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Protein

Caspase-3

Gene

CASP3

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Triggers cell adhesion in sympathetic neurons through RET cleavage (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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei121 – 1211By similarity
Active sitei163 – 1631By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Apoptosis

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:
CPP-32
Protein Yama
SREBP cleavage activity 1
Short name:
SCA-1
Cleaved into the following 2 chains:
Gene namesi
Name:CASP3
Synonyms:CPP32
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 99By similarityPRO_0000004561
Propeptidei10 – 2819By similarityPRO_0000004562Add
BLAST
Chaini29 – 175147Caspase-3 subunit p17PRO_0000004563Add
BLAST
Chaini176 – 277102Caspase-3 subunit p12PRO_0000004564Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei11 – 111N6-acetyllysineBy similarity
Modified residuei26 – 261PhosphoserineBy similarity
Modified residuei163 – 1631S-nitrosocysteine; in inhibited formBy similarity

Post-translational modificationi

Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10 generates the two active subunits. Additional processing of the propeptides is likely due to the autocatalytic activity of the activated protease. Active heterodimers between the small subunit of caspase-7 protease and the large subunit of caspase-3 also occur and vice versa (By similarity).By similarity
S-nitrosylated on its catalytic site cysteine in unstimulated human cell lines and denitrosylated upon activation of the Fas apoptotic pathway, associated with an increase in intracellular caspase activity. Fas therefore activates caspase-3 not only by inducing the cleavage of the caspase zymogen to its active subunits, but also by stimulating the denitrosylation of its active site thiol (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation, 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. Interacts with BIRC6/bruce.By similarity

Protein-protein interaction databases

DIPiDIP-987N.

Structurei

3D structure databases

ProteinModelPortaliQ60431.
SMRiQ60431. Positions 29-277.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C14A family.Curated

Phylogenomic databases

HOVERGENiHBG050802.
OrthoDBiEOG091G05YD.

Family and domain databases

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.

Q60431-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENNETSVDS KSIKNFEVKT IHGSKSMDSG IYLDSSYKMD YPEMGVCIII
60 70 80 90 100
NNKNFHKSTG MTPRSGTDVD AAKLRETFMA LKYEVRNKND LTREEIVELM
110 120 130 140 150
KNASKEDHSK RSSFVCVILS HGDEGVIFGT DGPIDLKKLT SYFRGDYCRS
160 170 180 190 200
LIGKPKLFII QACRGTELDC GIETDSGTED DMTCQKIPVE ADFLYAYSTA
210 220 230 240 250
PGYYSWRNPK DGSWFIQSLC SMLKLYAHKL EFMHILTRVN RKVATEFESF
260 270
SLDSTFHAKK QIPCIVSMLT KELYFYH
Length:277
Mass (Da):31,612
Last modified:November 1, 1996 - v1
Checksum:i0BF3A4590A2828A3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27463 mRNA. Translation: AAB01511.1.
PIRiS64710.
RefSeqiNP_001268511.1. NM_001281582.1.

Genome annotation databases

GeneIDi101828960.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27463 mRNA. Translation: AAB01511.1.
PIRiS64710.
RefSeqiNP_001268511.1. NM_001281582.1.

3D structure databases

ProteinModelPortaliQ60431.
SMRiQ60431. Positions 29-277.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-987N.

Protein family/group databases

MEROPSiC14.003.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi101828960.

Organism-specific databases

CTDi836.

Phylogenomic databases

HOVERGENiHBG050802.
OrthoDBiEOG091G05YD.

Family and domain databases

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_MESAU
AccessioniPrimary (citable) accession number: Q60431
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: September 7, 2016
This is version 100 of the entry and version 1 of the sequence. [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

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.