Apoptosis regulator ced-9 - Caenorhabditis elegans

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P41958 (CED9_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 93. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Apoptosis regulator ced-9

Alternative name(s):
Cell death protein 9

Gene names

Name:	ced-9
ORF Names:	T07C4.8

Organism

Caenorhabditis elegans

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	280 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a major role in programmed cell death (PCD, apoptosis). 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. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.8
Subunit structure	Interacts with ced-4 and egl-1. Ref.4 Ref.5 Ref.8
Subcellular location	Endomembrane system; Peripheral membrane protein. Mitochondrion membrane; Peripheral membrane protein. Note: Intracellular membranes, mitochondrial, and perinuclear region. Ref.4 Ref.6
Developmental stage	Abundant expression is seen in the embryos and the adults. Ref.3
Sequence similarities	Belongs to the Bcl-2 family.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Membrane Mitochondrion
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	anti-apoptosis Inferred from mutant phenotype. Source: WormBase apoptotic process Inferred from mutant phenotype. Source: WormBase embryo development ending in birth or egg hatching Inferred from mutant phenotype. Source: WormBase
Cellular component	endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell membrane fraction Inferred from direct assay Ref.4. Source: WormBase mitochondrial outer membrane Inferred from direct assay. Source: WormBase perinuclear region of cytoplasm Inferred from direct assay Ref.4. Source: WormBase
Molecular function	GTPase activator activity Inferred from direct assay. Source: WormBase protein binding Inferred from physical interaction Ref.4. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
ced-3	P42573	2	EBI-494110,EBI-494247
ced-4	P30429	18	EBI-494110,EBI-494118
egl-1	O61667	6	EBI-494110,EBI-495949

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 280

280

Apoptosis regulator ced-9

PRO_0000143097

Regions

Motif

80 – 99

BH4

Motif

160 – 179

BH1

Motif

213 – 229

BH2

Experimental info

Mutagenesis

149

Y → N in N1653; lethal phenotype. Ref.3

Mutagenesis

169

G → E in G169E; gain of function. Ref.3

Secondary structure

280

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P41958 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 7603675E490DD3EB
Show »

FASTA

280

31,824

        10         20         30         40         50         60 
MTRCTADNSL TNPAYRRRTM ATGEMKEFLG IKGTEPTDFG INSDAQDLPS PSRQASTRRM 

        70         80         90        100        110        120 
SIGESIDGKI NDWEEPRLDI EGFVVDYFTH RIRQNGMEWF GAPGLPCGVQ PEHEMMRVMG 

       130        140        150        160        170        180 
TIFEKKHAEN FETFCEQLLA VPRISFSLYQ DVVRTVGNAQ TDQCPMSYGR LIGLISFGGF 

       190        200        210        220        230        240 
VAAKMMESVE LQGQVRNLFV YTSLFIKTRI RNNWKEHNRS WDDFMTLGKQ MKEDYERAEA 

       250        260        270        280 
EKVGRRKQNR RWSMIGAGVT AGAIGIVGVV VCGRMMFSLK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2." Hengartner M.O., Horvitz H.R. Cell 76:665-676(1994) [PubMed: 7907274] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: Bristol N2.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[3]	"Interaction between the C. elegans cell-death regulators CED-9 and CED-4." Spector M.S., Desnoyers S., Hoeppner D.J., Hengartner M.O. Nature 385:653-656(1997) [PubMed: 9024666] [Abstract] Cited for: FUNCTION, DEVELOPMENTAL STAGE, MUTAGENESIS OF TYR-149 AND GLY-169. Strain: Bristol N2.
[4]	"Interaction and regulation of subcellular localization of CED-4 by CED-9." Wu D., Wallen H.D., Nunez G. Science 275:1126-1129(1997) [PubMed: 9027313] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CED-4.
[5]	"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: 9604928] [Abstract] Cited for: FUNCTION, INTERACTION WITH EGL-1.
[6]	"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: 10688797] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]	"Unique structural features of a BCL-2 family protein CED-9 and biophysical characterization of CED-9/EGL-1 interactions." Woo J.-S., Jung J.-S., Ha N.-C., Shin J., Kin K.-H., Lee W., Oh B.-H. Cell Death Differ. 10:1310-1319(2003) [PubMed: 12894216] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 68-242 IN COMPLEX WITH EGL-1.
[8]	"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: 15383288] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 68-237 IN COMPLEX WITH EGL-1, FUNCTION, INTERACTION WITH EGL-1 AND CED-4.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L26545 Genomic DNA. Translation: AAA20080.1.
Z29443 Genomic DNA. Translation: CAA82573.2.

PIR

A53189.
H88578.

RefSeq

NP_499284.1. NM_066883.4.

UniGene

Cel.37555.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OHU	X-ray	2.03	A/B	68-242	[»]
1TY4	X-ray	2.20	A/B	68-237	[»]
2A5Y	X-ray	2.60	A	48-251	[»]

ProteinModelPortal

P41958.

SMR

P41958. Positions 71-269.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-250N.

IntAct

P41958. 3 interactions.

STRING

P41958.

Protein family/group databases

TCDB

1.A.21.2.1. bcl-2 (Bcl-2) family.

Proteomic databases

PRIDE

P41958.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

T07C4.8; T07C4.8; T07C4.8.

GeneID

3565776.

KEGG

cel:T07C4.8.

NMPDR

fig|6239.3.peg.11431.

UCSC

T07C4.8.1. c. elegans.

Organism-specific databases

CTD

3565776.

WormBase

T07C4.8; CE25104; WBGene00000423; ced-9.

Phylogenomic databases

eggNOG

KOG4728.

GeneTree

EMGT00050000015773.

HOGENOM

HBG382823.

InParanoid

P41958.

OMA

LFIKTRI.

Gene expression databases

ArrayExpress

P41958.

Family and domain databases

InterPro

IPR002475. Bcl2-like_apoptosis.
IPR000712. Bcl2_BH.
IPR020717. Bcl2_BH1_motif_CS.
IPR003093. Bcl2_BH4.
[Graphical view]

Pfam

PF00452. Bcl-2. 1 hit.
PF02180. BH4. 1 hit.
[Graphical view]

SMART

SM00337. BCL. 1 hit.
SM00265. BH4. 1 hit.
[Graphical view]

PROSITE

PS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS01258. BH2. False negative.
PS01260. BH4_1. False negative.
PS50063. BH4_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

957817.

Entry information

Entry name

CED9_CAEEL

Accession

Primary (citable) accession number: P41958

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	September 21, 2011
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents