Phosphatase Subfamily Tensin - Revision history

Gerard: /* Domain Structure */

2018-05-04T19:00:42Z

‎Domain Structure

Gerard: /* Evolution */

2018-05-04T18:28:13Z

‎Evolution

Gerard: /* Domain Structure */

2017-04-20T18:45:55Z

‎Domain Structure

Mark: /* Domain Structure */

2015-10-15T07:06:33Z

‎Domain Structure

Mark at 16:16, 2 October 2015

2015-10-02T16:16:37Z

Mark: /* Functions */

2015-10-02T16:08:50Z

‎Functions

Mark: /* Domain Structure */

2015-10-02T16:06:24Z

‎Domain Structure

Mark: /* Domain Structure */

2015-06-26T00:59:48Z

‎Domain Structure

Mark: /* Domain Structure */

2015-06-26T00:59:30Z

‎Domain Structure

Mark: /* Evolution */

2015-06-26T00:37:33Z

‎Evolution

@@ Line 10: / Line 10: @@
 Tensins are long proteins, with an N-terminal phosphatase domain followed immediately by a PTEN_C2 domain, which acts as a lipid-binding domain. They have a poorly conserved middle region, SH2 and usually PTB domains at the C-terminus. Many Tensins also have an N-terminal C1 domain. Humans also have a homologous TNS4 protein which is N-terminally truncated and has lost the phosphatase domain. The phosphatase domain is quite divergent and often can not be picked by Pfam or SMART.
-TNS1 and TNS2 are predicted to be catalytically inactive, given the arginine residue is replaced by asparagine and lysine at CX<sub>5</sub>R motif, respectively. But, the catalytic activity of TNS2 has been reported. These may function as binding domains for phosphatidyl inositols.
+TNS1 and TNS2 are predicted to be catalytically inactive, given the arginine residue is replaced by asparagine and lysine at CX<sub>5</sub>R motif, respectively, though catalytic activity of TNS2 has been reported. These may function as binding domains for phosphatidyl inositols. The single orthologs in most invertebrates are predicted to be catalytically active.
 The functions of the phosphatase domain are not well understood:

@@ Line 5: / Line 5: @@
 ===Evolution===
-Tensins are found throughout [[holozoa]]. The domain combination is under dramatic changes during evolution. Drosophilids have a truncated ortholog ([http://www.sdbonline.org/sites/fly/cytoskel/blistery1.htm ''blistery'']) which lacks the phosphatase domain, though the full-length form is seen in mosquitoes. One of the four human members, TNS4, is also truncated. See domain section below.
+Tensins are found throughout [[holozoa]]. The domain combination is under dramatic changes during evolution. Drosophilids have a truncated ortholog ([http://www.sdbonline.org/sites/fly/cytoskel/blistery1.htm ''blistery'']) which lacks the phosphatase domain, though the full-length form is seen in mosquitoes. One of the four human members, TNS4, is also truncated.
 ===Domain Structure===

@@ Line 14: / Line 14: @@
 The functions of the phosphatase domain are not well understood:
 * TNS1. The phosphatase domain can bind to PPP1CA in focal adhesions <cite>Eto07</cite>.
-* TNS2. TNS2 induced in vivo dephosporylation of phosphatidylinositol 3,4,5-trisphosphate, though the activity could not be replaced in vitro <cite>Hafizi</cite>. Another report <cite>Koh</cite> showed TNS2 protein tyrosine phosphatase activity on IRS-1.
+* TNS2. TNS2 induced in vivo dephosporylation of phosphatidylinositol 3,4,5-trisphosphate, though the activity could not be replicated in vitro <cite>Hafizi</cite>. Another report <cite>Koh</cite> showed TNS2 protein tyrosine phosphatase activity on IRS-1.
 ===Functions===

@@ Line 8: / Line 8: @@
 ===Domain Structure===
-Tensins are long proteins, with an N-terminal phosphatase domain followed immediately by a PTEN_C2 domain, which acts as a lipid-binding domain. They have a poorly conserved middle region, SH2 and usually PTB domains at the C-terminus. Human TNS2 (TENC1) and many invertebrate Tensins also have an N-terminal C1 domain. Humans also have a homologous TNS4 protein which is N-terminally truncated and has lost the phosphatase domain. The phosphatase domain is quite divergent and often can not be picked by Pfam or SMART.
+Tensins are long proteins, with an N-terminal phosphatase domain followed immediately by a PTEN_C2 domain, which acts as a lipid-binding domain. They have a poorly conserved middle region, SH2 and usually PTB domains at the C-terminus. Many Tensins also have an N-terminal C1 domain. Humans also have a homologous TNS4 protein which is N-terminally truncated and has lost the phosphatase domain. The phosphatase domain is quite divergent and often can not be picked by Pfam or SMART.
 TNS1 and TNS2 are predicted to be catalytically inactive, given the arginine residue is replaced by asparagine and lysine at CX<sub>5</sub>R motif, respectively. But, the catalytic activity of TNS2 has been reported. These may function as binding domains for phosphatidyl inositols.

@@ Line 10: / Line 10: @@
 Tensins are long proteins, with an N-terminal phosphatase domain followed immediately by a PTEN_C2 domain, which acts as a lipid-binding domain. They have a poorly conserved middle region, SH2 and usually PTB domains at the C-terminus. Human TNS2 (TENC1) and many invertebrate Tensins also have an N-terminal C1 domain. Humans also have a homologous TNS4 protein which is N-terminally truncated and has lost the phosphatase domain. The phosphatase domain is quite divergent and often can not be picked by Pfam or SMART.
-TNS1 and TNS2 are predicted to be catalytically inactive, given the arginine residue is replaced by asparagine and lysine at CX<sub>5</sub>R motif, respectively. But, the catalytic activity of TNS2 has been reported (below). These may function as binding domains for phosphatidyl inositols.
+TNS1 and TNS2 are predicted to be catalytically inactive, given the arginine residue is replaced by asparagine and lysine at CX<sub>5</sub>R motif, respectively. But, the catalytic activity of TNS2 has been reported. These may function as binding domains for phosphatidyl inositols.
-===Functions===
+The functions of the phosphatase domain are not well understood:
-Tensin are localized to integrin-mediated focal adhesions. The PTB domain binds to the cytoplasmic region of integrins, and N-terminal regions bind actin. The SH2 domain interacts with a variety of tyrosine-phosphorylated proteins, including PI3K, FAK, and p130Cas. Several tensins are linked to cell migration and metastasis suppression and to signaling downstream of receptor tyrosine kinases.
+* TNS1. The phosphatase domain can bind to PPP1CA in focal adhesions <cite>Eto07</cite>.
-The catalytic functions of the phosphatase domain are not well understood. TNS2 induced in vivo dephosporylation of phosphatidylinositol 3,4,5-trisphosphate, though the activity could not be replaced in vitro <cite>Hafizi</cite>. Another report <cite>Koh</cite> showed TNS2 protein tyrosine phosphatase activity on IRS-1.
+===Functions===
 ===References===
@@ Line 21: / Line 23: @@
 #Hafizi pmid=20678486
 #Koh pmid=23401856
 </biblio>

@@ Line 8: / Line 8: @@
 ===Domain Structure===
-Tensins are long proteins, with an N-terminal phosphatase domain followed immediately by a PTEN_C2 domain, which acts as a lipid-binding domain. They have a poorly conserved middle region, SH2 and usually PTB domains at the C-terminus. Human TNS2 (TENC1) and many invertebrate Tensins also have an N-terminal C1 domain. Humans also have a homologous TNS4 protein which is N-terminally truncated and has lost the phosphatase domain. The phosphatase domain is divergent and not picked by by many domain tools.
+Tensins are long proteins, with an N-terminal phosphatase domain followed immediately by a PTEN_C2 domain, which acts as a lipid-binding domain. They have a poorly conserved middle region, SH2 and usually PTB domains at the C-terminus. Human TNS2 (TENC1) and many invertebrate Tensins also have an N-terminal C1 domain. Humans also have a homologous TNS4 protein which is N-terminally truncated and has lost the phosphatase domain. The phosphatase domain is quite divergent and often can not be picked by many domain tools.
 The TNS1 phosphatase domain is predicted to be catalytically inactive (The catalytic C is changed to N); TNS2 is predicted to be catalytically inactive, given arginine is replaced by lysine at CX<sub>5</sub>R motif, but catalytic activity has been reported (below). These may function as binding domains for phosphatidyl inositols.