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Protein

Caspase

Gene

Drice

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the activation cascade of caspases responsible for apoptosis execution. Acts downstream of rpr. Cleaves baculovirus p35 and lamin DmO in vitro.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei169 – 1691By similarity
Active sitei211 – 2111By similarity

GO - Molecular functioni

  • BIR domain binding Source: FlyBase
  • cysteine-type endopeptidase activity Source: FlyBase
  • cysteine-type endopeptidase activity involved in apoptotic process Source: FlyBase
  • cysteine-type endopeptidase activity involved in execution phase of apoptosis Source: FlyBase

GO - Biological processi

  • apoptotic process Source: FlyBase
  • developmental programmed cell death Source: FlyBase
  • neuron remodeling Source: FlyBase
  • nurse cell apoptotic process Source: FlyBase
  • positive regulation of compound eye retinal cell programmed cell death Source: FlyBase
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: FlyBase
  • programmed cell death Source: FlyBase
  • regulation of retinal cell programmed cell death Source: FlyBase
  • response to X-ray Source: FlyBase
  • salivary gland histolysis Source: FlyBase
  • spermatid differentiation Source: FlyBase
  • sterol regulatory element binding protein cleavage Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiR-DME-111459. Activation of caspases through apoptosome-mediated cleavage.
R-DME-111465. Apoptotic cleavage of cellular proteins.
R-DME-2028269. Signaling by Hippo.
R-DME-211227. Activation of DNA fragmentation factor.
R-DME-264870. Caspase-mediated cleavage of cytoskeletal proteins.
R-DME-351906. Apoptotic cleavage of cell adhesion proteins.
R-DME-418889. Ligand-independent caspase activation via DCC.

Protein family/group databases

MEROPSiC14.015.

Names & Taxonomyi

Protein namesi
Recommended name:
Caspase (EC:3.4.22.-)
Alternative name(s):
drICE
Cleaved into the following 2 chains:
Gene namesi
Name:Drice
Synonyms:ICE
ORF Names:CG7788
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0019972. Drice.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi29 – 291A → V: Abolishes binding to Diap2 but has no effect on Drice processing or activity. 1 Publication
Mutagenesisi211 – 2111C → A: No effect on binding to Diap2 but may effect stability of complex formed with Diap2. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 2828By similarityPRO_0000004666Add
BLAST
Chaini29 – 217189Caspase subunit p21By similarityPRO_0000004667Add
BLAST
Propeptidei218 – 23013By similarityPRO_0000004668Add
BLAST
Chaini231 – 339109Caspase subunit p12By similarityPRO_0000004669Add
BLAST

Keywords - PTMi

Zymogen

Proteomic databases

PaxDbiO01382.

Expressioni

Developmental stagei

Expressed at all stages where apoptosis occurs.

Gene expression databases

BgeeiO01382.
GenevisibleiO01382. DM.

Interactioni

Subunit structurei

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).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DroncQ9XYF43EBI-91422,EBI-108311

GO - Molecular functioni

  • BIR domain binding Source: FlyBase

Protein-protein interaction databases

BioGridi68378. 15 interactions.
DIPiDIP-21838N.
IntActiO01382. 2 interactions.
MINTiMINT-823464.
STRINGi7227.FBpp0084848.

Structurei

Secondary structure

1
339
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi90 – 10112Combined sources
Beta strandi105 – 1084Combined sources
Helixi118 – 12811Combined sources
Beta strandi132 – 1387Combined sources
Helixi141 – 15212Combined sources
Helixi156 – 1583Combined sources
Beta strandi159 – 16810Combined sources
Helixi180 – 1867Combined sources
Helixi189 – 1913Combined sources
Turni193 – 1953Combined sources
Helixi197 – 1993Combined sources
Beta strandi200 – 2023Combined sources
Beta strandi204 – 2118Combined sources
Beta strandi245 – 2528Combined sources
Turni261 – 2633Combined sources
Helixi266 – 27813Combined sources
Turni279 – 2813Combined sources
Helixi284 – 29613Combined sources
Helixi307 – 3093Combined sources
Beta strandi317 – 3204Combined sources
Beta strandi323 – 3253Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SIPX-ray3.50A/C78-230[»]
B/D231-339[»]
3SIRX-ray2.68A/B/C/D78-332[»]
ProteinModelPortaliO01382.
SMRiO01382. Positions 78-337.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C14A family.Curated

Phylogenomic databases

eggNOGiKOG3573. Eukaryota.
ENOG410ZQIE. LUCA.
GeneTreeiENSGT00760000118912.
InParanoidiO01382.
KOiK04397.
OMAiSYKIPVH.
OrthoDBiEOG7TTQ7K.
PhylomeDBiO01382.

