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Q9XWD6 (CED1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cell death abnormality protein 1
Gene names
Name:ced-1
ORF Names:Y47H9C.4
OrganismCaenorhabditis elegans
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length1111 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in programmed cell death/apoptosis. Acts by recruiting ced-6 to phagosomes which enables actin-dependent cytoskeletal reorganization and subsequent engulfment of the apoptotic cell corpse. Has a role in the association of ppk-3 and rab-7 with the phagosomal surface which is necessary for the incorporation of lysosomes to phagosomes during phagosome maturation. Activates the expression of unfolded protein response genes, which are involved in the immune response to live bacteria. Ref.1 Ref.3 Ref.4 Ref.5 Ref.7 Ref.8 Ref.10 Ref.11

Subunit structure

Interacts (via C-terminus) with ced-6 (via PTB domain). Ref.5

Subcellular location

Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle › phagosome membrane; Single-pass type I membrane protein. Note: Colocalizes with ced-6 and actin halos around early apoptotic cells. Temporally colocalizes with dyn-1 during engulfment of cell corpses. Ref.1

Tissue specificity

Expressed in engulfing cells and syncytium hypodermal cells. Ced-7 is necessary for clustering around cell corpses prior to engulfment. Ref.1

Domain

NPXY motif thought to be involved in signal transduction that activates the cell corpse internalization process. Ref.1

Post-translational modification

Phosphorylation of Tyr-1019, within the YXXL motif, is thought to initiate phagosomal formation. Ref.1

Disruption phenotype

Accumulation of cell corpses. Appears immunocompromised resulting in susceptibility to bacterial infection. Reduced or lack of association of ppk-3 and rab-7 with the phagosomal surface. Defective in the recruitment of lysosomes to phagosomes. Ref.3 Ref.4 Ref.5 Ref.8 Ref.10 Ref.11

Sequence similarities

Contains 6 EGF-like domains.

Contains 1 EMI domain.

Contains 1 FU (furin-like) repeat.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform a Ref.1 Ref.2 (identifier: Q9XWD6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform b Ref.2 (identifier: Q9XWD6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1042-1082: Missing.
Note: No experimental confirmation available.
Isoform c Ref.2 (identifier: Q9XWD6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1017-1082: Missing.
     1083-1083: E → K
Note: No experimental confirmation available.
Isoform d Ref.2 (identifier: Q9XWD6-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: MRLILLVLLA...QGDHVCTVKT → MCVPRDIGSR...PKFEFSYIFF
     50-1111: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 11111093Cell death abnormality protein 1
PRO_0000379932

Regions

Topological domain19 – 910892Extracellular Potential
Transmembrane911 – 93121Helical; Potential
Topological domain932 – 1111180Cytoplasmic Potential
Domain41 – 11373EMI
Domain118 – 14831EGF-like 1
Domain156 – 19136EGF-like 2
Domain199 – 23335EGF-like 3
Domain241 – 27636EGF-like 4
Domain421 – 45838EGF-like 5
Repeat629 – 68052FU
Domain681 – 71636EGF-like 6
Motif962 – 9654NPXY
Motif1019 – 10224YXXL
Compositional bias1030 – 103910Poly-Ser

