Punt is a Drosophila type II receptor serine/threonine kinase shared by activin-family and BMP-family signaling. It forms ligand-responsive complexes with Baboon to activate Smox-dependent signaling and with the BMP type I receptors Thickveins or Saxophone to activate Mad-dependent signaling. Punt binds activin and supports complex-dependent BMP binding. Its membrane distribution is tissue dependent: predominantly basolateral in wing-disc and salivary epithelia, but both apical and basolateral in ovarian follicle cells. These receptor functions regulate embryonic patterning, organ development, neuronal connectivity and metabolic responses.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004672 protein kinase activity | IEA GO_REF:0000002 | MODIFY | Summary: Punt is a shared type II receptor kinase for activin and BMP signaling. Reason: The broad kinase function is correct, but two distinct experimentally supported receptor functions should be retained. Punt cooperates with Babo for activin-family signaling and with Tkv/Sax for BMP signaling; it is not specific to one branch. Proposed replacements: activin receptor activity, type II BMP receptor activity Supporting Evidence: PMID:18820452 Only Drosophila Activin (dACT) and the Activin-like ligand Dawdle (DAW) signal through BABO in combination with the type II receptor PUNT and activate dSMAD2. PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. |
| GO:0004675 transmembrane receptor protein serine/threonine kinase activity | IEA GO_REF:0000120 | MODIFY | Summary: Punt is a shared type II receptor kinase for activin and BMP signaling. Reason: The broad kinase function is correct, but two distinct experimentally supported receptor functions should be retained. Punt cooperates with Babo for activin-family signaling and with Tkv/Sax for BMP signaling; it is not specific to one branch. Proposed replacements: activin receptor activity, type II BMP receptor activity Supporting Evidence: PMID:18820452 Only Drosophila Activin (dACT) and the Activin-like ligand Dawdle (DAW) signal through BABO in combination with the type II receptor PUNT and activate dSMAD2. PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: Punt uses ATP in its receptor-kinase catalytic domain. Reason: The curated serine/threonine receptor kinase reaction supplies independent biochemical support for ATP use. Supporting Evidence: file:DROME/put/put-uniprot.txt Reaction=L-seryl-[receptor-protein] + ATP = O-phospho-L-seryl- [receptor-protein] + ADP + H(+); |
| GO:0005886 plasma membrane | ISM PMID:8415726 Identification of a Drosophila activin receptor. | MODIFY | Summary: Punt occupies tissue-dependent plasma-membrane domains. Reason: The broader membrane claim is correct. Native localization experiments resolve basolateral membrane in wing-disc and salivary epithelia, and both basolateral and apical membrane in ovarian follicle cells. Preserve both specific domains rather than making apical and basolateral localization mutually exclusive. Proposed replacements: basolateral plasma membrane apical plasma membrane Supporting Evidence: PMID:35594316 In follicle cells of the egg chamber, both Punt and Wit were indiscriminately distributed basolaterally and apically file:DROME/put/put-uniprot.txt Highly restricted to the basolateral cell membrane in wing disc epithelial cells; basolateral localization is dependent on the BLT motif and on the AP-1 adapter protein complex |
| GO:0007154 cell communication | IEA GO_REF:0000117 | MODIFY | Summary: Punt transduces both activin-family and BMP-family signals. Reason: General communication/signaling annotations are true but uninformative compared with the experimentally supported two pathways. The shared type II receptor must not be assigned only the activin branch because of its historical name. Proposed replacements: activin receptor signaling pathway BMP signaling pathway Supporting Evidence: PMID:18820452 Only Drosophila Activin (dACT) and the Activin-like ligand Dawdle (DAW) signal through BABO in combination with the type II receptor PUNT and activate dSMAD2. PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. |
| GO:0007178 cell surface receptor protein serine/threonine kinase signaling pathway | IEA GO_REF:0000002 | MODIFY | Summary: Punt transduces both activin-family and BMP-family signals. Reason: General communication/signaling annotations are true but uninformative compared with the experimentally supported two pathways. The shared type II receptor must not be assigned only the activin branch because of its historical name. Proposed replacements: activin receptor signaling pathway BMP signaling pathway Supporting Evidence: PMID:18820452 Only Drosophila Activin (dACT) and the Activin-like ligand Dawdle (DAW) signal through BABO in combination with the type II receptor PUNT and activate dSMAD2. PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. |
| GO:0007391 dorsal closure | IMP PMID:17119021 The metalloprotease tolloid-related and its TGF-beta-like su... | KEEP AS NON CORE | Summary: Punt-dependent signaling contributes to embryonic dorsal closure. Reason: Dorsal-closure defects are independently documented in punt mutants and curated from primary studies. This is a developmental consequence of receptor signaling, not a ligand-binding specificity claim. Unavailable details of an individual source do not negate the independently established phenotype. Supporting Evidence: file:DROME/put/put-uniprot.txt Failure of dorsal closure resulting in a large hole in the dorsal cuticle (PubMed:7697719, PubMed:7697720, PubMed:9504926). |
| GO:0007391 dorsal closure | IMP PMID:7697720 Drosophila Dpp signaling is mediated by the punt gene produc... | KEEP AS NON CORE | Summary: Punt-dependent signaling contributes to embryonic dorsal closure. Reason: Dorsal-closure defects are independently documented in punt mutants and curated from primary studies. This is a developmental consequence of receptor signaling, not a ligand-binding specificity claim. Unavailable details of an individual source do not negate the independently established phenotype. Supporting Evidence: file:DROME/put/put-uniprot.txt Failure of dorsal closure resulting in a large hole in the dorsal cuticle (PubMed:7697719, PubMed:7697720, PubMed:9504926). |
| GO:0007391 dorsal closure | IMP PMID:9224720 Drosophila Jun kinase regulates expression of decapentaplegi... | KEEP AS NON CORE | Summary: Punt-dependent signaling contributes to embryonic dorsal closure. Reason: Dorsal-closure defects are independently documented in punt mutants and curated from primary studies. This is a developmental consequence of receptor signaling, not a ligand-binding specificity claim. Unavailable details of an individual source do not negate the independently established phenotype. Supporting Evidence: file:DROME/put/put-uniprot.txt Failure of dorsal closure resulting in a large hole in the dorsal cuticle (PubMed:7697719, PubMed:7697720, PubMed:9504926). |
| GO:0007411 axon guidance | IMP PMID:17119021 The metalloprotease tolloid-related and its TGF-beta-like su... | KEEP AS NON CORE | Summary: Punt is required for motoneuron axon guidance. Reason: The independently curated primary result places Punt in motoneuron pathfinding downstream of activin-family signals. The Tolloid-related study title foregrounding a protease is not evidence that the receptor annotation is misattributed. Supporting Evidence: file:DROME/put/put-uniprot.txt Required in motoneurons for axon guidance or outgrowth of ISNb and SNa axons (PubMed:17119022). |
