Sticks and stones (Sns) is a nephrin-related immunoglobulin-superfamily adhesion protein. It recognizes Kirre/Roughest on apposed cells, enabling myoblast fusion and organizing nephrocyte filtration diaphragms. Its extracellular Ig and fibronectin-type domains and intracellular signaling region couple cell recognition to tissue morphogenesis. Sns also contributes to eye organization, sensory-organ spacing and reproductive support-cell functions.
IMP PMID:20599904 Preferential adhesion maintains separation of ommatidia in t...
KEEP AS NON CORE
Summary: Sns participates in the differential adhesion and cellular arrangement of the developing compound eye. Retain this tissue-specific developmental association as noncore relative to its cell-adhesion mechanism; the evidence does not establish an independent photoreceptor fate-specification activity.
Reason: Sns participates in the differential adhesion and cellular arrangement of the developing compound eye. Retain this tissue-specific developmental association as noncore relative to its cell-adhesion mechanism; the evidence does not establish an independent photoreceptor fate-specification activity.
NAS PMID:20599904 Preferential adhesion maintains separation of ommatidia in t...
KEEP AS NON CORE
Summary: Sns participates in the differential adhesion and cellular arrangement of the developing compound eye. Retain this tissue-specific developmental association as noncore relative to its cell-adhesion mechanism; the evidence does not establish an independent photoreceptor fate-specification activity.
Reason: Sns participates in the differential adhesion and cellular arrangement of the developing compound eye. Retain this tissue-specific developmental association as noncore relative to its cell-adhesion mechanism; the evidence does not establish an independent photoreceptor fate-specification activity.
IPI PMID:18971929 The insect nephrocyte is a podocyte-like cell with a filtrat...
KEEP AS NON CORE
Summary: The primary study demonstrates binding of the Sns intracellular region to Mec2/podocin in the nephrocyte diaphragm complex. Preserve the experimentally supported interaction as noncore; generic protein binding does not describe the principal extracellular adhesion activity.
Reason: The primary study demonstrates binding of the Sns intracellular region to Mec2/podocin in the nephrocyte diaphragm complex. Preserve the experimentally supported interaction as noncore; generic protein binding does not describe the principal extracellular adhesion activity.
IPI PMID:23827685 An extracellular interactome of immunoglobulin and LRR prote...
MODIFY
Summary: Sns binds the extracellular adhesion protein Roughest; the interaction is part of the conserved nephrin/NEPH adhesion system. Cell adhesion molecule binding is more informative than generic protein binding, and the Drosophila heterocomplex is directly measured.
Reason: Sns binds the extracellular adhesion protein Roughest; the interaction is part of the conserved nephrin/NEPH adhesion system. Cell adhesion molecule binding is more informative than generic protein binding, and the Drosophila heterocomplex is directly measured.
IPI PMID:23827685 An extracellular interactome of immunoglobulin and LRR prote...
KEEP AS NON CORE
Summary: The extracellular interactome records an interaction with Unc-5. Retain the binding observation as noncore rather than infer a particular guidance pathway or ligand activity from this screen alone.
Reason: The extracellular interactome records an interaction with Unc-5. Retain the binding observation as noncore rather than infer a particular guidance pathway or ligand activity from this screen alone.
IPI PMID:24485456 Extracellular architecture of the SYG-1/SYG-2 adhesion compl...
MODIFY
Summary: Sns binds the extracellular adhesion protein Roughest; the interaction is part of the conserved nephrin/NEPH adhesion system. Cell adhesion molecule binding is more informative than generic protein binding, and the Drosophila heterocomplex is directly measured.
Reason: Sns binds the extracellular adhesion protein Roughest; the interaction is part of the conserved nephrin/NEPH adhesion system. Cell adhesion molecule binding is more informative than generic protein binding, and the Drosophila heterocomplex is directly measured.
Summary: Sns is a cell-surface adhesion molecule enriched at myoblast contacts and nephrocyte junctions. Primary localization supports the membrane/junction assignment independently of automated location propagation.
