CASP1_DROME
ID CASP1_DROME Reviewed; 323 AA.
AC O02002; Q9W1N0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Caspase-1;
DE EC=3.4.22.-;
DE Contains:
DE RecName: Full=Caspase-1 subunit p22;
DE Contains:
DE RecName: Full=Caspase-1 subunit p13;
DE Flags: Precursor;
GN Name=Dcp-1; ORFNames=CG5370;
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], AND PROTEIN SEQUENCE OF 216-248.
RC TISSUE=Embryo;
RX PubMed=8999799; DOI=10.1126/science.275.5299.536;
RA Song Z., McCall K., Steller H.;
RT "DCP-1, a Drosophila cell death protease essential for development.";
RL Science 275:536-540(1997).
RN [2]
RP ERRATUM OF PUBMED:8999799.
RA Song Z., McCall K., Steller H.;
RL Science 277:167-167(1997).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the activation cascade of caspases responsible
CC for apoptosis execution (By similarity). Proteolytically cleaves
CC poly(ADP-ribose) polymerase (PARP). Loss of zygotic DCP-1 function
CC causes larval lethality and melanotic tumors. {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged
CC heterodimers, each one formed by a 22 kDa (p22) and a 13 kDa (p13)
CC subunit.
CC -!- DEVELOPMENTAL STAGE: Present uniformly throughout embryos of stages 4
CC and 10. In stage 16 embryos, the expression becomes restricted to the
CC central nervous system, the developing gonads, and a portion of the
CC gut. In stage 17 embryos, expression is mainly localized in cells along
CC the midline of the central nervous system.
CC -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
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DR EMBL; AF001464; AAB58237.1; -; mRNA.
DR EMBL; AE013599; AAF47027.1; -; Genomic_DNA.
DR EMBL; BT010065; AAQ22534.1; -; mRNA.
DR RefSeq; NP_476974.1; NM_057626.4.
DR AlphaFoldDB; O02002; -.
DR SMR; O02002; -.
DR BioGRID; 63329; 46.
DR ELM; O02002; -.
DR IntAct; O02002; 1.
DR STRING; 7227.FBpp0071971; -.
DR MEROPS; C14.016; -.
DR PaxDb; O02002; -.
DR PRIDE; O02002; -.
DR EnsemblMetazoa; FBtr0072062; FBpp0071971; FBgn0010501.
DR GeneID; 37729; -.
DR KEGG; dme:Dmel_CG5370; -.
DR CTD; 37729; -.
DR FlyBase; FBgn0010501; Dcp-1.
DR VEuPathDB; VectorBase:FBgn0010501; -.
DR eggNOG; KOG3573; Eukaryota.
DR GeneTree; ENSGT00940000153232; -.
DR HOGENOM; CLU_036904_2_0_1; -.
DR InParanoid; O02002; -.
DR OMA; HEFFDIP; -.
DR OrthoDB; 984395at2759; -.
DR PhylomeDB; O02002; -.
DR BRENDA; 3.4.22.36; 1994.
DR Reactome; R-DME-198323; AKT phosphorylates targets in the cytosol.
DR Reactome; R-DME-448706; Interleukin-1 processing.
DR BioGRID-ORCS; 37729; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 37729; -.
DR PRO; PR:O02002; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0010501; Expressed in wing disc and 57 other tissues.
DR Genevisible; O02002; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:FlyBase.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; IDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IMP:FlyBase.
DR GO; GO:0006915; P:apoptotic process; IDA:FlyBase.
DR GO; GO:0009267; P:cellular response to starvation; IMP:FlyBase.
DR GO; GO:0007303; P:cytoplasmic transport, nurse cell to oocyte; TAS:FlyBase.
DR GO; GO:0097194; P:execution phase of apoptosis; IMP:FlyBase.
DR GO; GO:0007275; P:multicellular organism development; TAS:FlyBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IGI:FlyBase.
DR GO; GO:1900074; P:negative regulation of neuromuscular synaptic transmission; IMP:FlyBase.
DR GO; GO:0016322; P:neuron remodeling; IMP:FlyBase.
DR GO; GO:0045476; P:nurse cell apoptotic process; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0007300; P:ovarian nurse cell to oocyte transport; TAS:FlyBase.
DR GO; GO:0010508; P:positive regulation of autophagy; IDA:FlyBase.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IMP: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; IEA:UniProtKB-KW.
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 Apoptosis; Direct protein sequencing; Hydrolase; Protease;
KW Reference proteome; Thiol protease; Zymogen.
FT PROPEP 1..33
FT /evidence="ECO:0000305"
FT /id="PRO_0000004662"
FT CHAIN 34..202
FT /note="Caspase-1 subunit p22"
FT /id="PRO_0000004663"
FT PROPEP 203..215
FT /evidence="ECO:0000269|PubMed:8999799"
FT /id="PRO_0000004664"
FT CHAIN 216..323
FT /note="Caspase-1 subunit p13"
FT /id="PRO_0000004665"
FT ACT_SITE 154
FT /evidence="ECO:0000250"
FT ACT_SITE 196
FT /evidence="ECO:0000250"
SQ SEQUENCE 323 AA; 35927 MW; B5FF0FF75EB8E2BD CRC64;
MTDECVTRNY GVGIRSPNGS ENRGSFIMAD NTDAKGCTPE SLVVGGATAA SPLPANKFVA
RMPVERYASE YNMSHKHRGV ALIFNHEFFD IPSLKSRTGT NVDAQELKKA FENLGFAVSV
HKDCKLRDIL KHVGKAAELD HTDNDCLAVA ILSHGEHGYL YAKDTQYKLD NIWHYFTATF
CPSLAGKPKL FFIQACQGDR LDGGITLEKG VTETDGESST SYKIPIHADF LFSYSTIPGY
FSWRNINNGS WYMQSLIREL NANGKKYDLL TLLTFVNQRV ALDFESNVPA TPMMDRQKQI
PCLTSMLTRI LRFGDKPNGN KAG
