DRICE_DROME
ID DRICE_DROME Reviewed; 339 AA.
AC O01382; Q9VAH1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Caspase;
DE EC=3.4.22.-;
DE AltName: Full=drICE;
DE Contains:
DE RecName: Full=Caspase subunit p21;
DE Contains:
DE RecName: Full=Caspase subunit p12;
DE Flags: Precursor;
GN Name=Drice; Synonyms=ICE; ORFNames=CG7788;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=9184225; DOI=10.1093/emboj/16.10.2805;
RA Fraser A.G., Evan G.I.;
RT "Identification of a Drosophila melanogaster ICE/CED-3-related protease,
RT drICE.";
RL EMBO J. 16:2805-2813(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP HOMODIMERIZATION, AND INTERACTION WITH DRONC.
RC TISSUE=Embryo;
RX PubMed=10675329; DOI=10.1093/emboj/19.4.598;
RA Meier P., Silke J., Leevers S.J., Evan G.I.;
RT "The Drosophila caspase DRONC is regulated by DIAP1.";
RL EMBO J. 19:598-611(2000).
RN [6]
RP INTERACTION WITH DIAP2, AND MUTAGENESIS OF ALA-29 AND CYS-211.
RX PubMed=18166655; DOI=10.1083/jcb.200706027;
RA Ribeiro P.S., Kuranaga E., Tenev T., Leulier F., Miura M., Meier P.;
RT "DIAP2 functions as a mechanism-based regulator of drICE that contributes
RT to the caspase activity threshold in living cells.";
RL J. Cell Biol. 179:1467-1480(2007).
CC -!- FUNCTION: Involved in the activation cascade of caspases responsible
CC for apoptosis execution. Acts downstream of rpr. Cleaves baculovirus
CC p35 and lamin DmO in vitro.
CC -!- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged
CC heterodimers, each one formed by a 21 kDa (p21) and a 12 kDa (p12)
CC subunit. Inactive pro-form can homodimerize. Dronc and Drice can form a
CC stable complex (PubMed:10675329). Interacts with Diap2 (via BIR3
CC domain) to form a stable complex (PubMed:18166655).
CC {ECO:0000269|PubMed:10675329, ECO:0000269|PubMed:18166655}.
CC -!- INTERACTION:
CC O01382; Q9XYF4: Dronc; NbExp=3; IntAct=EBI-91422, EBI-108311;
CC -!- DEVELOPMENTAL STAGE: Expressed at all stages where apoptosis occurs.
CC -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
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DR EMBL; Y12261; CAA72937.1; -; mRNA.
DR EMBL; AE014297; AAF56939.1; -; Genomic_DNA.
DR EMBL; AY058451; AAL13680.1; -; mRNA.
DR RefSeq; NP_524551.2; NM_079827.3.
DR PDB; 3SIP; X-ray; 3.50 A; A/C=78-230, B/D=231-339.
DR PDB; 3SIR; X-ray; 2.68 A; A/B/C/D=78-332.
DR PDBsum; 3SIP; -.
DR PDBsum; 3SIR; -.
DR AlphaFoldDB; O01382; -.
DR SMR; O01382; -.
DR BioGRID; 68378; 24.
DR DIP; DIP-21838N; -.
DR ELM; O01382; -.
DR IntAct; O01382; 2.
DR MINT; O01382; -.
DR STRING; 7227.FBpp0084848; -.
DR MEROPS; C14.015; -.
DR PaxDb; O01382; -.
DR PRIDE; O01382; -.
DR EnsemblMetazoa; FBtr0085482; FBpp0084848; FBgn0019972.
DR GeneID; 43514; -.
DR KEGG; dme:Dmel_CG7788; -.
DR CTD; 43514; -.
DR FlyBase; FBgn0019972; Drice.
DR VEuPathDB; VectorBase:FBgn0019972; -.
DR eggNOG; KOG3573; Eukaryota.
DR GeneTree; ENSGT00940000153232; -.
DR HOGENOM; CLU_036904_2_0_1; -.
DR InParanoid; O01382; -.
DR OMA; MQRSQTE; -.
DR OrthoDB; 984395at2759; -.
DR PhylomeDB; O01382; -.
DR Reactome; R-DME-198323; AKT phosphorylates targets in the cytosol.
DR Reactome; R-DME-448706; Interleukin-1 processing.