Reason: Sns is a cell-surface adhesion molecule enriched at myoblast contacts and nephrocyte junctions. Primary localization supports the membrane/junction assignment independently of automated location propagation.
Sns and Kirre proteins localize to the ND at the entry point into the labyrinthine channels and, like their vertebrate counterparts, are essential for its formation.
IDA PMID:10859168 Drosophila SNS, a member of the immunoglobulin superfamily t...
ACCEPT
Summary: Sns is a cell-surface adhesion molecule enriched at myoblast contacts and nephrocyte junctions. Primary localization supports the membrane/junction assignment independently of automated location propagation.
Reason: Sns is a cell-surface adhesion molecule enriched at myoblast contacts and nephrocyte junctions. Primary localization supports the membrane/junction assignment independently of automated location propagation.
Sns and Kirre proteins localize to the ND at the entry point into the labyrinthine channels and, like their vertebrate counterparts, are essential for its formation.
IDA PMID:18971929 The insect nephrocyte is a podocyte-like cell with a filtrat...
ACCEPT
Summary: Sns is a cell-surface adhesion molecule enriched at myoblast contacts and nephrocyte junctions. Primary localization supports the membrane/junction assignment independently of automated location propagation.
Reason: Sns is a cell-surface adhesion molecule enriched at myoblast contacts and nephrocyte junctions. Primary localization supports the membrane/junction assignment independently of automated location propagation.
Sns and Kirre proteins localize to the ND at the entry point into the labyrinthine channels and, like their vertebrate counterparts, are essential for its formation.
Summary: Sns is a cell-surface adhesion molecule enriched at myoblast contacts and nephrocyte junctions. Primary localization supports the membrane/junction assignment independently of automated location propagation.
Reason: Sns is a cell-surface adhesion molecule enriched at myoblast contacts and nephrocyte junctions. Primary localization supports the membrane/junction assignment independently of automated location propagation.
Sns and Kirre proteins localize to the ND at the entry point into the labyrinthine channels and, like their vertebrate counterparts, are essential for its formation.
IDA PMID:18971929 The insect nephrocyte is a podocyte-like cell with a filtrat...
ACCEPT
Summary: Sns is a structural cell-adhesion component of the nephrocyte diaphragm. Direct localization and loss-of-function studies support its presence and role at this filtration junction.
Reason: Sns is a structural cell-adhesion component of the nephrocyte diaphragm. Direct localization and loss-of-function studies support its presence and role at this filtration junction.
Sns and Kirre proteins localize to the ND at the entry point into the labyrinthine channels and, like their vertebrate counterparts, are essential for its formation.
IDA PMID:19515699 Sns and Kirre, the Drosophila orthologs of Nephrin and Neph1...
ACCEPT
Summary: Sns is a structural cell-adhesion component of the nephrocyte diaphragm. Direct localization and loss-of-function studies support its presence and role at this filtration junction.
Reason: Sns is a structural cell-adhesion component of the nephrocyte diaphragm. Direct localization and loss-of-function studies support its presence and role at this filtration junction.
Sns and Kirre proteins localize to the ND at the entry point into the labyrinthine channels and, like their vertebrate counterparts, are essential for its formation.
IDA PMID:38878170 Phospholipid scramblase 1: an essential component of the nep...
ACCEPT
Summary: Sns is a structural cell-adhesion component of the nephrocyte diaphragm. Direct localization and loss-of-function studies support its presence and role at this filtration junction.
Reason: Sns is a structural cell-adhesion component of the nephrocyte diaphragm. Direct localization and loss-of-function studies support its presence and role at this filtration junction.
Sns and Kirre proteins localize to the ND at the entry point into the labyrinthine channels and, like their vertebrate counterparts, are essential for its formation.
IGI PMID:19515699 Sns and Kirre, the Drosophila orthologs of Nephrin and Neph1...
UNDECIDED
Summary: The accessible primary abstract establishes Sns-dependent adhesion between garland nephrocytes, but does not resolve whether the required molecular interaction is homophilic rather than SnsβKirre heterophilic binding. Preserve the experimental IGI assertion unresolved until the full mechanistic evidence can be checked.
