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Baculoviral IAP repeat-containing protein 7 (EC 2.3.2.27) (Kidney inhibitor of apoptosis protein) (KIAP) (Livin) (Melanoma inhibitor of apoptosis protein) (ML-IAP) (RING finger protein 50) (RING-type E3 ubiquitin transferase BIRC7) [Cleaved into: Baculoviral IAP repeat-containing protein 7 30kDa subunit (Truncated livin) (p30-Livin) (tLivin)]

 BIRC7_HUMAN             Reviewed;         298 AA.
Q96CA5; Q9BQV0; Q9H2A8; Q9HAP7;
11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
11-JUL-2002, sequence version 2.
27-SEP-2017, entry version 167.
RecName: Full=Baculoviral IAP repeat-containing protein 7;
EC=2.3.2.27 {ECO:0000269|PubMed:16729033};
AltName: Full=Kidney inhibitor of apoptosis protein;
Short=KIAP;
AltName: Full=Livin;
AltName: Full=Melanoma inhibitor of apoptosis protein;
Short=ML-IAP;
AltName: Full=RING finger protein 50;
AltName: Full=RING-type E3 ubiquitin transferase BIRC7 {ECO:0000305};
Contains:
RecName: Full=Baculoviral IAP repeat-containing protein 7 30kDa subunit;
Short=Truncated livin;
Short=p30-Livin;
Short=tLivin;
Name=BIRC7; Synonyms=KIAP, LIVIN, MLIAP, RNF50;
ORFNames=UNQ5800/PRO19607/PRO21344;
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 2).
TISSUE=Fetal kidney;
PubMed=11162435; DOI=10.1006/bbrc.2000.4027;
Lin J.-H., Deng G., Huang Q., Morser J.;
"KIAP, a novel member of the inhibitor of apoptosis protein family.";
Biochem. Biophys. Res. Commun. 279:820-831(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1
AND 2), AND TISSUE SPECIFICITY (ISOFORMS 1 AND 2).
TISSUE=Melanoma;
PubMed=11322947; DOI=10.1016/S0014-5793(01)02366-3;
Ashhab Y., Alian A., Polliack A., Panet A., Yehuda D.B.;
"Two splicing variants of a new inhibitor of apoptosis gene with
different biological properties and tissue distribution pattern.";
FEBS Lett. 495:56-60(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=11024045; DOI=10.1074/jbc.M003670200;
Kasof G.M., Gomes B.C.;
"Livin, a novel inhibitor of apoptosis protein family member.";
J. Biol. Chem. 276:3238-3246(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
GLN-223.
TISSUE=Skin;
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 MUTAGENESIS OF 87-GLU--GLU-88; ASP-120; CYS-124 AND
ASP-138.
PubMed=11084335; DOI=10.1016/S0960-9822(00)00781-8;
Vucic D., Stennicke H.R., Pisabarro M.T., Salvesen G.S., Dixit V.M.;
"ML-IAP, a novel inhibitor of apoptosis that is preferentially
expressed in human melanomas.";
Curr. Biol. 10:1359-1366(2000).
[8]
INTERACTION WITH SMAC.
PubMed=11801603; DOI=10.1074/jbc.M112045200;
Vucic D., Deshayes K., Ackerly H., Pisabarro M.T., Kadkhodayan S.,
Fairbrother W.J., Dixit V.M.;
"SMAC negatively regulates the anti-apoptotic activity of melanoma
inhibitor of apoptosis (ML-IAP).";
J. Biol. Chem. 277:12275-12279(2002).
[9]
ACTIVATION OF MAP KINASES.
PubMed=11865055; DOI=10.1128/MCB.22.6.1754-1766.2002;
Sanna M.G., da Silva Correia J., Ducrey O., Lee J., Nomoto K.,
Schrantz N., Deveraux Q.L., Ulevitch R.J.;
"IAP suppression of apoptosis involves distinct mechanisms: the
TAK1/JNK1 signaling cascade and caspase inhibition.";
Mol. Cell. Biol. 22:1754-1766(2002).
[10]
FUNCTION IN THE UBIQUITINATION OF DIABLO/SMAC, CATALYTIC ACTIVITY, AND
INTERACTION WITH DIABLO/SMAC.
