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Caspase (EC 3.4.22.-) (drICE) [Cleaved into: Caspase subunit p21; Caspase subunit p12]

 DRICE_DROME             Reviewed;         339 AA.
O01382; Q9VAH1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
13-FEB-2019, entry version 171.
RecName: Full=Caspase;
EC=3.4.22.-;
AltName: Full=drICE;
Contains:
RecName: Full=Caspase subunit p21;
Contains:
RecName: Full=Caspase subunit p12;
Flags: Precursor;
Name=Drice; Synonyms=ICE; ORFNames=CG7788;
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].
TISSUE=Embryo;
PubMed=9184225; DOI=10.1093/emboj/16.10.2805;
Fraser A.G., Evan G.I.;
"Identification of a Drosophila melanogaster ICE/CED-3-related
protease, drICE.";
EMBO J. 16:2805-2813(1997).
[2]
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).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
HOMODIMERIZATION, AND INTERACTION WITH DRONC.
TISSUE=Embryo;
PubMed=10675329; DOI=10.1093/emboj/19.4.598;
Meier P., Silke J., Leevers S.J., Evan G.I.;
"The Drosophila caspase DRONC is regulated by DIAP1.";
EMBO J. 19:598-611(2000).
[6]
INTERACTION WITH DIAP2, AND MUTAGENESIS OF ALA-29 AND CYS-211.
PubMed=18166655; DOI=10.1083/jcb.200706027;
Ribeiro P.S., Kuranaga E., Tenev T., Leulier F., Miura M., Meier P.;
"DIAP2 functions as a mechanism-based regulator of drICE that
contributes to the caspase activity threshold in living cells.";
J. Cell Biol. 179:1467-1480(2007).
-!- 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: 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). {ECO:0000269|PubMed:10675329,
ECO:0000269|PubMed:18166655}.
-!- INTERACTION:
Q9XYF4:Dronc; NbExp=3; IntAct=EBI-91422, EBI-108311;
-!- DEVELOPMENTAL STAGE: Expressed at all stages where apoptosis
occurs.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; Y12261; CAA72937.1; -; mRNA.
EMBL; AE014297; AAF56939.1; -; Genomic_DNA.
EMBL; AY058451; AAL13680.1; -; mRNA.
RefSeq; NP_524551.2; NM_079827.3.
UniGene; Dm.2333; -.
PDB; 3SIP; X-ray; 3.50 A; A/C=78-230, B/D=231-339.
PDB; 3SIR; X-ray; 2.68 A; A/B/C/D=78-332.
PDBsum; 3SIP; -.
PDBsum; 3SIR; -.
ProteinModelPortal; O01382; -.
SMR; O01382; -.
BioGrid; 68378; 24.
DIP; DIP-21838N; -.
ELM; O01382; -.
IntAct; O01382; 2.
MINT; O01382; -.
STRING; 7227.FBpp0084848; -.
MEROPS; C14.015; -.
PaxDb; O01382; -.
PRIDE; O01382; -.
EnsemblMetazoa; FBtr0085482; FBpp0084848; FBgn0019972.
GeneID; 43514; -.
KEGG; dme:Dmel_CG7788; -.
CTD; 43514; -.
FlyBase; FBgn0019972; Drice.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00940000153232; -.
InParanoid; O01382; -.
KO; K04397; -.
OMA; SWRNTTR; -.
OrthoDB; 984395at2759; -.
PhylomeDB; O01382; -.
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; 43514; -.
PRO; PR:O01382; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0019972; Expressed in 41 organ(s), highest expression level in embryo.
Genevisible; O01382; DM.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
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; IDA:FlyBase.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IDA:FlyBase.
GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
GO; GO:0016322; P:neuron remodeling; IMP:FlyBase.
GO; GO:0045476; P:nurse cell apoptotic process; IGI:FlyBase.
GO; GO:0046672; P:positive regulation of compound eye retinal cell programmed cell death; IMP:FlyBase.
GO; GO:2001269; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IDA:FlyBase.
GO; GO:0012501; P:programmed cell death; IDA:FlyBase.
GO; GO:0010623; P:programmed cell death involved in cell development; IMP:FlyBase.
GO; GO:0006508; P:proteolysis; IDA:FlyBase.
GO; GO:0046668; P:regulation of retinal cell programmed cell death; NAS:FlyBase.
GO; GO:0010165; P:response to X-ray; IMP:FlyBase.
GO; GO:0035070; P:salivary gland histolysis; IMP:FlyBase.
GO; GO:0048515; P:spermatid differentiation; IMP:FlyBase.
