DIAP1_DROME
ID DIAP1_DROME Reviewed; 438 AA.
AC Q24306; A4V1Z9; A9UN33; Q0E8E4; Q8MRM5; Q9VUX5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Death-associated inhibitor of apoptosis 1;
DE EC=2.3.2.27 {ECO:0000269|PubMed:14517550, ECO:0000269|PubMed:21145488, ECO:0000269|PubMed:22304967};
DE AltName: Full=Apoptosis 1 inhibitor;
DE AltName: Full=E3 ubiquitin-protein ligase th;
DE AltName: Full=Inhibitor of apoptosis 1;
DE AltName: Full=Protein thread;
DE AltName: Full=RING-type E3 ubiquitin transferase Diap1 {ECO:0000305};
GN Name=Diap1; Synonyms=Iap1, th; ORFNames=CG12284;
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 [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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Ovary;
RA Stapleton M., Booth B., Carlson J.W., Frise E., Kapadia B., Park S.,
RA Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-438.
RC STRAIN=Berkeley; TISSUE=Head;
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 [6]
RP INTERACTION WITH DRONC.
RC TISSUE=Embryo;
RX PubMed=10675329; DOI=10.1093/emboj/19.4.598;
RA Meier P., Silke J., Leevers S.J., Evan G.I.;
RT "The Drosophila caspase DRONC is regulated by DIAP1.";
RL EMBO J. 19:598-611(2000).
RN [7]
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 [8]
RP FUNCTION, INTERACTION WITH HTRA2, AND CLEAVAGE.
RX PubMed=17397804; DOI=10.1016/j.bbrc.2007.03.079;
RA Igaki T., Suzuki Y., Tokushige N., Aonuma H., Takahashi R., Miura M.;
RT "Evolution of mitochondrial cell death pathway: Proapoptotic role of
RT HtrA2/Omi in Drosophila.";
RL Biochem. Biophys. Res. Commun. 356:993-997(2007).
RN [9]
RP FUNCTION, INTERACTION WITH HTRA2, CLEAVAGE, AND MUTAGENESIS OF ILE-162 AND
RP ILE-165.
RC STRAIN=Berkeley; TISSUE=Testis;
RX PubMed=18259196; DOI=10.1038/cdd.2008.19;
RA Khan F.S., Fujioka M., Datta P., Fernandes-Alnemri T., Jaynes J.B.,
RA Alnemri E.S.;
RT "The interaction of DIAP1 with dOmi/HtrA2 regulates cell death in
RT Drosophila.";
RL Cell Death Differ. 15:1073-1083(2008).
RN [10]
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 [11]
RP FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE OF THE NEDD8 CONJUGATION
RP PATHWAY, AND CATALYTIC ACTIVITY.
RX PubMed=21145488; DOI=10.1016/j.molcel.2010.11.011;
RA Broemer M., Tenev T., Rigbolt K.T., Hempel S., Blagoev B., Silke J.,
RA Ditzel M., Meier P.;
RT "Systematic in vivo RNAi analysis identifies IAPs as NEDD8-E3 ligases.";
RL Mol. Cell 40:810-822(2010).
RN [12]
RP REVIEW ON FUNCTION.
RX PubMed=22095281; DOI=10.1038/cdd.2011.163;
RA Darding M., Meier P.;
RT "IAPs: guardians of RIPK1.";
RL Cell Death Differ. 19:58-66(2012).
RN [13]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22304967; DOI=10.1016/j.molcel.2011.12.032;
RA Hanson A.J., Wallace H.A., Freeman T.J., Beauchamp R.D., Lee L.A., Lee E.;
RT "XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt signaling.";
RL Mol. Cell 45:619-628(2012).
RN [14]
RP INTERACTION WITH UBR3.
RX PubMed=25146930; DOI=10.1038/cdd.2014.115;
RA Huang Q., Tang X., Wang G., Fan Y., Ray L., Bergmann A., Belenkaya T.Y.,
RA Ling X., Yan D., Lin Y., Ye X., Shi W., Zhou X., Lu F., Qu J., Lin X.;
RT "Ubr3 E3 ligase regulates apoptosis by controlling the activity of DIAP1 in
RT Drosophila.";
RL Cell Death Differ. 21:1961-1970(2014).
RN [15]
RP INTERACTION WITH UBR3.
