##gff-version 3 P55210 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:22223895;Dbxref=PMID:19413330,PMID:22223895 P55210 UniProtKB Propeptide 2 23 . . . ID=PRO_0000004616;Note=N-terminally processed;Ontology_term=ECO:0000305,ECO:0000305,ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12824163,ECO:0000305|PubMed:16916640,ECO:0000305|PubMed:23650375,ECO:0000305|PubMed:8755496;Dbxref=PMID:12824163,PMID:16916640,PMID:23650375,PMID:8755496 P55210 UniProtKB Chain 24 198 . . . ID=PRO_0000004617;Note=Caspase-7 subunit p20;Ontology_term=ECO:0000305,ECO:0000305,ECO:0000305,ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12824163,ECO:0000305|PubMed:16916640,ECO:0000305|PubMed:23650375,ECO:0000305|PubMed:27889207,ECO:0000305|PubMed:8755496;Dbxref=PMID:12824163,PMID:16916640,PMID:23650375,PMID:27889207,PMID:8755496 P55210 UniProtKB Propeptide 199 206 . . . ID=PRO_0000004618;Ontology_term=ECO:0000305,ECO:0000305,ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12824163,ECO:0000305|PubMed:16916640,ECO:0000305|PubMed:23650375,ECO:0000305|PubMed:27889207;Dbxref=PMID:12824163,PMID:16916640,PMID:23650375,PMID:27889207 P55210 UniProtKB Chain 207 303 . . . ID=PRO_0000004619;Note=Caspase-7 subunit p11;Ontology_term=ECO:0000305,ECO:0000305,ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12824163,ECO:0000305|PubMed:16916640,ECO:0000305|PubMed:27889207,ECO:0000305|PubMed:8755496;Dbxref=PMID:12824163,PMID:16916640,PMID:27889207,PMID:8755496 P55210 UniProtKB Region 1 30 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P55210 UniProtKB Region 38 41 . . . Note=Exosite;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22451931,ECO:0000269|PubMed:31586028,ECO:0000269|PubMed:34156061;Dbxref=PMID:22451931,PMID:31586028,PMID:34156061 P55210 UniProtKB Region 76 87 . . . Note=Loop L1;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:23897474;Dbxref=PMID:23897474 P55210 UniProtKB Region 187 196 . . . Note=Loop L2;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:23897474;Dbxref=PMID:23897474 P55210 UniProtKB Region 226 238 . . . Note=Loop L3;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:23897474;Dbxref=PMID:23897474 P55210 UniProtKB Region 274 288 . . . Note=Loop L4;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:23897474;Dbxref=PMID:23897474 P55210 UniProtKB Compositional bias 1 17 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P55210 UniProtKB Active site 144 144 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15314233;Dbxref=PMID:15314233 P55210 UniProtKB Active site 186 186 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11701129,ECO:0000269|PubMed:15314233,ECO:0000269|PubMed:16916640;Dbxref=PMID:11701129,PMID:15314233,PMID:16916640 P55210 UniProtKB Site 36 37 . . . Note=Cleavage%3B by CAPN1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19617626;Dbxref=PMID:19617626 P55210 UniProtKB Site 45 46 . . . Note=Cleavage%3B by CAPN1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19617626;Dbxref=PMID:19617626 P55210 UniProtKB Site 47 48 . . . Note=Cleavage%3B by CAPN1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19617626;Dbxref=PMID:19617626 P55210 UniProtKB Site 187 187 . . . Note=Involved in allosteric regulation;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15314233,ECO:0000269|PubMed:19581639;Dbxref=PMID:15314233,PMID:19581639 P55210 UniProtKB Site 223 223 . . . Note=Involved in allosteric regulation;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15314233,ECO:0000269|PubMed:19581639;Dbxref=PMID:15314233,PMID:19581639 P55210 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:22223895;Dbxref=PMID:19413330,PMID:22223895 P55210 UniProtKB Modified residue 30 30 . . . Note=Phosphoserine%3B by PAK2;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21555521,ECO:0000269|PubMed:27889207;Dbxref=PMID:21555521,PMID:27889207 P55210 UniProtKB Modified residue 37 37 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P55210 