gas7a

UniProt ID: A0A674PKV4
Organism: Takifugu rubripes
Review Status: DRAFT
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Gene Description

gas7a encodes Growth arrest-specific protein 7a in Takifugu rubripes, a member of the GAS7 family of F-BAR domain-containing proteins. The protein contains an N-terminal FCH (Fes/CIP4 homology) domain connected via a WW-FCH linker to a C-terminal F-BAR domain (residues 121-381). F-BAR domains form crescent-shaped dimers that sense and induce membrane curvature, typically associating with the cytoplasmic face of the plasma membrane. In mammals, GAS7 was originally identified as a gene upregulated during growth arrest and is required for neurite outgrowth in cultured cerebellar neurons. GAS7 family members have been shown to participate in membrane dynamics including clathrin-mediated endocytosis, where the F-BAR domain facilitates recruitment to sites of membrane invagination such as clathrin-coated pits. The Takifugu gas7a ortholog is predicted (PE level 4) with no direct experimental characterization, so functional inference relies on domain architecture and phylogenetic transfer from characterized mammalian orthologs via TreeGrafter/PANTHER.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0005737 cytoplasm
IEA
GO_REF:0000118
KEEP AS NON CORE
Summary: Cytoplasmic localization is consistent with GAS7 family biology. Mammalian GAS7 is a cytoplasmic protein that can associate peripherally with membranes via its F-BAR domain. The term is broad but correct as a general localization. Keeping as non-core since more specific localizations (plasma membrane, clathrin-coated pit) are also annotated.
GO:0005886 plasma membrane
IEA
GO_REF:0000118
ACCEPT
Summary: F-BAR domains are well-established plasma membrane-binding modules that sense and induce curvature at the cytoplasmic leaflet. Mammalian GAS7 has been shown to localize to the plasma membrane, consistent with the F-BAR domain architecture (CDD: cd07649 F-BAR_GAS7). This is a core localization for F-BAR proteins. Accept.
GO:0005905 clathrin-coated pit
IEA
GO_REF:0000118
ACCEPT
Summary: Clathrin-coated pit localization is consistent with the established role of F-BAR domain proteins in clathrin-mediated endocytosis. F-BAR proteins are recruited to nascent clathrin-coated pits where they contribute to membrane invagination. Mammalian GAS7 has been implicated in clathrin-dependent processes. This annotation is transferred via TreeGrafter from the PANTHER GAS7 subfamily (PTHR23065:SF57). Accept as reflecting a specific functional localization.
GO:0030136 clathrin-coated vesicle
IEA
GO_REF:0000118
KEEP AS NON CORE
Summary: Clathrin-coated vesicle localization extends from the role of GAS7/F-BAR proteins in clathrin-mediated endocytosis. As F-BAR domain proteins participate in the membrane invagination and scission steps that produce clathrin-coated vesicles, association with these structures is plausible. However, the primary site of action for F-BAR proteins is the clathrin-coated pit (membrane invagination stage) rather than the fully formed vesicle. Keeping as non-core since clathrin-coated pit is the more precise localization.
GO:0048268 clathrin coat assembly
IEA
GO_REF:0000118
ACCEPT
Summary: Involvement in clathrin coat assembly is consistent with the role of F-BAR domain proteins in clathrin-mediated endocytosis. F-BAR proteins cooperate with clathrin adaptors and other endocytic machinery during coat assembly by providing membrane curvature. Mammalian GAS7 has been linked to clathrin-dependent membrane dynamics. Accept as a core biological process annotation.
GO:0048812 neuron projection morphogenesis
IEA
GO_REF:0000118
ACCEPT
Summary: Mammalian GAS7 is required for neurite outgrowth in cultured cerebellar neurons and has been shown to promote neuron projection morphogenesis. This is one of the best-characterized functions of the GAS7 family. The annotation is transferred via TreeGrafter from characterized mammalian orthologs. While there is no direct evidence in Takifugu, the phylogenetic transfer is well-supported by the conservation of the F-BAR domain architecture. Accept.
GO:0072583 clathrin-dependent endocytosis
IEA
GO_REF:0000118
ACCEPT
Summary: Clathrin-dependent endocytosis is a well-established biological process for F-BAR domain proteins. The F-BAR domain provides membrane curvature sensing and generation during the invagination step of clathrin-mediated endocytosis. This is consistent with the other clathrin-related annotations (clathrin-coated pit, clathrin coat assembly) and the GAS7 family assignment via PANTHER. Accept as a core process.

