DIAP2_DROME
ID DIAP2_DROME Reviewed; 498 AA.
AC Q24307; A4UZI4; Q24115; Q24149; Q24177; Q960U3; Q9V7G1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Death-associated inhibitor of apoptosis 2;
DE AltName: Full=Apoptosis 2 inhibitor;
DE AltName: Full=IAP homolog A;
DE AltName: Full=IAP-like protein;
DE Short=ILP;
DE Short=dILP;
DE AltName: Full=Inhibitor of apoptosis 2;
GN Name=Diap2; Synonyms=DIHA, Iap2, Ilp; ORFNames=CG8293;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Eye imaginal disk;
RX PubMed=8548811; DOI=10.1016/0092-8674(95)90150-7;
RA Hay B.A., Wassarman D.A., Rubin G.M.;
RT "Drosophila homologs of baculovirus inhibitor of apoptosis proteins
RT function to block cell death.";
RL Cell 83:1253-1262(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=8552191; DOI=10.1038/379349a0;
RA Liston P., Roy N., Tamai K., Lefebvre C., Baird S., Cherton-Horvat G.,
RA Farahani R., McLean M., Ikeda J., Mackenzie A., Korneluk R.G.;
RT "Suppression of apoptosis in mammalian cells by NAIP and a related family
RT of IAP genes.";
RL Nature 379:349-353(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Canton-S;
RX PubMed=8654366; DOI=10.1002/j.1460-2075.1996.tb00629.x;
RA Duckett C.S., Nava V.E., Gedrich R.W., Clem R.J., van Dongen J.L.,
RA Gilfillan M.C., Shiels H., Hardwick J.M., Thompson C.B.;
RT "A conserved family of cellular genes related to the baculovirus iap gene
RT and encoding apoptosis inhibitors.";
RL EMBO J. 15:2685-2694(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Canton-S;
RA Ross J.L.;
RL Thesis (1991), Vanderbilt University / Nashville, United States.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-498.
RC TISSUE=Larva;
RX PubMed=8643514; DOI=10.1073/pnas.93.10.4974;
RA Uren A.G., Pakusch M., Hawkins C.J., Puls K.L., Vaux D.L.;
RT "Cloning and expression of apoptosis inhibitory protein homologs that
RT function to inhibit apoptosis and/or bind tumor necrosis factor receptor-
RT associated factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:4974-4978(1996).
RN [9]
RP INTERACTION WITH STRICA.
RX PubMed=11550090; DOI=10.1038/sj.cdd.4400864;
RA Doumanis J., Quinn L., Richardson H., Kumar S.;
RT "STRICA, a novel Drosophila melanogaster caspase with an unusual
RT serine/threonine-rich prodomain, interacts with DIAP1 and DIAP2.";
RL Cell Death Differ. 8:387-394(2001).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16894030; DOI=10.1128/mcb.00548-06;
RA Leulier F., Lhocine N., Lemaitre B., Meier P.;
RT "The Drosophila inhibitor of apoptosis protein DIAP2 functions in innate
RT immunity and is essential to resist gram-negative bacterial infection.";
RL Mol. Cell. Biol. 26:7821-7831(2006).
RN [11]
RP FUNCTION, DOMAIN, INTERACTION WITH DRICE; GRIM; HID AND RPR, DISRUPTION
RP PHENOTYPE, CLEAVAGE, AND MUTAGENESIS OF ASP-92; ASP-100; CYS-149; ASP-163;
RP CYS-249 AND ASP-263.
RX PubMed=18166655; DOI=10.1083/jcb.200706027;
RA Ribeiro P.S., Kuranaga E., Tenev T., Leulier F., Miura M., Meier P.;
RT "DIAP2 functions as a mechanism-based regulator of drICE that contributes
RT to the caspase activity threshold in living cells.";
RL J. Cell Biol. 179:1467-1480(2007).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY GRAM-NEGATIVE BACTERIA.
RX PubMed=17068333; DOI=10.1074/jbc.m608051200;
RA Huh J.R., Foe I., Muro I., Chen C.H., Seol J.H., Yoo S.J., Guo M.,
RA Park J.M., Hay B.A.;
RT "The Drosophila inhibitor of apoptosis (IAP) DIAP2 is dispensable for cell
RT survival, required for the innate immune response to gram-negative
RT bacterial infection, and can be negatively regulated by the reaper/hid/grim
RT family of IAP-binding apoptosis inducers.";
RL J. Biol. Chem. 282:2056-2068(2007).
