DBLOH_MOUSE
ID DBLOH_MOUSE Reviewed; 237 AA.
AC Q9JIQ3; Q542V8; Q9CZD1; Q9DCD3;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Diablo IAP-binding mitochondrial protein {ECO:0000312|MGI:MGI:1913843};
DE AltName: Full=Diablo homolog, mitochondrial {ECO:0000312|MGI:MGI:1913843};
DE AltName: Full=Direct IAP-binding protein with low pI {ECO:0000250|UniProtKB:Q9NR28};
DE AltName: Full=Second mitochondria-derived activator of caspase {ECO:0000303|PubMed:15178455};
DE Short=Smac {ECO:0000303|PubMed:15178455};
DE Flags: Precursor;
GN Name=Diablo {ECO:0000312|MGI:MGI:1913843};
GN Synonyms=Smac {ECO:0000303|PubMed:15178455};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Kidney;
RX PubMed=10929712; DOI=10.1016/s0092-8674(00)00009-x;
RA Verhagen A.M., Ekert P.G., Pakusch M., Silke J., Connolly L.M., Reid G.E.,
RA Moritz R.L., Simpson R.J., Vaux D.L.;
RT "Identification of DIABLO, a mammalian protein that promotes apoptosis by
RT binding to and antagonizing IAP proteins.";
RL Cell 102:43-53(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP INTERACTION WITH BEX3.
RX PubMed=15178455; DOI=10.1016/j.bbrc.2004.05.043;
RA Yoon K., Jang H.D., Lee S.Y.;
RT "Direct interaction of Smac with NADE promotes TRAIL-induced apoptosis.";
RL Biochem. Biophys. Res. Commun. 319:649-654(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INTERACTION WITH AREL1.
RX PubMed=23479728; DOI=10.1074/jbc.m112.436113;
RA Kim J.B., Kim S.Y., Kim B.M., Lee H., Kim I., Yun J., Jo Y., Oh T., Jo Y.,
RA Chae H.D., Shin D.Y.;
RT "Identification of a novel anti-apoptotic E3 ubiquitin ligase that
RT ubiquitinates antagonists of inhibitor of apoptosis proteins SMAC, HtrA2,
RT and ARTS.";
RL J. Biol. Chem. 288:12014-12021(2013).
CC -!- FUNCTION: Promotes apoptosis by activating caspases in the cytochrome
CC c/Apaf-1/caspase-9 pathway. Acts by opposing the inhibitory activity of
CC inhibitor of apoptosis proteins (IAP). Inhibits the activity of
CC BIRC6/bruce by inhibiting its binding to caspases (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:10929712}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with BIRC2/c-IAP1 (By
CC similarity). Interacts with BIRC6/bruce (By similarity). Interacts with
CC BIRC7/livin (By similarity). Interacts with the monomeric and dimeric
CC form of BIRC5/survivin (By similarity). Interacts with XIAP/BIRC4 (via
CC BIR3 domain) (By similarity). Interacts with BEX3 (PubMed:15178455).
CC Interacts with AREL1 (via HECT domain); in the cytoplasm following
CC induction of apoptosis (PubMed:23479728).
CC {ECO:0000250|UniProtKB:Q9NR28, ECO:0000269|PubMed:15178455,
CC ECO:0000269|PubMed:23479728}.
CC -!- INTERACTION:
CC PRO_0000021073; P98170: XIAP; Xeno; NbExp=3; IntAct=EBI-25438230, EBI-517127;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10929712}.
CC Note=Released into the cytosol when cells undergo apoptosis.
CC -!- TISSUE SPECIFICITY: Highest expression found in heart, liver, kidney
CC and testis. {ECO:0000269|PubMed:10929712}.
CC -!- DOMAIN: The mature N-terminus mediates interaction with XIAP/BIRC4.
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated by BIRC7/livin. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF203914; AAF82190.1; -; mRNA.
DR EMBL; AK012760; BAB28450.1; -; mRNA.
DR EMBL; AK002887; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK077198; BAC36676.1; -; mRNA.
DR EMBL; AK133194; BAE21552.1; -; mRNA.
DR EMBL; AC157931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS39270.1; -.
