MGSSHHHHHH SSGLVPRGSH MGSMSESFDC AKCNESLYGR KYIQTDSGPY CVPCYDNTFA NTCAECQQLI GHDSRELFYE DRHFHEGCFR CCRCQRSLAD EPFTCQDSEL LCNDCYCSAF SSQCSACGET VMPGSRKLEY GGQTWHEHCF LCSGCEQPLG SRSFVPDKGA HYCVPCYENK FAPRCARCSK TLTQGGVTYR DQPWHRECLV CTGCQTPLAG QQFTSRDEDP YCVACFGELF APKCSSCKRP IVGLGGGKYV SFEDRHWHHN CFSCARCSTS LVGQGFVPDG DQVLCQGCSQ AGP.
The FHL3 protein contains four complete LIM domains and an additional half LIM domain at the N-terminus. These LIM domains are crucial for protein-protein interactions and play significant roles in various cellular processes . The LIM domains are composed of two tandemly repeated zinc fingers, each binding a zinc atom through conserved cysteine residues .
FHL3 is involved in several biological functions, including:
FHL3 has been implicated in several diseases, particularly in cancer. Its expression levels can vary significantly in different types of cancers, where it may either suppress tumor growth or promote tumor progression . This dual role makes FHL3 a potential target for cancer therapy, as modulating its activity could influence cancer outcomes .
Recombinant FHL3 proteins are used in research to study its function and interactions. These studies help in understanding the molecular mechanisms underlying its role in various cellular processes and diseases. The recombinant form of FHL3 is particularly valuable for in vitro experiments, allowing researchers to investigate its properties in a controlled environment.