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Caspase-1 (EC 3.4.22.-) [Cleaved into: Caspase-1 subunit p22; Caspase-1 subunit p13]

 CASP1_DROME             Reviewed;         323 AA.
O02002; Q9W1N0;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
13-FEB-2019, entry version 160.
RecName: Full=Caspase-1;
EC=3.4.22.-;
Contains:
RecName: Full=Caspase-1 subunit p22;
Contains:
RecName: Full=Caspase-1 subunit p13;
Flags: Precursor;
Name=Dcp-1; ORFNames=CG5370;
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], AND PROTEIN SEQUENCE OF 216-248.
TISSUE=Embryo;
PubMed=8999799; DOI=10.1126/science.275.5299.536;
Song Z., McCall K., Steller H.;
"DCP-1, a Drosophila cell death protease essential for development.";
Science 275:536-540(1997).
[2]
ERRATUM.
Song Z., McCall K., Steller H.;
Science 277:167-167(1997).
[3]
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).
[4]
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
Celniker S.E.;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Involved in the activation cascade of caspases
responsible for apoptosis execution (By similarity).
Proteolytically cleaves poly(ADP-ribose) polymerase (PARP). Loss
of zygotic DCP-1 function causes larval lethality and melanotic
tumors. {ECO:0000250}.
-!- SUBUNIT: Heterotetramer that consists of two anti-parallel
arranged heterodimers, each one formed by a 22 kDa (p22) and a 13
kDa (p13) subunit.
-!- DEVELOPMENTAL STAGE: Present uniformly throughout embryos of
stages 4 and 10. In stage 16 embryos, the expression becomes
restricted to the central nervous system, the developing gonads,
and a portion of the gut. In stage 17 embryos, expression is
mainly localized in cells along the midline of the central nervous
system.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
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EMBL; AF001464; AAB58237.1; -; mRNA.
EMBL; AE013599; AAF47027.1; -; Genomic_DNA.
EMBL; BT010065; AAQ22534.1; -; mRNA.
RefSeq; NP_476974.1; NM_057626.4.
UniGene; Dm.4849; -.
ProteinModelPortal; O02002; -.
SMR; O02002; -.
BioGrid; 63329; 45.
ELM; O02002; -.
IntAct; O02002; 1.
STRING; 7227.FBpp0071971; -.
MEROPS; C14.016; -.
PaxDb; O02002; -.
PRIDE; O02002; -.
EnsemblMetazoa; FBtr0072062; FBpp0071971; FBgn0010501.
GeneID; 37729; -.
KEGG; dme:Dmel_CG5370; -.
CTD; 37729; -.
FlyBase; FBgn0010501; Dcp-1.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00940000153232; -.
InParanoid; O02002; -.
KO; K20008; -.
OMA; QRNGTDV; -.
OrthoDB; 984395at2759; -.
PhylomeDB; O02002; -.
BRENDA; 3.4.22.36; 1994.
Reactome; R-DME-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-DME-111469; SMAC, XIAP-regulated apoptotic response.
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; Caspase activation via Dependence Receptors in the absence of ligand.
Reactome; R-DME-449836; Other interleukin signaling.
GenomeRNAi; 37729; -.
PRO; PR:O02002; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0010501; Expressed in 57 organ(s), highest expression level in embryo.
Genevisible; O02002; DM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; ISS:FlyBase.
GO; GO:1990124; C:messenger ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0071598; C:neuronal ribonucleoprotein granule; IDA:UniProtKB.
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; IBA:GO_Central.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IMP:FlyBase.
GO; GO:0007015; P:actin filament organization; TAS:FlyBase.
GO; GO:0006915; P:apoptotic process; IDA:FlyBase.
GO; GO:0009267; P:cellular response to starvation; IMP:FlyBase.
GO; GO:0007303; P:cytoplasmic transport, nurse cell to oocyte; TAS:FlyBase.
GO; GO:0097194; P:execution phase of apoptosis; IMP:FlyBase.
GO; GO:0007275; P:multicellular organism development; TAS:FlyBase.
GO; GO:1900074; P:negative regulation of neuromuscular synaptic transmission; IMP:FlyBase.
GO; GO:0016322; P:neuron remodeling; IMP:FlyBase.
GO; GO:0045476; P:nurse cell apoptotic process; IMP:FlyBase.
GO; GO:0048477; P:oogenesis; IMP:FlyBase.
GO; GO:0007300; P:ovarian nurse cell to oocyte transport; TAS:FlyBase.
GO; GO:0010508; P:positive regulation of autophagy; IDA:FlyBase.
GO; GO:0016239; P:positive regulation of macroautophagy; IMP:FlyBase.
GO; GO:0012501; P:programmed cell death; IDA:FlyBase.
GO; GO:0010623; P:programmed cell death involved in cell development; IMP:FlyBase.
CDD; cd00032; CASc; 1.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR002398; Pept_C14.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PANTHER; PTHR10454; PTHR10454; 1.
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;
Apoptosis; Complete proteome; Direct protein sequencing; Hydrolase;
Protease; Reference proteome; Thiol protease; Zymogen.
PROPEP 1 33 {ECO:0000305}.
/FTId=PRO_0000004662.
CHAIN 34 202 Caspase-1 subunit p22.
/FTId=PRO_0000004663.
PROPEP 203 215 {ECO:0000269|PubMed:8999799}.
/FTId=PRO_0000004664.
CHAIN 216 323 Caspase-1 subunit p13.
/FTId=PRO_0000004665.
ACT_SITE 154 154 {ECO:0000250}.
ACT_SITE 196 196 {ECO:0000250}.
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


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