GO; GO:0035103; P:sterol regulatory element binding protein cleavage; IDA: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;
3D-structure; Apoptosis; Complete proteome; Hydrolase; Protease;
Reference proteome; Thiol protease; Zymogen.
PROPEP 1 28 {ECO:0000250}.
/FTId=PRO_0000004666.
CHAIN 29 217 Caspase subunit p21. {ECO:0000250}.
/FTId=PRO_0000004667.
PROPEP 218 230 {ECO:0000250}.
/FTId=PRO_0000004668.
CHAIN 231 339 Caspase subunit p12. {ECO:0000250}.
/FTId=PRO_0000004669.
ACT_SITE 169 169 {ECO:0000250}.
ACT_SITE 211 211 {ECO:0000250}.
MUTAGEN 29 29 A->V: Abolishes binding to Diap2 but has
no effect on Drice processing or
activity. {ECO:0000269|PubMed:18166655}.
MUTAGEN 211 211 C->A: No effect on binding to Diap2 but
may effect stability of complex formed
with Diap2.
{ECO:0000269|PubMed:18166655}.
CONFLICT 151 151 A -> S (in Ref. 1; CAA72937).
{ECO:0000305}.
CONFLICT 265 265 S -> T (in Ref. 1; CAA72937).
{ECO:0000305}.
STRAND 90 101 {ECO:0000244|PDB:3SIR}.
STRAND 105 108 {ECO:0000244|PDB:3SIP}.
HELIX 118 128 {ECO:0000244|PDB:3SIR}.
STRAND 132 138 {ECO:0000244|PDB:3SIR}.
HELIX 141 152 {ECO:0000244|PDB:3SIR}.
HELIX 156 158 {ECO:0000244|PDB:3SIP}.
STRAND 159 168 {ECO:0000244|PDB:3SIR}.
HELIX 180 186 {ECO:0000244|PDB:3SIR}.
HELIX 189 191 {ECO:0000244|PDB:3SIR}.
TURN 193 195 {ECO:0000244|PDB:3SIR}.
HELIX 197 199 {ECO:0000244|PDB:3SIR}.
STRAND 200 202 {ECO:0000244|PDB:3SIR}.
STRAND 204 211 {ECO:0000244|PDB:3SIR}.
STRAND 245 252 {ECO:0000244|PDB:3SIR}.
TURN 261 263 {ECO:0000244|PDB:3SIP}.
HELIX 266 278 {ECO:0000244|PDB:3SIR}.
TURN 279 281 {ECO:0000244|PDB:3SIR}.
HELIX 284 296 {ECO:0000244|PDB:3SIR}.
HELIX 307 309 {ECO:0000244|PDB:3SIP}.
STRAND 317 320 {ECO:0000244|PDB:3SIR}.
STRAND 323 325 {ECO:0000244|PDB:3SIR}.
SEQUENCE 339 AA; 37363 MW; E105ED29518507EC CRC64;
MDATNNGESA DQVGIRVGNP EQPNDHTDAL GSVGSGGAGS SGLVAGSSHP YGSGAIGQLA
NGYSSPSSSY RKNVAKMVTD RHAAEYNMRH KNRGMALIFN HEHFEVPTLK SRAGTNVDCE
NLTRVLKQLD FEVTVYKDCR YKDILRTIEY AASQNHSDSD CILVAILSHG EMGYIYAKDT
QYKLDNIWSF FTANHCPSLA GKPKLFFIQA CQGDRLDGGV TMQRSQTETD GDSSMSYKIP
VHADFLIAYS TVPGFYSWRN TTRGSWFMQS LCAELAANGK RLDILTLLTF VCQRVAVDFE
SCTPDTPEMH QQKQIPCITT MLTRILRFSD KQLAPAGRV


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Pathways :
WP1965: VEGF-receptor Signal Transduction
WP2359: Parkin-Ubiquitin Proteasomal System pathway
WP88: Toll Like Receptor signaling
WP1566: Citrate cycle (TCA cycle)
WP1614: 1- and 2-Methylnaphthalene degradation
WP1626: Benzoate degradation via CoA ligation
WP1634: Butanoate metabolism
WP1644: DNA replication
WP1655: Geraniol degradation
WP1663: Homologous recombination
WP1671: Methane metabolism
WP1672: Mismatch repair
WP1680: Oxidative phosphorylation
WP1693: Purine metabolism
WP1694: Pyrimidine metabolism
WP1711: Trinitrotoluene degradation
WP1718: Vitamin B6 metabolism
WP2272: Pathogenic Escherichia coli infection
WP2292: Chemokine signaling pathway

Related Genes :
[Drice ICE CG7788] Caspase (EC 3.4.22.-) (drICE) [Cleaved into: Caspase subunit p21; Caspase subunit p12]
[Casp2 Ich1 Nedd-2 Nedd2] Caspase-2 (CASP-2) (EC 3.4.22.55) (Neural precursor cell expressed developmentally down-regulated protein 2) (NEDD-2) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
[Casp3 Cpp32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (LICE) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CASP2 ICH1 NEDD2] Caspase-2 (CASP-2) (EC 3.4.22.55) (Neural precursor cell expressed developmentally down-regulated protein 2) (NEDD-2) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
