Caspase-2

Basic Information
Short Name	CASP2
UNP ID	P42575
Organism	Homo sapiens
Cys Site	Cys320
Family/Domain	Peptidase C14A family
Known Ligand	Ligand list
Function Type	Protease

Summary

Protein Function

Caspase-2 proteolytically cleaves other proteins. It belongs to a family of cysteine proteases called caspases that cleave proteins only at an amino acid following an aspartic acid residue. Within this family, caspase-2 is part of the Ich-1 subfamily. It is one of the most conserved caspases in different species of animal. Caspase-2 has a similar amino acid sequence to initiator caspases, including caspase 1, caspase-4, caspase-5, and caspase-9. It is produced as a zymogen, which contains a long pro-domain that is similar to that of caspase-9 and contains a protein interaction domain known as a CARD domain. Pro-caspase-2 contains two subunits, p19 and p12. (From Wikipedia)

Caspase-2 was discovered as the first mammalian apoptotic caspase. It is engaged as an initiator in both the extrinsic and the intrinsic pathways of apoptosis. Additionally, Caspase-2 serves in neuronal cells both as the default initiator and the default executioner caspase. (PMID: 12920126)

Cys Function & Property

The catalytic triad in Caspase-3 comprises Cys320, His277 and the backbone carbonyl oxygen atom of Arg219, which points towards the Nϵ atom of His277.

• Hydrophobic property:

• SASA:

Cys320: 11.39 A^2

Protein Sequence

MAAPSAGSWS TFQHKELMAA DRGRRILGVC GMHPHHQETL KKNRVVLAKQ
LLLSELLEHL LEKDIITLEM RELIQAKVGS FSQNVELLNL LPKRGPQAFD
AFCEALRETK QGHLEDMLLT TLSGLQHVLP PLSCDYDLSL PFPVCESCPL
YKKLRLSTDT VEHSLDNKDG PVCLQVKPCT PEFYQTHFQL AYRLQSRPRG
LALVLSNVHF TGEKELEFRS GGDVDHSTLV TLFKLLGYDV HVLCDQTAQE
MQEKLQNFAQ LPAHRVTDSC IVALLSHGVE GAIYGVDGKL LQLQEVFQLF
DNANCPSLQN KPKMFFIQAC RGDETDRGVD QQDGKNHAGS PGCEESDAGK
EKLPKMRLPT RSDMICGYAC LKGTAAMRNT KRGSWYIEAL AQVFSERACD
MHVADMLVKV NALIKDREGY APGTEFHRCK EMSEYCSTLC RHLYLFPGHP
PT

Structural Information

• Known structure with covalent ligand:
  

1PYO

• Protein structure:

Related Pathway

• Apoptosis
  

Experimental Evidence

Crystallography

Reference

1. Schweizer A, Briand C, Grütter M G. Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway[J]. Journal of Biological Chemistry, 2003, 278(43): 42441-42447. 12920126