1X61


Conserved Protein Domain Family
LIM1_TRIP6

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cd09350: LIM1_TRIP6 
Click on image for an interactive view with Cn3D
The first LIM domain of Thyroid receptor-interacting protein 6 (TRIP6)
The first LIM domain of Thyroid receptor-interacting protein 6 (TRIP6): TRIP6 is a member of the zyxin LIM protein family and contains three LIM zinc-binding domains at the C-terminal. TRIP6 protein localizes to focal adhesion sites and along actin stress fibers. Recruitment of this protein to the plasma membrane occurs in a lysophosphatidic acid (LPA)-dependent manner. TRIP6 recruits a number of molecules involved in actin assembly, cell motility, survival and transcriptional control. The function of TRIP6 in cell motility is regulated by Src-dependent phosphorylation at a Tyr residue. The phosphorylation activates the coupling to the Crk SH2 domain, which is required for the function of TRIP6 in promoting lysophosphatidic acid (LPA)-induced cell migration. TRIP6 can shuttle to the nucleus to serve as a coactivator of AP-1 and NF-kappaB transcriptional factors. Moreover, TRIP6 can form a ternary complex with the NHERF2 PDZ protein and LPA2 receptor to regulate LPA-induced activation of ERK and AKT, rendering cells resistant to chemotherapy. Recent evidence shows that TRIP6 antagonizes Fas-Induced apoptosis by enhancing the antiapoptotic effect of LPA in cells. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.
Statistics
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PSSM-Id: 188736
Aligned: 9 rows
Threshold Bit Score: 76.6733
Created: 26-Jul-2010
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Zn binding site
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1:Zn binding site [ion binding site]
Evidence:
  • Structure:1X61_A: Human Thyroid Receptor Interacting Protein 6 (Trip6) LIM1 domain binds Zn
  • Comment:The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The Zn binding residues of LIM domain are highly conserved.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1        #  #                  #  #  #   #                 #  # 
1X61_A         8 CGGCGEDVVGDgaGVVALDRVFHVGCFVCS-TCRAQLRGQHFYAVERRAYCEGCY 61  human
AAI44077     416 CARCGENVVGEgtGCTAMDQVFHVDCFTCI-ICNNKLRGQPFYAVEKKAYCEPCY 469 human
NP_001026738 408 CARCGENVVGEgtGCTAMDQVFHVECFTCM-MCNNKLRGQPFYAVEKKAYCEPCY 461 chicken
CAF89582     316 CARCGDNVVGDgsGCIAMEQVFHVECFTCI-TCHAHLRGQPFYALDKKSYCESCY 369 spotted green pufferfish
NP_001090015 432 CSRCGENVVGEgtGCTAMDQVFHVECFTCM-TCNSKLRGQPFYAVEKKAFCEPCY 485 African clawed frog
AAI71497     360 CSSCGENVVGEgtGCTAMDQVFHVDCFICM-TCGSKLRGKPFYAVEKKAYCEPCY 413 zebrafish
XP_002730765 404 CGKCNQKVMGEenGCSAMDQIFHIDCFTCV-TCNGRLRGKPFYALEGKSYCEECY 457 Saccoglossus kowalevskii
XP_798292    257 CSRCSNKVVGEnnGCTAMEQVYHVDCFTCEnNCGTKLRGQPFYALEGKAFCEHCY 311 purple urchin
XP_002601179  41 CGNCGQKVIVDeeGCSAMDKVFHVKCFTCT-TCGGRLSGKPFYAMENHPYCEECY 94  Florida lancelet

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