1X68,1X4L


Conserved Protein Domain Family
LIM4_FHL

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cd09347: LIM4_FHL 
Click on image for an interactive view with Cn3D
The fourth LIM domain of Four and a half LIM domains protein (FHL)
The fourth LIM domain of Four and a half LIM domains protein (FHL): LIM-only protein family consists of five members, designated FHL1, FHL2, FHL3, FHL5 and LIMPETin. The first four members are composed of four complete LIM domains arranged in tandem and an N-terminal single zinc finger domain with a consensus sequence equivalent to the C-terminal half of a LIM domain. LIMPETin is an exception, containing six LIM domains. FHL1, 2 and 3 are predominantly expressed in muscle tissues, and FHL5 is highly expressed in male germ cells. FHL proteins exert their roles as transcription co-activators or co-repressors through a wide array of interaction partners. For example, FHL1 binds to Myosin-binding protein C, regulating myosin filament formation and sarcomere assembly. FHL2 has shown to interact with more than 50 different proteins, including receptors, structural proteins, transcription factors and cofactors, signal transducers, splicing factors, DNA replication and repair enzymes, and metabolic enzymes. FHL3 interacts with many transcription factors, such as CREB, BKLF/KLF3, CtBP2, MyoD, and MZF_1. FHL5 is a tissue-specific coactivator of CREB/CREM family transcription factors. LIM domains are 50-60 amino acids in size and share 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 complexes.
Statistics
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PSSM-Id: 188733
Aligned: 15 rows
Threshold Bit Score: 90.8664
Created: 28-Jul-2010
Updated: 9-Sep-2024
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:1X4L_A: Human Four and half LIM domain proteins 2 LIM4 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        #  #                    #  #  #  #                 #  # 
1X68_A         8 CVACSKPISGLTGAKFicFQDSQWHSECFNCGKCSVSLVGKGFLTQNKEIFCQKCG 63  human
XP_002410816 276 CTACSKPITGIGGTRFisFEDRNWHNDCFICAMCNNSLVGKGFITDGPEILCPECA 331 black-legged tick
1X4L_A         8 CAGCTNPISGLGGTKYisFEERQWHNDCFNCKKCSLSLVGRGFLTERDDILCPDCG 63  human
NP_001167322 221 CASCNSPITGFGEGKYisFQDRQWHQPCFKCSRCSVSLVGAGFFPDRDQILCGDCN 276 Atlantic salmon
XP_002731816 422 CTSCSKPITGMGGTKFisFDNRNWHNDCFNCVKCQSSLVGQGFMTEEEDILCPVCG 477 Saccoglossus kowalevskii
ACA13258     500 CTKCTKPITGFGGCKFisFEDRHWHSECFLCGKCNSNLVGRGFLTSDDMIMCSECG 555 Schistosoma mansoni
CAX73099     229 CAKCTKAISGFGGCKFvtFEDKHWHSDCFNCSKCQTSLVGKGFLVSDDGVVCPECT 284 Schistosoma japonicum
XP_001377295 149 CDSCNKPIADPEGPSYisFQERQWHSDCFKCRKCNVSLVDKPFMTQQKEILCRVCG 204 gray short-tailed opossum
NP_001087877 222 CAACTKPITGQGGAKYisFEERQWHSDCFICTKCSKSLVGQKFLTQQDDVLCPACG 277 African clawed frog
NP_067293    222 CAACTKPITGLRGAKFicFQDRQWHSECFNCGKCSVSLVGEGFLTHNMEILCRKCG 277 house mouse

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