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0  structures 100  species 0  interactions 704  sequences 21  architectures

Family: Ten_N (PF06484)

Summary: Teneurin Intracellular Region

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Teneurin". More...

Teneurin Edit Wikipedia article

TENM1
Identifiers
Aliases TENM1, ODZ1, ODZ3, TEN-M1, TNM, TNM1, teneurin transmembrane protein 1
External IDs MGI: 1345185 HomoloGene: 56542 GeneCards: TENM1
Gene location (Human)
X chromosome (human)
Chr. X chromosome (human)[1]
X chromosome (human)
Genomic location for TENM1
Genomic location for TENM1
Band Xq25 Start 124,375,903 bp[1]
End 124,963,817 bp[1]
RNA expression pattern
PBB GE ODZ1 205728 at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001163278
NM_001163279
NM_014253

NM_011855

RefSeq (protein)

NP_001156750
NP_001156751
NP_055068

NP_035985

Location (UCSC) Chr X: 124.38 – 124.96 Mb Chr X: 42.53 – 43.43 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse
TENM2
Identifiers
Aliases TENM2, ODZ2, TEN-M2, TNM2, ten-2, teneurin transmembrane protein 2
External IDs MGI: 1345184 HomoloGene: 22672 GeneCards: TENM2
Gene location (Human)
Chromosome 5 (human)
Chr. Chromosome 5 (human)[1]
Chromosome 5 (human)
Genomic location for TENM2
Genomic location for TENM2
Band 5q34 Start 167,284,799 bp[1]
End 168,264,157 bp[1]
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001080428
NM_001122679

NM_001290702
NM_011856

RefSeq (protein)

NP_001073897
NP_001116151

n/a

Location (UCSC) Chr 5: 167.28 – 168.26 Mb Chr 5: 36.01 – 37.24 Mb
PubMed search [5] [6]
Wikidata
View/Edit Human View/Edit Mouse
TENM3
Identifiers
Aliases TENM3, MCOPCB9, ODZ3, TNM3, Ten-m3, ten-3, teneurin transmembrane protein 3
External IDs MGI: 1345183 HomoloGene: 22673 GeneCards: TENM3
Gene location (Human)
Chromosome 4 (human)
Chr. Chromosome 4 (human)[1]
Chromosome 4 (human)
Genomic location for TENM3
Genomic location for TENM3
Band 4q34.3-q35.1 Start 182,143,987 bp[1]
End 182,803,024 bp[1]
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001080477

NM_001145937
NM_011857

RefSeq (protein)

NP_001073946

n/a

Location (UCSC) Chr 4: 182.14 – 182.8 Mb Chr 4: 48.23 – 48.84 Mb
PubMed search [7] [8]
Wikidata
View/Edit Human View/Edit Mouse
TENM4
Identifiers
Aliases TENM4, Doc4, ODZ4, TNM4, Ten-M4, ETM5, teneurin transmembrane protein 4, ten-4
External IDs MGI: 2447063 HomoloGene: 8034 GeneCards: TENM4
Gene location (Human)
Chromosome 11 (human)
Chr. Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for TENM4
Genomic location for TENM4
Band 11q14.1 Start 78,652,831 bp[1]
End 79,440,948 bp[1]
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001098816

NM_011858
NM_001310760
NM_001310762

RefSeq (protein)

NP_001092286

NP_001297689
NP_001297691
NP_035988

Location (UCSC) Chr 11: 78.65 – 79.44 Mb Chr 11: 96.17 – 96.91 Mb
PubMed search [9] [10]
Wikidata
View/Edit Human View/Edit Mouse

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.[11]

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.[12]

Teneurin-3 regulates the structural and functional wiring of retinal ganglion cells in the vertebrate visual system.[13]

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

Teneurin Intracellular Region
Identifiers
Symbol Ten_N
Pfam PF06484
InterPro IPR009471

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.[14][15][16][17][18]

