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Entry version 164 (26 Feb 2020)
Sequence version 2 (14 Aug 2001)
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Protein

Cell death protein 3

Gene

ced-3

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Acts as a cysteine protease in controlling programmed cell death (apoptosis) by proteolytically activating or inactivating a wide range of substrates (PubMed:8654923, PubMed:3955651, PubMed:18722182, PubMed:26074078, PubMed:27723735). Component of the egl-1, ced-9, ced-4 and ced-3 apoptotic signaling cascade required for the initiation of programmed cell death in cells fated to die during embryonic and postembryonic development (PubMed:3955651, PubMed:17329362, PubMed:25432023, PubMed:27723735). During oogenesis, required for germline apoptosis downstream of ced-9 and ced-4 but independently of egl-1 (PubMed:9927601). By cleaving and activating ced-8, promotes phosphatidylserine exposure on the surface of apoptotic cells; phosphatidylserine is a specific marker only present at the surface of apoptotic cells and acts as a specific signal for engulfment (PubMed:24225442). By cleaving and converting dcr-1 into a deoxyribonuclease (DNase), promotes apoptotic chromosomal DNA fragmentation (PubMed:20223951). By cleaving mitochondrial fission protein drp-1, may regulate the removal of mitochondria during apoptosis (PubMed:18722182). During germline apoptosis, cleaves translation initiation factor ifg-1 (isoform p170) promoting cap-independent translation (PubMed:21909434). During male tail morphogenesis, promotes apoptosis of the tail-spike cell downstream of ced-4 but independently of egl-1 and ced-9 (PubMed:17329362). By cleaving cnt-1, prevents the activation of the prosurvival akt-1/2 signaling pathway and thus promotes apoptosis (PubMed:25383666). Downstream of ced-4, may play a role in sex-specific cell apoptosis by cleaving sex-determining protein fem-1 (PubMed:10764728). May regulate germline apoptosis in response to DNA damage, probably downstream of let-60/ras and mpk-1 pathway (PubMed:21901106). Cleaves ced-9 in vitro (PubMed:17371877, PubMed:18776901, PubMed:19575016, PubMed:25432023, PubMed:27723735). Cleaves csp-2 isoform b resulting in the removal of the propeptide and the generation of csp-2 subunit p31 in vitro (PubMed:9857046). Independently of its apoptotic role has additional functions. Probably by cleaving and thereby activating actin-severing protein gsnl-1, required for the elimination of transient presynaptic components during larval development downstream of egl-1, ced-9 and ced-4 pathway (PubMed:26074078). Together with ain-1, a component of the miRNA-induced-silencing complex (miRISC), regulates temporal cell fate patterning during larval development (PubMed:25432023). In complex with ubr-1, which is E3 ubiquitin-protein ligase and component of the N-end rule pathway, acts in seam cell fate patterning during larval development by cleaving the heterochronic protein lin-28, and promoting its degradation (PubMed:25432023, PubMed:28602583). Also cleaves heterochronic protein lin-14 and exonuclease disl-2 in vitro (PubMed:25432023). Downstream of calreticulin crt-1 and ced-4 and independently of egl-1 and ced-9, plays a role in the initial steps of axonal regrowth following axotomy (PubMed:22629231). Cleaves 14-3-3-like protein ftt-2, tubulin tbb-2 and calrecticulin crt-1 in vitro (PubMed:17371877). Plays also a role in resistance to S.typhimurium-mediated infection (PubMed:11226309).21 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Octomeric ced-4 activates zymogen autoprocessing and enhances activity of processed ced-3 (PubMed:18776901, PubMed:19575016, PubMed:27723735, PubMed:24065769, PubMed:20434985). Zymogen autoactivation is inhibited by csp-3 (PubMed:18776901). csp-3 has no effect on active ced-3 (PubMed:18776901). Zymogen autoactivation is inhibited by csp-2 (PubMed:19575016). Inhibited by cysteine protease inhibitor iodoacetic acid (CH3COOI) (PubMed:8654923, PubMed:9857046, PubMed:18776901, PubMed:19575016, PubMed:27723735). Inhibited by benzyloxycarbonyl-DEVD-fluoro-methyl ketone (zDEVD-fmk) (PubMed:8654923, PubMed:9857046, PubMed:25432023). Inhibited by benzyloxycarbonyl-VAD-fluoro-methyl ketone (zVAD-fmk) (PubMed:17371877, PubMed:21909434). Not inhibited by N-[N-(L-3-transcarboxirane-2-carbonyl)-leucyl]-agmatine (E-64) or by the serine and cysteine protease inhibitor L-1-chloro-3-[4-to-osylamido]-7-amino-2-heptanone (TLCK) (PubMed:8654923, PubMed:9857046).10 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei315By similarity1
Active sitei3583 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protease, Thiol protease
Biological processApoptosis