Reason: The accessible primary abstract establishes Sns-dependent adhesion between garland nephrocytes, but does not resolve whether the required molecular interaction is homophilic rather than SnsβKirre heterophilic binding. Preserve the experimental IGI assertion unresolved until the full mechanistic evidence can be checked.
IDA PMID:19270174 The immunoglobulin superfamily member Hbs functions redundan...
ACCEPT
Summary: Sns on fusion-competent myoblasts engages Kirre/Roughest on founder cells, directly supporting heterophilic recognition and adhesion. This adhesive mechanism also supports specialized nephrocyte contacts.
Reason: Sns on fusion-competent myoblasts engages Kirre/Roughest on founder cells, directly supporting heterophilic recognition and adhesion. This adhesive mechanism also supports specialized nephrocyte contacts.
Sns and Kirre proteins localize to the ND at the entry point into the labyrinthine channels and, like their vertebrate counterparts, are essential for its formation.
IMP PMID:15955848 A positive feedback loop between Dumbfounded and Rolling peb...
ACCEPT
Summary: Sns on fusion-competent myoblasts engages Kirre/Roughest on founder cells, directly supporting heterophilic recognition and adhesion. This adhesive mechanism also supports specialized nephrocyte contacts.
Reason: Sns on fusion-competent myoblasts engages Kirre/Roughest on founder cells, directly supporting heterophilic recognition and adhesion. This adhesive mechanism also supports specialized nephrocyte contacts.
Sns and Kirre proteins localize to the ND at the entry point into the labyrinthine channels and, like their vertebrate counterparts, are essential for its formation.
IMP PMID:21652648 The WASp-based actin polymerization machinery is required in...
KEEP AS NON CORE
Summary: Sns participates in the somatic support-cell machinery required for spermatid maturation/release. Retain this developmental role without implying a sperm-intrinsic enzymatic function.
Reason: Sns participates in the somatic support-cell machinery required for spermatid maturation/release. Retain this developmental role without implying a sperm-intrinsic enzymatic function.
IMP PMID:15955848 A positive feedback loop between Dumbfounded and Rolling peb...
ACCEPT
Summary: Sns is required on fusion-competent myoblasts for their adhesion to founder cells and subsequent muscle-fiber formation. The defining unfused-myoblast phenotype and receptor-ligand mechanism independently establish the gene-level myoblast-fusion role.
Reason: Sns is required on fusion-competent myoblasts for their adhesion to founder cells and subsequent muscle-fiber formation. The defining unfused-myoblast phenotype and receptor-ligand mechanism independently establish the gene-level myoblast-fusion role.
The Drosophila sticks-and-stones (sns) locus was identified on the basis of its mutant phenotype, the complete absence of body wall muscles and corresponding presence of unfused myoblasts.
IMP PMID:18003739 SCAR/WAVE and Arp2/3 are crucial for cytoskeletal remodeling...
ACCEPT
Summary: Sns is required on fusion-competent myoblasts for their adhesion to founder cells and subsequent muscle-fiber formation. The defining unfused-myoblast phenotype and receptor-ligand mechanism independently establish the gene-level myoblast-fusion role.
Reason: Sns is required on fusion-competent myoblasts for their adhesion to founder cells and subsequent muscle-fiber formation. The defining unfused-myoblast phenotype and receptor-ligand mechanism independently establish the gene-level myoblast-fusion role.
The Drosophila sticks-and-stones (sns) locus was identified on the basis of its mutant phenotype, the complete absence of body wall muscles and corresponding presence of unfused myoblasts.
IMP PMID:19270174 The immunoglobulin superfamily member Hbs functions redundan...
ACCEPT
Summary: Sns is required on fusion-competent myoblasts for their adhesion to founder cells and subsequent muscle-fiber formation. The defining unfused-myoblast phenotype and receptor-ligand mechanism independently establish the gene-level myoblast-fusion role.
Reason: Sns is required on fusion-competent myoblasts for their adhesion to founder cells and subsequent muscle-fiber formation. The defining unfused-myoblast phenotype and receptor-ligand mechanism independently establish the gene-level myoblast-fusion role.
The Drosophila sticks-and-stones (sns) locus was identified on the basis of its mutant phenotype, the complete absence of body wall muscles and corresponding presence of unfused myoblasts.
IMP PMID:11744371 The formation of syncytia within the visceral musculature of...
KEEP AS NON CORE
Summary: Mutations in sns disrupt fusion-dependent visceral muscle development. This is a tissue-specific consequence of its conserved adhesive myoblast-fusion mechanism.
Reason: Mutations in sns disrupt fusion-dependent visceral muscle development. This is a tissue-specific consequence of its conserved adhesive myoblast-fusion mechanism.
Mutations of genes that are involved in somatic myoblast fusion, such as sns, dumbfounded (duf) or myoblast city (mbc), also cause severe defects within the visceral musculature.
IGI PMID:26053791 The Cell Adhesion Molecules Roughest, Hibris, Kin of Irre an...
KEEP AS NON CORE
Summary: Sns contributes to positioning of sensory-bristle precursors through tissue adhesion. This specific morphogenesis role is retained as noncore relative to its underlying cell-recognition mechanism.
Reason: Sns contributes to positioning of sensory-bristle precursors through tissue adhesion. This specific morphogenesis role is retained as noncore relative to its underlying cell-recognition mechanism.
Summary: The broad developmental annotation is consistent with gene-specific muscle-fusion, eye-patterning and nephrocyte-development evidence. These are correct umbrella descriptions but less informative than the specific adhesion and junction-assembly functions; automated provenance itself is not their biological support.
Reason: The broad developmental annotation is consistent with gene-specific muscle-fusion, eye-patterning and nephrocyte-development evidence. These are correct umbrella descriptions but less informative than the specific adhesion and junction-assembly functions; automated provenance itself is not their biological support.
The Drosophila sticks-and-stones (sns) locus was identified on the basis of its mutant phenotype, the complete absence of body wall muscles and corresponding presence of unfused myoblasts.
Sns and Kirre proteins localize to the ND at the entry point into the labyrinthine channels and, like their vertebrate counterparts, are essential for its formation.
Summary: Sns is a cell-surface adhesion molecule enriched at myoblast contacts and nephrocyte junctions. Primary localization supports the membrane/junction assignment independently of automated location propagation.
Reason: Sns is a cell-surface adhesion molecule enriched at myoblast contacts and nephrocyte junctions. Primary localization supports the membrane/junction assignment independently of automated location propagation.
Sns and Kirre proteins localize to the ND at the entry point into the labyrinthine channels and, like their vertebrate counterparts, are essential for its formation.
GO:0016202 regulation of striated muscle tissue development
NAS PMID:20186342 The intracellular domain of Dumbfounded affects myoblast fus...
KEEP AS NON CORE
Summary: The gene participates in formation of striated muscle through myoblast recognition and fusion. Retain this broad regulatory developmental description as noncore; the more specific fusion annotations capture the direct role.
Reason: The gene participates in formation of striated muscle through myoblast recognition and fusion. Retain this broad regulatory developmental description as noncore; the more specific fusion annotations capture the direct role.
The Drosophila sticks-and-stones (sns) locus was identified on the basis of its mutant phenotype, the complete absence of body wall muscles and corresponding presence of unfused myoblasts.
IDA PMID:26053791 The Cell Adhesion Molecules Roughest, Hibris, Kin of Irre an...
ACCEPT
Summary: Sns is localized in the apical contact region of sensory-organ precursor cells in the wing-disc analysis. This is consistent with its membrane-adhesion role, without implying universal apical localization in every tissue.
Reason: Sns is localized in the apical contact region of sensory-organ precursor cells in the wing-disc analysis. This is consistent with its membrane-adhesion role, without implying universal apical localization in every tissue.