DR SignaLink; O01382; -.
DR BioGRID-ORCS; 43514; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43514; -.
DR PRO; PR:O01382; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0019972; Expressed in cleaving embryo and 32 other tissues.
DR Genevisible; O01382; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:1990525; F:BIR domain binding; IPI:FlyBase.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:FlyBase.
DR GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IDA:FlyBase.
DR GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IDA:FlyBase.
DR GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IGI:FlyBase.
DR GO; GO:0016322; P:neuron remodeling; IMP:FlyBase.
DR GO; GO:0045476; P:nurse cell apoptotic process; IGI:FlyBase.
DR GO; GO:0046672; P:positive regulation of compound eye retinal cell programmed cell death; IMP:FlyBase.
DR GO; GO:2001269; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IDA:FlyBase.
DR GO; GO:0012501; P:programmed cell death; IDA:FlyBase.
DR GO; GO:0010623; P:programmed cell death involved in cell development; IMP:FlyBase.
DR GO; GO:0006508; P:proteolysis; IDA:FlyBase.
DR GO; GO:0010165; P:response to X-ray; IMP:FlyBase.
DR GO; GO:0035070; P:salivary gland histolysis; IMP:FlyBase.
DR GO; GO:0048515; P:spermatid differentiation; IMP:FlyBase.
DR GO; GO:0035103; P:sterol regulatory element binding protein cleavage; IDA:FlyBase.
DR CDD; cd00032; CASc; 1.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR033139; Caspase_cys_AS.
DR InterPro; IPR016129; Caspase_his_AS.
DR InterPro; IPR002398; Pept_C14.
DR InterPro; IPR002138; Pept_C14_p10.
DR InterPro; IPR001309; Pept_C14_p20.
DR InterPro; IPR015917; Pept_C14A.
DR PANTHER; PTHR10454; PTHR10454; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00115; CASc; 1.
DR SUPFAM; SSF52129; SSF52129; 1.
DR PROSITE; PS01122; CASPASE_CYS; 1.
DR PROSITE; PS01121; CASPASE_HIS; 1.
DR PROSITE; PS50207; CASPASE_P10; 1.
DR PROSITE; PS50208; CASPASE_P20; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Hydrolase; Protease; Reference proteome;
KW Thiol protease; Zymogen.
FT PROPEP 1..28
FT /evidence="ECO:0000250"
FT /id="PRO_0000004666"
FT CHAIN 29..217
FT /note="Caspase subunit p21"
FT /evidence="ECO:0000250"
FT /id="PRO_0000004667"
FT PROPEP 218..230
FT /evidence="ECO:0000250"
FT /id="PRO_0000004668"
FT CHAIN 231..339
FT /note="Caspase subunit p12"
FT /evidence="ECO:0000250"
FT /id="PRO_0000004669"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 169
FT /evidence="ECO:0000250"
FT ACT_SITE 211
FT /evidence="ECO:0000250"
FT MUTAGEN 29
FT /note="A->V: Abolishes binding to Diap2 but has no effect
FT on Drice processing or activity."
FT /evidence="ECO:0000269|PubMed:18166655"
FT MUTAGEN 211
FT /note="C->A: No effect on binding to Diap2 but may affect
FT stability of complex formed with Diap2."
FT /evidence="ECO:0000269|PubMed:18166655"
FT CONFLICT 151
FT /note="A -> S (in Ref. 1; CAA72937)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="S -> T (in Ref. 1; CAA72937)"
FT /evidence="ECO:0000305"
FT STRAND 90..101
FT /evidence="ECO:0007829|PDB:3SIR"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:3SIP"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:3SIR"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:3SIR"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:3SIR"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:3SIP"
FT STRAND 159..168
FT /evidence="ECO:0007829|PDB:3SIR"
FT HELIX 180..186
FT /evidence="ECO:0007829|PDB:3SIR"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:3SIR"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:3SIR"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:3SIR"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:3SIR"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:3SIR"
FT STRAND 245..252
FT /evidence="ECO:0007829|PDB:3SIR"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:3SIP"
FT HELIX 266..278
FT /evidence="ECO:0007829|PDB:3SIR"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:3SIR"
FT HELIX 284..296
FT /evidence="ECO:0007829|PDB:3SIR"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:3SIP"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:3SIR"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:3SIR"
SQ 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