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-CEL-5660668 CLEC7A/inflammasome pathway
R-CEL-6798695 Neutrophil degranulation

Protein family/group databases

MEROPS protease database

More...
MEROPSi
C14.002

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cell death protein 3 (EC:3.4.22.607 Publications)
Alternative name(s):
Caspase ced-3Curated
Cleaved into the following 3 chains:
Cell death protein 3 subunit p171 Publication
Cell death protein 3 subunit p151 Publication
Cell death protein 3 subunit p131 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ced-3Imported
ORF Names:C48D1.2Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiCaenorhabditis elegans
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri6239 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditinaRhabditomorphaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001940 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome IV

Organism-specific databases

WormBase

More...
WormBasei
C48D1.2a ; CE29088 ; WBGene00000417 ; ced-3

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cytoplasm, Membrane, Mitochondrion, Nucleus, Synapse

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

RNAi-mediated knockdown causes a rupture of the vulva and an increase in laid oocytes in a small proportion of animals. In an ain-1 mutant background, enhances the proportion of animals arrested at the larval stage, with egg-laying defects and with a ruptured vulva.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi27L → F in n1040; increased autoprocessing in absence of ced-4. Autoprocessing is blocked in presence of npp-14 and reduced in presence of both ced-4 and npp-14. Loss of embryonic and postembryonic apoptosis resulting in survival of cells in the head, ventral cord, postdeirid sensilla and Q descendants in a ced-1 mutant background defective in cell-corpse clearance. Apoptosis is partially restored in a ced-1 (e1735) and npp-14 (sm160) double mutant background. 2 Publications1
Mutagenesisi30L → F in n2439; increased autoprocessing in absence of ced-4. Autoprocessing is blocked in presence of npp-14 and reduced in presence of both ced-4 and npp-14. Loss of embryonic and postembryonic apoptosis resulting in survival of cells in the anterior pharynx in a ced-1 mutant background defective in cell-corpse clearance. Apoptosis is partially restored in a ced-1 (e1735) and npp-14 (sm160) double mutant background. 1 Publication1
Mutagenesisi51R → H in n2449; normal autoprocessing. No effect on embryonic and postembryonic apoptosis in a ced-1 mutant background defective in cell-corpse clearance. 1 Publication1
Mutagenesisi65G → R in n718; increased autoprocessing in absence of ced-4. Autoprocessing is blocked in presence of npp-14 and reduced in presence of both ced-4 and npp-14. Loss of embryonic and postembryonic apoptosis resulting in survival of cells in the head, ventral cord, postdeirid sensilla and Q descendants in a ced-1 mutant background defective in cell-corpse clearance. Apoptosis is partially restored in a ced-1 (e1735) and npp-14 (sm160) double mutant background. 2 Publications1
Mutagenesisi358C → S: Loss of catalytic activity. Prevents cell death. Loss of processing. No effect on the interaction with ced-4. Loss of interaction with octomeric ced-4; when associated with 391-D--D-393. 4 Publications1
Mutagenesisi360G → S in n2433; loss of catalytic activity. Loss of processing. Severe reduction in the number of apoptotic cells in the anterior pharynx. Loss of embryonic apoptosis in a ced-1 mutant background defective in cell-corpse clearance. Impaired axonal regeneration following injury. Resistance to S.typhimurium-mediated killing. 4 Publications1
Mutagenesisi366G → R in ju1056; Loss of gsnl-1 cleavage. 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. 1 Publication1
Mutagenesisi391 – 393LFN → DDD: Loss of interaction with octomeric ced-4; when associated with S-358. 1 Publication3
Mutagenesisi449A → V in n1229/n1164; severe reduction in catalytic activity. Partially processed. Reduction in the number of apoptotic cells in the anterior pharynx. In a ced-1 mutant background, loss of embryonic and postembryonic apoptosis resulting in survival of cells in the head, ventral cord, postdeirid sensilla, Q descendants and cells of the anterior pharynx. 2 Publications1
Mutagenesisi474G → R in n2427/n2438; slight reduction in catalytic activity. Almost complete processing. Slight reduction in the number of apoptotic cells in the anterior pharynx. Reduction is higher in a drp-1 or fis-2 mutant background. Reduction in number of eggs laid. In a ced-9 (n1653) mutant background, causes 60 percent embryonic lethality. 3 Publications1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1250361

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_00004411171 – 2211 PublicationAdd BLAST221
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000004674222 – 374Cell death protein 3 subunit p17CuratedAdd BLAST153
ChainiPRO_0000004675375 – 503Cell death protein 3 subunit p15CuratedAdd BLAST129
ChainiPRO_0000441118389 – 503Cell death protein 3 subunit p13CuratedAdd BLAST115

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Autocatalytic cleavage removes the propeptide and generates the catalytic subunit p17 and two non-catalytic subunits p15 and p13; autoproteolysis is induced by ced-4 oligomer (PubMed:8654923, PubMed:9857046, PubMed:17371877, PubMed:18776901, PubMed:19575016, PubMed:27723735, PubMed:20434985). Cleaved by caspase csp-1 probably at Asp-144 and Asp-374 (PubMed:9857046).6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei221 – 222Cleavage; by autolysis1 Publication2
Sitei374 – 375Cleavage; by autolysis1 Publication2
Sitei388 – 389Cleavage; by autolysis1 Publication2

Keywords - PTMi

Autocatalytic cleavage, Zymogen

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P42573

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P42573

PeptideAtlas

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PeptideAtlasi
P42573

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Highly expressed in embryos and to a lesser extent in adults (PubMed:8242740). Expression is low throughout the larval stage (PubMed:8242740). Expressed in all cells, except intestinal cells and their precursors, starting at around 100-150 minutes post-fertilization and continuing throughout the comma stage of embryogenesis (PubMed:17329362). Not expressed after the 3-fold embryonic stage, and only expressed in 2-3 cells in larvae and adults (PubMed:17329362). In males, expressed in the tail at the L4 larval stage (PubMed:17329362). Expression in the tail-spike cell is restricted to the 3-fold embryonic stage prior to the tail-spike cell death (PubMed:17329362).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
WBGene00000417 Expressed in adult organism and 4 other tissues

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

The active form is probably a heterodimer of the p17 subunit with either the p15 or p13 subunit which are all derived from the precursor by autocatalysis (Probable).

Interacts with octomeric ced-4 (two ced-3 zymogens per one ced-4 octamer); the interaction causes the autoproteolytic cleavage and activation of ced-3 (PubMed:20434985, PubMed:24065769). Processed ced-3 also interacts with ced-4 octamer to form a stable holoenzyme (PubMed:20434985).

Interacts (via large subunit p17) with csp-3; the interaction prevents ced-3 autoactivation and delays ced-4-induced ced-3 processing (PubMed:18776901).

Interacts (via large subunit p17 or small subunit p13 or p15) with csp-2; the interaction inhibits ced-3 autoactivation (PubMed:19575016).

Interacts (via propeptide) with nucleoporin npp-14; the interaction tethers ced-3 to the nuclear membrane and prevents its autoprocessing in absence of ced-4 (PubMed:27723735).

Interacts with dct-1 (PubMed:11114722). May form a complex composed of ced-3, ced-4 and mac-1 (PubMed:10101135).

