Tmod1 tropomodulin 1 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Tmod1provided by MGI
Official Full Name: tropomodulin 1provided by MGI
Primary source: MGI:MGI:98775
See related: Ensembl:ENSMUSG00000028328 AllianceGenome:MGI:98775
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: Tmod; E-Tmod
Summary: Enables tropomyosin binding activity. Involved in lens fiber cell development. Acts upstream of or within adult locomotory behavior; muscle contraction; and myofibril assembly. Located in cortical cytoskeleton; membrane; and sarcomere. Is expressed in several structures, including central nervous system; heart; hemolymphoid system; musculature; and sensory organ. Used to study dilated cardiomyopathy. Orthologous to human TMOD1 (tropomodulin 1). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Broad expression in heart adult (RPKM 56.3), liver E14 (RPKM 21.5) and 15 other tissues See more
Orthologs: human all
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Genomic context

Location:: 4 B1; 4 24.49 cM

Exon count:: 12

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	4	NC_000070.7 (46038940..46116032)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	4	NC_000070.6 (46038940..46116032)

Chromosome 4 - NC_000070.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Tropomodulin1 exacerbates inflammatory response in macrophages by negatively regulating LPS-induced TLR4 endocytosis.
Title: Tropomodulin1 exacerbates inflammatory response in macrophages by negatively regulating LPS-induced TLR4 endocytosis.
Tropomodulin1 Expression Increases Upon Maturation in Dendritic Cells and Promotes Their Maturation and Immune Functions.
Title: Tropomodulin1 Expression Increases Upon Maturation in Dendritic Cells and Promotes Their Maturation and Immune Functions.
Tmod1 function in mouse and human erythroblasts, was investigated.
Title: Tropomodulin 1 controls erythroblast enucleation via regulation of F-actin in the enucleosome.
distinct F-actin organizations are present in small protrusions versus large paddles. Formation and/or maintenance of large paddle domains depends on a beta2-spectrin-actin network stabilized by Tmod1. alpha-Actinin-crosslinked F-actin bundles are enhanced in absence of Tmod1, indicating altered cytoskeleton organization.
Title: Tropomodulin 1 Regulation of Actin Is Required for the Formation of Large Paddle Protrusions Between Mature Lens Fiber Cells.
TMOD1 expression was upregulated significantly (p<0.05) in OSCC.
Title: Overexpression of TMOD1 is associated with enhanced regional lymph node metastasis in human oral cancer.
RNAi depletion of Tmod1 from either wild-type or Tmod4(-/-) muscle fibers leads to thin filament elongation by approximately 15%.
Title: Tropomodulin 1 directly controls thin filament length in both wild-type and tropomodulin 4-deficient skeletal muscle.
The C-terminal extension of Lmod2 and C terminal of Tmod1 are sufficient to produce a filament nucleator.
Title: How Leiomodin and Tropomodulin use a common fold for different actin assembly functions.
Calpain-mediated proteolysis of tropomodulin isoforms TMOD1 and TMOD4 leads to thin filament elongation in dystrophic skeletal muscle.
Title: Calpain-mediated proteolysis of tropomodulin isoforms leads to thin filament elongation in dystrophic skeletal muscle.
Role of Tmod1 protein's leucine rich repeat domain in the formation of neurite-like processes
Title: Role of tropomodulin's leucine rich repeat domain in the formation of neurite-like processes.
Tmods are novel regulators of actomyosin crossbridge formation and muscle contractility, and future investigations and models of skeletal muscle force production must incorporate Tmods.
Title: Pointed-end capping by tropomodulin modulates actomyosin crossbridge formation in skeletal muscle fibers.

Submit: New GeneRIF Correction See all GeneRIFs (24)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Targeted (4) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

D4Mit270 (e-PCR), detects polymorphism
- UniSTS:130060

G47819 (e-PCR)
- UniSTS:108588

Tmod1 (e-PCR), detects polymorphism
- UniSTS:464697

NoName (e-PCR)
- UniSTS:485008

BM383810 (e-PCR)
- UniSTS:261059

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables actin binding	ISO Inferred from Sequence Orthology more info
enables actin binding	ISS Inferred from Sequence or Structural Similarity more info
enables tropomyosin binding	IBA Inferred from Biological aspect of Ancestor more info
enables tropomyosin binding	IDA Inferred from Direct Assay more info	PubMed
enables tropomyosin binding	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in actin filament organization	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within adult locomotory behavior	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in lens fiber cell development	IGI Inferred from Genetic Interaction more info	PubMed
involved_in muscle contraction	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within muscle contraction	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in myofibril assembly	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within myofibril assembly	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in pointed-end actin filament capping	IEA Inferred from Electronic Annotation more info
NOT acts_upstream_of_or_within skeletal muscle myosin thick filament assembly	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of COP9 signalosome	IEA Inferred from Electronic Annotation more info
part_of COP9 signalosome	ISO Inferred from Sequence Orthology more info
located_in actin filament	ISO Inferred from Sequence Orthology more info
located_in actin filament	ISS Inferred from Sequence or Structural Similarity more info
located_in cortical cytoskeleton	IDA Inferred from Direct Assay more info	PubMed
is_active_in cytoskeleton	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoskeleton	TAS Traceable Author Statement more info	PubMed
located_in membrane	IDA Inferred from Direct Assay more info	PubMed
is_active_in myofibril	IBA Inferred from Biological aspect of Ancestor more info
located_in myofibril	IDA Inferred from Direct Assay more info	PubMed
located_in myofibril	ISO Inferred from Sequence Orthology more info
located_in myofibril	ISS Inferred from Sequence or Structural Similarity more info
located_in sarcomere	IDA Inferred from Direct Assay more info	PubMed
located_in sarcomere	ISO Inferred from Sequence Orthology more info
located_in sarcomere	ISS Inferred from Sequence or Structural Similarity more info
is_active_in striated muscle thin filament	IBA Inferred from Biological aspect of Ancestor more info
located_in striated muscle thin filament	IEA Inferred from Electronic Annotation more info
located_in striated muscle thin filament	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: tropomodulin-1

Names: erythrocyte tropomodulin

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001424904.1 → NP_001411833.1 tropomodulin-1 isoform 2

Status: VALIDATED

Source sequence(s)

AL732615
NM_001424905.1 → NP_001411834.1 tropomodulin-1 isoform 3

Status: VALIDATED

Source sequence(s)

AL732615
NM_001424906.1 → NP_001411835.1 tropomodulin-1 isoform 3

Status: VALIDATED

Source sequence(s)

AL732615
NM_001424907.1 → NP_001411836.1 tropomodulin-1 isoform 3

Status: VALIDATED

Source sequence(s)

AL732615
NM_021883.3 → NP_068683.1 tropomodulin-1 isoform 1

See identical proteins and their annotated locations for NP_068683.1

Status: VALIDATED

Source sequence(s)

AL732615

Consensus CDS

CCDS18143.1

UniProtKB/Swiss-Prot

P49813, Q3KP84, Q9ERR9

Related

ENSMUSP00000103402.3, ENSMUST00000107773.3

Conserved Domains (2) summary

cd00116
Location:195 → 289

LRR_RI; Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond ...

pfam03250
Location:3 → 143

Tropomodulin; Tropomodulin

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

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

Reference GRCm39 C57BL/6J

Genomic

NC_000070.7 Reference GRCm39 C57BL/6J

Range

46038940..46116032

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_006537772.5 → XP_006537835.1 tropomodulin-1 isoform X1

Conserved Domains (2) summary

pfam03250
Location:3 → 143

Tropomodulin

cl39015
Location:195 → 289

LRR_RI; Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond ...