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Protein

Apoptosis regulator ced-9

Gene

ced-9

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, apoptosis) (PubMed:7907274, PubMed:10688797). egl-1 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 (PubMed:9024666, PubMed:9027313, PubMed:9604928, PubMed:12894216, PubMed:15383288, PubMed:16208361). During larval development, required for the elimination of transient presynaptic components downstream of egl-1 and upstream of ced-4 and ced-3 apoptotic pathway (PubMed:26074078).7 Publications

GO - Molecular functioni

GO - Biological processi

  • actin filament depolymerization Source: UniProtKB
  • apoptotic process involved in development Source: UniProtKB
  • extrinsic apoptotic signaling pathway in absence of ligand Source: GO_Central
  • intrinsic apoptotic signaling pathway in response to DNA damage Source: GO_Central
  • mitophagy Source: WormBase
  • negative regulation of apoptotic process Source: WormBase
  • negative regulation of programmed cell death Source: WormBase
  • positive regulation of brood size Source: UniProtKB
  • positive regulation of embryonic development Source: UniProtKB
  • positive regulation of fertilization Source: UniProtKB
  • positive regulation of mitochondrial fusion Source: WormBase
  • positive regulation of oviposition Source: UniProtKB
  • positive regulation of synapse disassembly Source: UniProtKB
  • protein processing Source: UniProtKB

Keywordsi

Biological processApoptosis

Protein family/group databases

TCDBi1.A.21.2.1. the bcl-2 (bcl-2) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Apoptosis regulator ced-9
Alternative name(s):
Cell death protein 9
Gene namesi
Name:ced-9
ORF Names:T07C4.8
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiT07C4.8; CE25104; WBGene00000423; ced-9.

Subcellular locationi

GO - Cellular componenti

  • endomembrane system Source: UniProtKB-SubCell
  • membrane Source: WormBase
  • mitochondrial outer membrane Source: WormBase
  • mitochondrion Source: WormBase
  • neuronal cell body Source: UniProtKB
  • organelle membrane Source: WormBase
  • perinuclear region of cytoplasm Source: WormBase
  • presynapse Source: UniProtKB

Keywords - Cellular componenti

Cell junction, Membrane, Mitochondrion, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi149Y → N in n1653; no effect on the interaction with ced-4. Normal elimination of presynaptic components in RME neurons in adults. 2 Publications1
Mutagenesisi169G → E in n1950; gain of function mutant. No effect on the interaction with ced-4. Impaired elimination of presynaptic components in RME neurons in adults. Abnormal accumulation of F-actin at the non-eliminated transient synapses in DD neuron dorsal cord in L4 larvae. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001430971 – 280Apoptosis regulator ced-9Add BLAST280

Proteomic databases

EPDiP41958.
PaxDbiP41958.
PeptideAtlasiP41958.

PTM databases

iPTMnetiP41958.

Expressioni

Developmental stagei

Abundant expression is seen in embryos and adults.1 Publication

Gene expression databases

BgeeiWBGene00000423.

Interactioni

Subunit structurei

Interacts with asymmetric homodimer ced-4; the interaction sequesters ced-4 (PubMed:9024666, PubMed:9027313, PubMed:15383288, PubMed:16208361). Interacts with egl-1; the interaction results in ced-4 release (PubMed:9604928, PubMed:12894216, PubMed:15383288). Interacts with dre-1; the interaction inhibits ced-9 activity, either directly or indirectly (PubMed:23431138). Interacts with dct-1 (PubMed:11114722). May form a complex composed of ced-9, ced-4 and mac-1 (PubMed:10101135).9 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi533094. 4 interactors.
DIPiDIP-250N.
IntActiP41958. 3 interactors.
MINTiMINT-1526902.
STRINGi6239.T07C4.8.

Structurei

Secondary structure

1280
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi72 – 74Combined sources3
Helixi76 – 78Combined sources3
Helixi80 – 94Combined sources15
Helixi111 – 138Combined sources28
Beta strandi140 – 143Combined sources4
Helixi146 – 153Combined sources8
Turni154 – 157Combined sources4
Beta strandi161 – 163Combined sources3
Helixi168 – 185Combined sources18
Turni189 – 191Combined sources3
Helixi192 – 194Combined sources3
Helixi195 – 211Combined sources17
Helixi214 – 217Combined sources4
Helixi221 – 239Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OHUX-ray2.03A/B68-242[»]
1TY4X-ray2.20A/B68-237[»]
2A5YX-ray2.60A48-251[»]
ProteinModelPortaliP41958.
SMRiP41958.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41958.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi80 – 99BH4PROSITE-ProRule annotationAdd BLAST20
Motifi160 – 179BH1Sequence analysisAdd BLAST20
Motifi213 – 229BH2CuratedAdd BLAST17

Sequence similaritiesi

Belongs to the Bcl-2 family.Curated

Phylogenomic databases

eggNOGiKOG4728. Eukaryota.
ENOG41123S0. LUCA.
HOGENOMiHOG000111534.
InParanoidiP41958.
KOiK20094.
OMAiYVEVVEC.
OrthoDBiEOG091G0QL0.
PhylomeDBiP41958.

Family and domain databases

InterProiView protein in InterPro
IPR002475. Bcl2-like.
IPR020717. Bcl2_BH1_motif_CS.
IPR003093. Bcl2_BH4.
IPR026298. Blc2_fam.
IPR026309. BOK.
PANTHERiPTHR11256. PTHR11256. 1 hit.
PTHR11256:SF53. PTHR11256:SF53. 1 hit.
PfamiView protein in Pfam
PF00452. Bcl-2. 1 hit.
PF02180. BH4. 1 hit.
SMARTiView protein in SMART
SM00265. BH4. 1 hit.
SUPFAMiSSF56854. SSF56854. 1 hit.
PROSITEiView protein in PROSITE
PS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS50063. BH4_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P41958-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRCTADNSL TNPAYRRRTM ATGEMKEFLG IKGTEPTDFG INSDAQDLPS
60 70 80 90 100
PSRQASTRRM SIGESIDGKI NDWEEPRLDI EGFVVDYFTH RIRQNGMEWF
110 120 130 140 150
GAPGLPCGVQ PEHEMMRVMG TIFEKKHAEN FETFCEQLLA VPRISFSLYQ
160 170 180 190 200
DVVRTVGNAQ TDQCPMSYGR LIGLISFGGF VAAKMMESVE LQGQVRNLFV
210 220 230 240 250
YTSLFIKTRI RNNWKEHNRS WDDFMTLGKQ MKEDYERAEA EKVGRRKQNR
260 270 280
RWSMIGAGVT AGAIGIVGVV VCGRMMFSLK
Length:280
Mass (Da):31,824
Last modified:November 1, 1995 - v1
Checksum:i7603675E490DD3EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26545 Genomic DNA. Translation: AAA20080.1.
Z29443 Genomic DNA. Translation: CAA82573.2.
PIRiA53189.
H88578.
RefSeqiNP_499284.1. NM_066883.5.
UniGeneiCel.6305.

Genome annotation databases

EnsemblMetazoaiT07C4.8; T07C4.8; WBGene00000423.
GeneIDi3565776.
KEGGicel:CELE_T07C4.8.
UCSCiT07C4.8.1. c. elegans.

Similar proteinsi

Entry informationi

Entry nameiCED9_CAEEL
AccessioniPrimary (citable) accession number: P41958
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: August 30, 2017
This is version 139 of the entry and version 1 of the sequence. See 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
  3. SIMILARITY comments
    Index of protein domains and families