| GO:0007411 axon guidance | IMP PMID:17119022 The divergent TGF-beta ligand Dawdle utilizes an activin pat... | KEEP AS NON CORE | Summary: Punt is required for motoneuron axon guidance. Reason: The independently curated primary result places Punt in motoneuron pathfinding downstream of activin-family signals. The Tolloid-related study title foregrounding a protease is not evidence that the receptor annotation is misattributed. Supporting Evidence: file:DROME/put/put-uniprot.txt Required in motoneurons for axon guidance or outgrowth of ISNb and SNa axons (PubMed:17119022). |
| GO:0007424 open tracheal system development | IMP PMID:15848387 A molecular link between FGF and Dpp signaling in branch-spe... | KEEP AS NON CORE | Summary: Punt contributes to development of the embryonic tracheal system. Reason: The receptor mediates the Dpp/BMP branch required for tracheal development. This precise developmental context is peripheral to its dual ligand-receptor functions. Supporting Evidence: file:DROME/put/put-uniprot.txt Involved in dpp/BMP-like signaling during development of the embryonic gut tracheal system (PubMed:7697719, PubMed:7697720). |
| GO:0007428 primary branching, open tracheal system | IMP PMID:12015974 In vivo imaging reveals different cellular functions for FGF... | KEEP AS NON CORE | Summary: Dpp-receptor signaling supports primary tracheal branch morphogenesis. Reason: The cited study distinguishes Dpp-dependent branch outgrowth from FGF-dependent filopodia; independent punt mutant evidence includes failure of specific dorsal tracheal branches. Supporting Evidence: PMID:12015974 Dpp controls cellular functions allowing branch morphogenesis and outgrowth. file:DROME/put/put-uniprot.txt Tracheal dorsal branches fail to develop in parasegments 6 and 7 (PubMed:7697719). |
| GO:0007443 Malpighian tubule morphogenesis | IMP PMID:10502111 Mutations that alter the morphology of the malpighian tubule... | UNDECIDED | Summary: The specific Punt contribution to Malpighian tubule morphogenesis could not be independently resolved. Reason: The cached abstract reports a mutant survey but does not identify the relevant punt genotype or assay, and full text was unavailable. General BMP receptor function does not by itself establish this organ-specific claim. Retain uncertainty without alleging erroneous FlyBase attribution. |
| GO:0007476 imaginal disc-derived wing morphogenesis | IGI PMID:8616891 Direct and long-range action of a DPP morphogen gradient. | KEEP AS NON CORE | Summary: Punt-dependent BMP signaling contributes to wing morphogenesis. Reason: Clonal receptor manipulations establish Dpp-dependent wing organization, and independent curated punt phenotypes include adult wing and vein defects. This developmental output is retained as non-core. Supporting Evidence: file:DROME/put/put-uniprot.txt Involved in adult wing development and wing- vein formation (PubMed:7697720). |
| GO:0008258 head involution | IMP PMID:17119021 The metalloprotease tolloid-related and its TGF-beta-like su... | KEEP AS NON CORE | Summary: Punt mutants have head-involution defects. Reason: The phenotype is independently documented in the original receptor genetics and supports a developmental role. It does not determine whether every head phenotype is mediated by the activin or BMP branch. Supporting Evidence: file:DROME/put/put-uniprot.txt Defects in head involution (PubMed:7697720). |
| GO:0008258 head involution | IMP PMID:7697720 Drosophila Dpp signaling is mediated by the punt gene produc... | KEEP AS NON CORE | Summary: Punt mutants have head-involution defects. Reason: The phenotype is independently documented in the original receptor genetics and supports a developmental role. It does not determine whether every head phenotype is mediated by the activin or BMP branch. Supporting Evidence: file:DROME/put/put-uniprot.txt Defects in head involution (PubMed:7697720). |
| GO:0009791 post-embryonic development | IEA GO_REF:0000117 | MODIFY | Summary: The receptor has a specific post-embryonic role in wing morphogenesis. Reason: Replace the broad developmental-stage term with the documented imaginal-disc-derived wing morphogenesis output. Other tissue-specific functions remain separately reviewed. Proposed replacements: imaginal disc-derived wing morphogenesis Supporting Evidence: file:DROME/put/put-uniprot.txt Involved in adult wing development and wing- vein formation (PubMed:7697720). |
| GO:0009953 dorsal/ventral pattern formation | IGI PMID:7697719 An absolute requirement for both the type II and type I rece... | KEEP AS NON CORE | Summary: Punt-dependent BMP signaling patterns the embryonic dorsalβventral axis. Reason: Maternal/zygotic receptor genetics support the patterned developmental output. Retain the two original evidence rows consistently; this is not an activin-specific phenotype. Supporting Evidence: file:DROME/put/put-uniprot.txt Involved in dpp-signaling-dependent dorsoventral patterning of the epidermis during embryogenesis (PubMed:7697719, PubMed:7697720, PubMed:9504926). |
| GO:0009953 dorsal/ventral pattern formation | IMP PMID:7697720 Drosophila Dpp signaling is mediated by the punt gene produc... | KEEP AS NON CORE | Summary: Punt-dependent BMP signaling patterns the embryonic dorsalβventral axis. Reason: Maternal/zygotic receptor genetics support the patterned developmental output. Retain the two original evidence rows consistently; this is not an activin-specific phenotype. Supporting Evidence: file:DROME/put/put-uniprot.txt Involved in dpp-signaling-dependent dorsoventral patterning of the epidermis during embryogenesis (PubMed:7697719, PubMed:7697720, PubMed:9504926). |
| GO:0016020 membrane | IEA GO_REF:0000120 | MODIFY | Summary: Punt occupies tissue-dependent plasma-membrane domains. Reason: The broader membrane claim is correct. Native localization experiments resolve basolateral membrane in wing-disc and salivary epithelia, and both basolateral and apical membrane in ovarian follicle cells. Preserve both specific domains rather than making apical and basolateral localization mutually exclusive. Proposed replacements: basolateral plasma membrane apical plasma membrane Supporting Evidence: PMID:35594316 In follicle cells of the egg chamber, both Punt and Wit were indiscriminately distributed basolaterally and apically file:DROME/put/put-uniprot.txt Highly restricted to the basolateral cell membrane in wing disc epithelial cells; basolateral localization is dependent on the BLT motif and on the AP-1 adapter protein complex |
| GO:0016323 basolateral plasma membrane | IDA PMID:35594316 A juxtamembrane basolateral targeting motif regulates signal... | ACCEPT | Summary: Basolateral targeting is a native localization property of Punt in polarized epithelia. Reason: The primary localization study and its curated summary establish BLT-motif/AP-1-dependent basolateral localization. The electronic row reinforces the same claim. Supporting Evidence: file:DROME/put/put-uniprot.txt Highly restricted to the basolateral cell membrane in wing disc epithelial cells; basolateral localization is dependent on the BLT motif and on the AP-1 adapter protein complex |