RN [13]
RP REVIEW ON FUNCTION.
RX PubMed=19217783; DOI=10.1016/j.tcb.2009.01.004;
RA Broemer M., Meier P.;
RT "Ubiquitin-mediated regulation of apoptosis.";
RL Trends Cell Biol. 19:130-140(2009).
RN [14]
RP REVIEW ON FUNCTION.
RX PubMed=20888210; DOI=10.1016/j.ceb.2010.08.025;
RA Lopez J., Meier P.;
RT "To fight or die - inhibitor of apoptosis proteins at the crossroad of
RT innate immunity and death.";
RL Curr. Opin. Cell Biol. 22:872-881(2010).
RN [15]
RP FUNCTION, INTERACTION WITH DREDD, DOMAIN, AND MUTAGENESIS OF CYS-149;
RP ASP-163; CYS-249; ASP-263 AND CYS-466.
RX PubMed=22549468; DOI=10.1038/emboj.2012.121;
RA Meinander A., Runchel C., Tenev T., Chen L., Kim C.H., Ribeiro P.S.,
RA Broemer M., Leulier F., Zvelebil M., Silverman N., Meier P.;
RT "Ubiquitylation of the initiator caspase DREDD is required for innate
RT immune signalling.";
RL EMBO J. 31:2770-2783(2012).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24374974; DOI=10.1002/jcp.24541;
RA Verma P., Tapadia M.G.;
RT "Epithelial immune response in Drosophila malpighian tubules: interplay
RT between Diap2 and ion channels.";
RL J. Cell. Physiol. 229:1078-1095(2014).
CC -!- FUNCTION: Required for activation of NF-kappaB transcription factors in
CC the immune deficiency (Imd) signaling cascade which is essential for
CC innate immune responses upon infection by Gram-negative bacteria
CC (PubMed:16894030, PubMed:17068333). Promotes cytoplasmic cleavage of
CC Rel and its translocation to the nucleus where it drives expression of
CC antimicrobial peptides (PubMed:17068333, PubMed:24374974). Binds,
CC polyubiquitinates and activates Dredd which is required for Rel-
CC mediated induction of antimicrobial peptides (PubMed:22549468). Anti-
CC apoptotic protein which binds, ubiquitinates and inactivates the
CC effector caspase Drice (PubMed:18166655). Suppresses rpr and hid-
CC dependent cell death in the eye (PubMed:8548811). However, has also
CC been shown to have little, if any, role in the regulation of the
CC canonical caspase-dependent apoptosis pathway (PubMed:17068333). Plays
CC a role in regulating the expression of ion channels (PubMed:24374974).
CC {ECO:0000269|PubMed:16894030, ECO:0000269|PubMed:17068333,
CC ECO:0000269|PubMed:18166655, ECO:0000269|PubMed:22549468,
CC ECO:0000269|PubMed:24374974, ECO:0000269|PubMed:8548811}.
CC -!- SUBUNIT: Interacts with the caspase Strica (PubMed:11550090). Interacts
CC (via BIR2 domain) with rpr and grim (PubMed:18166655). Interacts (via
CC the BIR2 and BIR3 domains) with hid (PubMed:18166655). Interacts (via
CC BIR3 domain) with Drice (PubMed:18166655). Interacts with Dredd; likely
CC to bind Dredd simultaneously with Fadd to form a trimeric complex
CC (PubMed:22549468). {ECO:0000269|PubMed:11550090,
CC ECO:0000269|PubMed:18166655, ECO:0000269|PubMed:22549468}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24374974}. Cytoplasm
CC {ECO:0000269|PubMed:24374974}.
CC -!- TISSUE SPECIFICITY: Expressed in both principal and stellar cells of
CC the Malphigian tubules. {ECO:0000269|PubMed:24374974}.
CC -!- DEVELOPMENTAL STAGE: Expressed in Malpighian tubules from the 3rd
CC instar larval stage and expression continues in pupae and adults with
CC highest levels in adults (at protein level).
CC {ECO:0000269|PubMed:24374974}.
CC -!- INDUCTION: Constitutively expressed (PubMed:17068333). Up-regulated by
CC bacterial lipopolysaccharides (LPS) in Malpighian tubules but not in
CC salivary glands (PubMed:24374974). {ECO:0000269|PubMed:17068333,
CC ECO:0000269|PubMed:24374974}.
