[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), FUNCTION, AND DEVELOPMENTAL STAGE. PubMed=1286611 [NCBI, ExPASy, EBI, Israel, Japan] Yuan J., Horvitz H.R.; "The Caenorhabditis elegans cell death gene ced-4 encodes a novel protein and is expressed during the period of extensive programmed cell death."; Development 116:309-320(1992).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Bristol N2; DOI=10.1126/science.282.5396.2012; PubMed=9851916 [NCBI, ExPASy, EBI, Israel, Japan] The C. elegans sequencing consortium; "Genome sequence of the nematode C. elegans: a platform for investigating biology."; Science 282:2012-2018(1998).
[3]	FUNCTION, AND ALTERNATIVE SPLICING. DOI=10.1016/S0092-8674(00)80092-6; PubMed=8706125 [NCBI, ExPASy, EBI, Israel, Japan] Shaham S., Horvitz H.R.; "An alternatively spliced C. elegans ced-4 RNA encodes a novel cell death inhibitor."; Cell 86:201-208(1996).
[4]	FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CED-9. DOI=10.1126/science.275.5303.1126; PubMed=9027313 [NCBI, ExPASy, EBI, Israel, Japan] Wu D., Wallen H.D., Nunez G.; "Interaction and regulation of subcellular localization of CED-4 by CED-9."; Science 275:1126-1129(1997).
[5]	FUNCTION, AND SUBCELLULAR LOCATION. DOI=10.1126/science.287.5457.1485; PubMed=10688797 [NCBI, ExPASy, EBI, Israel, Japan] Chen F., Hersh B.M., Conradt B., Zhou Z., Riemer D., Gruenbaum Y., Horvitz H.R.; "Translocation of C. elegans CED-4 to nuclear membranes during programmed cell death."; Science 287:1485-1489(2000).
[6]	FUNCTION, AND INTERACTION WITH CED-9. DOI=10.1016/j.molcel.2004.08.022; PubMed=15383288 [NCBI, ExPASy, EBI, Israel, Japan] Yan N., Gu L., Kokel D., Chai J., Li W., Han A., Chen L., Xue D., Shi Y.; "Structural, biochemical, and functional analyses of CED-9 recognition by the proapoptotic proteins EGL-1 and CED-4."; Mol. Cell 15:999-1006(2004).

Comments

FUNCTION: Isoform a 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. Isoform b prevents PCD.
SUBUNIT: Interacts with ced-9.
INTERACTION:
Q07817:BCL2L1 (xeno); NbExp=2; IntAct=EBI-494118, EBI-78035;
Q14790:CASP8 (xeno); NbExp=1; IntAct=EBI-494118, EBI-78060;
P42573:ced-3; NbExp=3; IntAct=EBI-536271, EBI-494247;
P42573:ced-3; NbExp=3; IntAct=EBI-494118, EBI-494247;
P41958:ced-9; NbExp=7; IntAct=EBI-494118, EBI-494110;
SUBCELLULAR LOCATION: Mitochondrion. Note=In non cell death induced cells. Ced-9 is required for mitochondrial localization. Perinuclear in cell death induced cells.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	b
Synonyms	Long
Isoform ID	P30429-1
Note: Minor transcript.
This is the isoform sequence displayed in this entry.

Name	a
Synonyms	Short
Isoform ID	P30429-2
Note: Major transcript.
Features which should be applied to build the isoform sequence: VSP_013199.

DEVELOPMENTAL STAGE: Most abundant during embryogenesis and is also detected at later stages during periods of extensive programmed cell death.
MISCELLANEOUS: Mutants exhibit a block in almost all programmed cell deaths that normally occur during development.
SIMILARITY: Contains 1 CARD domain.
SIMILARITY: Contains 1 NB-ARC domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X69016; CAA48781.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U21324; AAA62564.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U21324; AAX22294.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S72566; S72566.

NP_001021203.1; -.

3D structure databases

PDB

2A5Y; X-ray; 2.60 A; B=1-571.

[ExPASy / RCSB / EBI]

PDBsum

2A5Y; -.

ModBase

P30429.

Protein-protein interaction databases

DIP

DIP:1016N; -.

IntAct

P30429; -.

Organism-specific databases

WormBase

WBGene00000418; ced-4.

WormPep

C35D10.9a; CE01203. [WormPep / WorfDB]
C35D10.9b; CE38154. [WormPep / WorfDB]

Gene expression databases

ArrayExpress

P30429; -.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0042981;	Biological process: regulation of apoptosis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR016854; Apop_reg_Ced-4.
IPR001315; CARD.
IPR002182; NB-ARC.
Graphical view of domain structure.

Pfam

PF00619; CARD; 1.
PF00931; NB-ARC; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF027202; Apop_reg_Ced-4; 1.