| GO:0016323 basolateral plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Basolateral targeting is a native localization property of Punt in polarized epithelia. Reason: The primary localization study and its curated summary establish BLT-motif/AP-1-dependent basolateral localization. The electronic row reinforces the same claim. Supporting Evidence: file:DROME/put/put-uniprot.txt Highly restricted to the basolateral cell membrane in wing disc epithelial cells; basolateral localization is dependent on the BLT motif and on the AP-1 adapter protein complex |
| GO:0016324 apical plasma membrane | EXP PMID:35594316 A juxtamembrane basolateral targeting motif regulates signal... | ACCEPT | Summary: Punt also occupies apical membrane in ovarian follicle cells. Reason: The localization study explicitly shows native Punt at apical as well as basolateral membrane in follicle cells; this is not simply an ectopic targeting-mutant phenotype. It coexists with tissue-restricted basolateral localization elsewhere. Supporting Evidence: PMID:35594316 In follicle cells of the egg chamber, both Punt and Wit were indiscriminately distributed basolaterally and apically |
| GO:0016324 apical plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Punt also occupies apical membrane in ovarian follicle cells. Reason: The localization study explicitly shows native Punt at apical as well as basolateral membrane in follicle cells; this is not simply an ectopic targeting-mutant phenotype. It coexists with tissue-restricted basolateral localization elsewhere. Supporting Evidence: PMID:35594316 In follicle cells of the egg chamber, both Punt and Wit were indiscriminately distributed basolaterally and apically |
| GO:0016362 activin receptor activity, type II | IDA PMID:8415726 Identification of a Drosophila activin receptor. | ACCEPT | Summary: Punt is a type II activin-family receptor. Reason: Direct activin binding and native dACT/Daw receptor signaling establish this activity. Daw signaling requires Punt rather than Wit in the reported culture context; this does not make Punt activin-exclusive. Supporting Evidence: PMID:8415726 it binds activin with high affinity and specificity. PMID:18820452 Only Drosophila Activin (dACT) and the Activin-like ligand Dawdle (DAW) signal through BABO in combination with the type II receptor PUNT and activate dSMAD2. PMID:19766717 In cell culture, Dawdle signaling is active in the presence of the Type-II receptor Punt but not Wit, demonstrating that the Type-II receptor also contributes to the specificity of the signaling complex. |
| GO:0016362 activin receptor activity, type II | IMP PMID:18820452 Distinct signaling of Drosophila Activin/TGF-beta family mem... | ACCEPT | Summary: Punt is a type II activin-family receptor. Reason: Direct activin binding and native dACT/Daw receptor signaling establish this activity. Daw signaling requires Punt rather than Wit in the reported culture context; this does not make Punt activin-exclusive. Supporting Evidence: PMID:8415726 it binds activin with high affinity and specificity. PMID:18820452 Only Drosophila Activin (dACT) and the Activin-like ligand Dawdle (DAW) signal through BABO in combination with the type II receptor PUNT and activate dSMAD2. PMID:19766717 In cell culture, Dawdle signaling is active in the presence of the Type-II receptor Punt but not Wit, demonstrating that the Type-II receptor also contributes to the specificity of the signaling complex. |
| GO:0016362 activin receptor activity, type II | IMP PMID:19766717 The Drosophila Activin-like ligand Dawdle signals preferenti... | ACCEPT | Summary: Punt is a type II activin-family receptor. Reason: Direct activin binding and native dACT/Daw receptor signaling establish this activity. Daw signaling requires Punt rather than Wit in the reported culture context; this does not make Punt activin-exclusive. Supporting Evidence: PMID:8415726 it binds activin with high affinity and specificity. PMID:18820452 Only Drosophila Activin (dACT) and the Activin-like ligand Dawdle (DAW) signal through BABO in combination with the type II receptor PUNT and activate dSMAD2. PMID:19766717 In cell culture, Dawdle signaling is active in the presence of the Type-II receptor Punt but not Wit, demonstrating that the Type-II receptor also contributes to the specificity of the signaling complex. |
| GO:0017002 activin receptor activity | IDA PMID:10320478 Drosophila dSmad2 and Atr-I transmit activin/TGFbeta signals... | MODIFY | Summary: The activin receptor activity is specifically type II. Reason: The historical Atr-II receptor is Punt. Its ligand-binding and heteromeric-complex behavior identify the type II subtype, already represented by more specific annotations. Proposed replacements: activin receptor activity, type II Supporting Evidence: PMID:8415726 it binds activin with high affinity and specificity. PMID:8289834 Atr-I binds activin efficiently when coexpressed with the distantly related Drosophila activin receptor Atr-II, with which it forms a heteromeric complex. |
| GO:0017002 activin receptor activity | IDA PMID:8415726 Identification of a Drosophila activin receptor. | MODIFY | Summary: The activin receptor activity is specifically type II. Reason: The historical Atr-II receptor is Punt. Its ligand-binding and heteromeric-complex behavior identify the type II subtype, already represented by more specific annotations. Proposed replacements: activin receptor activity, type II Supporting Evidence: PMID:8415726 it binds activin with high affinity and specificity. PMID:8289834 Atr-I binds activin efficiently when coexpressed with the distantly related Drosophila activin receptor Atr-II, with which it forms a heteromeric complex. |
| GO:0023052 signaling | IEA GO_REF:0000117 | MODIFY | Summary: Punt transduces both activin-family and BMP-family signals. Reason: General communication/signaling annotations are true but uninformative compared with the experimentally supported two pathways. The shared type II receptor must not be assigned only the activin branch because of its historical name. Proposed replacements: activin receptor signaling pathway BMP signaling pathway Supporting Evidence: PMID:18820452 Only Drosophila Activin (dACT) and the Activin-like ligand Dawdle (DAW) signal through BABO in combination with the type II receptor PUNT and activate dSMAD2. PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. |
| GO:0030509 BMP signaling pathway | IDA PMID:19766717 The Drosophila Activin-like ligand Dawdle signals preferenti... | ACCEPT | Summary: Punt is a core BMP-pathway type II receptor. Reason: Genetic and biochemical evidence independently establishes Punt as a receptor for the Dpp/BMP branch with Tkv/Sax. Studies of ligand processing, extracellular transport, receptor combinations and tissue outputs corroborate this shared function; their titles need not foreground Punt. BMP signaling is retained alongside activin signaling rather than treated as an incorrect name-based transfer. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. file:DROME/put/put-uniprot.txt Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad (PubMed:18820452, PubMed:19766717). |
| GO:0030509 BMP signaling pathway | IDA PMID:28924042 Alternative cleavage of the bone morphogenetic protein (BMP)... | ACCEPT | Summary: Punt is a core BMP-pathway type II receptor. Reason: Genetic and biochemical evidence independently establishes Punt as a receptor for the Dpp/BMP branch with Tkv/Sax. Studies of ligand processing, extracellular transport, receptor combinations and tissue outputs corroborate this shared function; their titles need not foreground Punt. BMP signaling is retained alongside activin signaling rather than treated as an incorrect name-based transfer. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. file:DROME/put/put-uniprot.txt Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad (PubMed:18820452, PubMed:19766717). |