[CASP10 MCH4] Caspase-10 (CASP-10) (EC 3.4.22.63) (Apoptotic protease Mch-4) (FAS-associated death domain protein interleukin-1B-converting enzyme 2) (FLICE2) (ICE-like apoptotic protease 4) [Cleaved into: Caspase-10 subunit p23/17; Caspase-10 subunit p12]
[Casp2 Ich1] Caspase-2 (CASP-2) (EC 3.4.22.55) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
[CASP3 CPP32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[Casp3 Cpp32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (IRP) (LICE) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CFLAR CASH CASP8AP1 CLARP MRIT] CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]
[Cflar Cash] CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]
[Casp4 Casp11 Caspl Ich3] Caspase-4 (CASP-4) (EC 3.4.22.64) (Caspase-11) (CASP-11) (Protease ICH-3) [Cleaved into: Caspase-4 subunit p10; Caspase-4 subunit p20]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CASP14] Caspase-14 (CASP-14) (EC 3.4.22.-) [Cleaved into: Caspase-14 subunit p17, mature form; Caspase-14 subunit p10, mature form; Caspase-14 subunit p20, intermediate form; Caspase-14 subunit p8, intermediate form]
[Casp7 Lice2 Mch3] Caspase-7 (CASP-7) (EC 3.4.22.60) (Apoptotic protease Mch-3) (Cysteine protease LICE2) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11]
[CASP4 ICH2] Caspase-4 (CASP-4) (EC 3.4.22.57) (ICE and Ced-3 homolog 2) (ICH-2) (ICE(rel)-II) (Mih1) (Protease TX) [Cleaved into: Caspase-4 subunit 1; Caspase-4 subunit 2]
[CASP7 MCH3] Caspase-7 (CASP-7) (EC 3.4.22.60) (Apoptotic protease Mch-3) (CMH-1) (ICE-like apoptotic protease 3) (ICE-LAP3) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11]
[CASP8 MCH5] Caspase-8 (CASP-8) (EC 3.4.22.61) (Apoptotic cysteine protease) (Apoptotic protease Mch-5) (CAP4) (FADD-homologous ICE/ced-3-like protease) (FADD-like ICE) (FLICE) (ICE-like apoptotic protease 5) (MORT1-associated ced-3 homolog) (MACH) [Cleaved into: Caspase-8 subunit p18; Caspase-8 subunit p10]
[Casp6] Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
[Dredd DCP2 CG7486] Caspase-8 (EC 3.4.22.61) (Death-related ced-3/NEDD2-like protein) [Cleaved into: Caspase-8 subunit p15; Caspase-8 subunit p10]
[CASP6 MCH2] Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
[csp-1 Y48E1B.13] Caspase A (EC 3.4.22.36) [Cleaved into: Caspase A subunit p16; Caspase A subunit p14]
[Casp6 Mch2] Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[gag-pol] Gag-Pol polyprotein [Cleaved into: Matrix protein p19; p2A; p2B; p10; Capsid protein p27, alternate cleaved 1; Capsid protein p27, alternate cleaved 2; Spacer peptide (SP) (p3); Nucleocapsid protein p12; Protease p15 (EC 3.4.23.-); Reverse transcriptase, beta-subunit (RT-beta); Reverse transcriptase, alpha-subunit (RT-alpha) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-) (pp32); p4]
[csp-2 Y73B6BL.7] Putative inactive caspase B [Cleaved into: Putative inactive caspase B subunit p31; Putative inactive caspase B subunit p17; Putative inactive caspase subunit p14]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[gag-pol] Gag-Pol polyprotein [Cleaved into: Matrix protein p19; p2A; p2B; p10; Capsid protein p27, alternate cleaved 1; Capsid protein p27, alternate cleaved 2; p3; Nucleocapsid protein p12; Protease p15 (EC 3.4.23.-); Reverse transcriptase beta-subunit (RT-beta); Reverse transcriptase alpha-subunit (RT-alpha) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-) (pp32); p4]

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