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Q05158 (CSRP2_COTJA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cysteine and glycine-rich protein 2
Alternative name(s):
Cysteine-rich protein 2
Short name=CRP2
Gene names
Name:CSRP2
OrganismCoturnix coturnix japonica (Japanese quail) (Coturnix japonica)
Taxonomic identifier93934 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePerdicinaeCoturnix

Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Nucleus.

Sequence similarities

Contains 2 LIM zinc-binding domains.

Ontologies

Keywords
   Biological processDifferentiation
   Cellular componentNucleus
   DomainLIM domain
Repeat
   LigandMetal-binding
Zinc
   Molecular functionDevelopmental protein
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processcell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

multicellular organismal development

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionzinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 194193Cysteine and glycine-rich protein 2
PRO_0000075725

Regions

Domain10 – 6152LIM zinc-binding 1
Domain120 – 17152LIM zinc-binding 2
Motif64 – 696Nuclear localization signal Potential
Compositional bias63 – 7816Gly-rich
Compositional bias177 – 18812Gly-rich

Secondary structure

................................. 194
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q05158 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: D59CA624D1C1269E

FASTA19420,911
        10         20         30         40         50         60 
MPNWGGGNKC GACGRTVYHA EEVQCDGRSF HRCCFLCMVC RKNLDSTTVA IHDAEVYCKS 

        70         80         90        100        110        120 
CYGKKYGPKG YGYGQGAGTL NMDRGERLGI KPESSPSPHR PTTNPNTSKF AQKFGGAEKC 

       130        140        150        160        170        180 
SRCGDSVYAA EKVIGAGKPW HKNCFRCAKC GKSLESTTLT EKEGEIYCKG CYAKNFGPKG 

       190 
FGYGQGAGAL VHAQ 

« Hide

References

[1]"Suppression in transformed avian fibroblasts of a gene (crp) encoding a cysteine-rich protein containing LIM domains."
Weiskirchen R., Bister K.
Oncogene 8:2317-2324(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Embryonic fibroblast.
[2]"Structure and intramodular dynamics of the amino-terminal LIM domain from quail cysteine- and glycine-rich protein CRP2."
Kontaxis G., Konrat R., Kraeutler B., Weiskirchen R., Bister K.
Biochemistry 37:7127-7134(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 8-67.
[3]"Solution structure of the carboxyl-terminal LIM domain from quail cysteine-rich protein CRP2."
Konrat R., Weiskirchen R., Krautler B., Bister K.
J. Biol. Chem. 272:12001-12007(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 117-175.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z21643 mRNA. Translation: CAA79759.1.
PIRS41761.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A7INMR-A1-81[»]
1CXXNMR-A82-194[»]
1IBINMR-A82-193[»]
1QLINMR-A82-194[»]
DisProtDP00438.
ProteinModelPortalQ05158.
SMRQ05158. Positions 1-194.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG051143.

Family and domain databases

Gene3D2.10.110.10. 2 hits.
InterProIPR001781. Znf_LIM.
[Graphical view]
PfamPF00412. LIM. 2 hits.
[Graphical view]
SMARTSM00132. LIM. 2 hits.
[Graphical view]
PROSITEPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ05158.

Entry information

Entry nameCSRP2_COTJA
AccessionPrimary (citable) accession number: Q05158
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families