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UniProtKB/Swiss-Prot entry Q60431


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CASP3_MESAU
Primary accession number Q60431
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 60)
Name and origin of the protein
Protein name Caspase-3 [Precursor]
Synonyms CASP-3
EC 3.4.22.56
Apopain
Cysteine protease CPP32
CPP-32
Yama protein
SREBP cleavage activity 1
SCA-1
Contains Caspase-3 subunit p17
Caspase-3 subunit p12
Gene name
Name: CASP3
Synonyms: CPP32
From
Mesocricetus auratus (Golden hamster) [TaxID: 10036] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Cricetidae; Cricetinae; Mesocricetus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=8605870 [NCBI, ExPASy, EBI, Israel, Japan]
Wang X., Zelenski N.G., Yang J., Sakai J., Brown M.S., Goldstein J.L.;
"Cleavage of sterol regulatory element binding proteins (SREBPs) by CPP32 during apoptosis.";
EMBO J. 15:1012-1020(1996).
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 (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: 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.
  • PTM: 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).
  • PTM: 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).
  • SIMILARITY: Belongs to the peptidase C14 family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U27463; AAB01511.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S64710; S64710.
3D structure databases
HSSP P42574; 1PAU. [HSSP ENTRY / PDB]
ModBase Q60431.
Protein family/group databases
MEROPS C14.003; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR015470; Casp3_like.
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 of domain structure.
PANTHER PTHR10454:SF30; Casp3_like; 1.
PTHR10454; Pept_C14_p45; 1.
Pfam PF00656; Peptidase_C14; 1.
Pfam graphical view of domain structure.
PRINTS PR00376; IL1BCENZYME.
SMART SM00115; CASc; 1.
SMART graphical view of domain structure.
PROSITE PS01122; CASPASE_CYS; 1.
PS01121; CASPASE_HIS; 1.
PS50207; CASPASE_P10; 1.
PS50208; CASPASE_P20; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q60431.
ProtoNet Q60431.
Phylogenomic databases
HOVERGEN Q60431; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Apoptosis; Cytoplasm; Hydrolase; Phosphoprotein; Protease; S-nitrosylation; Thiol protease; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
PROPEP   1     9  9     By similarity. PRO_0000004561
PROPEP   10    28  19     By similarity. PRO_0000004562
CHAIN   29   175  147     Caspase-3 subunit p17. PRO_0000004563
CHAIN   176   277  102     Caspase-3 subunit p12. PRO_0000004564
ACT_SITE   121   121        By similarity. 
ACT_SITE   163   163        By similarity. 
MOD_RES   26    26        Phosphoserine (By similarity). 
MOD_RES   163   163        S-nitrosocysteine; in inhibited form (By similarity). 
Sequence information
Length: 277 AA [This is the length of the unprocessed precursor] Molecular weight: 31612 Da [This is the MW of the unprocessed precursor] CRC64: 0BF3A4590A2828A3 [This is a checksum on the sequence]
        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 

Q60431 in FASTA format

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