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Caspase Dronc (EC 3.4.22.-) (NEDD2-like caspase) [Cleaved into: Caspase Nc subunit 1; Caspase Nc subunit 2]

 DRONC_DROME             Reviewed;         450 AA.
Q9XYF4;
23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
22-NOV-2017, entry version 159.
RecName: Full=Caspase Dronc;
EC=3.4.22.-;
AltName: Full=NEDD2-like caspase;
Contains:
RecName: Full=Caspase Nc subunit 1;
Contains:
RecName: Full=Caspase Nc subunit 2;
Flags: Precursor;
Name=Dronc {ECO:0000312|FlyBase:FBgn0026404};
Synonyms=Nc {ECO:0000312|EMBL:AAF50180.1};
ORFNames=CG8091 {ECO:0000312|FlyBase:FBgn0026404};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000305, ECO:0000312|EMBL:AAD26625.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND INDUCTION.
TISSUE=Embryo {ECO:0000269|PubMed:10200258};
PubMed=10200258; DOI=10.1073/pnas.96.8.4307;
Dorstyn L., Colussi P.A., Quinn L.M., Richardson H., Kumar S.;
"DRONC, an ecdysone-inducible Drosophila caspase.";
Proc. Natl. Acad. Sci. U.S.A. 96:4307-4312(1999).
[2] {ECO:0000305, ECO:0000312|EMBL:CAB53565.1}
NUCLEOTIDE SEQUENCE, FUNCTION, AND INTERACTION WITH DRICE AND DIAP1.
TISSUE=Embryo {ECO:0000269|PubMed:10675329};
PubMed=10675329; DOI=10.1093/emboj/19.4.598;
Meier P., Silke J., Leevers S.J., Evan G.I.;
"The Drosophila caspase DRONC is regulated by DIAP1.";
EMBO J. 19:598-611(2000).
[3] {ECO:0000312|EMBL:AAF50180.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4] {ECO:0000305, ECO:0000312|EMBL:AAF50180.1}
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5] {ECO:0000312|EMBL:AAL13976.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
TISSUE=Larva {ECO:0000269|PubMed:12537569}, and
Pupae {ECO:0000269|PubMed:12537569};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
FUNCTION.
PubMed=10984473; DOI=10.1074/jbc.M002935200;
Quinn L.M., Dorstyn L., Mills K., Colussi P.A., Chen P., Coombe M.,
Abrams J., Kumar S., Richardson H.;
"An essential role for the caspase dronc in developmentally programmed
cell death in Drosophila.";
J. Biol. Chem. 275:40416-40424(2000).
[7]
UBIQUITINATION AND SUBSEQUENT DEGRADATION.
PubMed=12021771; DOI=10.1038/ncb799;
Wilson R., Goyal L., Ditzel M., Zachariou A., Baker D.A., Agapite J.,
Steller H., Meier P.;
"The DIAP1 RING finger mediates ubiquitination of Dronc and is
indispensable for regulating apoptosis.";
Nat. Cell Biol. 4:445-450(2002).
[8] {ECO:0000305}
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 114-125 IN COMPLEX WITH
DIAP1, FUNCTION, AND MUTAGENESIS OF PHE-118.
PubMed=14517550; DOI=10.1038/nsb989;
Chai J., Yan N., Huh J.R., Wu J.-W., Li W., Hay B.A., Shi Y.;
"Molecular mechanism of Reaper-Grim-Hid-mediated suppression of DIAP1-
dependent Dronc ubiquitination.";
Nat. Struct. Biol. 10:892-898(2003).
-!- FUNCTION: Involved in the activation cascade of caspases
responsible for apoptosis execution. Effector of steroid-mediated
apoptosis during insect metamorphosis. Overexpression promotes
programmed cell death. Interaction with Diap1 is required to
suppress Dronc-mediated cell death; via Diap1-mediated
ubiquitination of Dronc. Rate-limiting caspase in rpr and hid
death pathway. {ECO:0000269|PubMed:10200258,
ECO:0000269|PubMed:10675329, ECO:0000269|PubMed:10984473,
ECO:0000269|PubMed:14517550}.
-!- SUBUNIT: Interacts with Diap1; residues 114-125 interact with the
second BIR domain of Diap1. Can form a stable complex with Drice.
Rpr can out-compete Dronc for binding Diap1, therefore removing
Diap1-mediated ubiquitination. {ECO:0000269|PubMed:10675329,
ECO:0000269|PubMed:14517550}.
