lmn-1 Lamin-1 [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: lmn-1
Official Full Name: Lamin-1
Primary source: WormBase:WBGene00003052
Locus tag: CELE_DY3.2
See related: AllianceGenome:WB:WBGene00003052
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 histone binding activity; identical protein binding activity; and structural molecule activity. Involved in several processes, including determination of adult lifespan; nuclear migration along microtubule; and nuclear pore localization. Located in nuclear envelope and nuclear periphery. Is expressed widely. Used to study Emery-Dreifuss muscular dystrophy; congenital muscular dystrophy; and progeria. Human ortholog(s) of this gene implicated in several diseases, including brain disease (multiple); intrinsic cardiomyopathy (multiple); lipodystrophy (multiple); neuromuscular disease (multiple); and type 2 diabetes mellitus (multiple). Orthologous to several human genes including LMNA (lamin A/C). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See lmn-1 in Genome Data Viewer

Location:: chromosome: I

Exon count:: 6

Sequence:: Chromosome: I; NC_003279.8 (8763041..8765631)

Chromosome I - NC_003279.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003279.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Caenorhabditis elegans models for striated muscle disorders caused by missense variants of human LMNA.
Title: Caenorhabditis elegans models for striated muscle disorders caused by missense variants of human LMNA.
Filament assembly of the C. elegans lamin in the absence of helix 1A.
Title: Filament assembly of the C. elegans lamin in the absence of helix 1A.
Lamin regulates the dietary restriction response via the mTOR pathway in Caenorhabditis elegans.
Title: Lamin regulates the dietary restriction response via the mTOR pathway in Caenorhabditis elegans.
PLK-1 promotes the merger of the parental genome into a single nucleus by triggering lamina disassembly.
Title: PLK-1 promotes the merger of the parental genome into a single nucleus by triggering lamina disassembly.
The coupling of the LMN-Y59C mutation with the ablation of CEC-4, a chromodomain protein that anchors H3K9-methylated chromatin at the nuclear envelope (NE), suppressed the muscle-associated disease phenotypes
Title: Loss of an H3K9me anchor rescues laminopathy-linked changes in nuclear organization and muscle function in an Emery-Dreifuss muscular dystrophy model.
The Caenorhabditis elegans lamin, LMN-1, is required for nuclear migration and interacts with the nucleoplasmic domain of the SUN protein UNC-84.
Title: The Caenorhabditis elegans SUN protein UNC-84 interacts with lamin to transfer forces from the cytoplasm to the nucleoskeleton during nuclear migration.
In LMN-1 Y59C (a point mutation)-expressing worms, there is abnormal retention at the nuclear envelope of a gene array bearing a muscle-specific promoter. This correlates with altered expression of a number of muscle-specific genes.
Title: An EDMD mutation in C. elegans lamin blocks muscle-specific gene relocation and compromises muscle integrity.
A laminopathic mutation disrupting lamin filament assembly causes disease-like phenotypes in Caenorhabditis elegans.
Title: A laminopathic mutation disrupting lamin filament assembly causes disease-like phenotypes in Caenorhabditis elegans.
documented that the single nuclear lamin of C. elegans assembles in low ionic strength Tris-HCl buffer into stable 10-nm filaments that exhibit a normal intermediate filament morphology
Title: The single nuclear lamin of Caenorhabditis elegans forms in vitro stable intermediate filaments and paracrystals with a reduced axial periodicity.
Both lamin Dm0 and C. elegans Ce-lamin bind directly to histone H2A in vitro and this binding requires a nuclear localization signal
Title: Specific and conserved sequences in D. melanogaster and C. elegans lamins and histone H2A mediate the attachment of lamins to chromosomes.

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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

DY3.2 (e-PCR)
- UniSTS:309504

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables histone binding	IDA Inferred from Direct Assay more info	PubMed
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables structural constituent of cytoskeleton	IBA Inferred from Biological aspect of Ancestor more info
enables structural molecule activity	IMP Inferred from Mutant Phenotype more info	PubMed

Process	Evidence Code	Pubs
involved_in cytoskeleton organization	IEA Inferred from Electronic Annotation more info
involved_in determination of adult lifespan	IGI Inferred from Genetic Interaction more info	PubMed
involved_in determination of adult lifespan	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in embryo development ending in birth or egg hatching	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in germ cell development	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in heterochromatin formation	IBA Inferred from Biological aspect of Ancestor more info
involved_in nuclear envelope organization	IBA Inferred from Biological aspect of Ancestor more info
involved_in nuclear migration	IBA Inferred from Biological aspect of Ancestor more info
involved_in nuclear migration along microtubule	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in nuclear pore localization	IBA Inferred from Biological aspect of Ancestor more info
involved_in nuclear pore localization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in nucleus organization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of cell population proliferation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein localization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein localization to nuclear envelope	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of chromosome segregation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of mitotic cell cycle	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in intermediate filament	IEA Inferred from Electronic Annotation more info
located_in lamin filament	ISS Inferred from Sequence or Structural Similarity more info	PubMed
located_in membrane	IEA Inferred from Electronic Annotation more info
is_active_in nuclear envelope	IBA Inferred from Biological aspect of Ancestor more info
located_in nuclear envelope	IDA Inferred from Direct Assay more info	PubMed
located_in nuclear envelope	IEA Inferred from Electronic Annotation more info
located_in nuclear inner membrane	IEA Inferred from Electronic Annotation more info
is_active_in nuclear lamina	IBA Inferred from Biological aspect of Ancestor more info
located_in nuclear periphery	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: Lamin-1

NP_492371.1

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_003279.8 Reference assembly

Range

8763041..8765631

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_059970.7 → NP_492371.1 Lamin-1 [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_492371.1

Status: REVIEWED

UniProtKB/Swiss-Prot

O62127, Q21443

Conserved Domains (3) summary

pfam00038
Location:44 → 386

Filament; Intermediate filament protein

pfam00932
Location:443 → 547

LTD; Lamin Tail Domain

cl19511
Location:57 → 147

DUF2317; Uncharacterized protein conserved in bacteria (DUF2317)