Family and domain databases

Gene3Di3.40.50.1460. 1 hit.
InterProiIPR029030. Caspase-like_dom.
IPR033139. Caspase_cys_AS.
IPR016129. Caspase_his_AS.
IPR002138. Pept_C14_p10.
IPR001309. Pept_C14_p20.
IPR015917. Pept_C14A.
[Graphical view]
PRINTSiPR00376. IL1BCENZYME.
SMARTiSM00115. CASc. 1 hit.
[Graphical view]
SUPFAMiSSF52129. SSF52129. 1 hit.
PROSITEiPS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O01382-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDATNNGESA DQVGIRVGNP EQPNDHTDAL GSVGSGGAGS SGLVAGSSHP
60 70 80 90 100
YGSGAIGQLA NGYSSPSSSY RKNVAKMVTD RHAAEYNMRH KNRGMALIFN
110 120 130 140 150
HEHFEVPTLK SRAGTNVDCE NLTRVLKQLD FEVTVYKDCR YKDILRTIEY
160 170 180 190 200
AASQNHSDSD CILVAILSHG EMGYIYAKDT QYKLDNIWSF FTANHCPSLA
210 220 230 240 250
GKPKLFFIQA CQGDRLDGGV TMQRSQTETD GDSSMSYKIP VHADFLIAYS
260 270 280 290 300
TVPGFYSWRN TTRGSWFMQS LCAELAANGK RLDILTLLTF VCQRVAVDFE
310 320 330
SCTPDTPEMH QQKQIPCITT MLTRILRFSD KQLAPAGRV
Length:339
Mass (Da):37,363
Last modified:December 1, 2000 - v2
Checksum:iE105ED29518507EC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti151 – 1511A → S in CAA72937 (PubMed:9184225).Curated
Sequence conflicti265 – 2651S → T in CAA72937 (PubMed:9184225).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12261 mRNA. Translation: CAA72937.1.
AE014297 Genomic DNA. Translation: AAF56939.1.
AY058451 mRNA. Translation: AAL13680.1.
RefSeqiNP_524551.2. NM_079827.3.
UniGeneiDm.2333.

Genome annotation databases

EnsemblMetazoaiFBtr0085482; FBpp0084848; FBgn0019972.
GeneIDi43514.
KEGGidme:Dmel_CG7788.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12261 mRNA. Translation: CAA72937.1.
AE014297 Genomic DNA. Translation: AAF56939.1.
AY058451 mRNA. Translation: AAL13680.1.
RefSeqiNP_524551.2. NM_079827.3.
UniGeneiDm.2333.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SIPX-ray3.50A/C78-230[»]
B/D231-339[»]
3SIRX-ray2.68A/B/C/D78-332[»]
ProteinModelPortaliO01382.
SMRiO01382. Positions 78-337.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68378. 15 interactions.
DIPiDIP-21838N.
IntActiO01382. 2 interactions.
MINTiMINT-823464.
STRINGi7227.FBpp0084848.

Protein family/group databases

MEROPSiC14.015.

Proteomic databases

PaxDbiO01382.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0085482; FBpp0084848; FBgn0019972.
GeneIDi43514.
KEGGidme:Dmel_CG7788.

Organism-specific databases

CTDi43514.
FlyBaseiFBgn0019972. Drice.

Phylogenomic databases

eggNOGiKOG3573. Eukaryota.
ENOG410ZQIE. LUCA.
GeneTreeiENSGT00760000118912.
InParanoidiO01382.
KOiK04397.
OMAiSYKIPVH.
OrthoDBiEOG7TTQ7K.
PhylomeDBiO01382.

Enzyme and pathway databases

ReactomeiR-DME-111459. Activation of caspases through apoptosome-mediated cleavage.
R-DME-111465. Apoptotic cleavage of cellular proteins.
R-DME-2028269. Signaling by Hippo.
R-DME-211227. Activation of DNA fragmentation factor.
R-DME-264870. Caspase-mediated cleavage of cytoskeletal proteins.
R-DME-351906. Apoptotic cleavage of cell adhesion proteins.
R-DME-418889. Ligand-independent caspase activation via DCC.

Miscellaneous databases

GenomeRNAii43514.
PROiO01382.

Gene expression databases

BgeeiO01382.
GenevisibleiO01382. DM.

Family and domain databases

Gene3Di3.40.50.1460. 1 hit.
InterProiIPR029030. Caspase-like_dom.
IPR033139. Caspase_cys_AS.
IPR016129. Caspase_his_AS.
IPR002138. Pept_C14_p10.
IPR001309. Pept_C14_p20.
IPR015917. Pept_C14A.
[Graphical view]
PRINTSiPR00376. IL1BCENZYME.
SMARTiSM00115. CASc. 1 hit.
[Graphical view]
SUPFAMiSSF52129. SSF52129. 1 hit.
PROSITEiPS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a Drosophila melanogaster ICE/CED-3-related protease, drICE."
    Fraser A.G., Evan G.I.
    EMBO J. 16:2805-2813(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryo.
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  5. "The Drosophila caspase DRONC is regulated by DIAP1."
    Meier P., Silke J., Leevers S.J., Evan G.I.
    EMBO J. 19:598-611(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION, INTERACTION WITH DRONC.
    Tissue: Embryo.
  6. "DIAP2 functions as a mechanism-based regulator of drICE that contributes to the caspase activity threshold in living cells."
    Ribeiro P.S., Kuranaga E., Tenev T., Leulier F., Miura M., Meier P.
    J. Cell Biol. 179:1467-1480(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DIAP2, MUTAGENESIS OF ALA-29 AND CYS-211.

Entry informationi

Entry nameiDRICE_DROME
AccessioniPrimary (citable) accession number: O01382
Secondary accession number(s): Q9VAH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 1, 2000
Last modified: July 6, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.