| GO:0030509 BMP signaling pathway | IDA PMID:9502733 The Drosophila gene Medea demonstrates the requirement for d... | ACCEPT | Summary: Punt is a core BMP-pathway type II receptor. Reason: Genetic and biochemical evidence independently establishes Punt as a receptor for the Dpp/BMP branch with Tkv/Sax. Studies of ligand processing, extracellular transport, receptor combinations and tissue outputs corroborate this shared function; their titles need not foreground Punt. BMP signaling is retained alongside activin signaling rather than treated as an incorrect name-based transfer. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. file:DROME/put/put-uniprot.txt Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad (PubMed:18820452, PubMed:19766717). |
| GO:0030509 BMP signaling pathway | IDA PMID:9693372 Interplay of signal mediators of decapentaplegic (Dpp): mole... | ACCEPT | Summary: Punt is a core BMP-pathway type II receptor. Reason: Genetic and biochemical evidence independently establishes Punt as a receptor for the Dpp/BMP branch with Tkv/Sax. Studies of ligand processing, extracellular transport, receptor combinations and tissue outputs corroborate this shared function; their titles need not foreground Punt. BMP signaling is retained alongside activin signaling rather than treated as an incorrect name-based transfer. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. file:DROME/put/put-uniprot.txt Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad (PubMed:18820452, PubMed:19766717). |
| GO:0030509 BMP signaling pathway | IGI PMID:7697719 An absolute requirement for both the type II and type I rece... | ACCEPT | Summary: Punt is a core BMP-pathway type II receptor. Reason: Genetic and biochemical evidence independently establishes Punt as a receptor for the Dpp/BMP branch with Tkv/Sax. Studies of ligand processing, extracellular transport, receptor combinations and tissue outputs corroborate this shared function; their titles need not foreground Punt. BMP signaling is retained alongside activin signaling rather than treated as an incorrect name-based transfer. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. file:DROME/put/put-uniprot.txt Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad (PubMed:18820452, PubMed:19766717). |
| GO:0030509 BMP signaling pathway | IGI PMID:7697720 Drosophila Dpp signaling is mediated by the punt gene produc... | ACCEPT | Summary: Punt is a core BMP-pathway type II receptor. Reason: Genetic and biochemical evidence independently establishes Punt as a receptor for the Dpp/BMP branch with Tkv/Sax. Studies of ligand processing, extracellular transport, receptor combinations and tissue outputs corroborate this shared function; their titles need not foreground Punt. BMP signaling is retained alongside activin signaling rather than treated as an incorrect name-based transfer. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. file:DROME/put/put-uniprot.txt Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad (PubMed:18820452, PubMed:19766717). |
| GO:0030509 BMP signaling pathway | IGI PMID:8616891 Direct and long-range action of a DPP morphogen gradient. | ACCEPT | Summary: Punt is a core BMP-pathway type II receptor. Reason: Genetic and biochemical evidence independently establishes Punt as a receptor for the Dpp/BMP branch with Tkv/Sax. Studies of ligand processing, extracellular transport, receptor combinations and tissue outputs corroborate this shared function; their titles need not foreground Punt. BMP signaling is retained alongside activin signaling rather than treated as an incorrect name-based transfer. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. file:DROME/put/put-uniprot.txt Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad (PubMed:18820452, PubMed:19766717). |
| GO:0030509 BMP signaling pathway | IMP PMID:12925593 Physical properties of Tld, Sog, Tsg and Dpp protein interac... | ACCEPT | Summary: Punt is a core BMP-pathway type II receptor. Reason: Genetic and biochemical evidence independently establishes Punt as a receptor for the Dpp/BMP branch with Tkv/Sax. Studies of ligand processing, extracellular transport, receptor combinations and tissue outputs corroborate this shared function; their titles need not foreground Punt. BMP signaling is retained alongside activin signaling rather than treated as an incorrect name-based transfer. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. file:DROME/put/put-uniprot.txt Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad (PubMed:18820452, PubMed:19766717). |
| GO:0030509 BMP signaling pathway | IMP PMID:15797386 Facilitated transport of a Dpp/Scw heterodimer by Sog/Tsg le... | ACCEPT | Summary: Punt is a core BMP-pathway type II receptor. Reason: Genetic and biochemical evidence independently establishes Punt as a receptor for the Dpp/BMP branch with Tkv/Sax. Studies of ligand processing, extracellular transport, receptor combinations and tissue outputs corroborate this shared function; their titles need not foreground Punt. BMP signaling is retained alongside activin signaling rather than treated as an incorrect name-based transfer. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. file:DROME/put/put-uniprot.txt Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad (PubMed:18820452, PubMed:19766717). |
| GO:0030509 BMP signaling pathway | IMP PMID:15936330 The crossveinless gene encodes a new member of the Twisted g... | ACCEPT | Summary: Punt is a core BMP-pathway type II receptor. Reason: Genetic and biochemical evidence independently establishes Punt as a receptor for the Dpp/BMP branch with Tkv/Sax. Studies of ligand processing, extracellular transport, receptor combinations and tissue outputs corroborate this shared function; their titles need not foreground Punt. BMP signaling is retained alongside activin signaling rather than treated as an incorrect name-based transfer. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. file:DROME/put/put-uniprot.txt Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad (PubMed:18820452, PubMed:19766717). |
| GO:0030509 BMP signaling pathway | IMP PMID:18820452 Distinct signaling of Drosophila Activin/TGF-beta family mem... | ACCEPT | Summary: Punt is a core BMP-pathway type II receptor. Reason: Genetic and biochemical evidence independently establishes Punt as a receptor for the Dpp/BMP branch with Tkv/Sax. Studies of ligand processing, extracellular transport, receptor combinations and tissue outputs corroborate this shared function; their titles need not foreground Punt. BMP signaling is retained alongside activin signaling rather than treated as an incorrect name-based transfer. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. file:DROME/put/put-uniprot.txt Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad (PubMed:18820452, PubMed:19766717). |