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).
[11]
FUNCTION, PROTEOLYTIC CLEAVAGE, AND SUBCELLULAR LOCATION.
PubMed=17294084; DOI=10.1007/s10495-006-0049-1;
Nachmias B., Lazar I., Elmalech M., Abed-El-Rahaman I., Asshab Y.,
Mandelboim O., Perlman R., Ben-Yehuda D.;
"Subcellular localization determines the delicate balance between the
anti- and pro-apoptotic activity of Livin.";
Apoptosis 12:1129-1142(2007).
[12]
FUNCTION, AND PROTEOLYTIC CLEAVAGE.
PubMed=18034418; DOI=10.1002/eji.200636600;
Nachmias B., Mizrahi S., Elmalech M., Lazar I., Ashhab Y., Gazit R.,
Markel G., Ben-Yehuda D., Mandelboim O.;
"Manipulation of NK cytotoxicity by the IAP family member Livin.";
Eur. J. Immunol. 37:3467-3476(2007).
[13]
REVIEW ON FUNCTION.
PubMed=19074843; DOI=10.1158/1535-7163.MCT-08-0480;
Wang L., Zhang Q., Liu B., Han M., Shan B.;
"Challenge and promise: roles for Livin in progression and therapy of
cancer.";
Mol. Cancer Ther. 7:3661-3669(2008).
[14]
REVIEW ON FUNCTION.
PubMed=21617971; DOI=10.1007/s11010-011-0873-7;
Yan B.;
"Research progress on Livin protein: an inhibitor of apoptosis.";
Mol. Cell. Biochem. 357:39-45(2011).
[15]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 63-179 IN COMPLEX WITH
PHAGE-AND SMAC-DERIVED PEPTIDES, AND ZINC-BINDING SITES.
PubMed=12846571; DOI=10.1021/bi034227t;
Franklin M.C., Kadkhodayan S., Ackerly H., Alexandru D.,
Distefano M.D., Elliott L.O., Flygare J.A., Mausisa G., Okawa D.C.,
Ong D., Vucic D., Deshayes K., Fairbrother W.J.;
"Structure and function analysis of peptide antagonists of melanoma
inhibitor of apoptosis (ML-IAP).";
Biochemistry 42:8223-8231(2003).
[16]
X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 63-159, AND ZINC-BINDING
SITES.
PubMed=15485396; DOI=10.1042/BJ20041108;
Vucic D., Franklin M.C., Wallweber H.J., Das K., Eckelman B.P.,
Shin H., Elliott L.O., Kadkhodayan S., Deshayes K., Salvesen G.S.,
Fairbrother W.J.;
"Engineering ML-IAP to produce an extraordinarily potent caspase 9
inhibitor: implications for Smac-dependent anti-apoptotic activity of
ML-IAP.";
Biochem. J. 385:11-20(2005).
-!- FUNCTION: Apoptotic regulator capable of exerting proapoptotic and
anti-apoptotic activities and plays crucial roles in apoptosis,
cell proliferation, and cell cycle control. Its anti-apoptotic
activity is mediated through the inhibition of CASP3, CASP7 and
CASP9, as well as by its E3 ubiquitin-protein ligase activity. As
it is a weak caspase inhibitor, its anti-apoptotic activity is
thought to be due to its ability to ubiquitinate DIABLO/SMAC
targeting it for degradation thereby promoting cell survival. May
contribute to caspase inhibition, by blocking the ability of
DIABLO/SMAC to disrupt XIAP/BIRC4-caspase interactions. Protects
against apoptosis induced by TNF or by chemical agents such as
adriamycin, etoposide or staurosporine. Suppression of apoptosis
is mediated by activation of MAPK8/JNK1, and possibly also of
MAPK9/JNK2. This activation depends on TAB1 and NR2C2/TAK1. In
vitro, inhibits CASP3 and proteolytic activation of pro-CASP9.
Isoform 1 blocks staurosporine-induced apoptosis. Isoform 2 blocks
etoposide-induced apoptosis. Isoform 2 protects against natural
killer (NK) cell killing whereas isoform 1 augments killing.
