Tropomodulin 3

TMOD3
Identifiers
Aliases	TMOD3 , UTMOD, tropomodulin 3
External IDs	OMIM: 605112; MGI: 1355315; HomoloGene: 8727; GeneCards: TMOD3; OMA:TMOD3 - orthologs
Gene location (Human) Chr. Chromosome 15 (human) [1] Band 15q21.2 Start 51,829,628 bp [1] End 51,947,295 bp [1]
Gene location (Mouse) Chr. Chromosome 9 (mouse) [2] Band 9 D|9 42.3 cM Start 75,404,989 bp [2] End 75,466,939 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in amniotic fluid oral cavity buccal mucosa cell gums lower lobe of lung gingival epithelium epithelium of colon skin of hip Achilles tendon mucosa of sigmoid colon Top expressed in lactiferous gland Ileal epithelium corneal stroma left lung lobe sciatic nerve cardiac muscle tissue of left ventricle seminal vesicula right lung lobe blood genital tubercle More reference expression data BioGPS n/a
Gene ontology Molecular function actin binding cadherin binding involved in cell-cell adhesion tropomyosin binding Cellular component cytoplasm cytoskeleton striated muscle thin filament myofibril Biological process pointed-end actin filament capping positive regulation of mitotic cell cycle phase transition actin cytoskeleton organization erythrocyte development cell-cell adhesion muscle contraction actin filament organization myofibril assembly Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 29766 50875 Ensembl ENSG00000138594 ENSMUSG00000058587 UniProt Q9NYL9 Q9JHJ0 RefSeq (mRNA) NM_014547 NM_016963 NM_001357828 RefSeq (protein) NP_055362 NP_058659 NP_001344757 Location (UCSC) Chr 15: 51.83 – 51.95 Mb Chr 9: 75.4 – 75.47 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Tropomodulin-3 is a protein that in humans is encoded by the TMOD3 gene. ^{[5] [6]}

Tropomodulin-3 (Tmod3) is a member of the tropomodulin family of actin-regulatory proteins that plays a key role in modulating the dynamics of the cytoskeleton by capping the pointed (minus) ends of actin filaments. Unlike some other tropomodulin isoforms, Tmod3 is widely expressed in non-muscle cells, where it contributes to essential cellular processes such as shape maintenance, motility, and adhesion. It regulates filament stability by preventing both polymerization and depolymerization at the pointed end, thus helping to define actin filament length and organization. ^[7] In endothelial cells, Tmod3 has been shown to inhibit cell motility through its capping activity, highlighting its role as a negative regulator of actin-driven migration. ^[8] Additionally, Tmod3 can bind not only to filamentous actin but also directly to actin monomers, suggesting a broader function in actin filament turnover and cytoskeletal remodeling. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000138594 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000058587 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Cox PR, Zoghbi HY (Apr 2000). "Sequencing, expression analysis, and mapping of three unique human tropomodulin genes and their mouse orthologs". Genomics. 63 (1): 97–107. doi:10.1006/geno.1999.6061. PMID   10662549.
6. "Entrez Gene: TMOD3 tropomodulin 3 (ubiquitous)".
7. Fischer RS, Yarmola EG, Weber KL, Speicher KD, Speicher DW, Bubb MR, et al. (2006-11-24). "Tropomodulin 3 Binds to Actin Monomers". The Journal of Biological Chemistry. 281 (47): 36454–36465. doi: 10.1074/jbc.M606315200 . ISSN   0021-9258. PMID   17012745.
8. Fischer RS, Fritz-Six KL, Fowler VM (April 2003). "Pointed-end capping by tropomodulin3 negatively regulates endothelial cell motility". The Journal of Cell Biology. 161 (2): 371–380. doi:10.1083/jcb.200209057. PMC   2172920 . PMID   12707310.

Further reading

• Weber KL, Fischer RS, Fowler VM (Oct 2007). "Tmod3 regulates polarized epithelial cell morphology". Journal of Cell Science. 120 (Pt 20): 3625–3632. doi: 10.1242/jcs.011445 . PMID   17928307.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, et al. (Nov 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–648. doi: 10.1016/j.cell.2006.09.026 . PMID   17081983.
• Fischer RS, Yarmola EG, Weber KL, Speicher KD, Speicher DW, Bubb MR, et al. (Nov 2006). "Tropomodulin 3 binds to actin monomers". Journal of Biological Chemistry. 281 (47): 36454–36465. doi: 10.1074/jbc.M606315200 . PMID   17012745.
• Pawlak G, McGarvey TW, Nguyen TB, Tomaszewski JE, Puthiyaveettil R, Malkowicz SB, et al. (Jun 2004). "Alterations in tropomyosin isoform expression in human transitional cell carcinoma of the urinary bladder". International Journal of Cancer. 110 (3): 368–373. doi:10.1002/ijc.20151. PMID   15095301. S2CID   875146.
• Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, et al. (Feb 2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nature Cell Biology. 6 (2): 97–105. doi:10.1038/ncb1086. PMID   14743216. S2CID   11683986.
• Fischer RS, Fritz-Six KL, Fowler VM (Apr 2003). "Pointed-end capping by tropomodulin3 negatively regulates endothelial cell motility". The Journal of Cell Biology. 161 (2): 371–380. doi:10.1083/jcb.200209057. PMC   2172920 . PMID   12707310.