General information | DisProt: | DP00438 | Name: | Cysteine and glycine-rich protein 2 | Synonym(s): | CSRP2_COTJA
Cysteine-rich protein 2
CRP2
| First appeared in release: | Release 3.0 (02/17/2006) | UniProt: | Q05158 | UniGene: | | SwissProt: | CSRP2_COTJA | TrEMBL: | | NCBI (GI): | 461908 | Source organism: | Coturnix coturnix japonica (Japanese quail) | Sequence length: | 194 | Percent disordered: | 25% | Homologues: | |
Native sequence |
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
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Functional narrative |
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.
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Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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Region 1 | Type: | Disordered | Name: | linker region | Location: | 68 - 115 | Length: | 48 | Region sequence: |
PKGYGYGQGAGTLNMDRGERLGIKPESSPSPHRPTTNPNTSKFAQKFG | Modification type: | Native
| PDB: | | Structural/functional type: | Function arises from the disordered state | Functional classes: | Unknown
| Functional subclasses: | Unknown
| Detection methods:
- Nuclear magnetic resonance (NMR) (299 K; pH: 7.2; 0.7 mM CRP2; 15N NOESY-HSQC; 20 mM potassium phosphate, 50 mM KCl, and 0.5 mM dithiothreitol; 90% H2O, 10% 2H2O; HNCO, HNCACB, CBCA(CO)NH and HCCH-TOCSY; three-dimensional 15N TOCSY-HSQC; two-dimensional 15N HSQC)
| References:
- Konrat R, Krautler B, Weiskirchen R, Bister K. "Structure of cysteine- and glycine-rich protein CRP2. Backbone dynamics reveal motional freedom and independent spatial orientation of the lim domains." J Biol Chem. 1998; 273(36): 23233-40. PubMed: 9722554
| Comments:From the 58-amino acid
linker region between the two autonomously folded LIM domains, approximately
50 central residues are structurally disordered in solution. The length of the flexible linker
region enables the two LIM domains
in the full-length CRP2 protein to sample a substantial conformational
space and allows for a significant variability in the
spatial separation of the two domains. It also provides a means
to display different surfaces of the two LIM domains and hence
differentially adjust the putative interaction site.
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