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Protein

Programmed cell death activator egl-1

Gene

egl-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a major role in programmed cell death (PCD or apoptosis) by negatively regulating ced-9. Binds to and directly inhibits the activity of ced-9, releasing the cell death activator ced-4 from a ced-9/ced-4 containing protein complex and allowing ced-4 to activate the cell-killing caspase ced-3.3 Publications

GO - Biological processi

  • apoptotic mitochondrial changes Source: WormBase
  • apoptotic process involved in development Source: UniProtKB
  • negative regulation of protein binding Source: WormBase
  • oviposition Source: WormBase
  • positive regulation of apoptotic process Source: WormBase
  • positive regulation of programmed cell death Source: WormBase
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
Programmed cell death activator egl-1
Alternative name(s):
Egg-laying defective protein 1
Gene namesi
Name:egl-1Imported
ORF Names:F23B12.9
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome V

Organism-specific databases

WormBaseiF23B12.9; CE35714; WBGene00001170; egl-1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: WormBase
  • intracellular membrane-bounded organelle Source: WormBase
  • mitochondrion Source: WormBase
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Mutants block programmed cell death.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 106106Programmed cell death activator egl-1PRO_0000086944Add
BLAST

Proteomic databases

PaxDbiO61667.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ced-9P419586EBI-495949,EBI-494110

Protein-protein interaction databases

BioGridi44947. 1 interaction.
IntActiO61667. 1 interaction.
MINTiMINT-1535277.
STRINGi6239.F23B12.9.

Structurei

Secondary structure

1
106
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi65 – 8420Combined sources
Helixi85 – 873Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TY4X-ray2.20C/D46-102[»]
ProteinModelPortaliO61667.
SMRiO61667. Positions 63-91.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO61667.

Family & Domainsi

Phylogenomic databases

eggNOGiENOG410K9GF. Eukaryota.
ENOG4110JBC. LUCA.
HOGENOMiHOG000017551.
InParanoidiO61667.
KOiK20104.
OMAiDAEMMSY.
OrthoDBiEOG7P2Z19.

Family and domain databases

InterProiIPR021543. EGL-1.
[Graphical view]
PfamiPF11430. EGL-1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O61667-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLMLTFASTS SDLLPMSNVF DVQSSVFYNE KNMFYSSSQD FSSCEDSSQF
60 70 80 90 100
ADDSGFFDDS EISSIGYEIG SKLAAMCDDF DAQMMSYSAH ASDRSLFHRL

LDFFAF
Length:106
Mass (Da):11,916
Last modified:March 29, 2005 - v2
Checksum:i2329D2DB0F019636
GO

Sequence cautioni

The sequence AAC39023.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF057309 mRNA. Translation: AAC39023.1. Different initiation.
Z77659 Genomic DNA. Translation: CAB82213.2.
PIRiT43032.
RefSeqiNP_506575.2. NM_074174.3.
UniGeneiCel.19641.

Genome annotation databases

EnsemblMetazoaiF23B12.9; F23B12.9; WBGene00001170.
GeneIDi179943.
KEGGicel:CELE_F23B12.9.
UCSCiF23B12.9. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF057309 mRNA. Translation: AAC39023.1. Different initiation.
Z77659 Genomic DNA. Translation: CAB82213.2.
PIRiT43032.
RefSeqiNP_506575.2. NM_074174.3.
UniGeneiCel.19641.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TY4X-ray2.20C/D46-102[»]
ProteinModelPortaliO61667.
SMRiO61667. Positions 63-91.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi44947. 1 interaction.
IntActiO61667. 1 interaction.
MINTiMINT-1535277.
STRINGi6239.F23B12.9.

Proteomic databases

PaxDbiO61667.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF23B12.9; F23B12.9; WBGene00001170.
GeneIDi179943.
KEGGicel:CELE_F23B12.9.
UCSCiF23B12.9. c. elegans.

Organism-specific databases

CTDi179943.
WormBaseiF23B12.9; CE35714; WBGene00001170; egl-1.

Phylogenomic databases

eggNOGiENOG410K9GF. Eukaryota.
ENOG4110JBC. LUCA.
HOGENOMiHOG000017551.
InParanoidiO61667.
KOiK20104.
OMAiDAEMMSY.
OrthoDBiEOG7P2Z19.

Miscellaneous databases

EvolutionaryTraceiO61667.
PROiO61667.

Family and domain databases

InterProiIPR021543. EGL-1.
[Graphical view]
PfamiPF11430. EGL-1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9."
    Conradt B., Horvitz H.R.
    Cell 93:519-529(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CED-9, DISRUPTION PHENOTYPE.
    Strain: Bristol N2Imported.
  2. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2Imported.
  3. "Translocation of C. elegans CED-4 to nuclear membranes during programmed cell death."
    Chen F., Hersh B.M., Conradt B., Zhou Z., Riemer D., Gruenbaum Y., Horvitz H.R.
    Science 287:1485-1489(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Structural, biochemical, and functional analyses of CED-9 recognition by the proapoptotic proteins EGL-1 and CED-4."
    Yan N., Gu L., Kokel D., Chai J., Li W., Han A., Chen L., Xue D., Shi Y.
    Mol. Cell 15:999-1006(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 46-102 IN COMPLEX WITH CED-9, FUNCTION, INTERACTION WITH CED-9.

Entry informationi

Entry nameiEGL1_CAEEL
AccessioniPrimary (citable) accession number: O61667
Secondary accession number(s): Q7JLC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: June 8, 2016
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.