DR RefSeq; NP_075721.3; NM_023232.3.
DR AlphaFoldDB; Q9JIQ3; -.
DR SMR; Q9JIQ3; -.
DR BioGRID; 211579; 5.
DR IntAct; Q9JIQ3; 2.
DR MINT; Q9JIQ3; -.
DR STRING; 10090.ENSMUSP00000107214; -.
DR iPTMnet; Q9JIQ3; -.
DR PhosphoSitePlus; Q9JIQ3; -.
DR EPD; Q9JIQ3; -.
DR MaxQB; Q9JIQ3; -.
DR PaxDb; Q9JIQ3; -.
DR PeptideAtlas; Q9JIQ3; -.
DR PRIDE; Q9JIQ3; -.
DR ProteomicsDB; 279167; -.
DR Antibodypedia; 1070; 720 antibodies from 45 providers.
DR DNASU; 66593; -.
DR Ensembl; ENSMUST00000111587; ENSMUSP00000107214; ENSMUSG00000029433.
DR Ensembl; ENSMUST00000125652; ENSMUSP00000115045; ENSMUSG00000029433.
DR GeneID; 66593; -.
DR KEGG; mmu:66593; -.
DR UCSC; uc008znx.1; mouse.
DR CTD; 56616; -.
DR MGI; MGI:1913843; Diablo.
DR VEuPathDB; HostDB:ENSMUSG00000029433; -.
DR eggNOG; ENOG502RA48; Eukaryota.
DR GeneTree; ENSGT00390000007237; -.
DR InParanoid; Q9JIQ3; -.
DR OMA; EDTIWQV; -.
DR OrthoDB; 1311341at2759; -.
DR PhylomeDB; Q9JIQ3; -.
DR TreeFam; TF102048; -.
DR Reactome; R-MMU-111457; Release of apoptotic factors from the mitochondria.
DR Reactome; R-MMU-111463; SMAC (DIABLO) binds to IAPs.
DR Reactome; R-MMU-111464; SMAC(DIABLO)-mediated dissociation of IAP:caspase complexes.
DR Reactome; R-MMU-111469; SMAC, XIAP-regulated apoptotic response.
DR Reactome; R-MMU-9627069; Regulation of the apoptosome activity.
DR BioGRID-ORCS; 66593; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Diablo; mouse.
DR PRO; PR:Q9JIQ3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9JIQ3; protein.
DR Bgee; ENSMUSG00000029433; Expressed in spermatocyte and 151 other tissues.
DR ExpressionAtlas; Q9JIQ3; baseline and differential.
DR Genevisible; Q9JIQ3; MM.
DR GO; GO:0035631; C:CD40 receptor complex; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
DR GO; GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; IDA:MGI.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:UniProtKB.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IDA:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IDA:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR InterPro; IPR009062; Smac/DIABLO-like_sf.
DR InterPro; IPR015142; Smac_DIABLO.
DR PANTHER; PTHR32247; PTHR32247; 1.
DR Pfam; PF09057; Smac_DIABLO; 1.
DR SUPFAM; SSF46984; SSF46984; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Mitochondrion; Phosphoprotein; Reference proteome;
KW Transit peptide; Ubl conjugation.
FT TRANSIT 1..53
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 54..237
FT /note="Diablo IAP-binding mitochondrial protein"
FT /id="PRO_0000021073"
FT REGION 206..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 54..58
FT /note="IAP-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 206..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 64
FT /note="Q -> H (in Ref. 1; AAF82190)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 237 AA; 26820 MW; 6961A7E76C780AC5 CRC64;
MAALRSWVTR SVCSLFRYRQ RFPVLANSKK RCFSELIKPW HKTVLTGFGM TLCAVPIAQK
SEPQSLSNEA LMRRAVSLVT DSTSTFLSQT TYALIEAITE YTKAVYTLVS LYRQYTSLLG
KMNSQEEDEV WQVIIGARVE MTSKQQEYLK LETTWMTAVG LSEMAAEAAY QTGADQASIT
ARNHIQLVKS QVQEVRQLSQ KAETKLAEAQ TKELHQKAQE VSDEGADQEE EAYLRED
