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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)DescriptionActionsGraphical viewLength
ChainiPRO_00000575931 – 174Gamma-crystallin EAdd BLAST174

Proteomic databases

PaxDbiP02528.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000045818.

Structurei

Secondary structure

1174
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Helixi10 – 12Combined sources3
Beta strandi13 – 19Combined sources7
Turni27 – 29Combined sources3
Beta strandi34 – 48Combined sources15
Turni49 – 51Combined sources3
Beta strandi52 – 58Combined sources7
Beta strandi60 – 65Combined sources6
Helixi66 – 69Combined sources4
Beta strandi72 – 74Combined sources3
Beta strandi78 – 82Combined sources5
Beta strandi89 – 95Combined sources7
Helixi96 – 98Combined sources3
Beta strandi99 – 107Combined sources9
Helixi112 – 115Combined sources4
Beta strandi123 – 129Combined sources7
Beta strandi131 – 136Combined sources6
Turni137 – 139Combined sources3
Beta strandi140 – 146Combined sources7
Beta strandi148 – 151Combined sources4
Helixi154 – 157Combined sources4
Beta strandi166 – 169Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02528.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 40Beta/gamma crystallin 'Greek key' 1PROSITE-ProRule annotationAdd BLAST39
Domaini41 – 83Beta/gamma crystallin 'Greek key' 2PROSITE-ProRule annotationAdd BLAST43
Domaini88 – 128Beta/gamma crystallin 'Greek key' 3PROSITE-ProRule annotationAdd BLAST41
Domaini129 – 171Beta/gamma crystallin 'Greek key' 4PROSITE-ProRule annotationAdd BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni84 – 87Connecting peptide4

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
PDB 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.
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...

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: November 2, 2016
This is version 135 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.