RX PubMed=26383956; DOI=10.1126/science.aac5677;
RA Zanet J., Benrabah E., Li T., Pelissier-Monier A., Chanut-Delalande H.,
RA Ronsin B., Bellen H.J., Payre F., Plaza S.;
RT "Pri sORF peptides induce selective proteasome-mediated protein
RT processing.";
RL Science 349:1356-1358(2015).
RN [16]
RP DEVELOPMENTAL STAGE.
RX PubMed=27462444; DOI=10.1038/celldisc.2015.47;
RA Hu L., Xu J., Yin M.X., Zhang L., Lu Y., Wu W., Xue Z., Ho M.S., Gao G.,
RA Zhao Y., Zhang L.;
RT "Ack promotes tissue growth via phosphorylation and suppression of the
RT Hippo pathway component Expanded.";
RL Cell Discov. 2:15047-15047(2016).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 215-310.
RX PubMed=11511363; DOI=10.1016/s1097-2765(01)00282-9;
RA Wu J.W., Cocina A.E., Chai J., Hay B.A., Shi Y.;
RT "Structural analysis of a functional DIAP1 fragment bound to grim and hid
RT peptides.";
RL Mol. Cell 8:95-104(2001).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 201-324 IN COMPLEX WITH DRONC,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=14517550; DOI=10.1038/nsb989;
RA Chai J., Yan N., Huh J.R., Wu J.-W., Li W., Hay B.A., Shi Y.;
RT "Molecular mechanism of Reaper-Grim-Hid-mediated suppression of DIAP1-
RT dependent Dronc ubiquitination.";
RL Nat. Struct. Biol. 10:892-898(2003).
CC -!- FUNCTION: Anti-apoptotic protein which functions as a caspase
CC regulator, using its E3 ubiquitin-protein ligase activity to smother
CC caspase activity. Binds, ubiquitinates and inactivates initiator
CC caspase Dronc, and effector caspases Drice and Dcp-1. Acts as a Nedd8-
CC E3 ubiquitin-protein ligase for Drice. Suppresses apoptosis by
CC targeting the apoptosome for ubiquitination and inactivation. Plays an
CC important role in cell motility. Overexpression suppresses rpr and hid-
CC dependent cell death in the eye. Interaction of Diap1 with Dronc is
CC required to suppress Dronc-mediated cell death through Diap1-mediated
CC ubiquitination of Dronc. Acts as a positive regulator of Wnt signaling.
CC {ECO:0000269|PubMed:14517550, ECO:0000269|PubMed:17397804,
CC ECO:0000269|PubMed:18259196, ECO:0000269|PubMed:21145488,
CC ECO:0000269|PubMed:22304967, ECO:0000269|PubMed:8548811}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:14517550,
CC ECO:0000269|PubMed:21145488, ECO:0000269|PubMed:22304967};
CC -!- SUBUNIT: Interacts (via BIR 2 domain) with Dronc (via residues 114-
CC 125). Rpr, hid and grim can outcompete Dronc for binding Diap1
CC therefore removing Diap1-mediated ubiquitination. Interacts (via BIR 2
CC domain) with HtrA2; this displaces any bound Dronc. Interacts with
CC Strica (PubMed:11550090). The N-terminally cleaved form interacts with
CC Ubr3 (via UBR-type zinc finger) (PubMed:25146930, PubMed:26383956); the
CC interaction promotes the recruitment and uniquitination of substrate
CC capases such as Dronc (PubMed:25146930). {ECO:0000269|PubMed:10675329,
CC ECO:0000269|PubMed:11550090, ECO:0000269|PubMed:14517550,
CC ECO:0000269|PubMed:17397804, ECO:0000269|PubMed:18259196,
CC ECO:0000269|PubMed:25146930, ECO:0000269|PubMed:26383956}.
CC -!- INTERACTION:
CC Q24306; P25843: chic; NbExp=2; IntAct=EBI-456419, EBI-156199;
CC Q24306; Q9XYF4: Dronc; NbExp=9; IntAct=EBI-456419, EBI-108311;
CC Q24306; Q24106: hid; NbExp=8; IntAct=EBI-456419, EBI-135509;
CC Q24306; Q86PE7: IKKepsilon; NbExp=3; IntAct=EBI-456419, EBI-987197;
CC Q24306; Q24475: rpr; NbExp=6; IntAct=EBI-456419, EBI-106786;
CC -!- DEVELOPMENTAL STAGE: Detected in wing disks (at protein level).
CC {ECO:0000269|PubMed:27462444}.
CC -!- PTM: Ubiquitinated and degraded by HtrA2 in apoptotic cells;
CC proteolytic cleavage at specific sites in the BIR domain linker region
CC generating inactive fragments. Mutation of one site reduces but does
CC not abolish cleavage as another site is selected by the protease.