UniProtKB Modified residue 173 173 . . . Note=Phosphothreonine%3B by PAK2;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21555521,ECO:0000269|PubMed:27889207;Dbxref=PMID:21555521,PMID:27889207 P55210 UniProtKB Modified residue 233 233 . . . Note=(Microbial infection) ADP-riboxanated arginine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:35338844,ECO:0000269|PubMed:35446120;Dbxref=PMID:35338844,PMID:35446120 P55210 UniProtKB Modified residue 239 239 . . . Note=Phosphoserine%3B by PAK2;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21555521,ECO:0000269|PubMed:27889207;Dbxref=PMID:21555521,PMID:27889207 P55210 UniProtKB Alternative sequence 1 36 . . . ID=VSP_045325;Note=In isoform 4. MADDQGCIEEQGVEDSANEDSVDAKPDRSSFVPSLF->MQRGLFSDGDT;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 P55210 UniProtKB Alternative sequence 1 1 . . . ID=VSP_000806;Note=In isoform Alpha'. M->MDCVGWPPGRKWHLEKNTSCGGSSGICASYVTQM;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:19054851,ECO:0000303|PubMed:8521391,ECO:0000303|PubMed:9070923;Dbxref=PMID:19054851,PMID:8521391,PMID:9070923 P55210 UniProtKB Alternative sequence 149 303 . . . ID=VSP_000807;Note=In isoform Beta. VIYGKDGVTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQADSGPINDTDANPRYKIPVEADFLFAYSTVPGYYSWRSPGRGSWFVQALCSILEEHGKDLEIMQILTRVNDRVARHFESQSDDPHFHEKKQIPCVVSMLTKELYFSQ->MESCSVTQAGVQRRDLGRLQPPPPRLAEGPSLMMASRPTRGPSMTQMLILDTRSQWKLTSSSPIPRFQAITRGGAQEEAPGLCKPSAPSWRSTEKTWKSCRSSPG;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:8521391;Dbxref=PMID:8521391 P55210 UniProtKB Natural variant 4 4 . . . ID=VAR_048617;Note=D->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|Ref.5;Dbxref=dbSNP:rs11555408,PMID:15489334 P55210 UniProtKB Natural variant 255 255 . . . ID=VAR_048618;Note=D->E;Dbxref=dbSNP:rs2227310 P55210 UniProtKB Mutagenesis 23 23 . . . Note=Abolished cleavage at the N-terminus%2C leading to impaired activation and thiol protease activity. In P7-D2A mutant%3B abolished cleavage and activation%2C leading to decreased but mesureable activity%3B when associated with A-198. D->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12824163,ECO:0000269|PubMed:22451931,ECO:0000269|PubMed:23650375,ECO:0000269|PubMed:34156061;Dbxref=PMID:12824163,PMID:22451931,PMID:23650375,PMID:34156061 P55210 UniProtKB Mutagenesis 30 30 . . . Note=Abolished phosphorylation by PAK2%3B when associated with A-173 and A-239. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21555521;Dbxref=PMID:21555521 P55210 UniProtKB Mutagenesis 30 30 . . . Note=Mimics phosphorylation%3B does not affect thiol protease activity. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27889207;Dbxref=PMID:27889207 P55210 UniProtKB Mutagenesis 38 41 . . . Note=Decreased ability to cleave PARP1 and PTGES3. KKKK->AAAA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22451931,ECO:0000269|PubMed:28863261;Dbxref=PMID:22451931,PMID:28863261 P55210 UniProtKB Mutagenesis 38 41 . . . Note=Decreased ability to cleave PARP1. KKKK->AKKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31586028;Dbxref=PMID:31586028 P55210 UniProtKB Mutagenesis 39 40 . . . Note=Does not affect ability to cleave PARP1. KK->AA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22451931,ECO:0000269|PubMed:31586028;Dbxref=PMID:22451931,PMID:31586028 P55210 UniProtKB Mutagenesis 39 40 . . . Note=Decreased ability to cleave PARP1. Decreased RNA-binding. KK->EE;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22451931,ECO:0000269|PubMed:31586028,ECO:0000269|PubMed:34156061;Dbxref=PMID:22451931,PMID:31586028,PMID:34156061 P55210 UniProtKB Mutagenesis 39 39 . . . Note=Decreased ability to cleave PARP1. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22451931;Dbxref=PMID:22451931 P55210 UniProtKB Mutagenesis 173 173 . . . Note=Abolished phosphorylation by PAK2%3B when associated with A-30 and A-239. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21555521;Dbxref=PMID:21555521 P55210 UniProtKB Mutagenesis 186 186 . . . Note=Abolished thiol protease activity. C->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11701129,ECO:0000269|PubMed:11752425,ECO:0000269|PubMed:12824163,ECO:0000269|PubMed:16916640,ECO:0000269|PubMed:27889207,ECO:0000269|PubMed:8576161;Dbxref=PMID:11701129,PMID:11752425,PMID:12824163,PMID:16916640,PMID:27889207,PMID:8576161 P55210 UniProtKB Mutagenesis 187 187 . . . Note=Does not significantly affect thiol protease catalytic efficiency. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19581639;Dbxref=PMID:19581639 P55210 UniProtKB Mutagenesis 187 187 . . . Note=Reduced thiol protease catalytic efficiency. R->M%2CA%2CG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19581639;Dbxref=PMID:19581639 P55210 UniProtKB Mutagenesis 187 187 . . . Note=Strongly reduced thiol protease catalytic efficiency. R->W%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19581639;Dbxref=PMID:19581639 P55210 UniProtKB Mutagenesis 192 192 . . . Note=Strongly reduced thiol protease activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16916640;Dbxref=PMID:16916640 P55210 UniProtKB Mutagenesis 195 206 . . . Note=In mutant II%3B prevents cleavage of loop L2 region%3B retains significant thiol protease activity. IQADSGPINDTD->LVPRGS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23897474;Dbxref=PMID:23897474 P55210 UniProtKB Mutagenesis 195 200 . . . Note=In mutant III%3B prevents cleavage of loop L2 region%3B abolished thiol protease activity. IQADSG->LVPRGS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23897474;Dbxref=PMID:23897474 P55210 UniProtKB Mutagenesis 198 204 . . . Note=In mutant IV%3B prevents cleavage of loop L2 region%3B retains significant thiol protease activity. DSGPIND->ASGPINDLVPRGS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23897474;Dbxref=PMID:23897474 P55210 UniProtKB Mutagenesis 198 198 . . . Note=Strongly reduced cleavage and activation by initiator caspases. Abolished cleavage and activation by initiator caspases%3B when associated with A-206. In P7-D2A mutant%3B abolished cleavage and activation%2C leading to decreased but mesureable activity%3B when associated with A-23. D->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12824163,ECO:0000269|PubMed:16916640,ECO:0000269|PubMed:23650375;Dbxref=PMID:12824163,PMID:16916640,PMID:23650375 P55210 UniProtKB Mutagenesis 206 206 . . . Note=Reduced cleavage and activation by initiator caspases. Abolished cleavage and activation by initiator caspases%3B when associated with A-198. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12824163,ECO:0000269|PubMed:16916640;Dbxref=PMID:12824163,PMID:16916640 P55210 UniProtKB Mutagenesis 223 223 . . . Note=Does not significantly affect thiol protease catalytic efficiency. Y->A%2CF%2CW%2CD%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19581639;Dbxref=PMID:19581639 P55210 UniProtKB Mutagenesis 229 229 . . . Note=Strongly reduced thiol protease catalytic efficiency. Y->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19581639;Dbxref=PMID:19581639 P55210 UniProtKB Mutagenesis 230 234 . . . Note=In esCasp-7 V3 mutant%3B promotes specificity toward alternate peptides with VEID%2C YVAD%2C WEHD%2C LETD or LEHD sequence%3B when associated with C-276. In esCasp-7 V4 mutant%3B promotes specificity toward alternate peptides with VEID%2C YVAD%2C WEHD%2C LETD or LEHD sequence%3B when associated with D-276. YSWRS->VSYRV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27032039;Dbxref=PMID:27032039 P55210 UniProtKB Mutagenesis 232 234 . . . Note=In dsCasp-7 mutant%3B unable to cleave DEVD and VEID peptides%3B when associated with F-276. WRS->HRE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27032039;Dbxref=PMID:27032039 P55210 UniProtKB Mutagenesis 233 233 . . . Note=Abolished ADP-riboxanation by C.violaceum CopC. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:35446120;Dbxref=PMID:35446120 P55210 UniProtKB Mutagenesis 239 239 . . . Note=Abolished phosphorylation by PAK2%3B when associated with A-30 and A-173. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21555521;Dbxref=PMID:21555521 P55210 UniProtKB Mutagenesis 239 239 . . . Note=Mimics phosphorylation%3B leading to inactivate thiol protease activity. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27889207;Dbxref=PMID:27889207 P55210 UniProtKB Mutagenesis 276 276 . . . Note=In esCasp-7 V3 mutant%3B promotes specificity toward alternate peptides with VEID%2C YVAD%2C WEHD%2C LETD or LEHD sequence%3B when associated with 230-V--V-234. Q->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27032039;Dbxref=PMID:27032039 P55210 UniProtKB Mutagenesis 276 276 . . . Note=In esCasp-7 V4 mutant%3B promotes specificity toward alternate peptides with VEID%2C YVAD%2C WEHD%2C LETD or LEHD sequence%3B when associated with 230-V--V-234. Q->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27032039;Dbxref=PMID:27032039 P55210 UniProtKB Mutagenesis 276 276 . . . Note=In dsCasp-7 mutant%3B unable to cleave DEVD sand VEID peptides%3B when associated with 232-H--E-234. Q->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27032039;Dbxref=PMID:27032039 P55210 UniProtKB Mutagenesis 290 290 . . . Note=Decreased phosphorylation by PAK2. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27889207;Dbxref=PMID:27889207 P55210 UniProtKB Mutagenesis 290 290 . . . Note=Does not significantly affect thiol protease catalytic activity. C->T%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19581639;Dbxref=PMID:19581639 P55210 UniProtKB Sequence conflict 194 194 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P55210 UniProtKB Helix 56 58 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JB8 P55210 UniProtKB Beta strand 64 66 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Beta strand 68 74 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Helix 80 82 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Helix 90 104 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Beta strand 106 113 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Helix 116 127 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Helix 131 133 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F1J P55210 UniProtKB Beta strand 137 143 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Beta strand 149 152 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Beta strand 155 158 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Helix 159 163 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Helix 164 166 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Turn 168 170 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Helix 172 174 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Beta strand 179 185 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Beta strand 188 190 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JB8 P55210 UniProtKB Turn 209 211 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR1 P55210 UniProtKB Turn 215 218 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Beta strand 219 225 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Beta strand 227 229 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HQ0 P55210 UniProtKB Beta strand 232 234 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Turn 235 237 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Helix 240 252 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Turn 253 255 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Helix 258 272 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Turn 276 278 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4ZVO P55210 UniProtKB Helix 280 282 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Beta strand 290 293 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2 P55210 UniProtKB Beta strand 296 298 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4JR2