IMP PMID:18003739 SCAR/WAVE and Arp2/3 are crucial for cytoskeletal remodeling...
UNDECIDED
Summary: The cited study addresses actin foci at myoblast-fusion sites, but its cached abstract does not resolve the Sns-specific actin-remodeling result. Sns-dependent fusion is firmly established; this particular downstream cytoskeletal assertion remains unresolved pending access to the full experimental analysis.
Reason: The cited study addresses actin foci at myoblast-fusion sites, but its cached abstract does not resolve the Sns-specific actin-remodeling result. Sns-dependent fusion is firmly established; this particular downstream cytoskeletal assertion remains unresolved pending access to the full experimental analysis.
The Drosophila sticks-and-stones (sns) locus was identified on the basis of its mutant phenotype, the complete absence of body wall muscles and corresponding presence of unfused myoblasts.
Summary: The broad developmental annotation is consistent with gene-specific muscle-fusion, eye-patterning and nephrocyte-development evidence. These are correct umbrella descriptions but less informative than the specific adhesion and junction-assembly functions; automated provenance itself is not their biological support.
Reason: The broad developmental annotation is consistent with gene-specific muscle-fusion, eye-patterning and nephrocyte-development evidence. These are correct umbrella descriptions but less informative than the specific adhesion and junction-assembly functions; automated provenance itself is not their biological support.
The Drosophila sticks-and-stones (sns) locus was identified on the basis of its mutant phenotype, the complete absence of body wall muscles and corresponding presence of unfused myoblasts.
Sns and Kirre proteins localize to the ND at the entry point into the labyrinthine channels and, like their vertebrate counterparts, are essential for its formation.
IMP PMID:18971929 The insect nephrocyte is a podocyte-like cell with a filtrat...
ACCEPT
Summary: Loss of Sns reduces or abolishes the nephrocyte diaphragm, demonstrating a direct structural adhesion contribution to assembly of the filtration junction.
Reason: Loss of Sns reduces or abolishes the nephrocyte diaphragm, demonstrating a direct structural adhesion contribution to assembly of the filtration junction.
Sns and Kirre proteins localize to the ND at the entry point into the labyrinthine channels and, like their vertebrate counterparts, are essential for its formation.
IMP PMID:19515699 Sns and Kirre, the Drosophila orthologs of Nephrin and Neph1...
ACCEPT
Summary: Loss of Sns reduces or abolishes the nephrocyte diaphragm, demonstrating a direct structural adhesion contribution to assembly of the filtration junction.
Reason: Loss of Sns reduces or abolishes the nephrocyte diaphragm, demonstrating a direct structural adhesion contribution to assembly of the filtration junction.
Sns and Kirre proteins localize to the ND at the entry point into the labyrinthine channels and, like their vertebrate counterparts, are essential for its formation.
Summary: The binding of Sns to Kirre/Roughest is supported by cell-recognition experiments and direct measurements of Drosophila heterocomplexes. This is a specific core molecular activity.
Reason: The binding of Sns to Kirre/Roughest is supported by cell-recognition experiments and direct measurements of Drosophila heterocomplexes. This is a specific core molecular activity.
IMP PMID:19515699 Sns and Kirre, the Drosophila orthologs of Nephrin and Neph1...
KEEP AS NON CORE
Summary: Sns mediates adhesion and fusion of garland nephrocytes into binucleate cells and supports their diaphragm formation. Retain the corresponding differentiation phenotype as a context-specific developmental consequence.
Reason: Sns mediates adhesion and fusion of garland nephrocytes into binucleate cells and supports their diaphragm formation. Retain the corresponding differentiation phenotype as a context-specific developmental consequence.
IMP PMID:18971929 The insect nephrocyte is a podocyte-like cell with a filtrat...
ACCEPT
Summary: Sns is an essential structural component of the nephrocyte filtration diaphragm; its depletion disrupts the junction and abolishes protein uptake. It participates in filtration without acting as an active solute pump.
Reason: Sns is an essential structural component of the nephrocyte filtration diaphragm; its depletion disrupts the junction and abolishes protein uptake. It participates in filtration without acting as an active solute pump.