CC -!- PTM: Caspase-dependent cleavage is required for suppression of Drice-
CC mediated cell death. {ECO:0000269|PubMed:18166655}.
CC -!- DISRUPTION PHENOTYPE: Normal development and viability
CC (PubMed:16894030, PubMed:17068333). Acute sensitivity to infection by
CC Gram-negative bacteria with failure to induce expression of
CC antibacterial peptide genes and inability to mount a proper innate
CC immune response (PubMed:16894030, PubMed:17068333, PubMed:24374974).
CC Loss of cleavage and nuclear translocation of Rel (PubMed:17068333,
CC PubMed:24374974). Increased activity of the effector caspase Drice and
CC increased apoptosis following x-ray irradiation (PubMed:18166655).
CC Reduced ion channel expression in Malpighian tubules (PubMed:24374974).
CC {ECO:0000269|PubMed:16894030, ECO:0000269|PubMed:17068333,
CC ECO:0000269|PubMed:18166655, ECO:0000269|PubMed:24374974}.
CC -!- SIMILARITY: Belongs to the IAP family. {ECO:0000305}.
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DR EMBL; L49441; AAC41610.1; -; mRNA.
DR EMBL; U45881; AAC46988.1; -; mRNA.
DR EMBL; U32373; AAC47155.1; -; mRNA.
DR EMBL; M96581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AE013599; AAF58095.1; -; Genomic_DNA.
DR EMBL; AE013599; AAO41389.1; -; Genomic_DNA.
DR EMBL; AY051844; AAK93268.1; -; mRNA.
DR EMBL; U38809; AAB08398.1; -; mRNA.
DR PIR; S68452; S68452.
DR PIR; S69545; S69545.
DR RefSeq; NP_477127.1; NM_057779.5.
DR RefSeq; NP_788362.1; NM_176182.2.
DR AlphaFoldDB; Q24307; -.
DR SMR; Q24307; -.
DR BioGRID; 62475; 179.
DR IntAct; Q24307; 3.
DR STRING; 7227.FBpp0086432; -.
DR MEROPS; I32.011; -.
DR PaxDb; Q24307; -.
DR DNASU; 36748; -.
DR EnsemblMetazoa; FBtr0087296; FBpp0086431; FBgn0015247.
DR EnsemblMetazoa; FBtr0087297; FBpp0086432; FBgn0015247.
DR GeneID; 36748; -.
DR KEGG; dme:Dmel_CG8293; -.
DR UCSC; CG8293-RB; d. melanogaster.
DR CTD; 36748; -.
DR FlyBase; FBgn0015247; Diap2.
DR VEuPathDB; VectorBase:FBgn0015247; -.
DR eggNOG; KOG1101; Eukaryota.
DR GeneTree; ENSGT00940000169803; -.
DR HOGENOM; CLU_016347_1_1_1; -.
DR InParanoid; Q24307; -.
DR OMA; ILEEPQM; -.
DR OrthoDB; 1340284at2759; -.
DR PhylomeDB; Q24307; -.
DR Reactome; R-DME-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-DME-111469; SMAC, XIAP-regulated apoptotic response.
DR Reactome; R-DME-209447; Activation of the IkappaB kinase complex, KEY:IRD5 dimer:KEY.
DR Reactome; R-DME-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-DME-5675482; Regulation of necroptotic cell death.
DR Reactome; R-DME-8948747; Regulation of PTEN localization.
DR Reactome; R-DME-8948751; Regulation of PTEN stability and activity.
DR SignaLink; Q24307; -.
DR BioGRID-ORCS; 36748; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36748; -.
DR PRO; PR:Q24307; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0015247; Expressed in second segment of antenna (Drosophila) and 22 other tissues.
DR Genevisible; Q24307; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
DR GO; GO:0089720; F:caspase binding; IPI:FlyBase.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IDA:FlyBase.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:FlyBase.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:FlyBase.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; TAS:Reactome.
DR GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR GO; GO:0022416; P:chaeta development; IMP:FlyBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:FlyBase.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:FlyBase.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:FlyBase.
DR GO; GO:0061057; P:peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
DR GO; GO:0006964; P:positive regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria; IMP:FlyBase.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IBA:GO_Central.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:FlyBase.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:FlyBase.
DR GO; GO:0016567; P:protein ubiquitination; IDA:FlyBase.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:FlyBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR CDD; cd00022; BIR; 3.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001370; BIR_rpt.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00653; BIR; 3.
DR SMART; SM00238; BIR; 3.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS01282; BIR_REPEAT_1; 3.
DR PROSITE; PS50143; BIR_REPEAT_2; 3.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cytoplasm; Immunity; Innate immunity; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..498
FT /note="Death-associated inhibitor of apoptosis 2"
FT /id="PRO_0000122368"
FT REPEAT 12..77
FT /note="BIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT REPEAT 116..180
FT /note="BIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT REPEAT 215..280
FT /note="BIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT ZN_FING 451..486
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT SITE 100..101
FT /note="Cleavage; by caspases"
FT /evidence="ECO:0000269|PubMed:18166655"
FT MUTAGEN 92
FT /note="D->E: No effect on caspase-mediated cleavage."
FT /evidence="ECO:0000269|PubMed:18166655"
FT MUTAGEN 100
FT /note="D->E: Loss of caspase-mediated cleavage, failure to
FT protect against Drice-mediated cell death and loss of
FT binding to Drice."
FT /evidence="ECO:0000269|PubMed:18166655"
FT MUTAGEN 149
FT /note="C->G: No effect on binding to Drice or Dredd."
FT /evidence="ECO:0000269|PubMed:18166655,
FT ECO:0000269|PubMed:22549468"
FT MUTAGEN 163
FT /note="D->A: No effect on binding to Drice. Loss of
FT immunity to Gram-negative bacteria; when associated with A-
FT 263."
FT /evidence="ECO:0000269|PubMed:18166655,
FT ECO:0000269|PubMed:22549468"
FT MUTAGEN 249
FT /note="C->G: Abolishes binding to Drice and fails to
FT inhibit cell death. No effect on binding to Dredd."
FT /evidence="ECO:0000269|PubMed:18166655,
FT ECO:0000269|PubMed:22549468"
FT MUTAGEN 263
FT /note="D->A: Abolishes binding to Drice. Loss of immunity
FT to Gram-negative bacteria; when associated with A-163."
FT /evidence="ECO:0000269|PubMed:18166655,
FT ECO:0000269|PubMed:22549468"
FT MUTAGEN 466
FT /note="C->Y: Fails to bind to Dredd and promote its
FT polyubiquitylation."
FT /evidence="ECO:0000269|PubMed:22549468"
FT CONFLICT 5
FT /note="G -> V (in Ref. 2; AAC46988)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="N -> K (in Ref. 2; AAC46988)"
FT /evidence="ECO:0000305"
FT CONFLICT 64..65
FT /note="ER -> AG (in Ref. 3; AAC47155)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="E -> K (in Ref. 1; AAC41610)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="A -> D (in Ref. 8; AAB08398)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="A -> S (in Ref. 3; AAC47155)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="Q -> P (in Ref. 1; AAC41610, 3; AAC47155 and 8;
FT AAB08398)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="P -> T (in Ref. 8; AAB08398)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="A -> T (in Ref. 2; AAC46988)"
FT /evidence="ECO:0000305"
FT CONFLICT 369..376
FT /note="ALEVREPP -> DWRCASR (in Ref. 3; AAC47155)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 498 AA; 54538 MW; 0D0303DB2B26FA22 CRC64;
MTELGMELES VRLATFGEWP LNAPVSAEDL VANGFFATGN WLEAECHFCH VRIDRWEYGD
QVAERHRRSS PICSMVLAPN HCGNVPRSQE SDNEGNSVVD SPESCSCPDL LLEANRLVTF
KDWPNPNITP QALAKAGFYY LNRLDHVKCV WCNGVIAKWE KNDNAFEEHK RFFPQCPRVQ
MGPLIEFATG KNLDELGIQP TTLPLRPKYA CVDARLRTFT DWPISNIQPA SALAQAGLYY
QKIGDQVRCF HCNIGLRSWQ KEDEPWFEHA KWSPKCQFVL LAKGPAYVSE VLATTAANAS
SQPATAPAPT LQADVLMDEA PAKEALALGI DGGVVRNAIQ RKLLSSGCAF STLDELLHDI
FDDAGAGAAL EVREPPEPSA PFIEPCQATT SKAASVPIPV ADSIPAKPQA AEAVANISKI
TDEIQKMSVA TPNGNLSLEE ENRQLKDARL CKVCLDEEVG VVFLPCGHLA TCNQCAPSVA
NCPMCRADIK GFVRTFLS
