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Diablo homolog, mitochondrial (Direct IAP-binding protein with low pI) (Second mitochondria-derived activator of caspase) (Smac)

 DBLOH_HUMAN             Reviewed;         239 AA.
Q9NR28; B2RDQ0; Q6W3F3; Q96LV0; Q9BT11; Q9HAV6;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
18-JUL-2018, entry version 178.
RecName: Full=Diablo homolog, mitochondrial;
AltName: Full=Direct IAP-binding protein with low pI;
AltName: Full=Second mitochondria-derived activator of caspase;
Short=Smac;
Flags: Precursor;
Name=DIABLO; Synonyms=SMAC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE,
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=10929711; DOI=10.1016/S0092-8674(00)00008-8;
Du C., Fang M., Li Y., Li L., Wang X.;
"Smac, a mitochondrial protein that promotes cytochrome c-dependent
caspase activation by eliminating IAP inhibition.";
Cell 102:33-42(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND CHARACTERIZATION.
PubMed=10950947; DOI=10.1074/jbc.C000533200;
Srinivasula S.M., Datta P., Fan X.J., Fernandes-Alnemri T., Huang Z.,
Alnemri E.S.;
"Molecular determinants of the caspase-promoting activity of
Smac/DIABLO and its role in the death receptor pathway.";
J. Biol. Chem. 275:36152-36157(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=14523016; DOI=10.1074/jbc.M308036200;
Fu J., Jin Y., Arend L.J.;
"Smac3, a novel Smac/DIABLO splicing variant, attenuates the stability
and apoptosis-inhibiting activity of X-linked inhibitor of apoptosis
protein.";
J. Biol. Chem. 278:52660-52672(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Stomach;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, AND INTERACTION WITH BIRC6/BRUCE.
PubMed=15200957; DOI=10.1016/j.molcel.2004.05.018;
Bartke T., Pohl C., Pyrowolakis G., Jentsch S.;
"Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3
ubiquitin ligase.";
Mol. Cell 14:801-811(2004).
[8]
UBIQUITINATION BY BIRC7/LIVIN, AND INTERACTION WITH BIRC7/LIVIN.
PubMed=16729033; DOI=10.1038/sj.cdd.4401959;
Ma L., Huang Y., Song Z., Feng S., Tian X., Du W., Qiu X., Heese K.,
Wu M.;
"Livin promotes Smac/DIABLO degradation by ubiquitin-proteasome
pathway.";
Cell Death Differ. 13:2079-2088(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
INTERACTION WITH BIRC5/SURVIVIN.
PubMed=21536684; DOI=10.1074/jbc.M111.237586;
Pavlyukov M.S., Antipova N.V., Balashova M.V., Vinogradova T.V.,
Kopantzev E.P., Shakhparonov M.I.;
"Survivin monomer plays an essential role in apoptosis regulation.";
J. Biol. Chem. 286:23296-23307(2011).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[13]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 56-239.
PubMed=10972280; DOI=10.1038/35022514;
Chai J., Du C., Wu J.W., Kyin S., Wang X., Shi Y.;
"Structural and biochemical basis of apoptotic activation by
Smac/DIABLO.";
Nature 406:855-862(2000).
[14]
STRUCTURE BY NMR OF 56-64 IN COMPLEX WITH XIAP.
PubMed=11140637; DOI=10.1038/35050006;
Liu Z., Sun C., Olejniczak E.T., Meadows R.P., Betz S.F., Oost T.,
Herrmann J., Wu J.C., Fesik S.W.;
"Structural basis for binding of Smac/DIABLO to the XIAP BIR3
domain.";
Nature 408:1004-1008(2000).
[15]
VARIANT DFNA64 LEU-126, AND CHARACTERIZATION OF DFNA64 LEU-126.
PubMed=21722859; DOI=10.1016/j.ajhg.2011.05.027;
Cheng J., Zhu Y., He S., Lu Y., Chen J., Han B., Petrillo M.,
Wrzeszczynski K.O., Yang S., Dai P., Zhai S., Han D., Zhang M.Q.,
Li W., Liu X., Li H., Chen Z.Y., Yuan H.;
"Functional mutation of SMAC/DIABLO, encoding a mitochondrial
proapoptotic protein, causes human progressive hearing loss DFNA64.";
Am. J. Hum. Genet. 89:56-66(2011).
