Tensin-1 (TNS1)
The protein contains 1735 amino acids for an estimated molecular weight of 185701 Da.
Involved in fibrillar adhesion formation. May be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. (updated: April 1, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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The reference OMIM entry for this protein is 600076
Tensin 1; tns1
Tensin; tns
DESCRIPTION
Tensin is an actin-binding protein that is concentrated in some submembranous cytoskeletal focal contacts (Weigt et al., 1992). In addition to its 3 actin-binding domains, the 200-kD tensin protein contains an Src homology 2 (SH2) motif that mediates protein-protein contacts and is shared by a variety of signal transduction molecules. In addition, tensin can bind to phosphotyrosine-containing proteins and can itself be phosphorylated, suggesting that tensin may be a link between the cytoskeleton and a signal transduction pathway. Tensin phosphorylation occurs during cell adhesion to extracellular matrix proteins.CLONING
Using avian tensin as probe, Chen et al. (2000) obtained overlapping clones of tensin from human heart and bovine pericyte cDNA libraries. The deduced 1,735-amino acid protein has a calculated molecular mass of 185 kD. Human and bovine tensins share 82% amino acid identity. In addition to the actin-binding domains and SH2 domain, tensin contains a region similar to PTEN (601728) and a 9-amino acid sequence that is repeated 4 times. Northern blot analysis revealed a major 10-kb transcript expressed in most tissues, with highest levels in heart, skeletal muscle, kidney, and lung. Heart and skeletal muscle also expressed a 9-kb transcript. Western blot analysis revealed an apparent molecular mass of 220 kD, and mutation analysis revealed that the discrepancy between the calculated and the apparent molecular masses was due to the reduced electrophoretic mobility of the central region of the tensin polypeptide. Expression of tensin in mouse fibroblasts resulted in staining at focal adhesions.GENE FUNCTION
Katz et al. (2000) presented evidence that overexpression of mammalian tensin activates both the JNK (601158) and p38 MAPK (600289) pathways. Tensin-mediated JNK activation was independent of the activities of Rac (602048) and Cdc42 (116952), but did depend on Sek (601335). Chen et al. (2002) determined that stable overexpression of both tensin-1 and -2 (TENC1; 607717) in HEK293 cells promoted cell migration on fibronectin (135600) in a cell migration assay. Fibroblasts from tensin-1-null mice migrated significantly slower than their normal counterparts in the cell migration assay, and tensin-2 expression was not upregulated to compensate for loss of tensin-1 function. Chen et al. (2000) found that tensin expression was reduced or absent in several prostate and breast cancer cell lines, while the levels of talin (186745) and focal adhesion kinase (600758) remained at normal levels. They also found that tensin is a substrate for a focal adhesion protease, calpain II (114230), and that incubation of cells with a calpain inhibitor prevented tensin cleavage and induced morphologic change. Chen et al. (2002) hypothesized that cleavage of tensin and other focal adhesion constituents by calpain disrupts maintenance of normal cell shape.GENE STRUCTURE
Chen et al. (2002) determined that the tensin gene contains 33 exons and spans about 150 kb. Exon 6 contains the putative start codon.MAPPING
Jankowski and Gumucio (1995) demonstrated that, in the mouse, genes for tensin, villin (193040), and desmin (125660) are closely linked on chromosome 1. This region is homologous to human chromosome 2; in the human, the desmin gene maps to 2q35 and the villin-1 gene to 2q35-q36. Jankowski and Gumucio (1995) used a rat DNA probe to study human/rodent somatic cell hybrids and ob ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 600076 was added.