-!- INTERACTION:
Q7KLI1:Dark; NbExp=3; IntAct=EBI-108311, EBI-3404349;
Q24306:Diap1; NbExp=9; IntAct=EBI-108311, EBI-456419;
O01382:Drice; NbExp=3; IntAct=EBI-108311, EBI-91422;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed in embryos during early
stages of development. In late third instar larvae, dramatic up-
regulation in salivary glands and midgut before histolysis of
these tissues. {ECO:0000269|PubMed:10200258}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
{ECO:0000269|PubMed:10200258}.
-!- INDUCTION: By ecdysone; exposure of salivary glands and midgut
isolated from second instar larvae results in a massive increase
in levels. {ECO:0000269|PubMed:10200258}.
-!- PTM: Ubiquitinated by Diap1, leading to its subsequent
degradation. {ECO:0000269|PubMed:12021771}.
-!- MISCELLANEOUS: The promiscuous caspase inhibitor p35 is neither
cleaved by Dronc in vitro nor blocks Dronc activity in vivo.
{ECO:0000269|PubMed:10675329}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF104357; AAD26625.1; -; mRNA.
EMBL; AJ242796; CAB53565.1; -; mRNA.
EMBL; AE014296; AAF50180.1; -; Genomic_DNA.
EMBL; AY058747; AAL13976.1; -; mRNA.
RefSeq; NP_524017.1; NM_079293.4.
UniGene; Dm.3230; -.
PDB; 1Q4Q; X-ray; 2.10 A; K/L/M/N/O/P/Q/R/S/T=114-125.
PDB; 2FP3; X-ray; 2.50 A; A=136-450.
PDB; 3J9K; EM; 4.10 A; B/D/F/H/J/L/N/P/R/T/V/X/Z/b/d/f=1-450.
PDBsum; 1Q4Q; -.
PDBsum; 2FP3; -.
PDBsum; 3J9K; -.
ProteinModelPortal; Q9XYF4; -.
SMR; Q9XYF4; -.
BioGrid; 64560; 56.
DIP; DIP-31484N; -.
IntAct; Q9XYF4; 4.
MINT; MINT-8048660; -.
STRING; 7227.FBpp0076076; -.
MEROPS; C14.019; -.
iPTMnet; Q9XYF4; -.
PaxDb; Q9XYF4; -.
PRIDE; Q9XYF4; -.
EnsemblMetazoa; FBtr0076347; FBpp0076076; FBgn0026404.
GeneID; 39173; -.
KEGG; dme:Dmel_CG8091; -.
CTD; 39173; -.
FlyBase; FBgn0026404; Dronc.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00760000118912; -.
InParanoid; Q9XYF4; -.
KO; K20009; -.
OMA; VMVLMTH; -.
OrthoDB; EOG091G0XCA; -.
PhylomeDB; Q9XYF4; -.
Reactome; R-DME-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-DME-448706; Interleukin-1 processing.
EvolutionaryTrace; Q9XYF4; -.
GenomeRNAi; 39173; -.
PRO; PR:Q9XYF4; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0026404; -.
Genevisible; Q9XYF4; DM.
GO; GO:0043293; C:apoptosome; IDA:FlyBase.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0050700; F:CARD domain binding; ISM:FlyBase.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:FlyBase.
GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IDA:FlyBase.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IBA:GO_Central.
GO; GO:0004175; F:endopeptidase activity; IDA:FlyBase.
GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:FlyBase.
GO; GO:0006915; P:apoptotic process; IMP:FlyBase.
GO; GO:0007417; P:central nervous system development; IMP:FlyBase.
GO; GO:0048749; P:compound eye development; IMP:FlyBase.
GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
GO; GO:0035234; P:ectopic germ cell programmed cell death; IMP:FlyBase.
GO; GO:0001700; P:embryonic development via the syncytial blastoderm; TAS:FlyBase.
GO; GO:0097194; P:execution phase of apoptosis; IBA:GO_Central.
GO; GO:0008258; P:head involution; IMP:FlyBase.
GO; GO:0007516; P:hemocyte development; IMP:FlyBase.
GO; GO:0035006; P:melanization defense response; IMP:FlyBase.
GO; GO:0007552; P:metamorphosis; TAS:FlyBase.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:FlyBase.
GO; GO:0016322; P:neuron remodeling; IMP:FlyBase.
GO; GO:0045476; P:nurse cell apoptotic process; IGI:FlyBase.
GO; GO:0046672; P:positive regulation of compound eye retinal cell programmed cell death; IMP:FlyBase.
GO; GO:2001269; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IDA:FlyBase.
