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Reviewed, UniProtKB/Swiss-Prot Q08DY9 (CASP3_BOVIN)

Last modified October 13, 2009. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Caspase-3
      Short name=CASP-3
    EC=3.4.22.56
Cleaved into the following 2 chains:
    1- Recommended name:
            Caspase-3 subunit p17
    2- Recommended name:
            Caspase-3 subunit p12
Gene names
Name: CASP3
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length275 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. Involved in the cleavage of huntingtin 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.

Subcellular location

Cytoplasm By similarity.

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
   PTMAcetylation
Phosphoprotein
S-nitrosylation
Zymogen
Gene Ontology (GO)
   Biological processapoptosis

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: InterPro

   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_0000261328
Propeptide10 – 2819 By similarity
PRO_0000261329
Chain29 – 175147Caspase-3 subunit p17
PRO_0000261330
Chain176 – 275100Caspase-3 subunit p12
PRO_0000261331

Sites

Active site1211 By similarity
Active site1631 By similarity

Amino acid modifications

Modified residue261Phosphoserine By similarity
Modified residue821N6-acetyllysine By similarity
Modified residue1631S-nitrosocysteine; in inhibited form By similarity

Sequences

Sequence LengthMass (Da)Tools
Q08DY9-1 [UniParc].

Last modified October 31, 2006. Version 1.
Checksum: 88E5A216E5C32FD1

FASTA27531,136
        10         20         30         40         50         60 
MENTENSVDS KSIKTSETKI LHGSKSMDSG ISLEESYKMD YPEMGLCIII NNKNFHENTG 

        70         80         90        100        110        120 
MACRSGTDVD AANLRETFMN LKYEVRIKND LTCKEMLELM SNVSKEDHSK RSSFICVLLS 

       130        140        150        160        170        180 
HGEEGIIFGT NGPVNLKKLA SFFRGDYCRS LTGKPKLFII QACRGTELDC GIETDSGAED 

       190        200        210        220        230        240 
DMACQKIPVE ADFLYAYSTA PGYFSWRNAK NGSWFIQALC EMLKKHAHRL ELMHILTRVN 

       250        260        270 
RKVAIEYESF STDSAFHAKK QIPCIMSMLT KELYF 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Brain cortex.

Cross-references

Sequence databases

BC123503 mRNA. Translation: AAI23504.1.
IPIIPI00698313.
RefSeqNP_001071308.1.
UniGeneBt.10084

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ08DY9.

Protein family/group databases

MEROPSC14.003.

Genome annotation databases

EnsemblENSBTAT00000021099; ENSBTAP00000021099; ENSBTAG00000015874; Bos taurus. [Genome view]
GeneID408016.
KEGGbta:408016.

Organism-specific databases

CTD408016.

Phylogenomic databases

HOVERGENQ08DY9.

Enzyme and pathway databases

BRENDA3.4.22.56. 251.

Family and domain databases

InterProIPR015470. Caspase_3_related.
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:SF30. Casp3_like. 1 hit.
PTHR10454. Pept_C14_p45. 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_BOVIN
AccessionPrimary (citable) accession number: Q08DY9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: October 31, 2006
Last modified: October 13, 2009
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents