline, and alanine (GPA), and an SH3 (Src-homology 3) domain at its C-terminus
Summary: Rvs proteins contribute to cortical actin patch organization, and RVS167 deletion in Candida produces defects in patch polarization.
Reason: Rvs proteins contribute to cortical actin patch organization, and RVS167 deletion in Candida produces defects in patch polarization. Conservation of the Rvs167 BAR/SH3 architecture supports participation in this process.
Supporting Evidence:
file:NEUCR/NCU04637/NCU04637-uniprot.txt
DR PANTHER; PTHR47174:SF1; REDUCED VIABILITY UPON STARVATION PROTEIN 167; 1.
Rvs161 consists solely of a BAR domain, whereas Rvs167 is composed of a BAR domain followed by a region rich in glycine, proline, and alanine (GPA), and an SH3 (Src-homology 3) domain at its C-terminus
The rvs161Delta mutant was more defective in endocytosis and morphogenesis than rvs167Delta, but both were strongly defective in polarizing actin patches.
Summary: The purified fungal Rvs complex induces membrane tubules, supporting the membrane-remodeling capacity of the conserved BAR domain.
Reason: The purified fungal Rvs complex induces membrane tubules, supporting the membrane-remodeling capacity of the conserved BAR domain. In vivo scission studies favor curvature sensing and stabilization as well as possible bending, so this annotation does not imply that NCU04637 alone initiates membrane invagination.
Supporting Evidence:
file:NEUCR/NCU04637/NCU04637-uniprot.txt
DR PANTHER; PTHR47174:SF1; REDUCED VIABILITY UPON STARVATION PROTEIN 167; 1.
Rvs161 consists solely of a BAR domain, whereas Rvs167 is composed of a BAR domain followed by a region rich in glycine, proline, and alanine (GPA), and an SH3 (Src-homology 3) domain at its C-terminus
Summary: The target is assigned specifically to the Rvs167 subfamily rather than Rvs161 by PANTHER, with the expected BAR-plus-SH3 architecture.
Reason: The target is assigned specifically to the Rvs167 subfamily rather than Rvs161 by PANTHER, with the expected BAR-plus-SH3 architecture. Formation of the Rvs161–Rvs167 heterodimer is a conserved fungal family property supported by biochemical work and the curated phylogenetic complex annotation.
Supporting Evidence:
file:NEUCR/NCU04637/NCU04637-uniprot.txt
DR PANTHER; PTHR47174:SF1; REDUCED VIABILITY UPON STARVATION PROTEIN 167; 1.
Rvs161 consists solely of a BAR domain, whereas Rvs167 is composed of a BAR domain followed by a region rich in glycine, proline, and alanine (GPA), and an SH3 (Src-homology 3) domain at its C-terminus
Core Functions
NCU04637 encodes a fungal Rvs167-family endocytic adaptor with an N-terminal BAR domain and a C-terminal SH3 domain.
Rvs161 consists solely of a BAR domain, whereas Rvs167 is composed of a BAR domain followed by a region rich in glycine, proline, and alanine (GPA), and an SH3 (Src-homology 3) domain at its C-terminus
These computational predictions are reviewed separately from the GOA annotation set used for this review. The assessments below are from this project and do not constitute official GO annotations or endorsement by GO/UniProt. They are not included in the existing annotation review above.
Review rationale: PANTHER assigns the target to the Rvs167 subfamily, and its BAR-plus-SH3 architecture matches the characterized fungal endocytic adaptor. Rvs proteins bind membranes and act at cortical actin patches, supporting cytoplasmic residence. Cytoplasm is broader than the supported cortical actin patch annotation already present in GOA. The exact medial-cortex distribution used as a hydration source remains unresolved, but is not needed to establish the broader compartment.
PMID:20610658: "We show that the purified Rvs161-Rvs167 complex binds to liposomes in a curvature-independent manner and promotes tubule formation in vitro."
PMID:20610658: "Rvs161 consists solely of a BAR domain, whereas Rvs167 is composed of a BAR domain followed by a region rich in glycine, proline, and alanine (GPA), and an SH3 (Src-homology 3) domain at its C-terminus"