{ECO:0000269|PubMed:11084335, ECO:0000269|PubMed:16729033,
ECO:0000269|PubMed:17294084, ECO:0000269|PubMed:18034418}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:16729033}.
-!- SUBUNIT: Binds to CASP9. Interaction with DIABLO/SMAC via the BIR
domain disrupts binding to CASP9 and apoptotic suppressor
activity. Interacts with TAB1. In vitro, interacts with CASP3 and
CASP7 via its BIR domain. {ECO:0000269|PubMed:11801603,
ECO:0000269|PubMed:12846571, ECO:0000269|PubMed:16729033}.
-!- INTERACTION:
Q08117:AES; NbExp=3; IntAct=EBI-517623, EBI-717810;
Q13490:BIRC2; NbExp=3; IntAct=EBI-517623, EBI-514538;
P55211:CASP9; NbExp=12; IntAct=EBI-517623, EBI-516799;
P26196:DDX6; NbExp=5; IntAct=EBI-517623, EBI-351257;
Q9NR28:DIABLO; NbExp=6; IntAct=EBI-517623, EBI-517508;
Q9H5Z6:FAM124B; NbExp=3; IntAct=EBI-517623, EBI-741626;
O43464:HTRA2; NbExp=2; IntAct=EBI-517623, EBI-517086;
O43189:PHF1; NbExp=3; IntAct=EBI-517623, EBI-530034;
O15160:POLR1C; NbExp=5; IntAct=EBI-517623, EBI-1055079;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17294084}.
Cytoplasm {ECO:0000269|PubMed:17294084}. Golgi apparatus
{ECO:0000269|PubMed:17294084}. Note=Nuclear, and in a filamentous
pattern throughout the cytoplasm. Full-length livin is detected
exclusively in the cytoplasm, whereas the truncated form (tLivin)
is found in the peri-nuclear region with marked localization to
the Golgi apparatus; the accumulation of tLivin in the nucleus
shows positive correlation with the increase in apoptosis.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=2; Synonyms=Livin alpha;
IsoId=Q96CA5-1; Sequence=Displayed;
Name=1; Synonyms=Livin beta;
IsoId=Q96CA5-2; Sequence=VSP_002459;
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed at very
low levels or not detectable in most adult tissues. Detected in
adult heart, placenta, lung, lymph node, spleen and ovary, and in
several carcinoma cell lines. Isoform 2 is detected in fetal
kidney, heart and spleen, and at lower levels in adult brain,
skeletal muscle and peripheral blood leukocytes.
-!- DOMAIN: The RING domain is essential for autoubiquitination.
-!- PTM: Autoubiquitinated and undergoes proteasome-mediated
degradation.
-!- PTM: The truncated protein (tLivin) not only loses its anti-
apoptotic effect but also acquires a pro-apoptotic effect.
-!- SIMILARITY: Belongs to the IAP family. {ECO:0000305}.
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EMBL; AF301009; AAG37878.1; -; mRNA.
EMBL; AJ309298; CAC37337.1; -; Genomic_DNA.
EMBL; AJ309298; CAC37338.1; -; Genomic_DNA.
EMBL; AF311388; AAG33622.1; -; mRNA.
EMBL; AY358835; AAQ89194.1; -; mRNA.
EMBL; AY358836; AAQ89195.1; -; mRNA.
EMBL; AL121827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC014475; AAH14475.1; -; mRNA.
CCDS; CCDS13512.1; -. [Q96CA5-2]
CCDS; CCDS13513.1; -. [Q96CA5-1]
PIR; JC7568; JC7568.
RefSeq; NP_071444.1; NM_022161.3. [Q96CA5-2]
RefSeq; NP_647478.1; NM_139317.2. [Q96CA5-1]
UniGene; Hs.256126; -.
PDB; 1OXN; X-ray; 2.20 A; A/B/C/D/E=63-179.
PDB; 1OXQ; X-ray; 2.30 A; A/B/C/D/E=63-179.
PDB; 1OY7; X-ray; 2.70 A; A/B/C/D/E=63-179.
PDB; 1TW6; X-ray; 1.71 A; A/B=63-172.
PDB; 2I3H; X-ray; 1.62 A; A/B=63-172.
PDB; 2I3I; X-ray; 2.30 A; A/B=63-172.
PDB; 3F7G; X-ray; 2.30 A; A/B/C/D/E=63-179.
PDB; 3F7H; X-ray; 1.80 A; A/B=63-172.
PDB; 3F7I; X-ray; 1.90 A; A/B=63-172.
PDB; 3GT9; X-ray; 1.70 A; A/B=63-172.
PDB; 3GTA; X-ray; 1.70 A; A/B=63-172.
PDB; 3UW5; X-ray; 1.71 A; A/B=63-159.
PDB; 4AUQ; X-ray; 2.18 A; B/E=239-298.
PDBsum; 1OXN; -.
PDBsum; 1OXQ; -.
PDBsum; 1OY7; -.
PDBsum; 1TW6; -.
PDBsum; 2I3H; -.
PDBsum; 2I3I; -.
PDBsum; 3F7G; -.
PDBsum; 3F7H; -.
PDBsum; 3F7I; -.
PDBsum; 3GT9; -.
PDBsum; 3GTA; -.
PDBsum; 3UW5; -.
PDBsum; 4AUQ; -.
ProteinModelPortal; Q96CA5; -.
SMR; Q96CA5; -.
BioGrid; 122670; 33.
DIP; DIP-33486N; -.
IntAct; Q96CA5; 33.
MINT; MINT-147031; -.
STRING; 9606.ENSP00000217169; -.
BindingDB; Q96CA5; -.
ChEMBL; CHEMBL1075127; -.
GuidetoPHARMACOLOGY; 2794; -.
MEROPS; I32.007; -.
iPTMnet; Q96CA5; -.
PhosphoSitePlus; Q96CA5; -.
BioMuta; BIRC7; -.
DMDM; 21759008; -.
MaxQB; Q96CA5; -.
PaxDb; Q96CA5; -.
PeptideAtlas; Q96CA5; -.
PRIDE; Q96CA5; -.
DNASU; 79444; -.
Ensembl; ENST00000217169; ENSP00000217169; ENSG00000101197. [Q96CA5-1]
Ensembl; ENST00000342412; ENSP00000345213; ENSG00000101197. [Q96CA5-2]
GeneID; 79444; -.
KEGG; hsa:79444; -.
UCSC; uc002yei.5; human. [Q96CA5-1]
CTD; 79444; -.
DisGeNET; 79444; -.
EuPathDB; HostDB:ENSG00000101197.12; -.
GeneCards; BIRC7; -.
HGNC; HGNC:13702; BIRC7.
HPA; HPA047850; -.
MIM; 605737; gene.
neXtProt; NX_Q96CA5; -.
OpenTargets; ENSG00000101197; -.
PharmGKB; PA25364; -.
eggNOG; KOG1101; Eukaryota.
eggNOG; ENOG410YPNM; LUCA.
GeneTree; ENSGT00500000044782; -.
HOGENOM; HOG000232059; -.
HOVERGEN; HBG099136; -.
InParanoid; Q96CA5; -.
KO; K16061; -.
OMA; RAPIRSC; -.
OrthoDB; EOG091G0CXH; -.
PhylomeDB; Q96CA5; -.
TreeFam; TF105356; -.
SignaLink; Q96CA5; -.
SIGNOR; Q96CA5; -.
EvolutionaryTrace; Q96CA5; -.
GeneWiki; BIRC7; -.
GenomeRNAi; 79444; -.
PMAP-CutDB; Q96CA5; -.
PRO; PR:Q96CA5; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101197; -.
CleanEx; HS_BIRC7; -.
ExpressionAtlas; Q96CA5; baseline and differential.
Genevisible; Q96CA5; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005815; C:microtubule organizing center; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; TAS:UniProtKB.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; NAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0007257; P:activation of JUN kinase activity; NAS:UniProtKB.
GO; GO:1990001; P:inhibition of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0070247; P:regulation of natural killer cell apoptotic process; IDA:UniProtKB.
GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
CDD; cd00022; BIR; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001370; BIR_rpt.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF00653; BIR; 1.
SMART; SM00238; BIR; 1.
SMART; SM00184; RING; 1.
PROSITE; PS01282; BIR_REPEAT_1; 1.