| GO:0030509 BMP signaling pathway | IMP PMID:22959350 Integration of a retrograde signal during synapse formation ... | ACCEPT | Summary: Punt is a core BMP-pathway type II receptor. Reason: Genetic and biochemical evidence independently establishes Punt as a receptor for the Dpp/BMP branch with Tkv/Sax. Studies of ligand processing, extracellular transport, receptor combinations and tissue outputs corroborate this shared function; their titles need not foreground Punt. BMP signaling is retained alongside activin signaling rather than treated as an incorrect name-based transfer. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. file:DROME/put/put-uniprot.txt Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad (PubMed:18820452, PubMed:19766717). |
| GO:0030509 BMP signaling pathway | IMP PMID:37054707 Heterodimerization-dependent secretion of bone morphogenetic... | ACCEPT | Summary: Punt is a core BMP-pathway type II receptor. Reason: Genetic and biochemical evidence independently establishes Punt as a receptor for the Dpp/BMP branch with Tkv/Sax. Studies of ligand processing, extracellular transport, receptor combinations and tissue outputs corroborate this shared function; their titles need not foreground Punt. BMP signaling is retained alongside activin signaling rather than treated as an incorrect name-based transfer. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. file:DROME/put/put-uniprot.txt Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad (PubMed:18820452, PubMed:19766717). |
| GO:0030509 BMP signaling pathway | IMP PMID:7697719 An absolute requirement for both the type II and type I rece... | ACCEPT | Summary: Punt is a core BMP-pathway type II receptor. Reason: Genetic and biochemical evidence independently establishes Punt as a receptor for the Dpp/BMP branch with Tkv/Sax. Studies of ligand processing, extracellular transport, receptor combinations and tissue outputs corroborate this shared function; their titles need not foreground Punt. BMP signaling is retained alongside activin signaling rather than treated as an incorrect name-based transfer. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. file:DROME/put/put-uniprot.txt Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad (PubMed:18820452, PubMed:19766717). |
| GO:0030509 BMP signaling pathway | IMP PMID:7697720 Drosophila Dpp signaling is mediated by the punt gene produc... | ACCEPT | Summary: Punt is a core BMP-pathway type II receptor. Reason: Genetic and biochemical evidence independently establishes Punt as a receptor for the Dpp/BMP branch with Tkv/Sax. Studies of ligand processing, extracellular transport, receptor combinations and tissue outputs corroborate this shared function; their titles need not foreground Punt. BMP signaling is retained alongside activin signaling rather than treated as an incorrect name-based transfer. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. file:DROME/put/put-uniprot.txt Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad (PubMed:18820452, PubMed:19766717). |
| GO:0030509 BMP signaling pathway | IMP PMID:9735359 Synergistic signaling by two BMP ligands through the SAX and... | ACCEPT | Summary: Punt is a core BMP-pathway type II receptor. Reason: Genetic and biochemical evidence independently establishes Punt as a receptor for the Dpp/BMP branch with Tkv/Sax. Studies of ligand processing, extracellular transport, receptor combinations and tissue outputs corroborate this shared function; their titles need not foreground Punt. BMP signaling is retained alongside activin signaling rather than treated as an incorrect name-based transfer. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. file:DROME/put/put-uniprot.txt Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad (PubMed:18820452, PubMed:19766717). |
| GO:0030718 germ-line stem cell population maintenance | IMP PMID:9695953 decapentaplegic is essential for the maintenance and divisio... | UNDECIDED | Summary: The exact Punt requirement in female germline stem-cell maintenance and division needs full-text verification. Reason: The abstract of PMID:9695953 identifies Dpp and Saxophone and describes receptor-mutant clones, but the Punt-specific assay cannot be verified from the available text. This does not establish a wrong-receptor attribution; retain uncertainty rather than rejecting a curated experimental claim. |
| GO:0032924 activin receptor signaling pathway | IDA PMID:10320478 Drosophila dSmad2 and Atr-I transmit activin/TGFbeta signals... | ACCEPT | Summary: Punt transduces activin-family signaling with Babo. Reason: Native dACT/Daw signaling activates Smox through Babo and Punt; independent biochemical receptor assembly establishes the core role. Early assays with vertebrate activin are used for receptor biochemistry, not as native Actbeta proof. Supporting Evidence: PMID:18820452 Only Drosophila Activin (dACT) and the Activin-like ligand Dawdle (DAW) signal through BABO in combination with the type II receptor PUNT and activate dSMAD2. PMID:19766717 In cell culture, Dawdle signaling is active in the presence of the Type-II receptor Punt but not Wit, demonstrating that the Type-II receptor also contributes to the specificity of the signaling complex. PMID:8289834 Atr-I binds activin efficiently when coexpressed with the distantly related Drosophila activin receptor Atr-II, with which it forms a heteromeric complex. |
| GO:0032924 activin receptor signaling pathway | IDA PMID:17119022 The divergent TGF-beta ligand Dawdle utilizes an activin pat... | ACCEPT | Summary: Punt transduces activin-family signaling with Babo. Reason: Native dACT/Daw signaling activates Smox through Babo and Punt; independent biochemical receptor assembly establishes the core role. Early assays with vertebrate activin are used for receptor biochemistry, not as native Actbeta proof. Supporting Evidence: PMID:18820452 Only Drosophila Activin (dACT) and the Activin-like ligand Dawdle (DAW) signal through BABO in combination with the type II receptor PUNT and activate dSMAD2. PMID:19766717 In cell culture, Dawdle signaling is active in the presence of the Type-II receptor Punt but not Wit, demonstrating that the Type-II receptor also contributes to the specificity of the signaling complex. PMID:8289834 Atr-I binds activin efficiently when coexpressed with the distantly related Drosophila activin receptor Atr-II, with which it forms a heteromeric complex. |
| GO:0032924 activin receptor signaling pathway | IDA PMID:18820452 Distinct signaling of Drosophila Activin/TGF-beta family mem... | ACCEPT | Summary: Punt transduces activin-family signaling with Babo. Reason: Native dACT/Daw signaling activates Smox through Babo and Punt; independent biochemical receptor assembly establishes the core role. Early assays with vertebrate activin are used for receptor biochemistry, not as native Actbeta proof. Supporting Evidence: PMID:18820452 Only Drosophila Activin (dACT) and the Activin-like ligand Dawdle (DAW) signal through BABO in combination with the type II receptor PUNT and activate dSMAD2. PMID:19766717 In cell culture, Dawdle signaling is active in the presence of the Type-II receptor Punt but not Wit, demonstrating that the Type-II receptor also contributes to the specificity of the signaling complex. PMID:8289834 Atr-I binds activin efficiently when coexpressed with the distantly related Drosophila activin receptor Atr-II, with which it forms a heteromeric complex. |
