2D8Z,2CUR,2CUQ


Conserved Protein Domain Family
LIM3_FHL

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cd09346: LIM3_FHL 
Click on image for an interactive view with Cn3D
The third LIM domain of Four and a half LIM domains protein (FHL)
The third 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: 188732
Aligned: 18 rows
Threshold Bit Score: 84.3017
Created: 12-May-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:2CUR_A: Human Four and half LIM domain proteins 1 LIM3 domain binds Zn
    View structure with Cn3D
  • 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        #  #                #  #  #  #                 #  # 
2D8Z_A         8 CVQCKKPITtGGVTYREQPWHKECFVCTACRKQLSGQRFTARDDFAYCLNCF 59  human
2CUR_A         8 CVKCNKAITsGGITYQDQPWHADCFVCVTCSKKLAGQRFTAVEDQYYCVDCY 59  human
XP_001377295  90 CNSCKKPITtGGLIYRERPWHRECFLCNGCKKQLFGEKFVCKDERPYCRDCY 141 gray short-tailed opossum
XP_002336912 111 CEKCRKVISmGGITYKDTPWHKECFVCTHCKKPMSGERFTSKDNNPYCINCY 162 black cottonwood
XP_002590623 168 CAICGKVISmGGITYKDKPYHKECFVCTHCKKQLSGERFTSKDDKPYCINCY 219 Florida lancelet
NP_001167322 162 CSHCKKALAtGGVSYKDETWHKECFVCTGCKIPLAGQPFTSQGDTPYCVKCF 213 Atlantic salmon
AAH61449     162 CAHCKQTLVqGGVTYRDEPWHKECFLCTGCKVQLAGQPFTTQGEDPYCVKCF 213 zebrafish
CAF92647     162 CRHCKKALTkGGVAYREEVWHKECFLCSGCSSPLAGQPFTSQGDTPYCIRCF 213 spotted green pufferfish
XP_001377282 163 CKSCKKPITaEGITYHEQPWHKECFLCTNCNKQLFGERFISKEEQPYCQDCY 214 gray short-tailed opossum
NP_001087877 163 CKSCRKAITkGGISFQEQQWHRECFVCTSCTKNLVGEKSTSRDESPYCVDCF 214 African clawed frog

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