Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cell death protein 3

Gene

ced-3

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a cysteine protease in controlling programmed cell death by proteolytically activating or inactivating a substrate protein or proteins, a potential substrate may be ced-4 (PubMed:8242740). Alternatively it might directly cause cell death by proteolytically cleaving proteins that are crucial for cell viability (PubMed:8242740). May regulate oocyte growth (PubMed:21901106). May regulate germline apoptosis in response to DNA damage, probably downstream of let-60/ras and mpk-1 pathway (PubMed:21901106).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei315By similarity1
Active sitei358By similarity1

GO - Molecular functioni

  • cysteine-type endopeptidase activator activity involved in apoptotic process Source: UniProtKB
  • cysteine-type endopeptidase activity Source: WormBase
  • cysteine-type endopeptidase activity involved in execution phase of apoptosis Source: WormBase
  • endopeptidase activity Source: WormBase
  • identical protein binding Source: IntAct

GO - Biological processi

  • actin filament depolymerization Source: UniProtKB
  • activation of cysteine-type endopeptidase activity Source: UniProtKB
  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • apoptotic process Source: WormBase
  • apoptotic process involved in development Source: UniProtKB
  • embryo development ending in birth or egg hatching Source: WormBase
  • execution phase of apoptosis Source: WormBase
  • negative regulation of cellular response to manganese ion Source: UniProtKB
  • positive regulation of apoptotic process involved in development Source: UniProtKB
  • positive regulation of cellular response to gamma radiation Source: UniProtKB
  • positive regulation of neuron apoptotic process Source: UniProtKB
  • positive regulation of oviposition Source: UniProtKB
  • positive regulation of protein processing Source: UniProtKB
  • positive regulation of synapse disassembly Source: UniProtKB
  • programmed cell death Source: WormBase
  • protein autoprocessing Source: UniProtKB
  • protein catabolic process Source: WormBase
  • regulation of cell adhesion Source: UniProtKB

Keywordsi

Molecular functionHydrolase, Protease, Thiol protease
Biological processApoptosis

Enzyme and pathway databases

ReactomeiR-CEL-198323. AKT phosphorylates targets in the cytosol.
R-CEL-448706. Interleukin-1 processing.

Protein family/group databases

MEROPSiC14.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell death protein 3 (EC:3.4.22.-)
Cleaved into the following 2 chains:
Gene namesi
Name:ced-3
ORF Names:C48D1.2
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome IV

Organism-specific databases

WormBaseiC48D1.2a; CE29088; WBGene00000417; ced-3.

Subcellular locationi

GO - Cellular componenti

  • caspase complex Source: UniProtKB
  • cytoplasm Source: WormBase
  • membrane Source: WormBase
  • mitochondrion Source: UniProtKB
  • neuronal cell body Source: UniProtKB
  • perinuclear region of cytoplasm Source: WormBase
  • presynapse Source: UniProtKB

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi27L → F in N1040; loss of function. 1 Publication1
Mutagenesisi65G → R in N718; loss of function. 1 Publication1
Mutagenesisi360G → S in N2433; loss of function. 1 Publication1
Mutagenesisi449A → V in N1229/N1164; loss of function. 1 Publication1
Mutagenesisi466A → V in N2430; loss of function. 1 Publication1
Mutagenesisi483E → K in N2426; loss of function. 1 Publication1
Mutagenesisi486S → F in N1163; loss of function. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1250361.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000046741 – 371Cell death protein 3 subunit 1Sequence analysisAdd BLAST371
ChainiPRO_0000004675372 – 503Cell death protein 3 subunit 2Sequence analysisAdd BLAST132

Post-translational modificationi

May be regulated by phosphorylation.

Keywords - PTMi

Phosphoprotein, Zymogen

Proteomic databases

EPDiP42573.
PaxDbiP42573.
PeptideAtlasiP42573.

Expressioni

Developmental stagei

Most abundant during embryogenesis and is also detected at later stages.

Gene expression databases

BgeeiWBGene00000417.
ExpressionAtlasiP42573. baseline.

Interactioni

Subunit structurei

Could be a heterodimer of two subunits derived from the precursor sequence by a probable autocatalytic mechanism.

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi43363. 5 interactors.
DIPiDIP-244N.
IntActiP42573. 3 interactors.
MINTiMINT-128934.
STRINGi6239.C48D1.2a.

Structurei

Secondary structure

1503
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi214 – 216Combined sources3
Helixi222 – 228Combined sources7
Turni231 – 233Combined sources3
Beta strandi243 – 249Combined sources7
Beta strandi254 – 256Combined sources3
Helixi262 – 275Combined sources14
Beta strandi278 – 285Combined sources8
Helixi288 – 298Combined sources11
Beta strandi306 – 317Combined sources12
Beta strandi320 – 322Combined sources3
Helixi331 – 336Combined sources6
Turni340 – 342Combined sources3
Beta strandi351 – 357Combined sources7
Beta strandi360 – 362Combined sources3
Turni411 – 414Combined sources4
Beta strandi415 – 421Combined sources7
Turni431 – 433Combined sources3
Helixi436 – 448Combined sources13
Turni449 – 451Combined sources3
Helixi454 – 468Combined sources15
Beta strandi471 – 473Combined sources3
Beta strandi476 – 478Combined sources3
Beta strandi483 – 486Combined sources4
Beta strandi489 – 491Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4M9RX-ray2.66A/B198-503[»]
ProteinModelPortaliP42573.
SMRiP42573.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 91CARDPROSITE-ProRule annotationAdd BLAST91

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi107 – 205Ser-richAdd BLAST99

Sequence similaritiesi

Belongs to the peptidase C14A family.Curated

Phylogenomic databases

eggNOGiKOG3573. Eukaryota.
ENOG410ZQIE. LUCA.
GeneTreeiENSGT00760000118912.
HOGENOMiHOG000016385.
InParanoidiP42573.
KOiK20106.
OMAiGYTVICK.
OrthoDBiEOG091G05YD.
PhylomeDBiP42573.

Family and domain databases

CDDicd00032. CASc. 1 hit.
InterProiView protein in InterPro
IPR001315. CARD.
IPR029030. Caspase-like_dom.
IPR033139. Caspase_cys_AS.
IPR016129. Caspase_his_AS.
IPR011029. DEATH-like_dom.
IPR002138. Pept_C14_p10.
IPR001309. Pept_C14_p20.
IPR015917. Pept_C14A.
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.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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
Checksum:i722D5831F94DAA69
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29052 Genomic DNA. Translation: AAA27982.2.
AF210702 mRNA. Translation: AAG42045.1.
Z81049 Genomic DNA. Translation: CAB61001.2.
PIRiA49429.
RefSeqiNP_001255708.1. NM_001268779.1.
UniGeneiCel.19438.

Genome annotation databases

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiCED3_CAEEL
AccessioniPrimary (citable) accession number: P42573
Secondary accession number(s): P45435, Q9GQQ4, Q9NAQ8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: August 14, 2001
Last modified: June 7, 2017
This is version 145 of the entry and version 2 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. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families