| GO:0032924 activin receptor signaling pathway | IDA PMID:9887103 The Drosophila activin receptor baboon signals through dSmad... | ACCEPT | Summary: Punt transduces activin-family signaling with Babo. Reason: Native dACT/Daw signaling activates Smox through Babo and Punt; independent biochemical receptor assembly establishes the core role. Early assays with vertebrate activin are used for receptor biochemistry, not as native Actbeta proof. Supporting Evidence: PMID:18820452 Only Drosophila Activin (dACT) and the Activin-like ligand Dawdle (DAW) signal through BABO in combination with the type II receptor PUNT and activate dSMAD2. PMID:19766717 In cell culture, Dawdle signaling is active in the presence of the Type-II receptor Punt but not Wit, demonstrating that the Type-II receptor also contributes to the specificity of the signaling complex. PMID:8289834 Atr-I binds activin efficiently when coexpressed with the distantly related Drosophila activin receptor Atr-II, with which it forms a heteromeric complex. |
| GO:0032924 activin receptor signaling pathway | IGI PMID:12581521 TGF-beta signaling activates steroid hormone receptor expres... | ACCEPT | Summary: Punt transduces activin-family signaling with Babo. Reason: Native dACT/Daw signaling activates Smox through Babo and Punt; independent biochemical receptor assembly establishes the core role. Early assays with vertebrate activin are used for receptor biochemistry, not as native Actbeta proof. Supporting Evidence: PMID:18820452 Only Drosophila Activin (dACT) and the Activin-like ligand Dawdle (DAW) signal through BABO in combination with the type II receptor PUNT and activate dSMAD2. PMID:19766717 In cell culture, Dawdle signaling is active in the presence of the Type-II receptor Punt but not Wit, demonstrating that the Type-II receptor also contributes to the specificity of the signaling complex. PMID:8289834 Atr-I binds activin efficiently when coexpressed with the distantly related Drosophila activin receptor Atr-II, with which it forms a heteromeric complex. |
| GO:0032924 activin receptor signaling pathway | IMP PMID:19766717 The Drosophila Activin-like ligand Dawdle signals preferenti... | ACCEPT | Summary: Punt transduces activin-family signaling with Babo. Reason: Native dACT/Daw signaling activates Smox through Babo and Punt; independent biochemical receptor assembly establishes the core role. Early assays with vertebrate activin are used for receptor biochemistry, not as native Actbeta proof. Supporting Evidence: PMID:18820452 Only Drosophila Activin (dACT) and the Activin-like ligand Dawdle (DAW) signal through BABO in combination with the type II receptor PUNT and activate dSMAD2. PMID:19766717 In cell culture, Dawdle signaling is active in the presence of the Type-II receptor Punt but not Wit, demonstrating that the Type-II receptor also contributes to the specificity of the signaling complex. PMID:8289834 Atr-I binds activin efficiently when coexpressed with the distantly related Drosophila activin receptor Atr-II, with which it forms a heteromeric complex. |
| GO:0032924 activin receptor signaling pathway | IMP PMID:25284780 Transforming growth factor Ξ²/activin signaling functions as ... | ACCEPT | Summary: Punt transduces activin-family signaling with Babo. Reason: Native dACT/Daw signaling activates Smox through Babo and Punt; independent biochemical receptor assembly establishes the core role. Early assays with vertebrate activin are used for receptor biochemistry, not as native Actbeta proof. Supporting Evidence: PMID:18820452 Only Drosophila Activin (dACT) and the Activin-like ligand Dawdle (DAW) signal through BABO in combination with the type II receptor PUNT and activate dSMAD2. PMID:19766717 In cell culture, Dawdle signaling is active in the presence of the Type-II receptor Punt but not Wit, demonstrating that the Type-II receptor also contributes to the specificity of the signaling complex. PMID:8289834 Atr-I binds activin efficiently when coexpressed with the distantly related Drosophila activin receptor Atr-II, with which it forms a heteromeric complex. |
| GO:0032924 activin receptor signaling pathway | IPI PMID:8289834 Two distinct transmembrane serine/threonine kinases from Dro... | ACCEPT | Summary: Punt transduces activin-family signaling with Babo. Reason: Native dACT/Daw signaling activates Smox through Babo and Punt; independent biochemical receptor assembly establishes the core role. Early assays with vertebrate activin are used for receptor biochemistry, not as native Actbeta proof. Supporting Evidence: PMID:18820452 Only Drosophila Activin (dACT) and the Activin-like ligand Dawdle (DAW) signal through BABO in combination with the type II receptor PUNT and activate dSMAD2. PMID:19766717 In cell culture, Dawdle signaling is active in the presence of the Type-II receptor Punt but not Wit, demonstrating that the Type-II receptor also contributes to the specificity of the signaling complex. PMID:8289834 Atr-I binds activin efficiently when coexpressed with the distantly related Drosophila activin receptor Atr-II, with which it forms a heteromeric complex. |
| GO:0035222 wing disc pattern formation | IMP PMID:9735359 Synergistic signaling by two BMP ligands through the SAX and... | KEEP AS NON CORE | Summary: Punt contributes to BMP-dependent wing-disc pattern formation. Reason: Receptor genetics and signaling through the Tkv/SaxβPunt complex support spatial wing patterning. This developmental role is distinct from the activin-dependent growth outputs of Babo. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. file:DROME/put/put-uniprot.txt Required for dpp/BMP-like signaling involved in imaginal disc development (PubMed:9504926). |
| GO:0036122 BMP binding | IDA PMID:7697720 Drosophila Dpp signaling is mediated by the punt gene produc... | ACCEPT | Summary: Punt binds BMP ligand as part of a type I/type II receptor complex. Reason: The primary specifies that Punt alone did not bind BMP2 under the assay conditions, whereas it bound BMP2 with Tkv or Sax. Retain complex-dependent ligand binding without claiming autonomous high-affinity BMP binding by isolated Punt. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. |
| GO:0042078 germ-line stem cell division | IMP PMID:9695953 decapentaplegic is essential for the maintenance and divisio... | UNDECIDED | Summary: The exact Punt requirement in female germline stem-cell maintenance and division needs full-text verification. Reason: The abstract of PMID:9695953 identifies Dpp and Saxophone and describes receptor-mutant clones, but the Punt-specific assay cannot be verified from the available text. This does not establish a wrong-receptor attribution; retain uncertainty rather than rejecting a curated experimental claim. |
| GO:0042593 glucose homeostasis | IMP PMID:28178568 Midgut-Derived Activin Regulates Glucagon-like Action in the... | KEEP AS NON CORE | Summary: Punt contributes to endocrine control of carbohydrate balance. Reason: Fat-body receptor knockdown suppresses AKH-associated hyperglycemia in the metabolic study. This is a tissue-specific signaling role, not direct sugar transport or catalysis. Supporting Evidence: PMID:28178568 RNAi stocks targeting Babo and Punt (Put), which encode a type I and II TGF-Ξ² receptors, respectively, were among the reagents exerting the greatest suppression of AKH-induced hyperglycemia in the primary RNAi screen |
