Teneurin

TENM1
Identifiers
Aliases	TENM1, ODZ1, ODZ3, TEN-M1, TNM, TNM1, teneurin transmembrane protein 1
External IDs	MGI: 1345185 HomoloGene: 56542 GeneCards: TENM1
Gene ontology Molecular function • heparin binding • protein homodimerization activity • protein heterodimerization activity Cellular component • cytoplasm • integral component of membrane • Golgi apparatus • nuclear speck • membrane • nuclear matrix • plasma membrane • integral component of plasma membrane • extracellular region • endoplasmic reticulum • perinuclear region of cytoplasm • cytoskeleton • nucleus Biological process • positive regulation of intracellular protein transport • regulation of transcription, DNA-templated • positive regulation of actin filament polymerization • positive regulation of MAP kinase activity • transcription, DNA-templated • nervous system development • positive regulation of peptidyl-serine phosphorylation • regulation of transcription from RNA polymerase III promoter • immune response • neuropeptide signaling pathway • positive regulation of filopodium assembly • signal transduction • negative regulation of cell proliferation Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	10178	23963
Ensembl	ENSG00000009694	ENSMUSG00000016150
UniProt	Q9UKZ4	Q9WTS4
RefSeq (mRNA)	NM_001163278 NM_001163279 NM_014253	NM_011855
RefSeq (protein)	NP_001156750.1 NP_001156751.1 NP_055068.2	NP_035985.2
Location (UCSC)	Chr X: 124.38 – 124.96 Mb	Chr X: 42.53 – 43.43 Mb
PubMed search	[1]	[2]
Wikidata

Teneurins are transmembrane proteins. The name refers to "ten-a" (from "tenascin-like protein, accessory") and "neurons", the primary site of teneurin expression. Ten-m refers to tenascin-like protein major are type II transmembrane glycoproteins.

Teneurins are highly conserved between Drosophila, C. elegans and vertebrates. In each species they are expressed by a subset of neurons as well as at sites of pattern formation and morphogenesis. In Drosophila, a teneurin known as ten-m or Odz is a pair-rule gene, and its expression is required for normal development. The knockdown of teneurin (ten-1) expression in C. elegans with RNAi leads to abnormal neuronal pathfinding and abnormal development of the gonads.

The intracellular domain of some, if not all, teneurins can be cleaved and transported to the cell nucleus, where it proposed to act as a transcription factor. A peptide derived from the terminus of the extracellular domain shares structural homology with certain neuropeptides.

There are four teneurin genes in vertebrates named teneurin-1 through -4. Other names found in the literature include Odz-1 through -4 and Tenm-1 through -4.

Homology

Teneurins are a family of phylogenetically conserved transmembrane glycoproteins expressed during pattern formation and morphogenesis.^[9]

History

Originally discovered as ten-m and ten-a in Drosophila melanogaster, the teneurin family is conserved from Caenorhabditis elegans (ten-1) to vertebrates, in which four paralogs exist (teneurin-1 to -4 or odz-1 to -4). Their distinct protein domain architecture is highly conserved between invertebrate and vertebrate teneurins, particularly in the extracellular part. The intracellular domains of Ten-a, Ten-m/Odz and C. elegans Ten-1 are significantly different, both in size and structure, from the comparable domains of vertebrate teneurins, but the extracellular domains of all of these proteins are remarkably similar.

Function

Teneurins translocate to the nucleus where they regulate transcriptional activity. Teneurins promote neurite outgrowth and cell adhesion. The intracellular domain interacts with the DNA-binding transcriptional repressors and also regulate the activity of transcription factors.

Additionally, they have been known to interact with the cytoskeleton adaptor protein, CAP/ponsin, suggesting cell signalling roles and regulation of actin organisation.^[10]

Teneurin-3 regulates the structural and functional wiring of retinal ganglion cells in the vertebrate visual system.^[11]

Structure

Ten-m1–4, exist as homodimers and undergo homophilic interactions in vertebrates.

C terminal domain

The large C-terminal extracellular domain consists of eight EGF-like repeats (see PROSITEDOC), a region of conserved cysteines and unique YD-repeats.

N terminal domain

The teneurin intracellular (IC) domain (∼300–400 aa) is located at the N-terminus and contains a number of conserved putative tyrosine phosphorylation sites, two EF-hand-like calcium-binding motifs, and two polyproline domains. These proline-rich stretches are characteristic of SH3-binding sites. There is considerable divergence between intracellular domains of invertebrate and vertebrate teneurins as well as between different invertebrate proteins.^{[12][13][14][15][16]}

This domain is found in the intracellular N-terminal region of the teneurin family.

Human genes

Human genes encoded teneurin domain proteins (TENM1-4) are list in the infoboxes.

References

Further reading