CC {ECO:0000269|PubMed:17397804, ECO:0000269|PubMed:18259196}.
CC -!- SIMILARITY: Belongs to the IAP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM50178.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; L49440; AAC41609.1; -; mRNA.
DR EMBL; AE014296; AAF49548.1; -; Genomic_DNA.
DR EMBL; AE014296; AAG22319.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11757.1; -; Genomic_DNA.
DR EMBL; BT031197; ABY20438.2; -; mRNA.
DR EMBL; AY119524; AAM50178.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001261916.1; NM_001274987.1.
DR RefSeq; NP_001261917.1; NM_001274988.1.
DR RefSeq; NP_001261918.1; NM_001274989.1.
DR RefSeq; NP_524101.2; NM_079377.3.
DR RefSeq; NP_730097.1; NM_168644.2.
DR RefSeq; NP_730098.1; NM_168645.2.
DR PDB; 1JD4; X-ray; 2.70 A; A/B=201-323.
DR PDB; 1JD5; X-ray; 1.90 A; A=201-323.
DR PDB; 1JD6; X-ray; 2.70 A; A=201-323.
DR PDB; 1Q4Q; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J=201-323.
DR PDB; 1SDZ; X-ray; 1.78 A; A=30-145.
DR PDB; 1SE0; X-ray; 1.75 A; A=30-145.
DR PDB; 3SIP; X-ray; 3.50 A; E/F=31-145.
DR PDB; 3SIQ; X-ray; 2.40 A; A/B/C/D/E/F=1-135.
DR PDBsum; 1JD4; -.
DR PDBsum; 1JD5; -.
DR PDBsum; 1JD6; -.
DR PDBsum; 1Q4Q; -.
DR PDBsum; 1SDZ; -.
DR PDBsum; 1SE0; -.
DR PDBsum; 3SIP; -.
DR PDBsum; 3SIQ; -.
DR AlphaFoldDB; Q24306; -.
DR SMR; Q24306; -.
DR BioGRID; 65064; 116.
DR IntAct; Q24306; 10.
DR MINT; Q24306; -.
DR STRING; 7227.FBpp0305795; -.
DR MEROPS; I32.009; -.
DR PaxDb; Q24306; -.
DR EnsemblMetazoa; FBtr0075499; FBpp0075254; FBgn0260635.
DR EnsemblMetazoa; FBtr0075500; FBpp0075255; FBgn0260635.
DR EnsemblMetazoa; FBtr0075501; FBpp0075256; FBgn0260635.
DR EnsemblMetazoa; FBtr0333617; FBpp0305793; FBgn0260635.
DR EnsemblMetazoa; FBtr0333618; FBpp0305794; FBgn0260635.
DR EnsemblMetazoa; FBtr0333619; FBpp0305795; FBgn0260635.
DR GeneID; 39753; -.
DR KEGG; dme:Dmel_CG12284; -.
DR CTD; 39753; -.
DR FlyBase; FBgn0260635; Diap1.
DR VEuPathDB; VectorBase:FBgn0260635; -.
DR eggNOG; KOG1101; Eukaryota.
DR HOGENOM; CLU_016347_1_0_1; -.
DR InParanoid; Q24306; -.
DR OMA; VQANYPH; -.
DR OrthoDB; 1340284at2759; -.
DR PhylomeDB; Q24306; -.
DR Reactome; R-DME-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-DME-111469; SMAC, XIAP-regulated apoptotic response.
DR Reactome; R-DME-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-DME-390150; DS ligand bound to FT receptor.
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; Q24306; -.
DR BioGRID-ORCS; 39753; 1 hit in 3 CRISPR screens.
DR EvolutionaryTrace; Q24306; -.
DR GenomeRNAi; 39753; -.
DR PRO; PR:Q24306; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0260635; Expressed in eye disc (Drosophila) and 69 other tissues.
DR ExpressionAtlas; Q24306; baseline and differential.
DR Genevisible; Q24306; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0089720; F:caspase binding; IPI:FlyBase.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:FlyBase.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IDA:FlyBase.
DR GO; GO:0061663; F:NEDD8 ligase activity; IDA:FlyBase.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI: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:0044390; F:ubiquitin-like protein conjugating enzyme binding; IPI:FlyBase.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; TAS:UniProtKB.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR GO; GO:0048800; P:antennal morphogenesis; IMP:FlyBase.