SMART

SM00114; CARD; 1.
SMART graphical view of domain structure.

PROSITE

PS50209; CARD; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P30429.

Genome annotation databases

Ensembl

C35D10.9; Caenorhabditis elegans. [Contig view]

GeneID

175643; -.

Other

NextBio

889028; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Apoptosis; ATP-binding; Complete proteome; Mitochondrion; Nucleotide-binding.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 571`	`571`	`Cell death protein 4.`	`PRO_0000089470`
`DOMAIN`	`1 91`	`91`	`CARD.`
`DOMAIN`	`116 440`	`325`	`NB-ARC.`
`NP_BIND`	`159 166`	`8`	`ATP (Potential).`
`VAR_SEQ`	`212 234`		`ARVVSDTDDSHSITDFINRVLSR -> K (in isoform a).`	`VSP_013199`
`HELIX`	`4 20`	`17`
`HELIX`	`23 26`	`4`
`HELIX`	`27 32`	`6`
`HELIX`	`38 45`	`8`
`STRAND`	`47 49`	`3`
`HELIX`	`50 64`	`15`
`STRAND`	`66 68`	`3`
`HELIX`	`69 77`	`9`
`HELIX`	`81 96`	`16`
`HELIX`	`101 104`	`4`
`TURN`	`105 108`	`4`
`HELIX`	`112 121`	`10`
`HELIX`	`134 147`	`14`
`STRAND`	`150 158`	`9`
`HELIX`	`165 175`	`11`
`TURN`	`181 183`	`3`
`STRAND`	`184 191`	`8`
`HELIX`	`199 211`	`13`
`TURN`	`234 236`	`3`
`HELIX`	`250 261`	`12`
`STRAND`	`267 274`	`8`
`HELIX`	`277 285`	`9`
`STRAND`	`289 296`	`8`
`HELIX`	`297 302`	`6`
`STRAND`	`307 311`	`5`
`HELIX`	`317 326`	`10`
`HELIX`	`336 348`	`13`
`HELIX`	`352 359`	`8`
`STRAND`	`364 366`	`3`
`HELIX`	`367 380`	`14`
`STRAND`	`389 395`	`7`
`HELIX`	`396 405`	`10`
`HELIX`	`409 414`	`6`
`HELIX`	`417 419`	`3`
`HELIX`	`429 435`	`7`
`HELIX`	`450 458`	`9`
`TURN`	`459 461`	`3`
`STRAND`	`462 464`	`3`
`STRAND`	`466 469`	`4`
`STRAND`	`471 473`	`3`
`STRAND`	`475 477`	`3`
`HELIX`	`480 487`	`8`
`HELIX`	`493 499`	`7`
`TURN`	`503 505`	`3`
`HELIX`	`559 562`	`4`

Sequence information

Length: 571 AA [This is the length of the unprocessed precursor]

Molecular weight: 65336 Da [This is the MW of the unprocessed precursor]

CRC64: 6BE9893946B79E6C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLCEIECRAL STAHTRLIHD FEPRDALTYL EGKNIFTEDH SELISKMSTR LERIANFLRI 

        70         80         90        100        110        120 
YRRQASELGP LIDFFNYNNQ SHLADFLEDY IDFAINEPDL LRPVVIAPQF SRQMLDRKLL 

       130        140        150        160        170        180 
LGNVPKQMTC YIREYHVDRV IKKLDEMCDL DSFFLFLHGR AGSGKSVIAS QALSKSDQLI 

       190        200        210        220        230        240 
GINYDSIVWL KDSGTAPKST FDLFTDILLM LARVVSDTDD SHSITDFINR VLSRSEDDLL 

       250        260        270        280        290        300 
NFPSVEHVTS VVLKRMICNA LIDRPNTLFV FDDVVQEETI RWAQELRLRC LVTTRDVEIS 

       310        320        330        340        350        360 
NAASQTCEFI EVTSLEIDEC YDFLEAYGMP MPVGEKEEDV LNKTIELSSG NPATLMMFFK 

       370        380        390        400        410        420 
SCEPKTFEKM AQLNNKLESR GLVGVECITP YSYKSLAMAL QRCVEVLSDE DRSALAFAVV 

       430        440        450        460        470        480 
MPPGVDIPVK LWSCVIPVDI CSNEEEQLDD EVADRLKRLS KRGALLSGKR MPVLTFKIDH 

       490        500        510        520        530        540 
IIHMFLKHVV DAQTIANGIS ILEQRLLEIG NNNVSVPERH IPSHFQKFRR SSASEMYPKT 

       550        560        570 
TEETVIRPED FPKFMQLHQK FYDSLKNFAC C

P30429 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools