2ATX


Conserved Protein Domain Family
Tc10

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cd04135: Tc10 
Click on image for an interactive view with Cn3D
Rho GTPase TC10 (Tc10)
TC10 is a Rho family protein that has been shown to induce microspike formation and neurite outgrowth in vitro. Its expression changes dramatically after peripheral nerve injury, suggesting an important role in promoting axonal outgrowth and regeneration. TC10 regulates translocation of insulin-stimulated GLUT4 in adipocytes and has also been shown to bind directly to Golgi COPI coat proteins. GTP-bound TC10 in vitro can bind numerous potential effectors. Depending on its subcellular localization and distinct functional domains, TC10 can differentially regulate two types of filamentous actin in adipocytes. TC10 mRNAs are highly expressed in three types of mouse muscle tissues: leg skeletal muscle, cardiac muscle, and uterus; they were also present in brain, with higher levels in adults than in newborns. TC10 has also been shown to play a role in regulating the expression of cystic fibrosis transmembrane conductance regulator (CFTR) through interactions with CFTR-associated ligand (CAL). The GTP-bound form of TC10 directs the trafficking of CFTR from the juxtanuclear region to the secretory pathway toward the plasma membrane, away from CAL-mediated DFTR degradation in the lysosome. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.
Statistics
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PSSM-Id: 206707
View PSSM: cd04135
Aligned: 4 rows
Threshold Bit Score: 350.086
Threshold Setting Gi: 28277785
Created: 3-Jan-2006
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
  next features
Conserved site includes 13 residues -Click on image for an interactive view with Cn3D
Feature 1:GTP/Mg2+ binding site [chemical binding site]
Evidence:
  • Structure:2ATX: Human TC10 binds GppNHp, a GTP analog and Mg2+, defined by 3.5A contacts
    View structure with Cn3D
  • Comment:Rho molecules assume an active conformation when bound to GTP and inactive when GTP is hydrolyzed to GDP
  • Comment:Mg2+ ion plays a key role in bringing together the functional regions of the phosphate-binding, switches I and II
  • Citation:PMID 9545299

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                ######                                      ## #                       
2ATX_B       19 LKCVVVGDGAVGKTCLLMSYANDAFPEEYVPTVFDHYAVSVTVGGKQYLLGLYDTAGQEDYDRLRPLSYPMTDVFLICFS 98
gi 32810418  19 LKCVVVGDGAVGKTCLLMSYANDAFPEEYVPTVFDHYAVSVTVEGKQYLLGLYDTAGQEDYDRLRPLSYPMTDVFLICFS 98
gi 28277785  10 LKCVVVGDGAVGKTCLLMSYANDAFPEEYVPTVFDHYAVSVTVGGKQYLLGLYDTAGQEDYDRLRPLSYPMTDVFLICFS 89
gi 49256197  22 LKCVVVGDGAVGKTCLLMSYANDAFPEQYVPTVFDHYAVTVNVGGKQYLLGLYDTAGQEDYDQLRPLSYPNTDVFLICFS 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                       # #                                        ##   
2ATX_B       99 VVNPASFQNVKEEWVPELKEyaPNVPFLLIGTQIDLRDDPktlarlndmkekpicvEQGQKLAKEIGACCYVECSALTQK 178
gi 32810418  99 VVNPASFQNVKEEWVPELKEyaPNVPFLLVGTQIDLRDDPktlarlndmkekplsvEQGQKLAKEIGAYCYVECSALTQK 178
gi 28277785  90 VVNPASFQNVREEWVPELQEyaPNIPYLLIGTQIDLRDDPktiaklndvkekpivtEQGQKLAKEIGACCYVECSALTQK 169
gi 49256197 102 VVNPASYQNVQEEWVSELRAcmPHVPYVLIGTQIDLRDDPitlarllhmkekpitqEQGMKLSKMIGAQCYLECSALTQK 181
                       170
                ....*....|....
Feature 1                     
2ATX_B      179 GLKTVFDEAIIAIL 192
gi 32810418 179 GLKTVFDEAIIAIL 192
gi 28277785 170 GLKTVFDEAIIAIL 183
gi 49256197 182 GLKNVFDEAILTVF 195

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