-!- FUNCTION: Promotes apoptosis by activating caspases in the
cytochrome c/Apaf-1/caspase-9 pathway. Acts by opposing the
inhibitory activity of inhibitor of apoptosis proteins (IAP).
Inhibits the activity of BIRC6/bruce by inhibiting its binding to
caspases. Isoform 3 attenuates the stability and apoptosis-
inhibiting activity of XIAP/BIRC4 by promoting XIAP/BIRC4
ubiquitination and degradation through the ubiquitin-proteasome
pathway. Isoform 3 also disrupts XIAP/BIRC4 interacting with
processed caspase-9 and promotes caspase-3 activation. Isoform 1
is defective in the capacity to down-regulate the XIAP/BIRC4
abundance. {ECO:0000269|PubMed:10929711,
ECO:0000269|PubMed:14523016, ECO:0000269|PubMed:15200957}.
-!- SUBUNIT: Homodimer. Interacts with BEX3 (By similarity). Interacts
with BIRC2/c-IAP1, BIRC3/c-IAP2, XIAP/BIRC4, BIRC6/bruce and
BIRC7/livin. Interacts with the monomeric and dimeric form of
BIRC5/survivin. {ECO:0000250, ECO:0000269|PubMed:11140637,
ECO:0000269|PubMed:15200957, ECO:0000269|PubMed:16729033,
ECO:0000269|PubMed:21536684}.
-!- INTERACTION:
Q6RW13-2:AGTRAP; NbExp=5; IntAct=EBI-517508, EBI-11522760;
Q15041:ARL6IP1; NbExp=8; IntAct=EBI-517508, EBI-714543;
Q13490:BIRC2; NbExp=6; IntAct=EBI-517508, EBI-514538;
Q13489:BIRC3; NbExp=2; IntAct=EBI-517508, EBI-517709;
O15392:BIRC5; NbExp=2; IntAct=EBI-517508, EBI-518823;
Q96CA5:BIRC7; NbExp=6; IntAct=EBI-517508, EBI-517623;
Q05655:PRKCD; NbExp=4; IntAct=EBI-517508, EBI-704279;
P98170:XIAP; NbExp=9; IntAct=EBI-517508, EBI-517127;
Q60989:Xiap (xeno); NbExp=3; IntAct=EBI-517508, EBI-517478;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14523016}.
Note=Released into the cytosol when cells undergo apoptosis.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9NR28-1; Sequence=Displayed;
Name=2; Synonyms=Diablo-S;
IsoId=Q9NR28-2; Sequence=VSP_004397;
Name=3; Synonyms=SMAC3;
IsoId=Q9NR28-3; Sequence=VSP_042785;
-!- TISSUE SPECIFICITY: Ubiquitously expressed with highest expression
in testis. Expression is also high in heart, liver, kidney,
spleen, prostate and ovary. Low in brain, lung, thymus and
peripheral blood leukocytes. Isoform 3 is ubiquitously expressed.
{ECO:0000269|PubMed:10929711, ECO:0000269|PubMed:14523016}.
-!- DOMAIN: The mature N-terminus mediates interaction with
XIAP/BIRC4.
-!- PTM: Ubiquitinated by BIRC7/livin. {ECO:0000269|PubMed:16729033}.
-!- DISEASE: Deafness, autosomal dominant, 64 (DFNA64) [MIM:614152]: A
form of non-syndromic sensorineural hearing loss. Sensorineural
deafness results from damage to the neural receptors of the inner
ear, the nerve pathways to the brain, or the area of the brain
that receives sound information. {ECO:0000269|PubMed:21722859}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
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EMBL; AF262240; AAF87716.1; -; mRNA.
EMBL; AY313210; AAQ86939.1; -; mRNA.
EMBL; AK024768; BAB14994.1; -; mRNA.
EMBL; AK057778; BAB71568.1; -; mRNA.
EMBL; AK315629; BAG37997.1; -; mRNA.
EMBL; AF298770; AAG22077.1; -; mRNA.
EMBL; AC048338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC004417; AAH04417.1; -; mRNA.
EMBL; BC011909; AAH11909.1; -; mRNA.
CCDS; CCDS9228.1; -. [Q9NR28-1]
CCDS; CCDS9229.1; -. [Q9NR28-3]
RefSeq; NP_001265231.1; NM_001278302.1.
RefSeq; NP_001265232.1; NM_001278303.1.
RefSeq; NP_001265233.1; NM_001278304.1. [Q9NR28-2]
RefSeq; NP_001265271.1; NM_001278342.1. [Q9NR28-3]
RefSeq; NP_063940.1; NM_019887.5. [Q9NR28-1]
RefSeq; NP_620308.1; NM_138930.3. [Q9NR28-2]
UniGene; Hs.169611; -.
PDB; 1FEW; X-ray; 2.20 A; A=56-239.
PDB; 1G3F; NMR; -; B=56-64.
PDB; 1G73; X-ray; 2.00 A; A/B=56-217.
PDB; 1OXQ; X-ray; 2.30 A; F=56-64.
PDB; 1TW6; X-ray; 1.71 A; C/D=56-64.
PDB; 1XB0; X-ray; 2.20 A; G/H/I/J/K/L=56-62.
PDB; 1XB1; X-ray; 2.70 A; G/H/I/J/K/L=56-62.
PDB; 3D9U; X-ray; 2.30 A; B=56-61.
PDB; 3UIH; X-ray; 2.40 A; P/Q=56-70.
PDB; 3UIJ; X-ray; 2.70 A; P/Q=56-70.
PDB; 4TX5; X-ray; 1.80 A; A/B=56-239.
PDBsum; 1FEW; -.
PDBsum; 1G3F; -.
PDBsum; 1G73; -.
PDBsum; 1OXQ; -.
PDBsum; 1TW6; -.
PDBsum; 1XB0; -.
PDBsum; 1XB1; -.
PDBsum; 3D9U; -.
PDBsum; 3UIH; -.
PDBsum; 3UIJ; -.
PDBsum; 4TX5; -.
ProteinModelPortal; Q9NR28; -.
SMR; Q9NR28; -.
BioGrid; 121157; 50.
DIP; DIP-27627N; -.
IntAct; Q9NR28; 48.
MINT; Q9NR28; -.
STRING; 9606.ENSP00000398495; -.
MoonDB; Q9NR28; Predicted.
iPTMnet; Q9NR28; -.
PhosphoSitePlus; Q9NR28; -.
DMDM; 18203316; -.
EPD; Q9NR28; -.
MaxQB; Q9NR28; -.
PaxDb; Q9NR28; -.
PeptideAtlas; Q9NR28; -.
PRIDE; Q9NR28; -.
ProteomicsDB; 82262; -.
ProteomicsDB; 82263; -. [Q9NR28-2]
ProteomicsDB; 82264; -. [Q9NR28-3]
TopDownProteomics; Q9NR28-1; -. [Q9NR28-1]
TopDownProteomics; Q9NR28-2; -. [Q9NR28-2]
TopDownProteomics; Q9NR28-3; -. [Q9NR28-3]
DNASU; 56616; -.
Ensembl; ENST00000353548; ENSP00000320343; ENSG00000184047. [Q9NR28-3]
Ensembl; ENST00000443649; ENSP00000398495; ENSG00000284934. [Q9NR28-1]
Ensembl; ENST00000464942; ENSP00000442360; ENSG00000184047. [Q9NR28-1]
GeneID; 56616; -.
KEGG; hsa:56616; -.
UCSC; uc010tab.4; human. [Q9NR28-1]
CTD; 56616; -.
DisGeNET; 56616; -.
EuPathDB; HostDB:ENSG00000184047.15; -.
GeneCards; DIABLO; -.
HGNC; HGNC:21528; DIABLO.
HPA; CAB003857; -.
HPA; CAB016688; -.
HPA; HPA001825; -.
MalaCards; DIABLO; -.
MIM; 605219; gene.
MIM; 614152; phenotype.
neXtProt; NX_Q9NR28; -.
OpenTargets; ENSG00000184047; -.
Orphanet; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
PharmGKB; PA134945044; -.
eggNOG; ENOG410IHTM; Eukaryota.
eggNOG; ENOG4111KJ0; LUCA.
GeneTree; ENSGT00390000007237; -.
HOGENOM; HOG000217916; -.
HOVERGEN; HBG051315; -.
