| | ARID2 (12q12) / TMPRSS2 (21q22.3) | ATF7IP (12p13.1) / TMPRSS2 (21q22.3) | ERG (21q22.2) / TMPRSS2 (21q22.3) |
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ETV1 (7p21.2) / TMPRSS2 (21q22.3) | ETV4 (17q21.31) / TMPRSS2 (21q22.3) | ETV5 (3q27.2) / TMPRSS2 (21q22.3) |
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NR4A1 (12q13.13) / TMPRSS2 (21q22.3) | TMPRSS2 (21q22.3) / ARFGEF2 (20q13.13) | TMPRSS2 (21q22.3) / ATF7IP (12p13.1) |
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TMPRSS2 (21q22.3) / ERG (21q22.2) | TMPRSS2 (21q22.3) / ETV1 (7p21.2) | TMPRSS2 (21q22.3) / ETV4 (17q21.31) |
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TMPRSS2 (21q22.3) / ETV5 (3q27.2) | TMPRSS2 (21q22.3) / FKBP5 (6p21.31) | TMPRSS2 (21q22.3) / GRHL2 (8q22.3) |
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TMPRSS2 (21q22.3) / MALAT1 (11q13.1) | TMPRSS2 (21q22.3) / SKIL (3q26.2) |
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| | TMPRSS2 is a 492 amino acid single-pass type II membrane protein. It contains a Serine protease domain (aa 255-492) of the S1 family, followed by a Scavenger receptor cysteine-rich domain (SRDR, aa 149-242) of group A; an LDL receptor class A (LDLRA, aa 113-148) domain forms a binding site for calcium; a predicted transmembrane domain (aa 84-106). Letters H, D and S in the serine protease domain indicate the position of the three catalytic residues histidine, aspartate and serine, respectively. |
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| Description | TMPRSS2 is a 492 amino acid type II transmembrane serine proteases (TTSPs) which are expressed at the cell surface and are thus ideally located to regulate cell-cell and cell-matrix interactions. |
| Expression | TMPRSS2 is expressed in normal and diseased human tissues. Especially, TMPRSS2 is highly expressed in small intestine, but also in lower levels in several other tissues. Also expressed in prostate, colon, stomach and salivary gland. |
| Localisation | Subcellular location: Cell membrane; Single-pass type II membrane protein.
Activated by cleavage and secreted. |
| Function | This gene was demonstrated to be up-regulated by androgenic hormones in prostate cancer cells and down-regulated in androgen-independent prostate cancer tissue. To containing intra- and extracellular domains, TMPRSS2 could work as a receptor for specific ligand(s) mediating signals between the environment and the cell. TMPRSS2 has been proposed to regulate epithelial sodium currents in the lung through proteolytic cleavage of the epithelial sodium channel and inflammatory responses in the prostate via the proteolytic activation of PAR-2. |
| Homology | TTPs (type II transmembrane serine proteases) contain an integral transmembrane domain and remain cell-surface-associated, even after proteolytic activation of the protease zymogen. Human TTSPs, which consists of 17 members, were grouped into four subfamilies based on similarity in domain structure and phylogenetic analysis of the serine protease domains, namely the matriptase, corin, hepsin/TMPRSS and HAT/DESC subfamilies. |
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| Prostate cancer genes associated with TMPRSS2-ERG gene fusion and prognostic of biochemical recurrence in multiple cohorts. |
| Barwick BG, Abramovitz M, Kodani M, Moreno CS, Nam R, Tang W, Bouzyk M, Seth A, Leyland-Jones B. |
| Br J Cancer. 2010 Feb 2;102(3):570-6. Epub 2010 Jan 12. |
| PMID 20068566 |
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| Type II transmembrane serine proteases. |
| Bugge TH, Antalis TM, Wu Q. |
| J Biol Chem. 2009 Aug 28;284(35):23177-81. Epub 2009 Jun 1. (REVIEW) |
| PMID 19487698 |
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| Type II transmembrane serine proteases in cancer and viral infections. |
| Choi SY, Bertram S, Glowacka I, Park YW, Pohlmann S. |
| Trends Mol Med. 2009 Jul;15(7):303-12. Epub 2009 Jul 4. (REVIEW) |
| PMID 19581128 |
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| Cloning of the TMPRSS2 gene, which encodes a novel serine protease with transmembrane, LDLRA, and SRCR domains and maps to 21q22.3. |
| Paoloni-Giacobino A, Chen H, Peitsch MC, Rossier C, Antonarakis SE. |
| Genomics. 1997 Sep 15;44(3):309-20. |
| PMID 9325052 |
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| Expression of transmembrane serine protease TMPRSS2 in mouse and human tissues. |
| Vaarala MH, Porvari KS, Kellokumpu S, Kyllonen AP, Vihko PT. |
| J Pathol. 2001 Jan;193(1):134-40. |
| PMID 11169526 |
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