2EHE


Conserved Protein Domain Family
LIM1_FHL

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cd09343: LIM1_FHL 
Click on image for an interactive view with Cn3D
The first LIM domain of Four and a half LIM domains protein (FHL)
The first 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 int eracts 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: 188729
Aligned: 10 rows
Threshold Bit Score: 90.5739
Created: 12-May-2010
Updated: 10-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:2EHE_A: Human Four And A Half LIM Domains Protein 3 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            #  #                  #  #  #  #                 #  #  
2EHE_A        14 FANTCAECQQLIGHDSrELFYEDRHFHEGCFRCCRCQRSLADEpFTCQDSELLCNDCYC 72  human
NP_730212    313 FANTCEECNKIIGIDSkDLSYKDKHWHEACFLCFKCHLSLVDKqFGAKADKIYCGNCYD 371 fruit fly
XP_416924     36 YSNTCEECKKPIGADCkDLSYKDRHWHETCFHCFQCKNSLVDKpFAAKEEHLLCTDCYS 94  chicken
NP_001087877  37 FANPCERCKKMIECNSkDLAYKDSHWHETCFRCDKCDHSLVEKpFAAKDELLLCIECYS 95  African clawed frog
AAX28516      44 FSHTCELCKEKITCDSkDLSFKDKHWHERCFFCSVCQGSLADKpFATKDNDLYCPECYD 102 Schistosoma japonicum
ACA13258     315 FANTCEQCKEKIGCDSkDLSFKERHWHEKCFKCSACTTSLADRpFATKEEQLYCSDCYD 373 Schistosoma mansoni
XP_002731816 237 FANTCEECSLKIGTDFkDLSYKDRHWHEQCFFCHECNTSLVDKpFAARDDDLFCSNCHD 295 Saccoglossus kowalevskii
NP_001004112  37 FANCCEVCSLPIGCNCkDLSYKDRHWHENCFKCAKCSRSLVDKpFAAKDELMLCTECYS 95  zebrafish
Q4R7A4        37 FSNYCEECKKPIESDSkDLCYKDRHWHGGCFKCTKCNHSLVEKpFAAKDERLLCTECYS 95  crab-eating macaque
CAG10299      36 FSNQCEVCQLLISCTSkDLSYKERHWHSECFLCVKCSRSLVERpFATKDDMLMCVECYS 94  spotted green pufferfish

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