O02002 (CASP1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Caspase-1
EC=3.4.22.-

Cleaved into the following 2 chains:

1. Caspase-1 subunit p22
2. Caspase-1 subunit p13

Gene names

Name:	Dcp-1
ORF Names:	CG5370

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	323 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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.
Subunit structure	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.
Sequence similarities	Belongs to the peptidase C14A family.

Ontologies

Keywords
Biological process	Apoptosis
Molecular function	Hydrolase Protease Thiol protease
PTM	Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	actin filament organization Traceable author statement PubMed 11139280. Source: FlyBase cleavage of lamin involved in execution phase of apoptosis Inferred from mutant phenotype PubMed 9422696. Source: FlyBase cytoplasmic transport, nurse cell to oocyte Traceable author statement PubMed 11139276PubMed 11139280. Source: FlyBase developmental programmed cell death Inferred from mutant phenotype PubMed 16980627. Source: FlyBase embryo development Inferred from mutant phenotype Ref.1. Source: FlyBase negative regulation of neuromuscular synaptic transmission Inferred from mutant phenotype PubMed 22153373. Source: FlyBase neuron remodeling Inferred from mutant phenotype PubMed 20445064. Source: FlyBase nurse cell apoptotic process Inferred from genetic interaction PubMed 17464325. Source: FlyBase salivary gland cell autophagic cell death Inferred from expression pattern PubMed 12593804. Source: FlyBase
Molecular_function	cysteine-type endopeptidase activity Inferred from direct assay Ref.1. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 33	33	Probable		PRO_0000004662
	Chain	34 – 202	169	Caspase-1 subunit p22		PRO_0000004663
	Propeptide	203 – 215	13			PRO_0000004664
	Chain	216 – 323	108	Caspase-1 subunit p13		PRO_0000004665
Sites
	Active site	154	1	By similarity
	Active site	196	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	O02002 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: B5FF0FF75EB8E2BD	FASTA	323	35,927
	10 20 30 40 50 60 MTDECVTRNY GVGIRSPNGS ENRGSFIMAD NTDAKGCTPE SLVVGGATAA SPLPANKFVA 70 80 90 100 110 120 RMPVERYASE YNMSHKHRGV ALIFNHEFFD IPSLKSRTGT NVDAQELKKA FENLGFAVSV 130 140 150 160 170 180 HKDCKLRDIL KHVGKAAELD HTDNDCLAVA ILSHGEHGYL YAKDTQYKLD NIWHYFTATF 190 200 210 220 230 240 CPSLAGKPKL FFIQACQGDR LDGGITLEKG VTETDGESST SYKIPIHADF LFSYSTIPGY 250 260 270 280 290 300 FSWRNINNGS WYMQSLIREL NANGKKYDLL TLLTFVNQRV ALDFESNVPA TPMMDRQKQI 310 320 PCLTSMLTRI LRFGDKPNGN KAG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DCP-1, a Drosophila cell death protease essential for development." Song Z., McCall K., Steller H. Science 275:536-540(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 216-248. Tissue: Embryo.
[2]	Erratum Song Z., McCall K., Steller H. Science 277:167-167(1997)
[3]	"The genome sequence of Drosophila melanogaster." 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. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." 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. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[5]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF001464 mRNA. Translation: AAB58237.1. AE013599 Genomic DNA. Translation: AAF47027.1. BT010065 mRNA. Translation: AAQ22534.1.
RefSeq	NP_476974.1. NM_057626.3.
UniGene	Dm.4849.
3D structure databases
ProteinModelPortal	O02002.
SMR	O02002. Positions 59-316.
ModBase	Search...
Protein-protein interaction databases
IntAct	O02002. 1 interaction.
STRING	7227.FBpp0071971.
Protein family/group databases
MEROPS	C14.016.
Proteomic databases
PaxDb	O02002.
PRIDE	O02002.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0072062; FBpp0071971; FBgn0010501.
GeneID	37729.
KEGG	dme:Dmel_CG5370.
Organism-specific databases
CTD	37729.
FlyBase	FBgn0010501. Dcp-1.
Phylogenomic databases
eggNOG	NOG279444.
GeneTree	ENSGT00700000104277.
InParanoid	O02002.
KO	K04489.
OMA	NIWHYFT.
OrthoDB	EOG4WDBTN.
PhylomeDB	O02002.
Enzyme and pathway databases
BRENDA	3.4.22.36. 1994.
Gene expression databases
Bgee	O02002.
GermOnline	CG5370. Drosophila melanogaster.
Family and domain databases
InterPro	IPR011600. Pept_C14_cat. IPR001309. Pept_C14_ICE_p20. IPR016129. Pept_C14_ICE_p20_AS. IPR002138. Pept_C14_p10. IPR002398. Pept_C14_p45. IPR015917. Pept_C14_p45_core. [Graphical view]
PANTHER	PTHR10454. PTHR10454. 1 hit.
Pfam	PF00656. Peptidase_C14. 1 hit. [Graphical view]
PRINTS	PR00376. IL1BCENZYME.
SMART	SM00115. CASc. 1 hit. [Graphical view]
PROSITE	PS01122. CASPASE_CYS. 1 hit. PS01121. CASPASE_HIS. 1 hit. PS50207. CASPASE_P10. 1 hit. PS50208. CASPASE_P20. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	37729.
NextBio	805112.

Entry information

Entry name

CASP1_DROME

Accession

Primary (citable) accession number: O02002
Secondary accession number(s): Q9W1N0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 1, 1997
Last modified:	April 3, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project