Core Functions

F-BAR domain-mediated participation in clathrin-dependent endocytosis, including membrane curvature sensing and generation at clathrin-coated pits during clathrin coat assembly

Cytoskeletal regulation contributing to neuron projection morphogenesis, consistent with the established role of GAS7 family members in neurite outgrowth

Directly Involved In:
Cellular Locations:

References

TreeGrafter-generated GO annotations

Deep Research

Falcon

(A0A674PKV4-deep-research-falcon.md)
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate. Falcon Edison Scientific Literature 2 artifacts 2026-06-18T20:05:16.833421

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Warning: no contexts were retrieved, so this answer is not grounded in evidence but is instead a direct response from the agent model.

No specific literature exists for gas7a in Takifugu rubripes. Based on UniProt domain annotations (F-BAR IPR037957, IPR031160; FCH IPR001060; BAR superfamily IPR027267), gas7a is predicted to function as a membrane-cytoskeleton adapter protein. F-BAR domains bind membranes via electrostatic interactions with phospholipids and coordinate membrane curvature with cytoskeletal organization. Gas7a likely localizes to plasma membrane and membrane protrusions where it scaffolds membrane-cytoskeleton coordination. This is not an enzyme but a structural adapter. Predicted roles include cell morphogenesis and membrane protrusion formation. This annotation is inferred from domain conservation only; no experimental data exists for this pufferfish gene.

