lov-1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0016020 membrane	IBA GO_REF:0000033	ACCEPT	Summary: LOV-1 is a multi-pass transmembrane protein with 11 predicted transmembrane helices according to UniProt. The membrane annotation is well-supported by phylogenetic inference across polycystin family members. Reason: LOV-1 is clearly a membrane protein based on its domain architecture (multiple TM domains, GPS region, PLAT domain). UniProt annotation indicates "Multi-pass membrane protein" and the IBA annotation is consistent with polycystin family conservation. Supporting Evidence: PMID:10517638 lov-1 encodes a putative membrane protein with a mucin-like, serine-threonine-rich amino terminus followed by two blocks of homology to human polycystins file:worm/lov-1/lov-1-deep-research-falcon.md model: Edison Scientific Literature
GO:0005262 calcium channel activity	IBA GO_REF:0000033	MODIFY	Summary: The IBA annotation infers calcium channel activity based on polycystin family membership. In mammals, polycystin-1 and polycystin-2 form a mechanosensitive cation channel. However, direct evidence for LOV-1 having intrinsic calcium channel activity is limited; rather, LOV-1 appears to function as a receptor that partners with the TRP channel PKD-2. Reason: LOV-1 is a PC1-family member that partners with the TRPP channel PKD-2. The channel activity likely resides primarily in PKD-2, while LOV-1 functions as a receptor component of the complex. A more accurate annotation would be "calcium channel regulator activity" or simply retain the broader "cation channel activity" annotation if the complex is considered a functional unit. However, given the IBA evidence across the polycystin family, this annotation is not entirely wrong but may be an over-annotation for LOV-1 specifically. Proposed replacements: ligand-gated ion channel activity Supporting Evidence: PMID:11553327 It has recently been demonstrated that polycystin-1 and polycystin-2 (encoded by PKD1 and PKD2, respectively) assemble to form a cation channel in vitro
GO:0050982 detection of mechanical stimulus	IBA GO_REF:0000033	ACCEPT	Summary: LOV-1 functions as a mechanosensory receptor in male-specific sensory neurons. The LOV-1/PKD-2 complex detects contact with the hermaphrodite during mating. This annotation is well-supported by phylogenetic inference and functional studies. Reason: LOV-1 is required for response to hermaphrodite contact during male mating, which is a mechanosensory behavior. The polycystin complex (PC1/PC2) functions as a mechanosensor in both mammals and C. elegans. The IBA annotation is appropriate. Supporting Evidence: PMID:10517638 lov-1 (for location of vulva), that is required for two male sensory behaviours: response and vulva location PMID:12411744 Based on the role of polycystins in C. elegans sensory neuron function and the conservation of PKD pathways we suggest that polycystins act as sensors of the extracellular environment
GO:0005929 cilium	IEA GO_REF:0000044	ACCEPT	Summary: LOV-1 localizes to sensory cilia in male-specific neurons. This is well-documented by multiple publications using GFP fusion proteins. Reason: The IEA annotation based on UniProt subcellular location is correct and supported by experimental evidence (IDA annotations with same GO term exist). LOV-1::GFP localizes to cilia and ciliary base. Supporting Evidence: PMID:11553327 LOV-1::GFP and PKD-2::GFP are expressed in the same male-specific sensory neurons and are concentrated in cilia and cell bodies
GO:0016020 membrane	IEA GO_REF:0000044	ACCEPT	Summary: Duplicate membrane annotation from UniProt subcellular location mapping. LOV-1 is a multi-pass transmembrane protein. Reason: This is a valid annotation. LOV-1 has 11 predicted transmembrane helices and is clearly membrane-localized. Duplicate annotations with different evidence codes are acceptable. Supporting Evidence: PMID:10517638 lov-1 encodes a putative membrane protein
GO:0070588 calcium ion transmembrane transport	IEA GO_REF:0000108	MODIFY	Summary: This annotation is inferred from the calcium channel activity annotation. Since the calcium channel activity annotation is questionable for LOV-1 specifically (channel activity may reside primarily in PKD-2), this inferred annotation is similarly uncertain. Reason: LOV-1 is part of a receptor-channel complex with PKD-2. The transport activity is more directly attributable to PKD-2. LOV-1's role is as a receptor/regulatory component. This annotation follows from the MF annotation which may be an over-annotation. Proposed replacements: regulation of metal ion transport Supporting Evidence: PMID:11553327 polycystin-1 and polycystin-2 (encoded by PKD1 and PKD2, respectively) assemble to form a cation channel in vitro