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

  1. ^ a b c d e f g h i j k l GRCh38: Ensembl release 89: ENSG00000009694 - Ensembl, May 2017 Cite error: Invalid <ref> tag; name "refGRCh38Ensembl" defined multiple times with different content (see the help page). Cite error: Invalid <ref> tag; name "refGRCh38Ensembl" defined multiple times with different content (see the help page). Cite error: Invalid <ref> tag; name "refGRCh38Ensembl" defined multiple times with different content (see the help page).
  2. ^ a b c d e f g h i j k l GRCm38: Ensembl release 89: ENSMUSG00000016150 - Ensembl, May 2017 Cite error: Invalid <ref> tag; name "refGRCm38Ensembl" defined multiple times with different content (see the help page). Cite error: Invalid <ref> tag; name "refGRCm38Ensembl" defined multiple times with different content (see the help page). Cite error: Invalid <ref> tag; name "refGRCm38Ensembl" defined multiple times with different content (see the help page).
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ "Human PubMed Reference:". 
  6. ^ "Mouse PubMed Reference:". 
  7. ^ "Human PubMed Reference:". 
  8. ^ "Mouse PubMed Reference:". 
  9. ^ "Human PubMed Reference:". 
  10. ^ "Mouse PubMed Reference:". 
  11. ^ Tucker RP, Chiquet-Ehrismann R, Chevron MP, Martin D, Hall RJ, Rubin BP (January 2001). "Teneurin-2 is expressed in tissues that regulate limb and somite pattern formation and is induced in vitro and in situ by FGF8". Dev. Dyn. 220 (1): 27–39. doi:10.1002/1097-0177(2000)9999:9999<::AID-DVDY1084>3.0.CO;2-B. PMID 11146505. 
  12. ^ Young TR, Leamey CA (2009). "Teneurins: important regulators of neural circuitry". Int J Biochem Cell Biol. 41 (5): 990–3. doi:10.1016/j.biocel.2008.06.014. PMID 18723111. 
  13. ^ Antinucci P, Nikolaou N, Meyer MP, Hindges R (2013). "Teneurin-3 specifies morphological and functional connectivity of retinal ganglion cells in the vertebrate visual system". Cell Rep. 5 (3): 582–92. doi:10.1016/j.celrep.2013.09.045. PMC 3898612Freely accessible. PMID 24183672. 
  14. ^ Minet AD, Rubin BP, Tucker RP, Baumgartner S, Chiquet-Ehrismann R (June 1999). "Teneurin-1, a vertebrate homologue of the Drosophila pair-rule gene ten-m, is a neuronal protein with a novel type of heparin-binding domain". J. Cell Sci. 112 (12): 2019–32. PMID 10341219. 
  15. ^ Bagutti C, Forro G, Ferralli J, Rubin B, Chiquet-Ehrismann R (July 2003). "The intracellular domain of teneurin-2 has a nuclear function and represses zic-1-mediated transcription". J. Cell Sci. 116 (Pt 14): 2957–66. doi:10.1242/jcs.00603. PMID 12783990. 
  16. ^ Tucker RP, Chiquet-Ehrismann R (February 2006). "Teneurins: a conserved family of transmembrane proteins involved in intercellular signaling during development". Dev. Biol. 290 (2): 237–45. doi:10.1016/j.ydbio.2005.11.038. PMID 16406038. 
  17. ^ Tucker RP, Kenzelmann D, Trzebiatowska A, Chiquet-Ehrismann R (2007). "Teneurins: transmembrane proteins with fundamental roles in development". Int. J. Biochem. Cell Biol. 39 (2): 292–7. doi:10.1016/j.biocel.2006.09.012. PMID 17095284. 
  18. ^ Kenzelmann D, Chiquet-Ehrismann R, Tucker RP (June 2007). "Teneurins, a transmembrane protein family involved in cell communication during neuronal development". Cell. Mol. Life Sci. 64 (12): 1452–6. doi:10.1007/s00018-007-7108-9. PMID 17502993. 

Further reading

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Teneurin Intracellular Region Provide feedback

This family is found in the intracellular N-terminal region of the Teneurin family of proteins. These proteins are 'pair-rule' genes and are involved in tissue patterning, specifically probably neural patterning. The intracellular domain is cleaved in response to homophilic interaction of the extracellular domain, and translocates to the nucleus. Here it probably carries out to some transcriptional regulatory activity ([1]). The length of this region and the conservation suggests that there may be two structural domains here (personal obs:C Yeats).

Literature references

  1. Bagutti C, Forro G, Ferralli J, Rubin B, Chiquet-Ehrismann R; , J Cell Sci 2003;116:2957-2966.: The intracellular domain of teneurin-2 has a nuclear function and represses zic-1-mediated transcription. PUBMED:12783990 EPMC:12783990


This tab holds annotation information from the InterPro database.

InterPro entry IPR009471

Teneurins are a family of phylogenetically conserved transmembrane glycoproteins expressed during pattern formation and morphogenesis [PUBMED:11146505]. 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 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.

The large C-terminal extracellular domain consists of eight EGF-like repeats (see PROSITEDOC), a region of conserved cysteines and unique YD-repeats. The N-terminal intracellular domain of vertebrate teneurins contains two EF-hand-like calcium-binding motifs and two polyproline regions involved in protein-protein interactions, followed by a single-span transmembrane domain. The intracellular domain is linked to the cytoskeleton through its interaction with the adaptor protein CAP/ponsin and can be cleaved near (or possibly in) the transmembrane domain and transported to the nucleus [PUBMED:12361962, PUBMED:10588872], giving teneurins the potential to act as transcription factors [PUBMED:12783990, PUBMED:12783990]. There is considerable divergence between intracellular domains of invertebrate and vertebrate teneurins as well as between different invertebrate proteins [PUBMED:10341219, PUBMED:12783990, PUBMED:16406038, PUBMED:17095284, PUBMED:17502993].

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

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

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Alignments

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(11)
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(3647)
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(63)
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(155)
RP55
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RP75
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Full
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(959)
NCBI
(3647)
Meta
(0)
RP15
(63)
RP35
(155)
RP55
(402)
RP75
(565)
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  Seed
(11)
Full
(704)
Representative proteomes UniProt
(959)
NCBI
(3647)
Meta
(0)
RP15
(63)
RP35
(155)
RP55
(402)
RP75
(565)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

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This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: ADDA_8545
Previous IDs: none
Type: Family
Author: Yeats C
Number in seed: 11
Number in full: 704
Average length of the domain: 151.10 aa
Average identity of full alignment: 32 %
Average coverage of the sequence by the domain: 11.20 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.2 20.2
Trusted cut-off 20.6 23.2
Noise cut-off 19.7 20.1
Model length: 373
Family (HMM) version: 11
Download: download the raw HMM for this family

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