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Caspase (EC 3.4.22.-) (drICE) [Cleaved into: Caspase subunit p21; Caspase subunit p12]

 DRICE_DROME             Reviewed;         339 AA.
O01382; Q9VAH1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
28-MAR-2018, entry version 164.
RecName: Full=Caspase;
EC=3.4.22.-;
AltName: Full=drICE;
Contains:
RecName: Full=Caspase subunit p21;
Contains:
RecName: Full=Caspase subunit p12;
Flags: Precursor;
Name=Drice; Synonyms=ICE; ORFNames=CG7788;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Embryo;
PubMed=9184225; DOI=10.1093/emboj/16.10.2805;
Fraser A.G., Evan G.I.;
"Identification of a Drosophila melanogaster ICE/CED-3-related
protease, drICE.";
EMBO J. 16:2805-2813(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
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).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Head;
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).
[5]
HOMODIMERIZATION, AND INTERACTION WITH DRONC.
TISSUE=Embryo;
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).
[6]
INTERACTION WITH DIAP2, AND MUTAGENESIS OF ALA-29 AND CYS-211.
PubMed=18166655; DOI=10.1083/jcb.200706027;
Ribeiro P.S., Kuranaga E., Tenev T., Leulier F., Miura M., Meier P.;
"DIAP2 functions as a mechanism-based regulator of drICE that
contributes to the caspase activity threshold in living cells.";
J. Cell Biol. 179:1467-1480(2007).
-!- FUNCTION: Involved in the activation cascade of caspases
responsible for apoptosis execution. Acts downstream of rpr.
Cleaves baculovirus p35 and lamin DmO in vitro.
-!- SUBUNIT: Heterotetramer that consists of two anti-parallel
arranged heterodimers, each one formed by a 21 kDa (p21) and a 12
kDa (p12) subunit. Inactive pro-form can homodimerize. Dronc and
Drice can form a stable complex (PubMed:10675329). Interacts with
Diap2 (via BIR3 domain) to form a stable complex
(PubMed:18166655). {ECO:0000269|PubMed:10675329,
ECO:0000269|PubMed:18166655}.
-!- INTERACTION:
Q9XYF4:Dronc; NbExp=4; IntAct=EBI-91422, EBI-108311;
-!- DEVELOPMENTAL STAGE: Expressed at all stages where apoptosis
occurs.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y12261; CAA72937.1; -; mRNA.
EMBL; AE014297; AAF56939.1; -; Genomic_DNA.
EMBL; AY058451; AAL13680.1; -; mRNA.
RefSeq; NP_524551.2; NM_079827.3.
UniGene; Dm.2333; -.
PDB; 3SIP; X-ray; 3.50 A; A/C=78-230, B/D=231-339.
PDB; 3SIR; X-ray; 2.68 A; A/B/C/D=78-332.
PDBsum; 3SIP; -.
PDBsum; 3SIR; -.
ProteinModelPortal; O01382; -.
SMR; O01382; -.
BioGrid; 68378; 25.
DIP; DIP-21838N; -.
ELM; O01382; -.
IntAct; O01382; 5.
MINT; O01382; -.
STRING; 7227.FBpp0084848; -.
MEROPS; C14.015; -.
PaxDb; O01382; -.
PRIDE; O01382; -.
EnsemblMetazoa; FBtr0085482; FBpp0084848; FBgn0019972.
GeneID; 43514; -.
KEGG; dme:Dmel_CG7788; -.
CTD; 43514; -.
FlyBase; FBgn0019972; Drice.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00760000118912; -.
InParanoid; O01382; -.
KO; K04397; -.
OMA; SGSWFVQ; -.
OrthoDB; EOG091G05YD; -.
PhylomeDB; O01382; -.
Reactome; R-DME-111459; Activation of caspases through apoptosome-mediated cleavage.
Reactome; R-DME-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-DME-2028269; Signaling by Hippo.
Reactome; R-DME-211227; Activation of DNA fragmentation factor.
Reactome; R-DME-264870; Caspase-mediated cleavage of cytoskeletal proteins.
Reactome; R-DME-351906; Apoptotic cleavage of cell adhesion proteins.
Reactome; R-DME-352238; Breakdown of the nuclear lamina.
Reactome; R-DME-418889; Ligand-independent caspase activation via DCC.
Reactome; R-DME-449836; Other interleukin signaling.
GenomeRNAi; 43514; -.
PRO; PR:O01382; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0019972; -.
