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Protein

Gamma-crystallin E

Gene

Cryge

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  • structural constituent of eye lens Source: RGD

GO - Biological processi

  • lens development in camera-type eye Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Eye lens protein

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-crystallin E
Alternative name(s):
Gamma-2
Gamma-E-crystallin
Gamma-crystallin 3-1
Gene namesi
Name:Cryge
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2423. Cryge.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 174174Gamma-crystallin EPRO_0000057593Add
BLAST

Proteomic databases

PaxDbiP02528.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000045818.

Structurei

Secondary structure

1
174
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97Combined sources
Helixi10 – 123Combined sources
Beta strandi13 – 197Combined sources
Turni27 – 293Combined sources
Beta strandi34 – 4815Combined sources
Turni49 – 513Combined sources
Beta strandi52 – 587Combined sources
Beta strandi60 – 656Combined sources
Helixi66 – 694Combined sources
Beta strandi72 – 743Combined sources
Beta strandi78 – 825Combined sources
Beta strandi89 – 957Combined sources
Helixi96 – 983Combined sources
Beta strandi99 – 1079Combined sources
Helixi112 – 1154Combined sources
Beta strandi123 – 1297Combined sources
Beta strandi131 – 1366Combined sources
Turni137 – 1393Combined sources
Beta strandi140 – 1467Combined sources
Beta strandi148 – 1514Combined sources
Helixi154 – 1574Combined sources
Beta strandi166 – 1694Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A5DX-ray2.30A/B2-174[»]
1ZGTX-ray1.45A2-174[»]
1ZIEX-ray1.44A2-174[»]
1ZIQX-ray1.72A2-174[»]
1ZIRX-ray1.36A2-174[»]
ProteinModelPortaliP02528.
SMRiP02528. Positions 2-174.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02528.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 4039Beta/gamma crystallin 'Greek key' 1PROSITE-ProRule annotationAdd
BLAST
Domaini41 – 8343Beta/gamma crystallin 'Greek key' 2PROSITE-ProRule annotationAdd
BLAST
Domaini88 – 12841Beta/gamma crystallin 'Greek key' 3PROSITE-ProRule annotationAdd
BLAST
Domaini129 – 17143Beta/gamma crystallin 'Greek key' 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni84 – 874Connecting peptide

Domaini

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

Sequence similaritiesi

Belongs to the beta/gamma-crystallin family.Curated
Contains 4 beta/gamma crystallin 'Greek key' domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IWCR. Eukaryota.
ENOG411298R. LUCA.
HOGENOMiHOG000234389.
HOVERGENiHBG003364.
InParanoidiP02528.
PhylomeDBiP02528.

Family and domain databases

InterProiIPR001064. Beta/gamma_crystallin.
IPR011024. G_crystallin-rel.
[Graphical view]
PfamiPF00030. Crystall. 2 hits.
[Graphical view]
PRINTSiPR01367. BGCRYSTALLIN.
SMARTiSM00247. XTALbg. 2 hits.
[Graphical view]
SUPFAMiSSF49695. SSF49695. 1 hit.
PROSITEiPS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P02528-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKITFYEDR GFQGRHYECS TDHSNLQPYF SRCNSVRVDS GCWMLYEQPN
60 70 80 90 100
FTGCQYFLRR GDYPDYQQWM GFSDSVRSCR LIPHSSSHRI RIYEREDYRG
110 120 130 140 150
QMVEITDDCP HLQDRFHFSD FHSFHVMEGY WVLYEMPNYR GRQYLLRPGE
160 170
YRRYHDWGAM NARVGSLRRI MDFY
Length:174
Mass (Da):21,264
Last modified:January 23, 2007 - v2
Checksum:i8DF9A2A101232BE2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19359 Genomic DNA. Translation: AAA40985.1.
J00716 mRNA. Translation: AAA40987.1.
X00271 Genomic DNA. Translation: CAA25073.1.
PIRiA02930. CYRTG1.
I49617.
I56381.
RefSeqiNP_775411.1. NM_173289.1.
UniGeneiRn.44578.

Genome annotation databases

GeneIDi24279.
KEGGirno:24279.
UCSCiRGD:2423. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19359 Genomic DNA. Translation: AAA40985.1.
J00716 mRNA. Translation: AAA40987.1.
X00271 Genomic DNA. Translation: CAA25073.1.
PIRiA02930. CYRTG1.
I49617.
I56381.
RefSeqiNP_775411.1. NM_173289.1.
UniGeneiRn.44578.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A5DX-ray2.30A/B2-174[»]
1ZGTX-ray1.45A2-174[»]
1ZIEX-ray1.44A2-174[»]
1ZIQX-ray1.72A2-174[»]
1ZIRX-ray1.36A2-174[»]
ProteinModelPortaliP02528.
SMRiP02528. Positions 2-174.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000045818.

Proteomic databases

PaxDbiP02528.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24279.
KEGGirno:24279.
UCSCiRGD:2423. rat.

Organism-specific databases

CTDi12968.
RGDi2423. Cryge.

Phylogenomic databases

eggNOGiENOG410IWCR. Eukaryota.
ENOG411298R. LUCA.
HOGENOMiHOG000234389.
HOVERGENiHBG003364.
InParanoidiP02528.
PhylomeDBiP02528.

Miscellaneous databases

EvolutionaryTraceiP02528.
PROiP02528.

Family and domain databases

InterProiIPR001064. Beta/gamma_crystallin.
IPR011024. G_crystallin-rel.
[Graphical view]
PfamiPF00030. Crystall. 2 hits.
[Graphical view]
PRINTSiPR01367. BGCRYSTALLIN.
SMARTiSM00247. XTALbg. 2 hits.
[Graphical view]
SUPFAMiSSF49695. SSF49695. 1 hit.
PROSITEiPS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    Tissue: Lens.

Entry informationi

Entry nameiCRGE_RAT
AccessioniPrimary (citable) accession number: P02528
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

There are six different gamma crystallins identified in rat lens.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.