GO:0005515 protein binding	IPI PMID:15563610 ATP-2 interacts with the PLAT domain of LOV-1 and is involve...	MODIFY	Summary: LOV-1 physically interacts with ATP-2 (F1-ATP synthase beta subunit) via its PLAT domain. This interaction is documented in PMID:15563610. Reason: The generic "protein binding" annotation is uninformative. LOV-1 interacts with ATP-2 via its PLAT domain, which should be captured with a more specific term. The annotation should be replaced with "protein domain specific binding" which better reflects the documented PLAT domain-mediated interaction. Proposed replacements: protein domain specific binding Supporting Evidence: PMID:15563610 ATP-2, the beta subunit of the ATP synthase, physically associates with the LOV-1 PLAT domain and that this interaction is evolutionarily conserved
GO:0005515 protein binding	IPI PMID:16481400 Casein kinase II and calcineurin modulate TRPP function and ...	MODIFY	Summary: LOV-1 interacts with KIN-10, the regulatory subunit of casein kinase II. This interaction was identified in a yeast two-hybrid screen and validated. Reason: Generic "protein binding" is uninformative. The interaction with KIN-10 (casein kinase II regulatory subunit) is through the LOV-1 C-terminus. A more specific term would be preferable. Proposed replacements: protein domain specific binding Supporting Evidence: PMID:16481400 We identified the regulatory subunit of the serine-threonine casein kinase II (CK2) as a binding partner of LOV-1 and human PC-1
GO:0071683 sensory dendrite	NAS PMID:11553327 The Caenorhabditis elegans autosomal dominant polycystic kid...	ACCEPT	Summary: LOV-1 localizes to sensory structures of male-specific neurons. The neurons expressing LOV-1 have ciliated sensory endings. This annotation captures localization to the sensory process. Reason: LOV-1::GFP is concentrated in the sensory endings of ray, hook, and CEM neurons. These sensory neurons have ciliated dendrites. The NAS annotation is appropriate based on the published expression pattern. Supporting Evidence: PMID:11553327 LOV-1::GFP and PKD-2::GFP are expressed in the same male-specific sensory neurons and are concentrated in cilia and cell bodies
GO:1902435 regulation of male mating behavior	NAS PMID:10517638 A polycystic kidney-disease gene homologue required for male...	ACCEPT	Summary: LOV-1 is required for male mating behavior. Loss of lov-1 function results in defects in response to hermaphrodite contact and vulva location during mating. Reason: This accurately describes LOV-1 function. The gene was identified based on male mating defects and is named for the vulva location defect. LOV-1 is required for proper execution of male mating behavior. Supporting Evidence: PMID:10517638 Here we identify a gene, lov-1 (for location of vulva), that is required for two male sensory behaviours: response and vulva location
GO:0019904 protein domain specific binding	IPI PMID:17581863 STAM and Hrs down-regulate ciliary TRP receptors.	ACCEPT	Summary: LOV-1 interacts with STAM-1A (signal transduction adaptor molecule) via its C-terminus. This interaction is involved in endosomal trafficking and degradation of the LOV-1/PKD-2 complex. Reason: The protein domain specific binding annotation is appropriate for this interaction. LOV-1 C-terminus interacts with STAM-1A C-terminus, representing a domain-specific interaction. Supporting Evidence: PMID:17581863 signal transduction adaptor molecule STAM-1A interacts with C. elegans LOV-1 (PC1), and that STAM functions with hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs) on early endosomes to direct the LOV-1-PKD-2 complex for lysosomal degradation
GO:0034606 response to hermaphrodite contact	IMP PMID:10517638 A polycystic kidney-disease gene homologue required for male...	ACCEPT	Summary: lov-1 mutant males are defective in response behavior - the initial sensory response when males contact a hermaphrodite. This is one of the two core behavioral phenotypes of lov-1 mutants. Reason: This is a core function of LOV-1. The original paper identified lov-1 mutants based on defects in response and vulva location behaviors. This annotation is well-supported by mutant phenotype analysis. Supporting Evidence: PMID:10517638 lov-1 (for location of vulva), that is required for two male sensory behaviours: response and vulva location
