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FLASH GENE

Symbol

TMOD3

contributors: mct - updated : 12-10-2016

HGNC name	tropomodulin 3 (ubiquitous)
HGNC id	11873

FLASH GENE DNA RNA EXPRESSION PROTEIN DISORDER ANIMAL & CELL MODELS

RNA

TRANSCRIPTS	type	messenger

identification nb exons type bp product Protein kDa AA specific expression Year Pubmed NM_014547 10 - 4682 NP_055362 - 352 - 2007 17928307

EXPRESSION

Type	ubiquitous

expressed in	(based on citations)
organ(s)	System Organ level 1 Organ level 2 Organ level 3 Organ level 4 Level Pubmed Species Stage Rna symbol Cardiovascular heart         Nervous brain         Homo sapiens Urinary kidney

tissue

System Tissue Tissue level 1 Tissue level 2 Level Pubmed Species Stage Rna symbol Blood / hematopoietic bone marrow       Homo sapiens Muscular striatum skeletal     Homo sapiens

cells

System Cell Pubmed Species Stage Rna symbol Blood/Hematopoietic megakaryocyte Homo sapiens Blood/Hematopoietic platelet Homo sapiens Endocrine islet cell (alpha,beta...)

cell lineage

cell lines

fluid/secretion

at STAGE

PROTEIN

PHYSICAL PROPERTIES

STRUCTURE

motifs/domains	a N terminal tropomyosin binding domain and
	a C terminal actin-binding domain, and C-terminal (LRR) domain having roles in the formation of neurite-like processes

HOMOLOGY

interspecies

homolog to murineTmod3

Homologene

FAMILY

tropomodulin family

CATEGORY

motor/contractile

SUBCELLULAR LOCALIZATION	plasma membrane,junction
	intracellular
	intracellular,cytoplasm,cytoskeleton
text	localizes to lateral cell membranes in polarized epithelia of several cell types
	TMOD1, TMOD2 and TMOD3 are associated with the cytoskeleton of non-muscle cells and their expression has distinct consequences on cell morphology

basic FUNCTION	blocking the elongation and depolymerization of the actin filaments at the pointed end
	TMOD3-capped tropomyosin-actin filaments provide likely crucial links in the spectrin membrane skeleton of polarized epithelial cells, enabling the membrane skeleton to maintain cell shape
	TMOD3 and TMOD4 compensate for the absence of TMOD1 structurally but not functionally
	TMOD1-TMOD3 but not TMOD4 nucleate actin filament assembly
	is an actin-capping protein that binds to the two tropomyosins (TM) at the pointed end of the actin filament to prevent further actin polymerization and depolymerization
	is a protein that binds and caps the pointed ends of actin filaments in erythroid and nonerythoid cell types
	novel function for TMOD3 in regulating actin remodeling or turnover in cells
	regulation of actin polymerization by TMOD3 controls megakaryocyte actin organization and platelet biogenesis
	TMOD1, TMOD2, TMOD3 regulates the length of actin filaments by capping the pointed ends in a tropomyosin (TM)-dependent manner
	cap pointed ends of actin filaments and to be enriched in leading-edge ruffles and lamellipodia

CELLULAR PROCESS

PHYSIOLOGICAL PROCESS

PATHWAY

metabolism

signaling

a component

INTERACTION

DNA

RNA

small molecule

protein	TMOD3 binds actin monomers over an extended interface and nucleating activity depends on actin monomer binding and pointed end-capping activities, contributed by N- and C-terminal domains of TMOD3, respectivelyv
	TMOD3 is a novel AKT2 effector regulating insulin-stimulated SLC2A4 exocytosis through cortical actin remodeling
	two actin-related binding partners of PLS3, are CORO1C, and TMOD3

cell & other

REGULATION

ASSOCIATED DISORDERS

corresponding disease(s)

Other morbid association(s)

Type Gene Modification Chromosome rearrangement Protein expression Protein Function constitutional     --low   leads to impaired definitive erythropoiesis due to reduced progenitors, impaired erythroblastic island formation, and defective erythroblast cell-cycle progression and enucleation

Susceptibility

Variant & Polymorphism

Candidate gene
Marker	serum anti-TPM3, anti-TMOD3, anti-STOML2 could be new markers for the early diagnosis of endometriosis
Therapy target

ANIMAL & CELL MODELS