GO; GO:0012501; P:programmed cell death; IDA:FlyBase.
GO; GO:0010623; P:programmed cell death involved in cell development; IMP:FlyBase.
GO; GO:0016540; P:protein autoprocessing; IDA:FlyBase.
GO; GO:0051291; P:protein heterooligomerization; IDA:FlyBase.
GO; GO:0010506; P:regulation of autophagy; IGI:FlyBase.
GO; GO:0010941; P:regulation of cell death; IMP:FlyBase.
GO; GO:0046668; P:regulation of retinal cell programmed cell death; NAS:FlyBase.
GO; GO:0035070; P:salivary gland histolysis; IMP:FlyBase.
GO; GO:0007423; P:sensory organ development; IMP:FlyBase.
GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
GO; GO:0031638; P:zymogen activation; IDA:FlyBase.
CDD; cd00032; CASc; 1.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00115; CASc; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS01122; CASPASE_CYS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Complete proteome; Cytoplasm; Hydrolase;
Protease; Reference proteome; Thiol protease; Ubl conjugation;
Zymogen.
PROPEP 1 134 {ECO:0000303|PubMed:10200258}.
/FTId=PRO_0000004670.
CHAIN 135 320 Caspase Nc subunit 1.
/FTId=PRO_0000004671.
PROPEP 321 324 {ECO:0000303|PubMed:10200258}.
/FTId=PRO_0000004672.
CHAIN 325 450 Caspase Nc subunit 2.
/FTId=PRO_0000004673.
DOMAIN 64 109 CARD. {ECO:0000255}.
REGION 114 125 Required for binding th.
ACT_SITE 271 271 {ECO:0000250|UniProtKB:P29466}.
ACT_SITE 318 318 {ECO:0000250|UniProtKB:P29466}.
MUTAGEN 118 118 F->E: Disrupts interaction with Diap1.
{ECO:0000269|PubMed:14517550}.
STRAND 195 202 {ECO:0000244|PDB:2FP3}.
HELIX 216 229 {ECO:0000244|PDB:2FP3}.
STRAND 232 237 {ECO:0000244|PDB:2FP3}.
HELIX 242 253 {ECO:0000244|PDB:2FP3}.
HELIX 256 260 {ECO:0000244|PDB:2FP3}.
STRAND 264 270 {ECO:0000244|PDB:2FP3}.
STRAND 280 282 {ECO:0000244|PDB:2FP3}.
STRAND 288 290 {ECO:0000244|PDB:2FP3}.
HELIX 291 296 {ECO:0000244|PDB:2FP3}.
TURN 300 302 {ECO:0000244|PDB:2FP3}.
HELIX 304 306 {ECO:0000244|PDB:2FP3}.
STRAND 311 316 {ECO:0000244|PDB:2FP3}.
STRAND 366 371 {ECO:0000244|PDB:2FP3}.
TURN 380 382 {ECO:0000244|PDB:2FP3}.
HELIX 385 400 {ECO:0000244|PDB:2FP3}.
TURN 401 403 {ECO:0000244|PDB:2FP3}.
HELIX 406 418 {ECO:0000244|PDB:2FP3}.
STRAND 419 423 {ECO:0000244|PDB:2FP3}.
STRAND 425 427 {ECO:0000244|PDB:2FP3}.
STRAND 431 436 {ECO:0000244|PDB:2FP3}.
SEQUENCE 450 AA; 51141 MW; 640A9725202A7E65 CRC64;
MQPPELEIGM PKRHREHIRK NLNILVEWTN YERLAMECVQ QGILTVQMLR NTQDLNGKPF
NMDEKDVRVE QHRRLLLKIT QRGPTAYNLL INALRNINCL DAAVLLESVD ESDSRPPFIS
LNERRTSRKS ADIVDTPSPE ASEGPCVSKL RNEPLGALTP YVGVVDGPEV KKSKKIHGGD
SAILGTYKMQ SRFNRGVLLM VNIMDYPDQN RRRIGAEKDS KSLIHLFQEL NFTIFPYGNV
NQDQFFKLLT MVTSSSYVQN TECFVMVLMT HGNSVEGKEK VEFCDGSVVD MQKIKDHFQT
AKCPYLVNKP KVLMFPFCRG DEYDLGHPKN QGNLMEPVYT AQEEKWPDTQ TEGIPSPSTN
VPSLADTLVC YANTPGYVTH RDLDTGSWYI QKFCQVMADH AHDTDLEDIL KKTSEAVGNK
RTKKGSMQTG AYDNLGFNKK LYFNPGFFNE


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