Artifacts

📄 View Raw YAML

id: A0A674PKV4
gene_symbol: gas7a
product_type: PROTEIN
status: DRAFT
taxon:
  id: NCBITaxon:31033
  label: Takifugu rubripes
description: >-
  gas7a encodes Growth arrest-specific protein 7a in Takifugu rubripes, a member
  of the GAS7 family of F-BAR domain-containing proteins. The protein contains an
  N-terminal FCH (Fes/CIP4 homology) domain connected via a WW-FCH linker to a
  C-terminal F-BAR domain (residues 121-381). F-BAR domains form crescent-shaped
  dimers that sense and induce membrane curvature, typically associating with the
  cytoplasmic face of the plasma membrane. In mammals, GAS7 was originally
  identified as a gene upregulated during growth arrest and is required for neurite
  outgrowth in cultured cerebellar neurons. GAS7 family members have been shown to
  participate in membrane dynamics including clathrin-mediated endocytosis, where
  the F-BAR domain facilitates recruitment to sites of membrane invagination such
  as clathrin-coated pits. The Takifugu gas7a ortholog is predicted (PE level 4)
  with no direct experimental characterization, so functional inference relies on
  domain architecture and phylogenetic transfer from characterized mammalian
  orthologs via TreeGrafter/PANTHER.
existing_annotations:
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IEA
  original_reference_id: GO_REF:0000118
  qualifier: located_in
  review:
    summary: >-
      Cytoplasmic localization is consistent with GAS7 family biology. Mammalian
      GAS7 is a cytoplasmic protein that can associate peripherally with
      membranes via its F-BAR domain. The term is broad but correct as a general
      localization. Keeping as non-core since more specific localizations (plasma
      membrane, clathrin-coated pit) are also annotated.
    action: KEEP_AS_NON_CORE
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000118
  qualifier: located_in
  review:
    summary: >-
      F-BAR domains are well-established plasma membrane-binding modules that
      sense and induce curvature at the cytoplasmic leaflet. Mammalian GAS7 has
      been shown to localize to the plasma membrane, consistent with the F-BAR
      domain architecture (CDD: cd07649 F-BAR_GAS7). This is a core localization
      for F-BAR proteins. Accept.
    action: ACCEPT
- term:
    id: GO:0005905
    label: clathrin-coated pit
  evidence_type: IEA
  original_reference_id: GO_REF:0000118
  qualifier: located_in
  review:
    summary: >-
      Clathrin-coated pit localization is consistent with the established role of
      F-BAR domain proteins in clathrin-mediated endocytosis. F-BAR proteins are
      recruited to nascent clathrin-coated pits where they contribute to membrane
      invagination. Mammalian GAS7 has been implicated in clathrin-dependent
      processes. This annotation is transferred via TreeGrafter from the PANTHER
      GAS7 subfamily (PTHR23065:SF57). Accept as reflecting a specific functional
      localization.
    action: ACCEPT
- term:
    id: GO:0030136
    label: clathrin-coated vesicle
  evidence_type: IEA
  original_reference_id: GO_REF:0000118
  qualifier: located_in
  review:
    summary: >-
      Clathrin-coated vesicle localization extends from the role of GAS7/F-BAR
      proteins in clathrin-mediated endocytosis. As F-BAR domain proteins
      participate in the membrane invagination and scission steps that produce
      clathrin-coated vesicles, association with these structures is plausible.
      However, the primary site of action for F-BAR proteins is the
      clathrin-coated pit (membrane invagination stage) rather than the fully
      formed vesicle. Keeping as non-core since clathrin-coated pit is the more
      precise localization.
    action: KEEP_AS_NON_CORE
- term:
    id: GO:0048268
    label: clathrin coat assembly
  evidence_type: IEA
  original_reference_id: GO_REF:0000118
  qualifier: involved_in
  review:
    summary: >-
      Involvement in clathrin coat assembly is consistent with the role of F-BAR
      domain proteins in clathrin-mediated endocytosis. F-BAR proteins cooperate
      with clathrin adaptors and other endocytic machinery during coat assembly
      by providing membrane curvature. Mammalian GAS7 has been linked to
      clathrin-dependent membrane dynamics. Accept as a core biological process
      annotation.
    action: ACCEPT
- term:
    id: GO:0048812
    label: neuron projection morphogenesis
  evidence_type: IEA
  original_reference_id: GO_REF:0000118
  qualifier: involved_in
  review:
    summary: >-
      Mammalian GAS7 is required for neurite outgrowth in cultured cerebellar
      neurons and has been shown to promote neuron projection morphogenesis.
      This is one of the best-characterized functions of the GAS7 family.
      The annotation is transferred via TreeGrafter from characterized mammalian
      orthologs. While there is no direct evidence in Takifugu, the phylogenetic
      transfer is well-supported by the conservation of the F-BAR domain
      architecture. Accept.
    action: ACCEPT
- term:
    id: GO:0072583
    label: clathrin-dependent endocytosis
  evidence_type: IEA
  original_reference_id: GO_REF:0000118
  qualifier: involved_in
  review:
    summary: >-
      Clathrin-dependent endocytosis is a well-established biological process for
      F-BAR domain proteins. The F-BAR domain provides membrane curvature sensing
      and generation during the invagination step of clathrin-mediated endocytosis.
      This is consistent with the other clathrin-related annotations (clathrin-coated
      pit, clathrin coat assembly) and the GAS7 family assignment via PANTHER.
      Accept as a core process.
    action: ACCEPT
core_functions:
- description: >-
    F-BAR domain-mediated participation in clathrin-dependent endocytosis,
    including membrane curvature sensing and generation at clathrin-coated pits
    during clathrin coat assembly
  directly_involved_in:
  - id: GO:0072583
    label: clathrin-dependent endocytosis
  - id: GO:0048268
    label: clathrin coat assembly
  locations:
  - id: GO:0005905
    label: clathrin-coated pit
- description: >-
    Cytoskeletal regulation contributing to neuron projection morphogenesis,
    consistent with the established role of GAS7 family members in neurite
    outgrowth
  directly_involved_in:
  - id: GO:0048812
    label: neuron projection morphogenesis
  locations:
  - id: GO:0005886
    label: plasma membrane
references:
- id: GO_REF:0000118
  title: TreeGrafter-generated GO annotations
  findings: []