| GO:0045464 R8 cell fate specification | IMP PMID:28853393 Parallel Activin and BMP signaling coordinates R7/R8 photore... | KEEP AS NON CORE | Summary: Punt participates in retinal signaling that establishes R8 subtype. Reason: The full retinal study places the shared receptor in parallel TGF-beta-family signaling. The downstream Babo/Smox branch supports an activin contribution; this contextual cell-fate annotation does not imply exclusive activin receptor usage. Supporting Evidence: PMID:28853393 We find that the Activin receptor Baboon is required in R8 to receive non-redundant signaling from the three Activin ligands, activating the transcription factor dSmad2. |
| GO:0045705 negative regulation of salivary gland boundary specification | TAS PMID:11598957 Organ formation in Drosophila: specification and morphogenes... | UNDECIDED | Summary: The salivary-gland-boundary claim could not be verified from the available review abstract. Reason: The source describes organ specification and morphogenesis broadly but does not expose the Punt-specific evidence or regulatory sign. General Dpp receptor function is insufficient to decide this precise boundary annotation; no miscitation is alleged. |
| GO:0045819 positive regulation of glycogen catabolic process | IMP PMID:28178568 Midgut-Derived Activin Regulates Glucagon-like Action in the... | KEEP AS NON CORE | Summary: Punt-dependent signaling promotes AKH-associated glycogen mobilization. Reason: The metabolic study identifies Punt in the fat-body activin-receptor axis controlling AKH responsiveness. Glycogen catabolism is a downstream regulated outcome, not a reaction catalyzed by Punt. Supporting Evidence: PMID:28178568 RNAi stocks targeting Babo and Punt (Put), which encode a type I and II TGF-Ξ² receptors, respectively, were among the reagents exerting the greatest suppression of AKH-induced hyperglycemia in the primary RNAi screen PMID:28178568 AKH signaling in the fly fat body regulates circulating carbohydrate levels via both glycogen breakdown and glucose/trehalose production. |
| GO:0048179 activin receptor complex | IPI PMID:10320478 Drosophila dSmad2 and Atr-I transmit activin/TGFbeta signals... | ACCEPT | Summary: Punt is a subunit of activin-family receptor complexes. Reason: Direct heteromeric association of Atr-II/Punt with Atr-I/Babo and native ligand signaling support complex membership. Wit-containing complexes in other experiments do not exclude Punt-containing complexes. Supporting Evidence: PMID:8289834 Atr-I binds activin efficiently when coexpressed with the distantly related Drosophila activin receptor Atr-II, with which it forms a heteromeric complex. PMID:18820452 Only Drosophila Activin (dACT) and the Activin-like ligand Dawdle (DAW) signal through BABO in combination with the type II receptor PUNT and activate dSMAD2. |
| GO:0048179 activin receptor complex | IPI PMID:16098524 The Drosophila type II receptor, Wishful thinking, binds BMP... | ACCEPT | Summary: Punt is a subunit of activin-family receptor complexes. Reason: Direct heteromeric association of Atr-II/Punt with Atr-I/Babo and native ligand signaling support complex membership. Wit-containing complexes in other experiments do not exclude Punt-containing complexes. Supporting Evidence: PMID:8289834 Atr-I binds activin efficiently when coexpressed with the distantly related Drosophila activin receptor Atr-II, with which it forms a heteromeric complex. PMID:18820452 Only Drosophila Activin (dACT) and the Activin-like ligand Dawdle (DAW) signal through BABO in combination with the type II receptor PUNT and activate dSMAD2. |
| GO:0048179 activin receptor complex | IPI PMID:8289834 Two distinct transmembrane serine/threonine kinases from Dro... | ACCEPT | Summary: Punt is a subunit of activin-family receptor complexes. Reason: Direct heteromeric association of Atr-II/Punt with Atr-I/Babo and native ligand signaling support complex membership. Wit-containing complexes in other experiments do not exclude Punt-containing complexes. Supporting Evidence: PMID:8289834 Atr-I binds activin efficiently when coexpressed with the distantly related Drosophila activin receptor Atr-II, with which it forms a heteromeric complex. PMID:18820452 Only Drosophila Activin (dACT) and the Activin-like ligand Dawdle (DAW) signal through BABO in combination with the type II receptor PUNT and activate dSMAD2. |
| GO:0048179 activin receptor complex | IPI PMID:9887103 The Drosophila activin receptor baboon signals through dSmad... | ACCEPT | Summary: Punt is a subunit of activin-family receptor complexes. Reason: Direct heteromeric association of Atr-II/Punt with Atr-I/Babo and native ligand signaling support complex membership. Wit-containing complexes in other experiments do not exclude Punt-containing complexes. Supporting Evidence: PMID:8289834 Atr-I binds activin efficiently when coexpressed with the distantly related Drosophila activin receptor Atr-II, with which it forms a heteromeric complex. PMID:18820452 Only Drosophila Activin (dACT) and the Activin-like ligand Dawdle (DAW) signal through BABO in combination with the type II receptor PUNT and activate dSMAD2. |
| GO:0048185 activin binding | IDA PMID:16098524 The Drosophila type II receptor, Wishful thinking, binds BMP... | ACCEPT | Summary: Punt binds activin ligand. Reason: The original Atr-II study directly shows high-affinity activin binding. The binding annotation is retained across evidence rows; the use of vertebrate activin in historical biochemistry is distinguished from the separate evidence for native fly ligands. Supporting Evidence: PMID:8415726 it binds activin with high affinity and specificity. PMID:8289834 Atr-I binds activin efficiently when coexpressed with the distantly related Drosophila activin receptor Atr-II, with which it forms a heteromeric complex. |
| GO:0048185 activin binding | IDA PMID:8289834 Two distinct transmembrane serine/threonine kinases from Dro... | ACCEPT | Summary: Punt binds activin ligand. Reason: The original Atr-II study directly shows high-affinity activin binding. The binding annotation is retained across evidence rows; the use of vertebrate activin in historical biochemistry is distinguished from the separate evidence for native fly ligands. Supporting Evidence: PMID:8415726 it binds activin with high affinity and specificity. PMID:8289834 Atr-I binds activin efficiently when coexpressed with the distantly related Drosophila activin receptor Atr-II, with which it forms a heteromeric complex. |
| GO:0048185 activin binding | IDA PMID:8415726 Identification of a Drosophila activin receptor. | ACCEPT | Summary: Punt binds activin ligand. Reason: The original Atr-II study directly shows high-affinity activin binding. The binding annotation is retained across evidence rows; the use of vertebrate activin in historical biochemistry is distinguished from the separate evidence for native fly ligands. Supporting Evidence: PMID:8415726 it binds activin with high affinity and specificity. PMID:8289834 Atr-I binds activin efficiently when coexpressed with the distantly related Drosophila activin receptor Atr-II, with which it forms a heteromeric complex. |
| GO:0048185 activin binding | IGI PMID:7697719 An absolute requirement for both the type II and type I rece... | ACCEPT | Summary: Punt binds activin ligand. Reason: The original Atr-II study directly shows high-affinity activin binding. The binding annotation is retained across evidence rows; the use of vertebrate activin in historical biochemistry is distinguished from the separate evidence for native fly ligands. Supporting Evidence: PMID:8415726 it binds activin with high affinity and specificity. PMID:8289834 Atr-I binds activin efficiently when coexpressed with the distantly related Drosophila activin receptor Atr-II, with which it forms a heteromeric complex. |