Amino acid modifications

Modified residue10191Phosphotyrosine Ref.1
Glycosylation661N-linked (GlcNAc...) Ref.9
Glycosylation3331N-linked (GlcNAc...) Ref.6 Ref.9 Ref.10
Glycosylation3451N-linked (GlcNAc...) Potential
Glycosylation4561N-linked (GlcNAc...) Potential
Disulfide bond45 ↔ 106 Potential
Disulfide bond71 ↔ 80 Potential
Disulfide bond105 ↔ 117 Potential
Disulfide bond121 ↔ 130 By similarity
Disulfide bond125 ↔ 136 By similarity
Disulfide bond138 ↔ 147 By similarity
Disulfide bond160 ↔ 172 By similarity
Disulfide bond166 ↔ 179 By similarity
Disulfide bond181 ↔ 190 By similarity
Disulfide bond203 ↔ 215 By similarity
Disulfide bond209 ↔ 221 By similarity
Disulfide bond223 ↔ 232 By similarity
Disulfide bond245 ↔ 257 By similarity
Disulfide bond251 ↔ 264 By similarity
Disulfide bond266 ↔ 275 By similarity
Disulfide bond425 ↔ 439 By similarity
Disulfide bond431 ↔ 446 By similarity
Disulfide bond448 ↔ 457 By similarity
Disulfide bond685 ↔ 697 By similarity
Disulfide bond691 ↔ 704 By similarity
Disulfide bond706 ↔ 715 By similarity

Natural variations

Alternative sequence1 – 4949MRLIL…CTVKT → MCVPRDIGSRVKTHTPTSHH RTPSPRTLRTKNVLRTICTP KFEFSYIFF in isoform d. Ref.2
VSP_053133
Alternative sequence50 – 11111062Missing in isoform d. Ref.2
VSP_053134
Alternative sequence1017 – 108266Missing in isoform c. Ref.2
VSP_053135
Alternative sequence1042 – 108241Missing in isoform b. Ref.2
VSP_053136
Alternative sequence10831E → K in isoform c. Ref.2
VSP_053137

Experimental info

Mutagenesis1241P → L in n1995; increase in corpses in L1 head. Ref.1
Mutagenesis1361C → Y in n2091; increase in corpses in L1 head. Ref.1
Mutagenesis3301C → Y in n2089; increase in corpses in L1 head. Ref.1
Mutagenesis4481C → Y in e1797, n2000, and n2092; increase in corpses in L1 head. Ref.1
Mutagenesis5011C → Y in n1951; increase in corpses in L1 head. Ref.1
Mutagenesis8031C → Y in e1801; increase in corpses in L1 head. Ref.1
Mutagenesis9621N → A: 85% loss of activity. Ref.1
Mutagenesis9651Y → A: 71% loss of activity. Ref.1
Mutagenesis10191Y → A: 54% loss of activity. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform a [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: A39F374C008F9874

FASTA1,111118,804
        10         20         30         40         50         60 
MRLILLVLLA TWQVVVDTRA PTFPDKLTQQ LQQQGTTEPQ GDHVCTVKTI VDDYELKKVI 

        70         80         90        100        110        120 
HTVVYNDTEQ CLNPLTGFQC TVEKRGQKAS YQRQLVKKEK YVKQCCDGYY QTKDHFCLPD 

       130        140        150        160        170        180 
CNPPCKKGKC IEPGKCECDP GYGGKYCASS CSVGTWGLGC SKSCDCENGA NCDPELGTCI 

       190        200        210        220        230        240 
CTSGFQGERC EKPCPDNKWG PNCVKSCPCQ NGGKCNKEGK CVCSDGWGGE FCLNKCEEGK 

       250        260        270        280        290        300 
FGAECKFECN CQNGATCDNT NGKCICKSGY HGALCENECS VGFFGSGCTQ KCDCLNNQNC 

       310        320        330        340        350        360 
DSSSGECKCI GWTGKHCDIG CSRGRFGLQC KQNCTCPGLE FSDSNASCDA KTGQCQCESG 

       370        380        390        400        410        420 
YKGPKCDERK CDAEQYGADC SKTCTCVREN TLMCAPNTGF CRCKPGFYGD NCELACSKDS 

       430        440        450        460        470        480 
YGPNCEKQAM CDWNHASECN PETGSCVCKP GRTGKNCSEP CPLDFYGPNC AHQCQCNQRG 

       490        500        510        520        530        540 
VGCDGADGKC QCDRGWTGHR CEHHCPADTF GANCEKRCKC PKGIGCDPIT GECTCPAGLQ 

