ID   DBLOH_PONAB             Reviewed;         239 AA.
AC   Q5RBH2;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Diablo IAP-binding mitochondrial protein {ECO:0000250|UniProtKB:Q9JIQ3};
DE   AltName: Full=Diablo homolog, mitochondrial {ECO:0000250|UniProtKB:Q9NR28};
DE   AltName: Full=Direct IAP-binding protein with low pI {ECO:0000250|UniProtKB:Q9NR28};
DE   AltName: Full=Second mitochondria-derived activator of caspase {ECO:0000250|UniProtKB:Q9NR28};
DE            Short=Smac {ECO:0000250|UniProtKB:Q9NR28};
DE   Flags: Precursor;
GN   Name=DIABLO {ECO:0000250|UniProtKB:Q9NR28};
GN   Synonyms=SMAC {ECO:0000250|UniProtKB:Q9NR28};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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) (By similarity). inhibitory
CC       activity of inhibitor of apoptosis proteins (IAP). Inhibits the
CC       activity of BIRC6/bruce by inhibiting its binding to caspases (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with BEX3 (By
CC       similarity). Interacts with BIRC2/c-IAP1 (via BIR3 domain) (By
CC       similarity). Interacts with BIRC6/bruce (By similarity). Interacts with
CC       BIRC7/livin (By similarity). Interacts with XIAP/BIRC4 (via BIR3
CC       domain) (By similarity). Interacts with the monomeric and dimeric form
CC       of BIRC5/survivin (By similarity). Interacts with AREL1 (via HECT
CC       domain); in the cytoplasm following induction of apoptosis (By
CC       similarity). {ECO:0000250|UniProtKB:Q9JIQ3,
CC       ECO:0000250|UniProtKB:Q9NR28}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9NR28}.
CC       Note=Released into the cytosol when cells undergo apoptosis.
CC       {ECO:0000250|UniProtKB:Q9NR28}.
CC   -!- DOMAIN: The mature N-terminus mediates interaction with XIAP/BIRC4.
CC       {ECO:0000250|UniProtKB:Q9NR28}.
CC   -!- PTM: Ubiquitinated by BIRC7/livin. {ECO:0000250|UniProtKB:Q9NR28}.
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DR   EMBL; CR858676; CAH90888.1; -; mRNA.
DR   RefSeq; NP_001125507.1; NM_001132035.2.
DR   AlphaFoldDB; Q5RBH2; -.
DR   SMR; Q5RBH2; -.
DR   STRING; 9601.ENSPPYP00000005770; -.
DR   GeneID; 100172416; -.
DR   KEGG; pon:100172416; -.
DR   CTD; 56616; -.
DR   eggNOG; ENOG502RA48; Eukaryota.
DR   InParanoid; Q5RBH2; -.
DR   OrthoDB; 1311341at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:InterPro.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Apoptosis; Mitochondrion; Reference proteome; Transit peptide;
KW   Ubl conjugation.
FT   TRANSIT         1..55
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           56..239
FT                   /note="Diablo IAP-binding mitochondrial protein"
FT                   /id="PRO_0000043071"
FT   REGION          217..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           56..60
FT                   /note="IAP-binding"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   239 AA;  27146 MW;  E1681A68B000D682 CRC64;
     MAVLKSWLSR SVTLLFRYRQ CLCVPVVANF KKRCFSELIR PWHKTVTVGF GVTLCAVPIA
     QKSEPHSLSS EALMRRAVSL VTDSTSTFLS QTTYALIEAI TEYTKAVYTL TSLYRQYTSL
     LGKMNSQEED EVWQVIIGAR AEMTSKHQEY LKLETTWMTA VGLSEMAAEA AYQTGADQAP
     ITARNHIQLV KLQVEEVHQL SRKAETKLAE AQIEELRQKT QEEGEERAES EQEAYLRED