PROSITE; PS50143; BIR_REPEAT_2; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Complete proteome;
Cytoplasm; Golgi apparatus; Metal-binding; Nucleus; Polymorphism;
Protease inhibitor; Reference proteome; Thiol protease inhibitor;
Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc;
Zinc-finger.
CHAIN 1 298 Baculoviral IAP repeat-containing protein
7.
/FTId=PRO_0000122362.
CHAIN 53 298 Baculoviral IAP repeat-containing protein
7 30kDa subunit.
/FTId=PRO_0000416092.
REPEAT 90 155 BIR.
ZN_FING 252 286 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
COMPBIAS 64 69 Poly-Glu.
METAL 124 124 Zinc.
METAL 127 127 Zinc.
METAL 144 144 Zinc.
METAL 151 151 Zinc.
SITE 52 53 Cleavage; by CASP3 and CASP7.
VAR_SEQ 216 233 Missing (in isoform 1).
{ECO:0000303|PubMed:11024045,
ECO:0000303|PubMed:12975309}.
/FTId=VSP_002459.
VARIANT 223 223 E -> Q (in dbSNP:rs1077019).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_020253.
MUTAGEN 87 88 EE->AA: No change in SMAC interaction and
anti-apoptotic activity.
{ECO:0000269|PubMed:11084335}.
MUTAGEN 120 120 D->A: Abolishes inhibition of caspases,
SMAC binding and anti-apoptotic activity.
{ECO:0000269|PubMed:11084335}.
MUTAGEN 124 124 C->A: Abolishes inhibition of caspases
and anti-apoptotic activity.
{ECO:0000269|PubMed:11084335}.
MUTAGEN 138 138 D->A: Abolishes inhibition of caspases,
SMAC binding and anti-apoptotic activity.
{ECO:0000269|PubMed:11084335}.
HELIX 82 84 {ECO:0000244|PDB:2I3H}.
HELIX 87 92 {ECO:0000244|PDB:2I3H}.
TURN 93 96 {ECO:0000244|PDB:2I3H}.
TURN 100 102 {ECO:0000244|PDB:2I3H}.
HELIX 105 110 {ECO:0000244|PDB:2I3H}.
STRAND 113 115 {ECO:0000244|PDB:2I3H}.
STRAND 117 120 {ECO:0000244|PDB:3UW5}.
STRAND 122 124 {ECO:0000244|PDB:2I3H}.
TURN 125 127 {ECO:0000244|PDB:2I3H}.
STRAND 130 132 {ECO:0000244|PDB:2I3H}.
HELIX 140 147 {ECO:0000244|PDB:2I3H}.
HELIX 152 158 {ECO:0000244|PDB:2I3H}.
HELIX 160 166 {ECO:0000244|PDB:2I3H}.
HELIX 168 171 {ECO:0000244|PDB:2I3H}.
HELIX 243 249 {ECO:0000244|PDB:4AUQ}.
TURN 253 255 {ECO:0000244|PDB:4AUQ}.
STRAND 256 259 {ECO:0000244|PDB:4AUQ}.
STRAND 262 265 {ECO:0000244|PDB:4AUQ}.
TURN 273 275 {ECO:0000244|PDB:4AUQ}.
HELIX 276 278 {ECO:0000244|PDB:4AUQ}.
TURN 283 285 {ECO:0000244|PDB:4AUQ}.
STRAND 291 294 {ECO:0000244|PDB:4AUQ}.
SEQUENCE 298 AA; 32798 MW; B2EAAEE531BEC101 CRC64;
MGPKDSAKCL HRGPQPSHWA AGDGPTQERC GPRSLGSPVL GLDTCRAWDH VDGQILGQLR
PLTEEEEEEG AGATLSRGPA FPGMGSEELR LASFYDWPLT AEVPPELLAA AGFFHTGHQD
KVRCFFCYGG LQSWKRGDDP WTEHAKWFPS CQFLLRSKGR DFVHSVQETH SQLLGSWDPW
EEPEDAAPVA PSVPASGYPE LPTPRREVQS ESAQEPGGVS PAEAQRAWWV LEPPGARDVE
AQLRRLQEER TCKVCLDRAV SIVFVPCGHL VCAECAPGLQ LCPICRAPVR SRVRTFLS


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