GO:0034606 response to hermaphrodite contact	IMP PMID:11553327 The Caenorhabditis elegans autosomal dominant polycystic kid...	ACCEPT	Summary: Confirms the response behavior defect in lov-1 mutants and demonstrates that lov-1 and pkd-2 act in the same pathway. Reason: This annotation provides additional evidence for LOV-1 function in response behavior, demonstrating the phenotype is consistent across studies. Supporting Evidence: PMID:11553327 Mutations in either lov-1 or pkd-2 result in identical male sensory behavioral defects. Also, pkd-2;lov-1 double mutants are no more severe than either of the single mutants, indicating that lov-1 and pkd-2 act together.
GO:0034606 response to hermaphrodite contact	IMP PMID:12411744 Towards understanding the polycystins.	ACCEPT	Summary: Confirms response behavior defects in lov-1 mutants in the context of polycystin functional studies. Reason: Additional confirmation of LOV-1 role in response behavior from an independent study. Supporting Evidence: PMID:12411744 Mutation analysis in C. elegans showed similarly compromised male mating behaviors in all single and double lov-1 and pkd-2 mutants
GO:0034606 response to hermaphrodite contact	IMP PMID:15563610 ATP-2 interacts with the PLAT domain of LOV-1 and is involve...	ACCEPT	Summary: Demonstrates that ATP-2 and LOV-1 act in the same pathway for response behavior. Reason: Confirms LOV-1 role in response behavior and extends understanding of the pathway to include ATP-2 as a signaling component. Supporting Evidence: PMID:15563610 atp-2, lov-1, and pkd-2 act in the same molecular pathway
GO:0034608 vulval location	IMP PMID:10517638 A polycystic kidney-disease gene homologue required for male...	ACCEPT	Summary: lov-1 mutant males are defective in vulva location - the behavior where males scan the hermaphrodite body to locate the vulva for spicule insertion. This is the phenotype for which the gene is named. Reason: This is a core function of LOV-1 and the basis for the gene name (Location Of Vulva). Well-supported by mutant analysis in the original paper. Supporting Evidence: PMID:10517638 Here we identify a gene, lov-1 (for location of vulva), that is required for two male sensory behaviours: response and vulva location
GO:0034608 vulval location	IMP PMID:11553327 The Caenorhabditis elegans autosomal dominant polycystic kid...	ACCEPT	Summary: Confirms vulva location defect in lov-1 mutants and shows lov-1 and pkd-2 act together. Reason: Confirms the vulva location phenotype and demonstrates genetic pathway relationship with pkd-2. Supporting Evidence: PMID:11553327 Mutations in either lov-1 or pkd-2 result in identical male sensory behavioral defects
GO:0034608 vulval location	IMP PMID:12411744 Towards understanding the polycystins.	ACCEPT	Summary: Confirms vulva location phenotype in context of polycystin function studies. Reason: Additional confirmation of vulva location phenotype from independent study. Supporting Evidence: PMID:12411744 Mutation analysis in C. elegans showed similarly compromised male mating behaviors in all single and double lov-1 and pkd-2 mutants
GO:0034608 vulval location	IMP PMID:15563610 ATP-2 interacts with the PLAT domain of LOV-1 and is involve...	ACCEPT	Summary: Demonstrates vulva location defects and ATP-2 pathway involvement. Reason: Confirms vulva location phenotype and extends pathway understanding. Supporting Evidence: PMID:15563610 atp-2, lov-1, and pkd-2 act in the same molecular pathway
GO:0005515 protein binding	IPI PMID:17581863 STAM and Hrs down-regulate ciliary TRP receptors.	MODIFY	Summary: Duplicate annotation for protein binding with STAM-1. This appears to be redundant with the protein domain specific binding annotation. Reason: This is a less informative duplicate of the protein domain specific binding annotation (GO:0019904) from the same reference. The interaction with STAM-1A is domain-specific and should be annotated with the more informative term. Proposed replacements: protein domain specific binding Supporting Evidence: PMID:17581863 signal transduction adaptor molecule STAM-1A interacts with C. elegans LOV-1 (PC1)
GO:0005929 cilium	IDA PMID:15563610 ATP-2 interacts with the PLAT domain of LOV-1 and is involve...	ACCEPT	Summary: LOV-1 localizes to cilia in male-specific sensory neurons, demonstrated by GFP fusion protein imaging. Reason: Direct observation of LOV-1::GFP localization to cilia. Well-supported experimental evidence. Supporting Evidence: PMID:15563610 The C. elegans polycystins LOV-1 and PKD-2 are required for male mating behaviors and are localized to sensory cilia
GO:0060179 male mating behavior	IMP PMID:15563610 ATP-2 interacts with the PLAT domain of LOV-1 and is involve...	ACCEPT	Summary: lov-1 mutants show defects in male mating behavior, specifically in response and vulva location steps. Reason: This is a core function of LOV-1. The gene is required for proper male mating behavior. Supporting Evidence: PMID:15563610 Disrupting the function of the ATP synthase or overexpression of atp-2 results in a male mating behavior defect