InParanoid; Q9NR28; -.
KO; K10522; -.
OMA; YAKAVHT; -.
OrthoDB; EOG091G0L3E; -.
PhylomeDB; Q9NR28; -.
TreeFam; TF102048; -.
Reactome; R-HSA-111457; Release of apoptotic factors from the mitochondria.
Reactome; R-HSA-111463; SMAC binds to IAPs.
Reactome; R-HSA-111464; SMAC-mediated dissociation of IAP:caspase complexes.
SIGNOR; Q9NR28; -.
ChiTaRS; DIABLO; human.
EvolutionaryTrace; Q9NR28; -.
GeneWiki; Diablo_homolog; -.
GenomeRNAi; 56616; -.
PMAP-CutDB; Q9NR28; -.
PRO; PR:Q9NR28; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000184047; -.
CleanEx; HS_DIABLO; -.
ExpressionAtlas; Q9NR28; baseline and differential.
Genevisible; Q9NR28; HS.
GO; GO:0035631; C:CD40 receptor complex; ISS:BHF-UCL.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005758; C:mitochondrial intermembrane space; TAS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; TAS:UniProtKB.
GO; GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; TAS:ProtInc.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; TAS:ProtInc.
GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; TAS:UniProtKB.
InterPro; IPR009062; Smac/DIABLO-like_sf.
InterPro; IPR015142; Smac_DIABLO.
PANTHER; PTHR32247; PTHR32247; 1.
Pfam; PF09057; Smac_DIABLO; 1.
SUPFAM; SSF46984; SSF46984; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Complete proteome;
Deafness; Direct protein sequencing; Disease mutation; Mitochondrion;
Non-syndromic deafness; Reference proteome; Transit peptide;
Ubl conjugation.
TRANSIT 1 55 Mitochondrion.
CHAIN 56 239 Diablo homolog, mitochondrial.
/FTId=PRO_0000021072.
MOTIF 56 60 IAP-binding.
VAR_SEQ 1 60 MAALKSWLSRSVTSFFRYRQCLCVPVVANFKKRCFSELIRP
WHKTVTIGFGVTLCAVPIA -> MKSDFYF (in
isoform 2).
{ECO:0000303|PubMed:10950947}.
/FTId=VSP_004397.
VAR_SEQ 62 105 Missing (in isoform 3).
{ECO:0000303|PubMed:14523016}.
/FTId=VSP_042785.
VARIANT 126 126 S -> L (in DFNA64; does not increase
apoptotic activity compared to wild-type;
enhances the degradation of mutant and
wild-type protein via heterodimerization;
cells expressing the mutant protein show
increased susceptibility to calcium-
induced loss of mitochondrial potential
compared to wild-type, indicating
increased sensitivity to mitochondrial
stress and suggestive of mitochondrial
dysfunction; dbSNP:rs387906893).
{ECO:0000269|PubMed:21722859}.
/FTId=VAR_066487.
CONFLICT 32 32 K -> E (in Ref. 4; BAB71568).
{ECO:0000305}.
CONFLICT 44 44 K -> R (in Ref. 4; BAB14994).
{ECO:0000305}.
CONFLICT 165 165 E -> K (in Ref. 4; BAB71568).
{ECO:0000305}.
STRAND 57 59 {ECO:0000244|PDB:1XB0}.
HELIX 71 120 {ECO:0000244|PDB:4TX5}.
STRAND 123 125 {ECO:0000244|PDB:1FEW}.
HELIX 126 173 {ECO:0000244|PDB:4TX5}.
HELIX 177 239 {ECO:0000244|PDB:4TX5}.
SEQUENCE 239 AA; 27131 MW; 70C2AE0DC654D031 CRC64;
MAALKSWLSR SVTSFFRYRQ CLCVPVVANF KKRCFSELIR PWHKTVTIGF GVTLCAVPIA
QKSEPHSLSS EALMRRAVSL VTDSTSTFLS QTTYALIEAI TEYTKAVYTL TSLYRQYTSL
LGKMNSEEED EVWQVIIGAR AEMTSKHQEY LKLETTWMTA VGLSEMAAEA AYQTGADQAS
ITARNHIQLV KLQVEEVHQL SRKAETKLAE AQIEELRQKT QEEGEERAES EQEAYLRED


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