O01382 (ICE_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Caspase
EC=3.4.22.-

Alternative name(s):
drICE

Cleaved into the following 2 chains:

1. Caspase subunit p21
2. Caspase subunit p12

Gene names

Name:	Ice
ORF Names:	CG7788

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	339 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. Acts downstream of rpr. Cleaves baculovirus p35 and lamin DmO in vitro.
Subunit structure	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. Nc and Ice can form a stable complex. Ref.5
Developmental stage	Expressed at all stages where apoptosis occurs.
Sequence similarities	Belongs to the peptidase C14A family.

Ontologies

Keywords
Biological process	Apoptosis
Molecular function	Hydrolase Protease Thiol protease
PTM	Zymogen
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	developmental programmed cell death Inferred from mutant phenotype PubMed 16980627. Source: FlyBase neuron remodeling Inferred from mutant phenotype PubMed 20445064. Source: FlyBase nurse cell apoptotic process Inferred from genetic interaction PubMed 17464325. Source: FlyBase positive regulation of compound eye retinal cell programmed cell death Inferred from mutant phenotype PubMed 16485033. Source: FlyBase proteolysis Traceable author statement PubMed 14644196. Source: FlyBase response to X-ray Inferred from mutant phenotype PubMed 16887831. Source: FlyBase salivary gland histolysis Inferred from mutant phenotype PubMed 16485033. Source: FlyBase spermatid differentiation Inferred from mutant phenotype PubMed 16887831. Source: FlyBase sterol regulatory element binding protein cleavage Inferred from direct assay PubMed 19224859. Source: FlyBase
Molecular_function	cysteine-type endopeptidase activity Inferred from direct assay PubMed 16222340. Source: FlyBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Nc	Q9XYF4	2	EBI-91422,EBI-108311

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 28

28

By similarity

PRO_0000004666

Chain

29 – 217

189

Caspase subunit p21 By similarity

PRO_0000004667

Propeptide

218 – 230

13

By similarity

PRO_0000004668

Chain

231 – 339

109

Caspase subunit p12 By similarity

PRO_0000004669

Sites

Active site

169

1

By similarity

Active site

211

1

By similarity

Experimental info

Sequence conflict

151

1

A → S in CAA72937. Ref.1

Sequence conflict

265

1

S → T in CAA72937. Ref.1

Secondary structure

1

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339

Helix Strand Turn

Details...

Beta strand

90 – 101

12

Helix

118 – 128

11

Beta strand

132 – 138

7

Helix

141 – 152

12

Beta strand

159 – 168

10

Helix

180 – 186

7

Helix

189 – 191

3

Turn

193 – 195

3

Helix

197 – 199

3

Beta strand

200 – 202

3

Beta strand

204 – 211

8

Beta strand

245 – 252

8

Helix

266 – 278

13

Turn

279 – 281

3

Helix

284 – 296

13

Beta strand

317 – 320

4

Beta strand

323 – 325

3

Sequences

	Sequence		Length	Mass (Da)
	O01382 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: E105ED29518507EC	FASTA	339	37,363
	10 20 30 40 50 60 MDATNNGESA DQVGIRVGNP EQPNDHTDAL GSVGSGGAGS SGLVAGSSHP YGSGAIGQLA 70 80 90 100 110 120 NGYSSPSSSY RKNVAKMVTD RHAAEYNMRH KNRGMALIFN HEHFEVPTLK SRAGTNVDCE 130 140 150 160 170 180 NLTRVLKQLD FEVTVYKDCR YKDILRTIEY AASQNHSDSD CILVAILSHG EMGYIYAKDT 190 200 210 220 230 240 QYKLDNIWSF FTANHCPSLA GKPKLFFIQA CQGDRLDGGV TMQRSQTETD GDSSMSYKIP 250 260 270 280 290 300 VHADFLIAYS TVPGFYSWRN TTRGSWFMQS LCAELAANGK RLDILTLLTF VCQRVAVDFE 310 320 330 SCTPDTPEMH QQKQIPCITT MLTRILRFSD KQLAPAGRV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] 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 NC. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y12261 mRNA. Translation: CAA72937.1.
AE014297 Genomic DNA. Translation: AAF56939.1.
AY058451 mRNA. Translation: AAL13680.1.

RefSeq

NP_524551.2. NM_079827.2.

UniGene

Dm.2333.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3SIP	X-ray	3.50	A/C	78-230	[»]
			B/D	231-339	[»]
3SIR	X-ray	2.68	A/B/C/D	78-332	[»]

ProteinModelPortal

O01382.

SMR

O01382. Positions 78-337.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-21838N.

IntAct

O01382. 2 interactions.

MINT

MINT-823464.

STRING

7227.FBpp0084848.

Protein family/group databases

MEROPS

C14.015.

Proteomic databases

PaxDb

O01382.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0085482; FBpp0084848; FBgn0019972.

GeneID

43514.

KEGG

dme:Dmel_CG7788.

Organism-specific databases

CTD

43514.

FlyBase

FBgn0019972. Ice.

Phylogenomic databases

eggNOG

NOG279444.

GeneTree

ENSGT00700000104277.

InParanoid

O01382.

KO

K04489.

OMA

DANPRHK.

OrthoDB

EOG4WDBTN.

PhylomeDB

O01382.

Gene expression databases

Bgee

O01382.

GermOnline

CG7788. 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

43514.

NextBio

834329.

Entry information

Entry name

ICE_DROME

Accession

Primary (citable) accession number: O01382
Secondary accession number(s): Q9VAH1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	December 1, 2000
Last modified:	April 3, 2013
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project