| GO:0048666 neuron development | IMP PMID:16437159 Baboon/dSmad2 TGF-beta signaling is required during late lar... | KEEP AS NON CORE | Summary: Punt contributes to development of adult-specific neurons. Reason: The independently curated experimental role supports neuronal differentiation before metamorphosis. It is a developmental output rather than the defining receptor activity. Supporting Evidence: file:DROME/put/put-uniprot.txt Involved in differentiation of dorsal cluster and ellipsoid body adult-specific neurons prior to metamorphosis (PubMed:16437159). |
| GO:0060391 positive regulation of SMAD protein signal transduction | IDA PMID:9502733 The Drosophila gene Medea demonstrates the requirement for d... | ACCEPT | Summary: Punt-containing receptor complexes positively activate SMAD signaling. Reason: Punt acts with type I receptors to initiate phosphorylation and activation of Smox or Mad, depending on the receptor/ligand branch. The term describes a direct upstream signaling contribution, not a claim that Punt is the physiological kinase for every R-Smad. Supporting Evidence: PMID:10320478 dSMAD2 is phosphorylated by ATR-I and PUNT, but not by activated THICK VEINS, and translocates to the nucleus upon activation. file:DROME/put/put-uniprot.txt Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad (PubMed:18820452, PubMed:19766717). |
| GO:0070724 BMP receptor complex | IPI PMID:7697720 Drosophila Dpp signaling is mediated by the punt gene produc... | ACCEPT | Summary: Punt assembles with BMP type I receptors. Reason: BMP2 binding and biochemical complex formation with Tkv or Sax establish BMP receptor-complex membership independently of the activin pathway. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. |
| GO:0071333 cellular response to glucose stimulus | IMP PMID:25284780 Transforming growth factor Ξ²/activin signaling functions as ... | KEEP AS NON CORE | Summary: Punt signaling participates in the cellular response to dietary sugars. Reason: The sugar-sensing pathway study links endocrine Daw to midgut activin signaling, and independent receptor genetics support a role in carbohydrate responses. This is signal reception rather than direct glucose sensing or binding by Punt. Supporting Evidence: PMID:25284780 Dawdle then acts via circulation to activate TGF-Ξ²/Activin signaling in the midgut, culminating in the repression of digestive enzymes that are highly expressed during starvation. PMID:28178568 RNAi stocks targeting Babo and Punt (Put), which encode a type I and II TGF-Ξ² receptors, respectively, were among the reagents exerting the greatest suppression of AKH-induced hyperglycemia in the primary RNAi screen |
| GO:0098821 BMP receptor activity | IDA PMID:15797386 Facilitated transport of a Dpp/Scw heterodimer by Sog/Tsg le... | ACCEPT | Summary: Punt is a BMP receptor as well as an activin receptor. Reason: Complex-dependent BMP binding with Tkv/Sax and BMP-responsive Mad activation establish this core activity. Native receptor specificity is assessed from the functional evidence rather than the historical activin-receptor name. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. |
| GO:0098821 BMP receptor activity | IDA PMID:19766717 The Drosophila Activin-like ligand Dawdle signals preferenti... | ACCEPT | Summary: Punt is a BMP receptor as well as an activin receptor. Reason: Complex-dependent BMP binding with Tkv/Sax and BMP-responsive Mad activation establish this core activity. Native receptor specificity is assessed from the functional evidence rather than the historical activin-receptor name. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. |
| GO:0098821 BMP receptor activity | IDA PMID:28924042 Alternative cleavage of the bone morphogenetic protein (BMP)... | ACCEPT | Summary: Punt is a BMP receptor as well as an activin receptor. Reason: Complex-dependent BMP binding with Tkv/Sax and BMP-responsive Mad activation establish this core activity. Native receptor specificity is assessed from the functional evidence rather than the historical activin-receptor name. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. |
| GO:0098821 BMP receptor activity | IDA PMID:9693372 Interplay of signal mediators of decapentaplegic (Dpp): mole... | ACCEPT | Summary: Punt is a BMP receptor as well as an activin receptor. Reason: Complex-dependent BMP binding with Tkv/Sax and BMP-responsive Mad activation establish this core activity. Native receptor specificity is assessed from the functional evidence rather than the historical activin-receptor name. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. |
| GO:0098821 BMP receptor activity | IMP PMID:12925593 Physical properties of Tld, Sog, Tsg and Dpp protein interac... | ACCEPT | Summary: Punt is a BMP receptor as well as an activin receptor. Reason: Complex-dependent BMP binding with Tkv/Sax and BMP-responsive Mad activation establish this core activity. Native receptor specificity is assessed from the functional evidence rather than the historical activin-receptor name. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. |
| GO:0098821 BMP receptor activity | IMP PMID:15936330 The crossveinless gene encodes a new member of the Twisted g... | ACCEPT | Summary: Punt is a BMP receptor as well as an activin receptor. Reason: Complex-dependent BMP binding with Tkv/Sax and BMP-responsive Mad activation establish this core activity. Native receptor specificity is assessed from the functional evidence rather than the historical activin-receptor name. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. |
| GO:0098821 BMP receptor activity | IMP PMID:18820452 Distinct signaling of Drosophila Activin/TGF-beta family mem... | ACCEPT | Summary: Punt is a BMP receptor as well as an activin receptor. Reason: Complex-dependent BMP binding with Tkv/Sax and BMP-responsive Mad activation establish this core activity. Native receptor specificity is assessed from the functional evidence rather than the historical activin-receptor name. Supporting Evidence: PMID:7697720 punt will bind BMP2 in concert with tkv or sax, forming complexes with these receptors. |
| GO:1904398 positive regulation of neuromuscular junction development | IMP PMID:22959350 Integration of a retrograde signal during synapse formation ... | KEEP AS NON CORE | Summary: Punt contributes to signaling that promotes neuromuscular junction development. Reason: The glial-Maverick study implicates muscle Punt in modulating the Gbb retrograde pathway and synaptic growth. This does not establish that Punt directly mediates every presynaptic BMP signal or that Maverick is equivalent to Actbeta. Supporting Evidence: PMID:22959350 Here we show that NMJ glia release the TGF-Ξ² ligand Maverick (Mav), which likely activates the muscle activin-type receptor Punt to potently modulate Gbb-dependent retrograde signaling and synaptic growth. |
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Download this section (compressed HTML)punt (put) encodes a transforming growth factor beta type II receptor that functions in both Dpp/BMP and Activin signaling. Pathway specificity in signaling output is determined by which type I receptor (Dpp/BMP or Activin one) is engaged in the complex with the product of put.
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