GO:0097730 non-motile cilium	IDA PMID:10517638 A polycystic kidney-disease gene homologue required for male...	ACCEPT	Summary: LOV-1 is expressed in sensory neurons with non-motile (primary) cilia. The ray, hook, and CEM neurons have sensory cilia that do not beat. Reason: The sensory cilia of C. elegans sensory neurons are non-motile cilia. LOV-1 localizes to these structures. Supporting Evidence: PMID:10517638 lov-1 is expressed in adult males in sensory neurons of the rays, hook and head
GO:0097730 non-motile cilium	IDA PMID:17581863 STAM and Hrs down-regulate ciliary TRP receptors.	ACCEPT	Summary: Confirms LOV-1 localization to non-motile cilia with additional detail about ciliary base localization. Reason: Additional evidence for ciliary localization showing both cilium proper and ciliary base localization. Supporting Evidence: PMID:17581863 In a stam-1 mutant, both LOV-1 and PKD-2 improperly accumulate at the ciliary base
GO:0007617 mating behavior	IMP PMID:10517638 A polycystic kidney-disease gene homologue required for male...	ACCEPT	Summary: lov-1 mutants are defective in mating behavior. This is a broader term than "male mating behavior" but accurately describes the phenotype. Reason: LOV-1 is required for mating behavior. This broader term encompasses the specific defects in response and vulva location. Supporting Evidence: PMID:10517638 lov-1 (for location of vulva), that is required for two male sensory behaviours
GO:0007617 mating behavior	IMP PMID:11553327 The Caenorhabditis elegans autosomal dominant polycystic kid...	ACCEPT	Summary: Confirms mating behavior defects in lov-1 mutants. Reason: Additional evidence for mating behavior requirement. Supporting Evidence: PMID:11553327 Mutations in either lov-1 or pkd-2 result in identical male sensory behavioral defects
GO:0007617 mating behavior	IGI PMID:11553327 The Caenorhabditis elegans autosomal dominant polycystic kid...	ACCEPT	Summary: The IGI annotation based on genetic interaction with pkd-2 supports the mating behavior annotation. Double mutants are no more severe than single mutants. Reason: The genetic interaction evidence shows lov-1 and pkd-2 act in the same pathway for mating behavior. Supporting Evidence: PMID:11553327 pkd-2;lov-1 double mutants are no more severe than either of the single mutants, indicating that lov-1 and pkd-2 act together
GO:0043025 neuronal cell body	IDA PMID:10517638 A polycystic kidney-disease gene homologue required for male...	ACCEPT	Summary: LOV-1::GFP is observed in cell bodies of male-specific neurons in addition to cilia. Reason: LOV-1 is expressed in and localizes to neuronal cell bodies, as demonstrated by GFP fusion imaging. Supporting Evidence: PMID:11553327 LOV-1::GFP and PKD-2::GFP are expressed in the same male-specific sensory neurons and are concentrated in cilia and cell bodies
GO:0007617 mating behavior	IMP PMID:15563610 ATP-2 interacts with the PLAT domain of LOV-1 and is involve...	ACCEPT	Summary: Confirms mating behavior defects and extends to ATP-2 pathway. Reason: Additional evidence for mating behavior requirement. Supporting Evidence: PMID:15563610 Disrupting the function of the ATP synthase or overexpression of atp-2 results in a male mating behavior defect
GO:0019904 protein domain specific binding	IPI PMID:15563610 ATP-2 interacts with the PLAT domain of LOV-1 and is involve...	ACCEPT	Summary: LOV-1 PLAT domain interacts with ATP-2 N-terminus. This is a well-characterized domain-specific interaction. Reason: The interaction between LOV-1 PLAT domain and ATP-2 is specific and evolutionarily conserved. Appropriate annotation. Supporting Evidence: PMID:15563610 ATP-2, the beta subunit of the ATP synthase, physically associates with the LOV-1 PLAT domain and that this interaction is evolutionarily conserved

Gene Description

Existing Annotations Review

Core Functions

LOV-1 functions as a mechanosensory receptor in male sensory cilia, forming a complex with PKD-2 (TRPP2/Polycystin-2) to detect mechanical stimuli during male mating behavior. LOV-1 acts as the receptor component that partners with the ion channel PKD-2.

LOV-1 PLAT domain mediates interactions with signaling partners ATP-2 (ATP synthase beta subunit), KIN-10 (CK2 regulatory subunit), and STAM-1 (endosomal adaptor) for signal transduction and receptor trafficking.

References

Tags

Deep Research

Falcon

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