Component of a complex containing at least ced-3, ubr-1 and possibly ate-1 (PubMed:28602583). Within complex interacts (via the p17 subunit) with ubr-1; this interaction is required for the ced-3-mediated cleavage and subsequent degradation of the heterochronic protein lin-28 (PubMed:28602583).

Interacts with ate-1 (isoform a and isoform d); interaction with ate-1 (isoform a) is in the presence or absent of ubr-1 (PubMed:28602583).

Curated8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
43363, 6 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1358 ced-3-ced-4-mac-1 complex
CPX-1360 ced-3-ced-4 caspase complex

Database of interacting proteins

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DIPi
DIP-244N

Protein interaction database and analysis system

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IntActi
P42573, 6 interactors

Molecular INTeraction database

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MINTi
P42573

STRING: functional protein association networks

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STRINGi
6239.C48D1.2a

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1503
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P42573

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 91CARDPROSITE-ProRule annotationAdd BLAST91

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni389 – 404Required for interaction with ced-41 PublicationAdd BLAST16

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The CARD domain is involved in ced-4 binding.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase C14A family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3573 Eukaryota
ENOG410ZQIE LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00970000196149

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_036904_5_2_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P42573

KEGG Orthology (KO)

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KOi
K20106

Identification of Orthologs from Complete Genome Data

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OMAi
GYTVICK

Database of Orthologous Groups

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OrthoDBi
1092723at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P42573

Family and domain databases

Conserved Domains Database

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CDDi
cd00032 CASc, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001315 CARD
IPR029030 Caspase-like_dom_sf
IPR033139 Caspase_cys_AS
IPR016129 Caspase_his_AS
IPR011029 DEATH-like_dom_sf
IPR002398 Pept_C14
IPR002138 Pept_C14_p10
IPR001309 Pept_C14_p20
IPR015917 Pept_C14A

The PANTHER Classification System

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PANTHERi
PTHR10454 PTHR10454, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00619 CARD, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00376 IL1BCENZYME

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00114 CARD, 1 hit
SM00115 CASc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47986 SSF47986, 1 hit
SSF52129 SSF52129, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50209 CARD, 1 hit
PS01122 CASPASE_CYS, 1 hit
PS01121 CASPASE_HIS, 1 hit
PS50207 CASPASE_P10, 1 hit
PS50208 CASPASE_P20, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P42573-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMRQDRRSLL ERNIMMFSSH LKVDEILEVL IAKQVLNSDN GDMINSCGTV
60 70 80 90 100
REKRREIVKA VQRRGDVAFD AFYDALRSTG HEGLAEVLEP LARSVDSNAV
110 120 130 140 150
EFECPMSPAS HRRSRALSPA GYTSPTRVHR DSVSSVSSFT SYQDIYSRAR
160 170 180 190 200
SRSRSRALHS SDRHNYSSPP VNAFPSQPSS ANSSFTGCSS LGYSSSRNRS
210 220 230 240 250
FSKASGPTQY IFHEEDMNFV DAPTISRVFD EKTMYRNFSS PRGMCLIINN
260 270 280 290 300
EHFEQMPTRN GTKADKDNLT NLFRCMGYTV ICKDNLTGRG MLLTIRDFAK
310 320 330 340 350
HESHGDSAIL VILSHGEENV IIGVDDIPIS THEIYDLLNA ANAPRLANKP
360 370 380 390 400
KIVFVQACRG ERRDNGFPVL DSVDGVPAFL RRGWDNRDGP LFNFLGCVRP
410 420 430 440 450
QVQQVWRKKP SQADILIAYA TTAQYVSWRN SARGSWFIQA VCEVFSTHAK
460 470 480 490 500
DMDVVELLTE VNKKVACGFQ TSQGSNILKQ MPEMTSRLLK KFYFWPEARN

SAV
Length:503
Mass (Da):56,617
Last modified:August 14, 2001 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i722D5831F94DAA69
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D3YT61D3YT61_CAEEL
Cell death protein 3 subunit p17
ced-3 C48D1.2, CELE_C48D1.2
287Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
L29052 Genomic DNA Translation: AAA27982.2
AF210702 mRNA Translation: AAG42045.1
BX284604 Genomic DNA Translation: CAB61001.2