Sns and Kirre proteins localize to the ND at the entry point into the labyrinthine channels and, like their vertebrate counterparts, are essential for its formation.
IMP PMID:23291470 An in vivo functional analysis system for renal gene discove...
ACCEPT
Summary: Sns is an essential structural component of the nephrocyte filtration diaphragm; its depletion disrupts the junction and abolishes protein uptake. It participates in filtration without acting as an active solute pump.
Reason: Sns is an essential structural component of the nephrocyte filtration diaphragm; its depletion disrupts the junction and abolishes protein uptake. It participates in filtration without acting as an active solute pump.
Sns and Kirre proteins localize to the ND at the entry point into the labyrinthine channels and, like their vertebrate counterparts, are essential for its formation.
Summary: Sns on fusion-competent myoblasts engages Kirre/Roughest on founder cells, directly supporting heterophilic recognition and adhesion. This adhesive mechanism also supports specialized nephrocyte contacts.
Reason: Sns on fusion-competent myoblasts engages Kirre/Roughest on founder cells, directly supporting heterophilic recognition and adhesion. This adhesive mechanism also supports specialized nephrocyte contacts.
Sns and Kirre proteins localize to the ND at the entry point into the labyrinthine channels and, like their vertebrate counterparts, are essential for its formation.
NAS PMID:19515699 Sns and Kirre, the Drosophila orthologs of Nephrin and Neph1...
ACCEPT
Summary: Sns on fusion-competent myoblasts engages Kirre/Roughest on founder cells, directly supporting heterophilic recognition and adhesion. This adhesive mechanism also supports specialized nephrocyte contacts.
Reason: Sns on fusion-competent myoblasts engages Kirre/Roughest on founder cells, directly supporting heterophilic recognition and adhesion. This adhesive mechanism also supports specialized nephrocyte contacts.
Sns and Kirre proteins localize to the ND at the entry point into the labyrinthine channels and, like their vertebrate counterparts, are essential for its formation.
IPI PMID:19270174 The immunoglobulin superfamily member Hbs functions redundan...
ACCEPT
Summary: Sns on fusion-competent myoblasts engages Kirre/Roughest on founder cells, directly supporting heterophilic recognition and adhesion. This adhesive mechanism also supports specialized nephrocyte contacts.
Reason: Sns on fusion-competent myoblasts engages Kirre/Roughest on founder cells, directly supporting heterophilic recognition and adhesion. This adhesive mechanism also supports specialized nephrocyte contacts.
Sns and Kirre proteins localize to the ND at the entry point into the labyrinthine channels and, like their vertebrate counterparts, are essential for its formation.
GO:0098636 protein complex involved in cell adhesion
IPI PMID:23827685 An extracellular interactome of immunoglobulin and LRR prote...
ACCEPT
Summary: The extracellular SnsβKirre/Roughest adhesion complex is physically supported by the interactome and independent heterocomplex affinity measurements. This provides a specific complex context for its cell-adhesion activity.
Reason: The extracellular SnsβKirre/Roughest adhesion complex is physically supported by the interactome and independent heterocomplex affinity measurements. This provides a specific complex context for its cell-adhesion activity.
theDrosophila homologs of SYG-1(Rst and Duf/Kirre) and of SYG-2(SNS and Hbs)all form hetero-complexes withaffinities between 1 to 4 ΞΌM
GO:0160108 animal gross anatomical part developmental process
IEA GO_REF:0000117
KEEP AS NON CORE
Summary: The broad developmental annotation is consistent with gene-specific muscle-fusion, eye-patterning and nephrocyte-development evidence. These are correct umbrella descriptions but less informative than the specific adhesion and junction-assembly functions; automated provenance itself is not their biological support.
Reason: The broad developmental annotation is consistent with gene-specific muscle-fusion, eye-patterning and nephrocyte-development evidence. These are correct umbrella descriptions but less informative than the specific adhesion and junction-assembly functions; automated provenance itself is not their biological support.
The Drosophila sticks-and-stones (sns) locus was identified on the basis of its mutant phenotype, the complete absence of body wall muscles and corresponding presence of unfused myoblasts.
Sns and Kirre proteins localize to the ND at the entry point into the labyrinthine channels and, like their vertebrate counterparts, are essential for its formation.
NAS PMID:11684662 Characterization of Drosophila hibris, a gene related to hum...
ACCEPT
Summary: Sns has a well-established gene-level role in myoblast fusion, with its cytoplasmic domain required for precursor formation. The Hibris-focused reference alone is not used to infer the Sns mechanism; direct Sns experiments support the process.
Reason: Sns has a well-established gene-level role in myoblast fusion, with its cytoplasmic domain required for precursor formation. The Hibris-focused reference alone is not used to infer the Sns mechanism; direct Sns experiments support the process.
The Drosophila sticks-and-stones (sns) locus was identified on the basis of its mutant phenotype, the complete absence of body wall muscles and corresponding presence of unfused myoblasts.
The Drosophila sticks-and-stones (sns) locus was identified on the basis of its mutant phenotype, the complete absence of body wall muscles and corresponding presence of unfused myoblasts.
Sns and Kirre proteins localize to the ND at the entry point into the labyrinthine channels and, like their vertebrate counterparts, are essential for its formation.
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.
Sns has established gene-level developmental roles, but the selected isoform B contains an extra 63-residue insertion with a predicted membrane-spanning segment. Gene-level Sns-dependent muscle and tissue morphogenesis is strongly supported. Membrane association is supported by the retained hydrophobic regions and direct Sns cell-surface localization.
Review rationale: Sns has established gene-level developmental roles, but the selected isoform B contains an extra 63-residue insertion with a predicted membrane-spanning segment. All shared residues are conserved, yet an additional membrane crossing could change presentation of the signaling tail required in fusion and differentiation. The accessible experiments do not resolve this topology or establish function of this exact longer form. Thus the prediction remains uncertain for the selected sequence, without disputing Sns gene-level differentiation biology.
Supporting Evidence:
PMID:10859168: "The Drosophila sticks-and-stones (sns) locus was identified on the basis of its mutant phenotype, the complete absence of body wall muscles and corresponding presence of unfused myoblasts."
file:DROME/sns/sns-bioinformatics/RESULTS.md: "The selected record predicts transmembrane segments 1089β1112 (within the insertion) and 1141β1166 (in the shared sequence)."
Review rationale: Gene-level Sns-dependent muscle and tissue morphogenesis is strongly supported. The exact selected isoform has a specific extra hydrophobic insertion that could alter the membrane topology required to couple extracellular adhesion to intracellular signaling. Its consequence is untested, so the morphology claim is not refuted but remains uncertain for this sequence. Mere agreement with the existing broad automated annotation would not resolve that issue.
Supporting Evidence:
PMID:10859168: "The Drosophila sticks-and-stones (sns) locus was identified on the basis of its mutant phenotype, the complete absence of body wall muscles and corresponding presence of unfused myoblasts."
PMID:20599904: "These results strongly suggest expression of Hbs and Sns is sufficient to render ommatidia less adhesive to other ommatidia than to IOCs."
file:DROME/sns/sns-bioinformatics/RESULTS.md: "The selected record predicts transmembrane segments 1089β1112 (within the insertion) and 1141β1166 (in the shared sequence)."
Review rationale: Membrane association is supported by the retained hydrophobic regions and direct Sns cell-surface localization. The extra hydrophobic insertion raises signaling-topology questions but does not undermine membrane association itself. The prediction is broader than the existing plasma-membrane and nephrocyte-diaphragm annotations.
Supporting Evidence:
PMID:10859168: "SNS is enriched at the membrane and clusters at discrete sites, coincident with the occurrence of myoblast fusion."
file:DROME/sns/sns-bioinformatics/RESULTS.md: "The selected record predicts transmembrane segments 1089β1112 (within the insertion) and 1141β1166 (in the shared sequence)."