Genevisible; O01382; DM.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:1990525; F:BIR domain binding; IPI:FlyBase.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:FlyBase.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IDA:FlyBase.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IDA:FlyBase.
GO; GO:0006915; P:apoptotic process; TAS: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:0006508; P:proteolysis; IDA:FlyBase.
GO; GO:0046668; P:regulation of retinal cell programmed cell death; NAS:FlyBase.
GO; GO:0010165; P:response to X-ray; IMP:FlyBase.
GO; GO:0035070; P:salivary gland histolysis; IMP:FlyBase.
GO; GO:0048515; P:spermatid differentiation; IMP:FlyBase.
GO; GO:0035103; P:sterol regulatory element binding protein cleavage; IDA:FlyBase.
CDD; cd00032; CASc; 1.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00115; CASc; 1.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS01122; CASPASE_CYS; 1.
PROSITE; PS01121; CASPASE_HIS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Complete proteome; Hydrolase; Protease;
Reference proteome; Thiol protease; Zymogen.
PROPEP 1 28 {ECO:0000250}.
/FTId=PRO_0000004666.
CHAIN 29 217 Caspase subunit p21. {ECO:0000250}.
/FTId=PRO_0000004667.
PROPEP 218 230 {ECO:0000250}.
/FTId=PRO_0000004668.
CHAIN 231 339 Caspase subunit p12. {ECO:0000250}.
/FTId=PRO_0000004669.
ACT_SITE 169 169 {ECO:0000250}.
ACT_SITE 211 211 {ECO:0000250}.
MUTAGEN 29 29 A->V: Abolishes binding to Diap2 but has
no effect on Drice processing or
activity. {ECO:0000269|PubMed:18166655}.
MUTAGEN 211 211 C->A: No effect on binding to Diap2 but
may effect stability of complex formed
with Diap2.
{ECO:0000269|PubMed:18166655}.
CONFLICT 151 151 A -> S (in Ref. 1; CAA72937).
{ECO:0000305}.
CONFLICT 265 265 S -> T (in Ref. 1; CAA72937).
{ECO:0000305}.
STRAND 90 101 {ECO:0000244|PDB:3SIR}.
STRAND 105 108 {ECO:0000244|PDB:3SIP}.
HELIX 118 128 {ECO:0000244|PDB:3SIR}.
STRAND 132 138 {ECO:0000244|PDB:3SIR}.
HELIX 141 152 {ECO:0000244|PDB:3SIR}.
HELIX 156 158 {ECO:0000244|PDB:3SIP}.
STRAND 159 168 {ECO:0000244|PDB:3SIR}.
HELIX 180 186 {ECO:0000244|PDB:3SIR}.
HELIX 189 191 {ECO:0000244|PDB:3SIR}.
TURN 193 195 {ECO:0000244|PDB:3SIR}.
HELIX 197 199 {ECO:0000244|PDB:3SIR}.
STRAND 200 202 {ECO:0000244|PDB:3SIR}.
STRAND 204 211 {ECO:0000244|PDB:3SIR}.
STRAND 245 252 {ECO:0000244|PDB:3SIR}.
TURN 261 263 {ECO:0000244|PDB:3SIP}.
HELIX 266 278 {ECO:0000244|PDB:3SIR}.
TURN 279 281 {ECO:0000244|PDB:3SIR}.
HELIX 284 296 {ECO:0000244|PDB:3SIR}.
HELIX 307 309 {ECO:0000244|PDB:3SIP}.
STRAND 317 320 {ECO:0000244|PDB:3SIR}.
STRAND 323 325 {ECO:0000244|PDB:3SIR}.
SEQUENCE 339 AA; 37363 MW; E105ED29518507EC CRC64;
MDATNNGESA DQVGIRVGNP EQPNDHTDAL GSVGSGGAGS SGLVAGSSHP YGSGAIGQLA
NGYSSPSSSY RKNVAKMVTD RHAAEYNMRH KNRGMALIFN HEHFEVPTLK SRAGTNVDCE
NLTRVLKQLD FEVTVYKDCR YKDILRTIEY AASQNHSDSD CILVAILSHG EMGYIYAKDT
QYKLDNIWSF FTANHCPSLA GKPKLFFIQA CQGDRLDGGV TMQRSQTETD GDSSMSYKIP
VHADFLIAYS TVPGFYSWRN TTRGSWFMQS LCAELAANGK RLDILTLLTF VCQRVAVDFE
SCTPDTPEMH QQKQIPCITT MLTRILRFSD KQLAPAGRV


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