DR GO; GO:0006915; P:apoptotic process; IPI:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0022416; P:chaeta development; IMP:FlyBase.
DR GO; GO:0097340; P:inhibition of cysteine-type endopeptidase activity; IDA:FlyBase.
DR GO; GO:1990001; P:inhibition of cysteine-type endopeptidase activity involved in apoptotic process; IMP:FlyBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:FlyBase.
DR GO; GO:0046673; P:negative regulation of compound eye retinal cell programmed cell death; IMP:FlyBase.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:FlyBase.
DR GO; GO:2001271; P:negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis; IDA:FlyBase.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IGI:FlyBase.
DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IMP:FlyBase.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:FlyBase.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:FlyBase.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IMP:FlyBase.
DR GO; GO:0045116; P:protein neddylation; IDA:FlyBase.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:FlyBase.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0045035; P:sensory organ precursor cell division; IGI:FlyBase.
DR GO; GO:0007289; P:spermatid nucleus differentiation; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd00022; BIR; 2.
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; 2.
DR SMART; SM00238; BIR; 2.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS01282; BIR_REPEAT_1; 2.
DR PROSITE; PS50143; BIR_REPEAT_2; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Metal-binding; Reference proteome; Repeat;
KW Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Wnt signaling pathway; Zinc; Zinc-finger.
FT CHAIN 1..438
FT /note="Death-associated inhibitor of apoptosis 1"
FT /id="PRO_0000122367"
FT REPEAT 44..110
FT /note="BIR 1"
FT REPEAT 226..293
FT /note="BIR 2"
FT ZN_FING 391..426
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 194..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT SITE 162..163
FT /note="Cleavage; by HtrA2"
FT SITE 165..166
FT /note="Cleavage; by HtrA2"
FT MUTAGEN 162
FT /note="I->D: Destroys cleavage site."
FT /evidence="ECO:0000269|PubMed:18259196"
FT MUTAGEN 165
FT /note="I->D: Destroys cleavage site."
FT /evidence="ECO:0000269|PubMed:18259196"
FT CONFLICT 319
FT /note="S -> T (in Ref. 1; AAC41609)"
FT /evidence="ECO:0000305"
FT CONFLICT 324..325
FT /note="VA -> DT (in Ref. 1; AAC41609)"
FT /evidence="ECO:0000305"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1SDZ"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:1SE0"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:3SIQ"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:1SE0"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1SE0"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1SE0"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1SE0"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1SE0"
FT HELIX 96..103
FT /evidence="ECO:0007829|PDB:1SE0"
FT TURN 108..112
FT /evidence="ECO:0007829|PDB:1SE0"
FT HELIX 122..128
FT /evidence="ECO:0007829|PDB:1SE0"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:3SIP"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:1JD5"
FT HELIX 226..232
FT /evidence="ECO:0007829|PDB:1JD5"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:1JD5"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1Q4Q"
FT HELIX 244..249
FT /evidence="ECO:0007829|PDB:1JD5"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:1JD5"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:1JD5"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:1JD5"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:1JD5"
FT HELIX 279..286
FT /evidence="ECO:0007829|PDB:1JD5"
FT HELIX 291..297
FT /evidence="ECO:0007829|PDB:1JD5"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:1JD5"
FT HELIX 309..317
FT /evidence="ECO:0007829|PDB:1JD5"
SQ SEQUENCE 438 AA; 48038 MW; 24CA8BC13F5DEF31 CRC64;
MASVVADLPS YGPIAFDQVD NNTNATQLFK NNINKTRMND LNREETRLKT FTDWPLDWLD
KRQLAQTGMY FTHAGDKVKC FFCGVEIGCW EQEDQPVPEH QRWSPNCPLL RRRTTNNVPI
NAEALDRILP PISYDICGAN DSTLEMREHA YAEGVIPMSQ LIQSIGMNAV NAAGSVTGTA
APQPRVTVAT HASTATQATG DVQPETCRPS AASGNYFPQY PEYAIETARL RTFEAWPRNL
KQKPHQLAEA GFFYTGVGDR VRCFSCGGGL MDWNDNDEPW EQHALWLSQC RFVKLMKGQL
YIDTVAAKPV LAEEKEESSS IGGVAVASTQ ASEEEQQTSL SSEEAVSGDV APSVAPTAAT
RIFNKIVEAT AVATPSTNSS GSTSIPEEKL CKICYGAEYN TAFLPCGHVV ACAKCASSVT
KCPLCRKPFT DVMRVYFS
