gsnl-1 Gelsolin-like protein 1 [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: gsnl-1
Official Full Name: Gelsolin-like protein 1
Primary source: WormBase:WBGene00010593
Locus tag: CELE_K06A4.3
See related: AllianceGenome:WB:WBGene00010593
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Caenorhabditis elegans (strain: Bristol N2)
Lineage: Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
Summary: Enables actin filament binding activity; actin monomer binding activity; and phosphatidylinositol-4,5-bisphosphate binding activity. Involved in several processes, including actin filament depolymerization; barbed-end actin filament capping; and positive regulation of synapse pruning. Located in actin cytoskeleton and striated muscle dense body. Is expressed in body wall musculature; enteric muscle; hypodermis; and reproductive system. Human ortholog(s) of this gene implicated in Finnish type amyloidosis and nephrotic syndrome type 21. Orthologous to several human genes including CAPG (capping actin protein, gelsolin like). [provided by Alliance of Genome Resources, Jan 2025]
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Genomic context

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See gsnl-1 in Genome Data Viewer

Location:: chromosome: V

Exon count:: 10

Sequence:: Chromosome: V; NC_003283.11 (9497042..9499376)

Chromosome V - NC_003283.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003283.11

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

GSNL-1 acts downstream of the cell death pathway in synapse elimination. Cleavage of GSNL-1 by CED-3 induces synapse elimination.
Title: The Cell Death Pathway Regulates Synapse Elimination through Cleavage of Gelsolin in Caenorhabditis elegans Neurons.
Calcium-sensitive activity and conformation of Caenorhabditis elegans gelsolin-like protein 1 are altered by mutations in the first gelsolin-like domain.
Title: Calcium-sensitive activity and conformation of Caenorhabditis elegans gelsolin-like protein 1 are altered by mutations in the first gelsolin-like domain.
GSNL-1 is a novel member of the gelsolin family of actin regulatory proteins with four gelsolin-like repeats
Title: Caenorhabditis elegans gelsolin-like protein 1 is a novel actin filament-severing protein with four gelsolin-like repeats.
Both conserved and different utilization of G domains between C. elegans GSNL-1 and mammalian gelsolin for actin regulatory functions.
Title: Distinct roles of four gelsolin-like domains of Caenorhabditis elegans gelsolin-like protein-1 in actin filament severing, barbed end capping, and phosphoinositide binding.

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Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

K06A4.3 (e-PCR)
- UniSTS:321561

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables actin binding	IEA Inferred from Electronic Annotation more info
enables actin filament binding	IBA Inferred from Biological aspect of Ancestor more info
enables actin filament binding	IDA Inferred from Direct Assay more info	PubMed
enables actin filament binding	IEA Inferred from Electronic Annotation more info
enables actin monomer binding	IDA Inferred from Direct Assay more info	PubMed
enables phosphatidylinositol-4,5-bisphosphate binding	IBA Inferred from Biological aspect of Ancestor more info
enables phosphatidylinositol-4,5-bisphosphate binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in actin filament capping	IEA Inferred from Electronic Annotation more info
involved_in actin filament depolymerization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in actin filament severing	IBA Inferred from Biological aspect of Ancestor more info
involved_in actin filament severing	IDA Inferred from Direct Assay more info	PubMed
involved_in actin polymerization or depolymerization	IBA Inferred from Biological aspect of Ancestor more info
involved_in barbed-end actin filament capping	IBA Inferred from Biological aspect of Ancestor more info
involved_in barbed-end actin filament capping	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of synapse pruning	IGI Inferred from Genetic Interaction more info	PubMed
involved_in positive regulation of synapse pruning	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in actin cytoskeleton	HDA more info	PubMed
is_active_in actin cytoskeleton	IBA Inferred from Biological aspect of Ancestor more info
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytoskeleton	IEA Inferred from Electronic Annotation more info
located_in striated muscle dense body	HDA more info	PubMed

General protein information

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Preferred Names: Gelsolin-like protein 1

NP_505448.1

Confirmed by transcript evidence

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_003283.11 Reference assembly

Range

9497042..9499376

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_073047.8 → NP_505448.1 Gelsolin-like protein 1 [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_505448.1

Status: REVIEWED

UniProtKB/Swiss-Prot

Q21253

Conserved Domains (4) summary

cd11289
Location:134 → 225

gelsolin_S2_like; Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins

cd11290
Location:12 → 118

gelsolin_S1_like; Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins

cd11291
Location:359 → 455

gelsolin_S6_like; Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins

cd11292
Location:249 → 347

gelsolin_S3_like; Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins