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

Directly Involved In:
clathrin-dependent endocytosis clathrin coat assembly
Cellular Locations:
clathrin-coated pit

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

Directly Involved In:
neuron projection morphogenesis
Cellular Locations:
plasma membrane

References

GO_REF:0000118
TreeGrafter-generated GO annotations

External Prediction Reviews

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.

ProtNLM2 External predictions

View prediction review YAML · A0A674PKV4-protnlm-predictions-review.yaml · Review status: COMPLETE

The GAS7-family architecture supports cytoplasmic membrane association, consistent with an existing cytoplasmic annotation.

Source documents: genes/TAKRU/A0A674PKV4/A0A674PKV4-uniprot.txt · genes/TAKRU/A0A674PKV4/A0A674PKV4-goa.tsv · publications/PMID_31628328.md

Review score: 2 = concordant with evidence; 1 = uncertain; 0 = discordant with evidence. This is an assessment score, not a model probability.

GO:0005737 cytoplasm GO_CC
CNN — Correct but not novel Review score: 2/2
Prediction method: ProtNLM2 · Version: UniProt 2024_06 pilot
Review rationale: The target contains the GAS7-specific F-BAR domain, supporting a peripheral membrane-associated cytoplasmic protein. Experiments on GAS7 show assembly on membranes during phagocytic-cup formation (PMID:31628328), providing biological grounding for broad cytoplasmic localization. The exact cytoplasm term is already in the cached GOA record. Membrane or vesicle association supplies additional context, but does not by itself establish a more specific cytoplasmic compartment for this target.
Supporting Evidence:
  • file:TAKRU/A0A674PKV4/A0A674PKV4-uniprot.txt: "ID A0A674PKV4_TAKRU Unreviewed; 401 AA. ... DR InterPro; IPR037957; GAS7_F-BAR. ... DR PANTHER; PTHR23065:SF57; GROWTH ARREST-SPECIFIC PROTEIN 7; 1. ... FT DOMAIN 121..381 ... FT /note="F-BAR""
  • PMID:31628328: "sheet formation on flat membranes"

Deep Research

Falcon

(A0A674PKV4-deep-research-falcon.md)

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