10         20         30         40         50         60
         |          |          |          |          |          |
MPNWGGGNKC GACGRTVYHA EEVQCDGRSF HRCCFLCMVC RKNLDSTTVA IHDAEVYCKS - 60
CYGKKYGPKG YGYGQGAGTL NMDRGERLGI KPESSPSPHR PTTNPNTSKF AQKFGGAEKC - 120
SRCGDSVYAA EKVIGAGKPW HKNCFRCAKC GKSLESTTLT EKEGEIYCKG CYAKNFGPKG - 180
FGYGQGAGAL VHAQ

The cysteine- and glycine-rich CRP proteins are encoded by a gene family that includes three related but distinct members: the CSRP1 gene originally identified in human (2), the CSRP2 gene first isolated from quail (3), and the CSRP3 gene originally cloned from rat and chicken (4). The CRP1, CRP2, and CRP3 proteins contain 192–194 amino acid residues, display overall amino acid sequence identities ranging from 63 to 79%, and share identical domain topologies. They contain two LIM motifs in their amino acid sequences, an amino-terminal LIM1 domain, and a carboxyl-terminal LIM2 domain, each followed by a 12-amino acid glycine-rich repeat. The LIM motif occurs in single or multiple copies in many proteins of diverse regulatory functions and is defined by two cysteine-rich zinc finger structures separated by a 2-amino acid spacer. The CSRP genes and their protein products play a key role in regulatory processes linked to cell growth and differentiation. Interacts with zyxin. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression. Totally down-regulated in transformed cells.