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P02528 (CRGE_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Gamma-crystallin E
Alternative name(s):
Gamma-2
Gamma-E-crystallin
Gamma-crystallin 3-1
Gene names
Name:Cryge
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length174 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Crystallins are the dominant structural components of the vertebrate eye lens.

Domain

Has a two-domain beta-structure, folded into four very similar Greek key motifs.

Miscellaneous

There are six different gamma crystallins identified in rat lens.

Sequence similarities

Belongs to the beta/gamma-crystallin family.

Contains 4 beta/gamma crystallin 'Greek key' domains.

Ontologies

Keywords
   DomainRepeat
   Molecular functionEye lens protein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processlens development in camera-type eye

Inferred from expression pattern. Source: RGD

   Molecular functionstructural constituent of eye lens

Traceable author statement Ref.3. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 174173Gamma-crystallin E
PRO_0000057593

Regions

Domain2 – 4039Beta/gamma crystallin 'Greek key' 1
Domain41 – 8343Beta/gamma crystallin 'Greek key' 2
Domain88 – 12841Beta/gamma crystallin 'Greek key' 3
Domain129 – 17143Beta/gamma crystallin 'Greek key' 4
Region84 – 874Connecting peptide

Secondary structure

1 .................................... 174
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02528 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 8DF9A2A101232BE2

FASTA17421,264
        10         20         30         40         50         60 
MGKITFYEDR GFQGRHYECS TDHSNLQPYF SRCNSVRVDS GCWMLYEQPN FTGCQYFLRR 

        70         80         90        100        110        120 
GDYPDYQQWM GFSDSVRSCR LIPHSSSHRI RIYEREDYRG QMVEITDDCP HLQDRFHFSD 

       130        140        150        160        170 
FHSFHVMEGY WVLYEMPNYR GRQYLLRPGE YRRYHDWGAM NARVGSLRRI MDFY

« Hide

References

[1]"Extensive intragenic sequence homology in two distinct rat lens gamma-crystallin cDNAs suggests duplications of a primordial gene."
Moormann R.J.M., den Dunnen J.T., Bloemendal H., Schoenmakers J.G.G.
Proc. Natl. Acad. Sci. U.S.A. 79:6876-6880(1982) [PubMed: 6294661] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Nucleotide sequence of the rat gamma-crystallin gene region and comparison with an orthologous human region."
den Dunnen J.T., van Neck J.W., Cremers F.P.M., Lubsen N.H., Schoenmakers J.G.G.
Gene 78:201-213(1989) [PubMed: 2777080] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Strict co-linearity of genetic and protein folding domains in an intragenically duplicated rat lens gamma-crystallin gene."
Moormann R.J.M., den Dunnen J.T., Mulleners L., Andreoli P., Bloemendal H., Schoenmakers J.G.G.
J. Mol. Biol. 171:353-368(1983) [PubMed: 6319707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Towards a molecular understanding of phase separation in the lens: a comparison of the X-ray structures of two high Tc gamma-crystallins, gammaE and gammaF, with two low Tc gamma-crystallins, gammaB and gammaD."
Norledge B.V., Hay R.E., Bateman O.A., Slingsby C., Driessen H.P.C.
Exp. Eye Res. 65:609-630(1997) [PubMed: 9367641] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Tissue: Lens.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M19359 Genomic DNA. Translation: AAA40985.1.
J00716 mRNA. Translation: AAA40987.1.
X00271 Genomic DNA. Translation: CAA25073.1.
IPIIPI00189745.
PIRCYRTG1. A02930.
I49617.
I56381.
RefSeqNP_775411.1. NM_173289.1.
UniGeneRn.44578.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A5DX-ray2.30A/B2-174[»]
1ZGTX-ray1.45A2-173[»]
1ZIEX-ray1.44A2-173[»]
1ZIQX-ray1.72A2-173[»]
1ZIRX-ray1.36A2-173[»]
ProteinModelPortalP02528.
SMRP02528. Positions 2-174.
ModBaseSearch...

Protein-protein interaction databases

STRINGP02528.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000019963; ENSRNOP00000019963; ENSRNOG00000014790.
GeneID24279.
KEGGrno:24279.
UCSCNM_173289. rat.

Organism-specific databases

CTD12968.
RGD2423. Cryge.

Phylogenomic databases

eggNOGroNOG12856.
GeneTreeENSGT00560000076658.
HOVERGENHBG003364.
InParanoidP02528.
OMAHRLRIYE.
OrthoDBEOG4SQWZP.
PhylomeDBP02528.

Gene expression databases

GenevestigatorP02528.
GermOnlineENSRNOG00000014790. Rattus norvegicus.

Family and domain databases

InterProIPR001064. Beta/gamma_crystallin.
IPR011024. G_crystallin-rel.
[Graphical view]
Gene3DG3DSA:2.60.20.10. Crystallin. 2 hits.
PfamPF00030. Crystall. 2 hits.
[Graphical view]
PRINTSPR01367. BGCRYSTALLIN.
SMARTSM00247. XTALbg. 2 hits.
[Graphical view]
SUPFAMSSF49695. G_crystallin_SF. 1 hit.
PROSITEPS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio602860.

Entry information

Entry nameCRGE_RAT
AccessionPrimary (citable) accession number: P02528
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: September 21, 2011
This is version 102 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

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