| IED ID | IndEnz0002004471 |
| Enzyme Type ID | protease004471 |
| Protein Name |
Caspase-7 CASP-7 EC 3.4.22.60 Apoptotic protease Mch-3 CMH-1 ICE-like apoptotic protease 3 ICE-LAP3 Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11 |
| Gene Name | CASP7 MCH3 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MADDQGCIEEQGVEDSANEDSVDAKPDRSSFVPSLFSKKKKNVTMRSIKTTRDRVPTYQYNMNFEKLGKCIIINNKNFDKVTGMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKKASEEDHTNAACFACILLSHGEENVIYGKDGVTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQADSGPINDTDANPRYKIPVEADFLFAYSTVPGYYSWRSPGRGSWFVQALCSILEEHGKDLEIMQILTRVNDRVARHFESQSDDPHFHEKKQIPCVVSMLTKELYFSQ |
| Enzyme Length | 303 |
| Uniprot Accession Number | P55210 |
| Absorption | |
| Active Site | ACT_SITE 144; /evidence=ECO:0000250; ACT_SITE 186; /evidence=ECO:0000269|PubMed:11701129 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by isatin sulfonamides. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-.; EC=3.4.22.60; Evidence={ECO:0000269|PubMed:11701129}; |
| DNA Binding | |
| EC Number | 3.4.22.60 |
| Enzyme Function | FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution (PubMed:8521391, PubMed:8576161, PubMed:8567622, PubMed:9070923, PubMed:11701129). Cleaves and activates sterol regulatory element binding proteins (SREBPs) (PubMed:8521391, PubMed:8576161, PubMed:8567622, PubMed:9070923). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death (PubMed:8521391, PubMed:8576161, PubMed:8567622, PubMed:9070923). Cleaves phospholipid scramblase proteins XKR4, XKR8 and XKR9 (By similarity). {ECO:0000250|UniProtKB:P97864, ECO:0000269|PubMed:11701129, ECO:0000269|PubMed:8521391, ECO:0000269|PubMed:8567622, ECO:0000269|PubMed:8576161, ECO:0000269|PubMed:9070923}.; FUNCTION: [Isoform Beta]: Lacks enzymatic activity. {ECO:0000269|PubMed:8521391}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (3); Beta strand (13); Chain (2); Compositional bias (1); Helix (11); Initiator methionine (1); Modified residue (2); Mutagenesis (1); Natural variant (2); Propeptide (2); Region (1); Sequence conflict (1); Turn (6) |
| Keywords | 3D-structure;Acetylation;Alternative splicing;Apoptosis;Cytoplasm;Hydrolase;Phosphoprotein;Protease;Reference proteome;Thiol protease;Zymogen |
| Interact With | Q13490; P83105; P42858; Q8N4N3-2; P43364; Q16236; Q9GZT8; Q13177; P27986-2; P21673; Q86WV1-2; P17405; P98170 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | MOD_RES 2; /note="N-acetylalanine"; /evidence="ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895"; MOD_RES 37; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163" |
| Post Translational Modification | PTM: Cleavages by granzyme B or caspase-10 generate the two active subunits. Propeptide domains can also be cleaved efficiently by caspase-3. Active heterodimers between the small subunit of caspase-7 and the large subunit of caspase-3, and vice versa, also occur. {ECO:0000269|PubMed:8755496}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (40) |
| Cross Reference PDB | 1F1J; 1GQF; 1I4O; 1I51; 1K86; 1K88; 1KMC; 1SHJ; 1SHL; 2QL5; 2QL7; 2QL9; 2QLB; 2QLF; 2QLJ; 3EDR; 3H1P; 3IBC; 3IBF; 3R5K; 4FDL; 4FEA; 4HQ0; 4HQR; 4JB8; 4JJ8; 4JR1; 4JR2; 4LSZ; 4ZVO; 4ZVP; 4ZVQ; 4ZVR; 4ZVS; 4ZVT; 4ZVU; 5IC6; 5K20; 5V6U; 5V6Z; |
| Mapped Pubmed ID | 10453075; 10564664; 10873833; 11084335; 11257230; 11257231; 11423904; 11448953; 11752425; 11943137; 12107159; 12145703; 12804035; 12824163; 12970753; 14583630; 14584591; 14623896; 14679087; 14960576; 15033720; 15314233; 15511269; 15650747; 16123041; 16213496; 16385451; 16498457; 16916640; 16918502; 17023557; 17094969; 17353931; 17504820; 17532763; 17697120; 17880920; 17978580; 18072206; 18086147; 18154733; 18459962; 18521960; 18596415; 18619610; 18780184; 18785314; 19022247; 19052714; 19058873; 19141860; 19219602; 19241192; 19269008; 19323650; 19414860; 19530232; 19531679; 19573080; 19581639; 19604093; 19605487; 19617626; 19655253; 19738422; 19759058; 19770576; 19773279; 19782763; 19826114; 19913121; 19996278; 20159985; 20235792; 20379614; 20402676; 20453000; 20566630; 20567846; 20628086; 20661084; 20800603; 20819778; 20855536; 20950443; 20959405; 21044950; 21142842; 21157428; 21484410; 21555521; 21674661; 21936563; 22184066; 22441531; 22451931; 22548721; 22584050; 22795132; 22986525; 23614665; 23650375; 23765963; 23868333; 23897474; 23979166; 24040159; 24407236; 24434142; 24556848; 24779913; 25416956; 25435190; 25784056; 26045308; 26307684; 26988918; 27031226; 27032039; 27084536; 27358062; 27367566; 27889207; 28165150; 28863261; 28940929; 29659498; 29842999; 30069746; 30451870; 30503768; 30725182; 30794682; 30918127; 31586028; 31601152; 31701491; 31819117; 32051334; 32619291; 32686156; 32951155; 33469117; 34156061; 7489707; 9230442; 9325343; 9525868; 9922454; |
| Motif | |
| Gene Encoded By | |
| Mass | 34,277 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.60; |