Protein sequence database of the Protein Information Resource

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PIRi
A49429

NCBI Reference Sequences

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RefSeqi
NP_001255708.1, NM_001268779.1

Genome annotation databases

Ensembl metazoan genome annotation project

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EnsemblMetazoai
C48D1.2a.1; C48D1.2a.1; WBGene00000417

Database of genes from NCBI RefSeq genomes

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GeneIDi
178272

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
cel:CELE_C48D1.2

UCSC genome browser

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UCSCi
C48D1.2 c. elegans

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29052 Genomic DNA Translation: AAA27982.2
AF210702 mRNA Translation: AAG42045.1
BX284604 Genomic DNA Translation: CAB61001.2
PIRiA49429
RefSeqiNP_001255708.1, NM_001268779.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4M9RX-ray2.66A/B198-503[»]
4M9SX-ray3.21E/F/G/H390-397[»]
4M9XX-ray3.34C/D390-395[»]
4M9YX-ray4.20C/D390-397[»]
4M9ZX-ray3.40E/F/G/H390-397[»]
SMRiP42573
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi43363, 6 interactors
ComplexPortaliCPX-1358 ced-3-ced-4-mac-1 complex
CPX-1360 ced-3-ced-4 caspase complex
DIPiDIP-244N
IntActiP42573, 6 interactors
MINTiP42573
STRINGi6239.C48D1.2a

Chemistry databases

ChEMBLiCHEMBL1250361

Protein family/group databases

MEROPSiC14.002

Proteomic databases

EPDiP42573
PaxDbiP42573
PeptideAtlasiP42573

Genome annotation databases

EnsemblMetazoaiC48D1.2a.1; C48D1.2a.1; WBGene00000417
GeneIDi178272
KEGGicel:CELE_C48D1.2
UCSCiC48D1.2 c. elegans

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
178272
WormBaseiC48D1.2a ; CE29088 ; WBGene00000417 ; ced-3

Phylogenomic databases

eggNOGiKOG3573 Eukaryota
ENOG410ZQIE LUCA
GeneTreeiENSGT00970000196149
HOGENOMiCLU_036904_5_2_1
InParanoidiP42573
KOiK20106
OMAiGYTVICK
OrthoDBi1092723at2759
PhylomeDBiP42573

Enzyme and pathway databases

ReactomeiR-CEL-5660668 CLEC7A/inflammasome pathway
R-CEL-6798695 Neutrophil degranulation

Miscellaneous databases

Protein Ontology

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PROi
PR:P42573

Gene expression databases

BgeeiWBGene00000417 Expressed in adult organism and 4 other tissues

Family and domain databases

CDDicd00032 CASc, 1 hit
InterProiView protein in InterPro
IPR001315 CARD
IPR029030 Caspase-like_dom_sf
IPR033139 Caspase_cys_AS
IPR016129 Caspase_his_AS
IPR011029 DEATH-like_dom_sf
IPR002398 Pept_C14
IPR002138 Pept_C14_p10
IPR001309 Pept_C14_p20
IPR015917 Pept_C14A
PANTHERiPTHR10454 PTHR10454, 1 hit
PfamiView protein in Pfam
PF00619 CARD, 1 hit
PRINTSiPR00376 IL1BCENZYME
SMARTiView protein in SMART
SM00114 CARD, 1 hit
SM00115 CASc, 1 hit
SUPFAMiSSF47986 SSF47986, 1 hit
SSF52129 SSF52129, 1 hit
PROSITEiView protein in PROSITE
PS50209 CARD, 1 hit
PS01122 CASPASE_CYS, 1 hit
PS01121 CASPASE_HIS, 1 hit
PS50207 CASPASE_P10, 1 hit
PS50208 CASPASE_P20, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCED3_CAEEL
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P42573
Secondary accession number(s): P45435, Q9GQQ4, Q9NAQ8
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: August 14, 2001
Last modified: February 26, 2020
This is version 164 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  4. Peptidase families
    Classification of peptidase families and list of entries
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