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NameCaspase-3
Synonyms
  • 3.4.22.56
  • Apopain
  • CASP-3
  • CPP-32
  • CPP32
  • Cysteine protease CPP32
  • Protein Yama
  • SCA-1
  • SREBP cleavage activity 1
Gene NameCASP3
OrganismHuman
Amino acid sequence
>lcl|BSEQ0016333|Caspase-3
MENTENSVDSKSIKNLEPKIIHGSESMDSGISLDNSYKMDYPEMGLCIIINNKNFHKSTG
MTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLS
HGEEGIIFGTNGPVDLKKITNFFRGDRCRSLTGKPKLFIIQACRGTELDCGIETDSGVDD
DMACHKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVN
RKVATEFESFSFDATFHAKKQIPCIVSMLTKELYFYH
Number of residues277
Molecular Weight31607.58
Theoretical pI6.51
GO Classification
Functions
  • cysteine-type endopeptidase activity
  • phospholipase A2 activator activity
  • cyclin-dependent protein serine/threonine kinase inhibitor activity
  • cysteine-type endopeptidase activity involved in execution phase of apoptosis
  • peptidase activity
  • cysteine-type endopeptidase activity involved in apoptotic process
  • aspartic-type endopeptidase activity
Processes
  • keratinocyte differentiation
  • wound healing
  • execution phase of apoptosis
  • programmed cell death
  • erythrocyte differentiation
  • response to X-ray
  • hippo signaling
  • negative regulation of cyclin-dependent protein serine/threonine kinase activity
  • cellular response to organic cyclic compound
  • response to glucocorticoid
  • cell fate commitment
  • response to lipopolysaccharide
  • positive regulation of neuron apoptotic process
  • hippocampus development
  • cellular response to DNA damage stimulus
  • apoptotic DNA fragmentation
  • extrinsic apoptotic signaling pathway
  • neuron apoptotic process
  • extracellular matrix disassembly
  • cellular component disassembly involved in execution phase of apoptosis
  • response to amino acid
  • extracellular matrix organization
  • B cell homeostasis
  • apoptotic signaling pathway
  • response to estradiol
  • negative regulation of activated T cell proliferation
  • extrinsic apoptotic signaling pathway in absence of ligand
  • activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c
  • response to hydrogen peroxide
  • response to tumor necrosis factor
  • glial cell apoptotic process
  • sensory perception of sound
  • regulation of cysteine-type endopeptidase activity involved in apoptotic process
  • intrinsic apoptotic signaling pathway
  • apoptotic process
  • proteolysis
  • response to nicotine
  • heart development
  • T cell homeostasis
  • response to glucose
  • negative regulation of apoptotic process
  • platelet formation
  • response to drug
  • response to cobalt ion
  • neurotrophin TRK receptor signaling pathway
  • neuron differentiation
  • response to antibiotic
  • response to UV
  • response to hypoxia
  • negative regulation of B cell proliferation
  • learning or memory
Components
  • membrane raft
  • plasma membrane
  • death-inducing signaling complex
  • cytosol
  • nucleoplasm
  • nucleus
General FunctionPhospholipase a2 activator activity
Specific FunctionInvolved 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. Triggers cell adhesion in sympathetic neurons through RET cleavage.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID561666
UniProtKB IDP42574
UniProtKB Entry NameCASP3_HUMAN
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0016334|Caspase-3 (CASP3)
ATGGAGAACACTGAAAACTCAGTGGATTCAAAATCCATTAAAAATTTGGAACCAAAGATC
ATACATGGAAGCGAATCAATGGACTCTGGAATATCCCTGGACAACAGTTATAAAATGGAT
TATCCTGAGATGGGTTTATGTATAATAATTAATAATAAGAATTTTCATAAAAGCACTGGA
ATGACATCTCGGTCTGGTACAGATGTCGATGCAGCAAACCTCAGGGAAACATTCAGAAAC
TTGAAATATGAAGTCAGGAATAAAAATGATCTTACACGTGAAGAAATTGTGGAATTGATG
CGTGATGTTTCTAAAGAAGATCACAGCAAAAGGAGCAGTTTTGTTTGTGTGCTTCTGAGC
CATGGTGAAGAAGGAATAATTTTTGGAACAAATGGACCTGTTGACCTGAAAAAAATAACA
AACTTTTTCAGAGGGGATCGTTGTAGAAGTCTAACTGGAAAACCCAAACTTTTCATTATT
CAGGCCTGCCGTGGTACAGAACTGGACTGTGGCATTGAGACAGACAGTGGTGTTGATGAT
GACATGGCGTGTCATAAAATACCAGTGGAGGCCGACTTCTTGTATGCATACTCCACAGCA
CCTGGTTATTATTCTTGGCGAAATTCAAAGGATGGCTCCTGGTTCATCCAGTCGCTTTGT
GCCATGCTGAAACAGTATGCCGACAAGCTTGAATTTATGCACATTCTTACCCGGGTTAAC
CGAAAGGTGGCAACAGAATTTGAGTCCTTTTCCTTTGACGCTACTTTTCATGCAAAGAAA
CAGATTCCATGTATTGTTTCCATGCTCACAAAAGAACTCTATTTTTATCACTAA
GenBank Gene IDU13737
GeneCard IDNot Available
GenAtlas IDCASP3
HGNC IDHGNC:1504
Chromosome Location4
Locus4q34
References
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  2. Tewari M, Quan LT, O'Rourke K, Desnoyers S, Zeng Z, Beidler DR, Poirier GG, Salvesen GS, Dixit VM: Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell. 1995 Jun 2;81(5):801-9. 7774019
  3. Pelletier M, Cartron PF, Delaval F, Meflah K, Vallette FM, Oliver L: Caspase 3 activation is controlled by a sequence located in the N-terminus of its large subunit. Biochem Biophys Res Commun. 2004 Mar 26;316(1):93-9. 15003516
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  6. Nicholson DW, Ali A, Thornberry NA, Vaillancourt JP, Ding CK, Gallant M, Gareau Y, Griffin PR, Labelle M, Lazebnik YA, et al.: Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature. 1995 Jul 6;376(6535):37-43. 7596430
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