       550        560        570        580        590        600 
GANCDIGCPE GSYGPGCKLH CKCVNGKCDK ETGECTCQPG FFGSDCSTTC SKGKYGESCE 

       610        620        630        640        650        660 
LSCPCSDASC SKQTGKCLCP LGTKGVSCDQ KCDPNTFGFL CQETVTPSPC ASTDPKNGVC 

       670        680        690        700        710        720 
LSCPPGSSGI HCEHNCPAGS YGDGCQQVCS CADGHGCDPT TGECICEPGY HGKTCSEKCP 

       730        740        750        760        770        780 
DGKYGYGCAL DCPKCASGST CDHINGLCIC PAGLEGALCT RPCSAGFWGN GCRQVCRCTS 

       790        800        810        820        830        840 
EYKQCNAQTG ECSCPAGFQG DRCDKPCEDG YYGPDCIKKC KCQGTATSSC NRVSGACHCH 

       850        860        870        880        890        900 
PGFTGEFCHA LCPESTFGLK CSKECPKDGC GDGYECDAAI GCCHVDQMSC GKAKQEFEAL 

       910        920        930        940        950        960 
NGAGRSTGLT WFFVLLIVAL CGGLGLIALF YRNKYQKEKD PDMPTVSFHK APNNDEGREF 

       970        980        990       1000       1010       1020 
QNPLYSRQSV FPDSDAFSSE NNGNHQGGPP NGLLTLEEEE LENKKIHGRS AAGRGNNDYA 

      1030       1040       1050       1060       1070       1080 
SLDEVAGEGS SSSASASASR RGLNSSEQSR RPLLEEHDEE EFDEPHENSI SPAHAVTTSN 

      1090       1100       1110 
HNENPYADIS SPDPVTQNSA NKKRAQDNLY T

« Hide

Isoform b [UniParc].

Checksum: 75254D0DD5643AE5
Show »

FASTA1,070114,181
Isoform c [UniParc].

Checksum: 0A6D57A3A80BCDCA
Show »

FASTA1,045111,723
Isoform d [UniParc].

Checksum: 7AC8FDAF4DC6A65A
Show »

FASTA495,762

References

« Hide 'large scale' references
[1]"CED-1 is a transmembrane receptor that mediates cell corpse engulfment in C. elegans."
Zhou Z., Hartwieg E., Horvitz H.R.
Cell 104:43-56(2001) [PubMed: 11163239] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION OF NPXY AND YXXL MOTIFS, PHOSPHORYLATION AT TYR-1019, MUTAGENESIS OF PRO-124; CYS-136; CYS-330; CYS-448; CYS-501; CYS-803; ASN-962; TYR-965 AND TYR-1019.
Tissue: Embryo.
[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], ALTERNATIVE SPLICING.
Strain: Bristol N2.
[3]"Mutations affecting programmed cell deaths in the nematode Caenorhabditis elegans."
Hedgecock E.M., Sulston J.E., Thomson J.N.
Science 220:1277-1279(1983) [PubMed: 6857247] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[4]"Genes required for the engulfment of cell corpses during programmed cell death in Caenorhabditis elegans."
Ellis R.E., Jacobson D.M., Horvitz H.R.
Genetics 129:79-94(1991) [PubMed: 1936965] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[5]"Interaction of CED-6/GULP, an adapter protein involved in engulfment of apoptotic cells with CED-1 and CD91/low density lipoprotein receptor-related protein (LRP)."
Su H.P., Nakada-Tsukui K., Tosello-Trampont A.-C., Li Y., Bu G., Henson P.M., Ravichandran K.S.
J. Biol. Chem. 277:11772-11779(2002) [PubMed: 11729193] [Abstract]
Cited for: INTERACTION WITH CED-6.
[6]"Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins."
Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J., Kasai K., Takahashi N., Isobe T.
Nat. Biotechnol. 21:667-672(2003) [PubMed: 12754521] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-333, MASS SPECTROMETRY.
Strain: Bristol N2.
[7]"Two pathways converge at CED-10 to mediate actin rearrangement and corpse removal in C. elegans."
Kinchen J.M., Cabello J., Klingele D., Wong K., Feichtinger R., Schnabel H., Schnabel R., Hengartner M.O.
Nature 434:93-99(2005) [PubMed: 15744306] [Abstract]
Cited for: FUNCTION.
[8]"C. elegans Dynamin mediates the signaling of phagocytic receptor CED-1 for the engulfment and degradation of apoptotic cells."
Yu X., Odera S., Chuang C.H., Lu N., Zhou Z.
Dev. Cell 10:743-757(2006) [PubMed: 16740477] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[9]"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins."
Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T.
Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed: 17761667] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-66 AND ASN-333, MASS SPECTROMETRY.
Strain: Bristol N2.
[10]"Unfolded protein response genes regulated by CED-1 are required for Caenorhabditis elegans innate immunity."
Haskins K.A., Russell J.F., Gaddis N., Dressman H.K., Aballay A.
Dev. Cell 15:87-97(2008) [PubMed: 18606143] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[11]"Phagocytic receptor CED-1 initiates a signaling pathway for degrading engulfed apoptotic cells."
Yu X., Lu N., Zhou Z.
PLoS Biol. 6:E61-E61(2008) [PubMed: 18351800] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF332568 mRNA. Translation: AAG60061.1.
AL032657 Genomic DNA. Translation: CAA21739.1.
AL032657 Genomic DNA. Translation: CAD27614.1.
AL032657 Genomic DNA. Translation: CAD27615.1.
AL032657 Genomic DNA. Translation: CAL44979.1.
PIRT26972.
RefSeqNP_001021772.1. NM_001026601.2.
NP_001021773.1. NM_001026602.2.
NP_001076621.1. NM_001083152.1.
NP_740922.1. NM_170927.3.
UniGeneCel.7093.

3D structure databases

HSSPHSSP built from PDB template 1TOZ based on UniProtKB P46531.
ProteinModelPortalQ9XWD6.
SMRQ9XWD6. Positions 104-368, 658-892.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9XWD6. 1 interaction.
MINTMINT-223151.
STRINGQ9XWD6.

Proteomic databases

PRIDEQ9XWD6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaY47H9C.4a; Y47H9C.4a; Y47H9C.4.
GeneID173064.
KEGGcel:Y47H9C.4.
UCSCY47H9C.4a. c. elegans.

Organism-specific databases

CTD173064.
WormBaseY47H9C.4a; CE20264; WBGene00000415; ced-1.
Y47H9C.4b; CE30361; WBGene00000415; ced-1.
Y47H9C.4c; CE30362; WBGene00000415; ced-1.
Y47H9C.4d; CE40433; WBGene00000415; ced-1.

Phylogenomic databases

GeneTreeEMGT00050000000207.
HOGENOMHBG378567.
InParanoidQ9XWD6.
OMASGACHCH.
PhylomeDBQ9XWD6.

Gene expression databases

ArrayExpressQ9XWD6.

Family and domain databases

InterProIPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000742. EGF_3.
IPR002049. EGF_laminin.
IPR011489. EMI_domain.
IPR006212. Furin_repeat.
[Graphical view]
PfamPF00053. Laminin_EGF. 5 hits.
[Graphical view]
SMARTSM00181. EGF. 6 hits.
SM00180. EGF_Lam. 7 hits.
SM00261. FU. 5 hits.
[Graphical view]
PROSITEPS00022. EGF_1. 15 hits.
PS01186. EGF_2. 11 hits.
PS50026. EGF_3. 6 hits.
PS51041. EMI. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio878121.

Entry information

Entry nameCED1_CAEEL
AccessionPrimary (citable) accession number: Q9XWD6
Secondary accession number(s): Q0E7J9, Q8T3A6, Q8T3A7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: November 1, 1999
Last modified: November 16, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents