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Q60431 (CASP3_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Caspase-3

Short name=CASP-3
EC=3.4.22.56
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:

  1. Caspase-3 subunit p17
  2. Caspase-3 subunit p12
Gene names
Name:CASP3
Synonyms:CPP32
OrganismMesocricetus auratus (Golden hamster)
Taxonomic identifier10036 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Protein attributes

Sequence length277 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

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.

Subunit structure

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. Interacts with BIRC6/bruce By similarity.

Subcellular location

Cytoplasm.

Post-translational modification

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.

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.

Sequence similarities

Belongs to the peptidase C14A family.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
   Molecular functionHydrolase
Protease
Thiol protease
   PTMPhosphoprotein
S-nitrosylation
Zymogen
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 99 By similarity
PRO_0000004561
Propeptide10 – 2819 By similarity
PRO_0000004562
Chain29 – 175147Caspase-3 subunit p17
PRO_0000004563
Chain176 – 277102Caspase-3 subunit p12
PRO_0000004564

Sites

Active site1211 By similarity
Active site1631 By similarity

Amino acid modifications

Modified residue261Phosphoserine By similarity
Modified residue1631S-nitrosocysteine; in inhibited form By similarity

Sequences

Sequence LengthMass (Da)Tools
Q60431 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 0BF3A4590A2828A3

FASTA27731,612
        10         20         30         40         50         60 
MENNETSVDS KSIKNFEVKT IHGSKSMDSG IYLDSSYKMD YPEMGVCIII NNKNFHKSTG 

        70         80         90        100        110        120 
MTPRSGTDVD AAKLRETFMA LKYEVRNKND LTREEIVELM KNASKEDHSK RSSFVCVILS 

       130        140        150        160        170        180 
HGDEGVIFGT DGPIDLKKLT SYFRGDYCRS LIGKPKLFII QACRGTELDC GIETDSGTED 

       190        200        210        220        230        240 
DMTCQKIPVE ADFLYAYSTA PGYYSWRNPK DGSWFIQSLC SMLKLYAHKL EFMHILTRVN 

       250        260        270 
RKVATEFESF SLDSTFHAKK QIPCIVSMLT KELYFYH 

« Hide

References

[1]"Cleavage of sterol regulatory element binding proteins (SREBPs) by CPP32 during apoptosis."
Wang X., Zelenski N.G., Yang J., Sakai J., Brown M.S., Goldstein J.L.
EMBO J. 15:1012-1020(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U27463 mRNA. Translation: AAB01511.1.
PIRS64710.

3D structure databases

ProteinModelPortalQ60431.
SMRQ60431. Positions 29-277.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-987N.

Protein family/group databases

MEROPSC14.003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG050802.

Family and domain databases

InterProIPR015470. Caspase_3.
IPR011600. Pept_C14_cat.
IPR001309. Pept_C14_ICE_p20.
IPR016129. Pept_C14_ICE_p20_AS.
IPR002138. Pept_C14_p10.
IPR002398. Pept_C14_p45.
IPR015917. Pept_C14_p45_core.
[Graphical view]
PANTHERPTHR10454. PTHR10454. 1 hit.
PTHR10454:SF30. PTHR10454:SF30. 1 hit.
PfamPF00656. Peptidase_C14. 1 hit.
[Graphical view]
PRINTSPR00376. IL1BCENZYME.
SMARTSM00115. CASc. 1 hit.
[Graphical view]
PROSITEPS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCASP3_MESAU
AccessionPrimary (citable) accession number: Q60431
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 3, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families