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Protein

Caspase-3

Gene

CASP3

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei121 – 1211By similarity
Active sitei163 – 1631By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Apoptosis

Protein family/group databases

MEROPSiC14.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Caspase-3 (EC:3.4.22.56)
Short name:
CASP-3
Cleaved into the following 2 chains:
Gene namesi
Name:CASP3
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: AgBase
  • nucleus Source: AgBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 99By similarityPRO_0000004581
Propeptidei10 – 2819By similarityPRO_0000004582Add
BLAST
Chaini29 – 175147Caspase-3 subunit p17By similarityPRO_0000004583Add
BLAST
Chaini176 – 277102Caspase-3 subunit p12By similarityPRO_0000004584Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei11 – 111N6-acetyllysineBy similarity
Modified residuei26 – 261PhosphoserineBy similarity
Modified residuei163 – 1631S-nitrosocysteine; in inhibited formBy similarity

Post-translational modificationi

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).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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation, Zymogen

Proteomic databases

PaxDbiQ95ND5.
PeptideAtlasiQ95ND5.

Interactioni

Subunit structurei

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). Subunit p17 interacts with asfivirus A224L protein. Interacts with BIRC6/bruce (By similarity).By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000016724.

Structurei

3D structure databases

ProteinModelPortaliQ95ND5.
SMRiQ95ND5. Positions 29-277.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C14A family.Curated

Phylogenomic databases

eggNOGiKOG3573. Eukaryota.
ENOG410ZQIE. LUCA.
HOGENOMiHOG000231878.
HOVERGENiHBG050802.
InParanoidiQ95ND5.
KOiK02187.

Family and domain databases

Gene3Di3.40.50.1460. 1 hit.
InterProiIPR029030. Caspase-like_dom.
IPR015470. Caspase_3.
IPR033139. Caspase_cys_AS.
IPR016129. Caspase_his_AS.
IPR002138. Pept_C14_p10.
IPR001309. Pept_C14_p20.
IPR015917. Pept_C14A.
[Graphical view]
PANTHERiPTHR10454:SF30. PTHR10454:SF30. 1 hit.
PRINTSiPR00376. IL1BCENZYME.
SMARTiSM00115. CASc. 1 hit.
[Graphical view]
SUPFAMiSSF52129. SSF52129. 1 hit.
PROSITEiPS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q95ND5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENNKTSVDS KSIKTLETKI LHGSKSMDSG ISLDVSYKMD YPEMGLCIII
60 70 80 90 100
NNKNFDKNTG MACRSGTDVD AANLRETFTN LKYEVRNKND LTREEILELM
110 120 130 140 150
HSVSKEDHSK RSSFICVLLS HGEEGKIFGT NGPVDLKKLT SFFRGDCCRT
160 170 180 190 200
LTGKPKLFII QACRGTELDC GIETDSGTED DMACQKIPVE ADFLYAYSTA
210 220 230 240 250
PGYYSWRNSK DGSWFIQSLC AALKQYVHKL ELMHILTRVN RKVAVEFESF
260 270
STDSTFHAKK QIPCIVSMLT KELYFYH
Length:277
Mass (Da):31,379
Last modified:December 1, 2001 - v1
Checksum:i616C0F56141B012B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029345 mRNA. Translation: BAB55544.1.
RefSeqiNP_999296.1. NM_214131.1.
UniGeneiSsc.15886.

Genome annotation databases

GeneIDi397244.
KEGGissc:397244.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029345 mRNA. Translation: BAB55544.1.
RefSeqiNP_999296.1. NM_214131.1.
UniGeneiSsc.15886.

3D structure databases

ProteinModelPortaliQ95ND5.
SMRiQ95ND5. Positions 29-277.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000016724.

Protein family/group databases

MEROPSiC14.003.

Proteomic databases

PaxDbiQ95ND5.
PeptideAtlasiQ95ND5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397244.
KEGGissc:397244.

Organism-specific databases

CTDi836.

Phylogenomic databases

eggNOGiKOG3573. Eukaryota.
ENOG410ZQIE. LUCA.
HOGENOMiHOG000231878.
HOVERGENiHBG050802.
InParanoidiQ95ND5.
KOiK02187.

Family and domain databases

Gene3Di3.40.50.1460. 1 hit.
InterProiIPR029030. Caspase-like_dom.
IPR015470. Caspase_3.
IPR033139. Caspase_cys_AS.
IPR016129. Caspase_his_AS.
IPR002138. Pept_C14_p10.
IPR001309. Pept_C14_p20.
IPR015917. Pept_C14A.
[Graphical view]
PANTHERiPTHR10454:SF30. PTHR10454:SF30. 1 hit.
PRINTSiPR00376. IL1BCENZYME.
SMARTiSM00115. CASc. 1 hit.
[Graphical view]
SUPFAMiSSF52129. SSF52129. 1 hit.
PROSITEiPS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Porcine caspase-3: its cloning and activity during apoptosis of PK15 cells induced by porcine Fas ligand."
    Muneta Y., Shimojima Y., Mori Y.
    J. Interferon Cytokine Res. 21:409-415(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "African swine fever virus IAP homologue inhibits caspase activation and promotes cell survival in mammalian cells."
    Nogal M.L., Gonzalez de Buitrago G., Rodriguez C., Cubelos B., Carrascosa A.L., Salas M.L., Revilla Y.
    J. Virol. 75:2535-2543(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ASFIVIRUS A224L.

Entry informationi

Entry nameiCASP3_PIG
AccessioniPrimary (citable) accession number: Q95ND5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: December 1, 2001
Last modified: July 6, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.