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Protein

Caspase-3

Gene

casp3

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Important mediator of apoptosis. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond (By similarity).By similarity

Catalytic activityi

Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei131By similarity1
Active sitei174By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

BRENDAi3.4.22.56. 6725.

Protein family/group databases

MEROPSiC14.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Caspase-3 (EC:3.4.22.56)
Short name:
CASP-3
Alternative name(s):
Apopain
Cysteine protease CPP32
Short name:
xCPP32
Cleaved into the following 2 chains:
Gene namesi
Name:casp3
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-865327. casp3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000004594? – 186Caspase-3 subunit p17
PropeptideiPRO_00000045931 – ?By similarity
ChainiPRO_0000004595187 – 282Caspase-3 subunit p12Add BLAST96

Keywords - PTMi

Zymogen

Interactioni

Subunit structurei

Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 17 kDa (p17) and a 12 kDa (p12) subunit.By similarity

Structurei

3D structure databases

ProteinModelPortaliP55866.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C14A family.Curated

Phylogenomic databases

HOVERGENiHBG050802.
KOiK02187.

Family and domain databases

CDDicd00032. CASc. 1 hit.
Gene3Di3.40.50.1460. 1 hit.
InterProiIPR029030. Caspase-like_dom.
IPR015470. Caspase_3.
IPR033139. Caspase_cys_AS.
IPR016129. Caspase_his_AS.
IPR002138. Pept_C14_p10.
IPR001309. Pept_C14_p20.
IPR015917. Pept_C14A.
[Graphical view]
PANTHERiPTHR10454:SF30. PTHR10454:SF30. 1 hit.
PRINTSiPR00376. IL1BCENZYME.
SMARTiSM00115. CASc. 1 hit.
[Graphical view]
SUPFAMiSSF52129. SSF52129. 1 hit.
PROSITEiPS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P55866-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEESQNGVKY GGDATDAKEY FTIQPRSLQN CDLKDIERKT KFAHLQNYRT
60 70 80 90 100
NYPEMGMCLI INNKNFHSSN MAVRNGTDVD ALKLHETFTG LGYEVMVCND
110 120 130 140 150
QKSSDIIGRL KKISEEDHSK RSSFVCAILS HGEEDGSICG VDVPIHIKNL
160 170 180 190 200
TDLFRGDRCK TLVGKPKIFF IQACRGTELD SGIETDSCSE PREEIQRIPV
210 220 230 240 250
EADFLYAYST VPGYCSWRDK MDGSWFIQSL CKMIKLYGSH LELIQILTCV
260 270 280
NHMVALDFET FHAKKQIPCV VSMLTKSFYF FK
Length:282
Mass (Da):32,125
Last modified:November 1, 1997 - v1
Checksum:iCB390E6980CAB77F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89784 mRNA. Translation: BAA14018.1.
RefSeqiNP_001081225.1. NM_001087756.1.
UniGeneiXl.17957.

Genome annotation databases

GeneIDi397720.
KEGGixla:397720.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89784 mRNA. Translation: BAA14018.1.
RefSeqiNP_001081225.1. NM_001087756.1.
UniGeneiXl.17957.

3D structure databases

ProteinModelPortaliP55866.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC14.003.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397720.
KEGGixla:397720.

Organism-specific databases

CTDi836.
XenbaseiXB-GENE-865327. casp3.

Phylogenomic databases

HOVERGENiHBG050802.
KOiK02187.

Enzyme and pathway databases

BRENDAi3.4.22.56. 6725.

Family and domain databases

CDDicd00032. CASc. 1 hit.
Gene3Di3.40.50.1460. 1 hit.
InterProiIPR029030. Caspase-like_dom.
IPR015470. Caspase_3.
IPR033139. Caspase_cys_AS.
IPR016129. Caspase_his_AS.
IPR002138. Pept_C14_p10.
IPR001309. Pept_C14_p20.
IPR015917. Pept_C14A.
[Graphical view]
PANTHERiPTHR10454:SF30. PTHR10454:SF30. 1 hit.
PRINTSiPR00376. IL1BCENZYME.
SMARTiSM00115. CASc. 1 hit.
[Graphical view]
SUPFAMiSSF52129. SSF52129. 1 hit.
PROSITEiPS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCASP3_XENLA
AccessioniPrimary (citable) accession number: P55866
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The subunits are derived from the precursor sequence by a probable autocatalytic mechanism and probably by other caspases.By similarity

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

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.