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Protein

Caspase-3

Gene

casp3

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

Keywordsi

Molecular functionHydrolase, Protease, Thiol protease
Biological processApoptosis

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

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

Proteomic databases

PRIDEiP55866

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
InterProiView protein in InterPro
IPR029030 Caspase-like_dom_sf
IPR033139 Caspase_cys_AS
IPR016129 Caspase_his_AS
IPR002138 Pept_C14_p10
IPR001309 Pept_C14_p20
IPR015917 Pept_C14A
PRINTSiPR00376 IL1BCENZYME
SMARTiView protein in SMART
SM00115 CASc, 1 hit
SUPFAMiSSF52129 SSF52129, 1 hit
PROSITEiView protein in PROSITE
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.

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

Similar proteinsi

Entry informationi

Entry nameiCASP3_XENLA
AccessioniPrimary (citable) accession number: P55866
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: May 23, 2018
This is version 101 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

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

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