BIRC7_MOUSE
ID BIRC7_MOUSE Reviewed; 285 AA.
AC A2AWP0; A0AUK9;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Baculoviral IAP repeat-containing protein 7;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q96CA5};
DE AltName: Full=Livin;
DE AltName: Full=RING-type E3 ubiquitin transferase BIRC7 {ECO:0000305};
DE Contains:
DE RecName: Full=Baculoviral IAP repeat-containing protein 7 30 kDa subunit;
DE Short=Truncated livin;
DE Short=p30-Livin;
DE Short=tLivin;
GN Name=Birc7; Synonyms=Livin;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-266.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Apoptotic regulator capable of exerting proapoptotic and
CC anti-apoptotic activities and plays crucial roles in apoptosis, cell
CC proliferation, and cell cycle control. Its anti-apoptotic activity is
CC mediated through the inhibition of CASP3, CASP7 and CASP9, as well as
CC by its E3 ubiquitin-protein ligase activity. As it is a weak caspase
CC inhibitor, its anti-apoptotic activity is thought to be due to its
CC ability to ubiquitinate DIABLO/SMAC targeting it for degradation
CC thereby promoting cell survival. May contribute to caspase inhibition,
CC by blocking the ability of DIABLO/SMAC to disrupt XIAP/BIRC4-caspase
CC interactions. Protects against apoptosis induced by TNF or by chemical
CC agents such as adriamycin, etoposide or staurosporine. Suppression of
CC apoptosis is mediated by activation of MAPK8/JNK1, and possibly also of
CC MAPK9/JNK2. This activation depends on TAB1 and MAP3K7/TAK1. In vitro,
CC inhibits CASP3 and proteolytic activation of pro-CASP9.
CC {ECO:0000250|UniProtKB:Q96CA5}.
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:0000250|UniProtKB:Q96CA5};
CC -!- SUBUNIT: Binds to caspase-9. Interaction with DIABLO/SMAC via the BIR
CC domain disrupts binding to caspase-9 and apoptotic suppressor activity.
CC Interacts with TAB1. In vitro, interacts with caspase-3 and caspase-7
CC via its BIR domain. {ECO:0000250|UniProtKB:Q96CA5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96CA5}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96CA5}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q96CA5}. Note=Nuclear, and in a filamentous
CC pattern throughout the cytoplasm. Full-length livin is detected
CC exclusively cytoplasm, whereas the truncated form (tLivin) is found in
CC the peri-nuclear region with marked localization to the Golgi
CC apparatus; the accumulation of tLivin in the nucleus shows positive
CC correlation with the increase in apoptosis.
CC {ECO:0000250|UniProtKB:Q96CA5}.
CC -!- DOMAIN: The RING domain is essential for autoubiquitination.
CC {ECO:0000250|UniProtKB:Q96CA5}.
CC -!- PTM: Autoubiquitinated and undergoes proteasome-mediated degradation.
CC {ECO:0000250|UniProtKB:Q96CA5}.
CC -!- PTM: The truncated protein (tLivin) not only loses its anti-apoptotic
CC effect but also acquires a pro-apoptotic effect.
CC {ECO:0000250|UniProtKB:Q96CA5}.
CC -!- SIMILARITY: Belongs to the IAP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI07261.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI25014.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; AL954707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC107260; AAI07261.1; ALT_INIT; mRNA.
DR EMBL; BC125013; AAI25014.1; ALT_INIT; mRNA.
DR CCDS; CCDS50840.1; -.
DR RefSeq; NP_001156719.1; NM_001163247.1.
DR AlphaFoldDB; A2AWP0; -.
DR SMR; A2AWP0; -.
DR BioGRID; 236795; 1.
DR STRING; 10090.ENSMUSP00000104503; -.
DR PhosphoSitePlus; A2AWP0; -.
DR PaxDb; A2AWP0; -.
DR PRIDE; A2AWP0; -.
DR ProteomicsDB; 273785; -.
DR Antibodypedia; 15058; 661 antibodies from 44 providers.
DR Ensembl; ENSMUST00000108875; ENSMUSP00000104503; ENSMUSG00000038840.
DR GeneID; 329581; -.
DR KEGG; mmu:329581; -.
DR UCSC; uc008oke.2; mouse.
DR CTD; 79444; -.
DR MGI; MGI:2676458; Birc7.
DR VEuPathDB; HostDB:ENSMUSG00000038840; -.
DR eggNOG; KOG1101; Eukaryota.
DR GeneTree; ENSGT00940000160406; -.
DR HOGENOM; CLU_016347_2_1_1; -.
DR InParanoid; A2AWP0; -.
DR OMA; WWVLEPP; -.
DR OrthoDB; 1340284at2759; -.
DR PhylomeDB; A2AWP0; -.
DR TreeFam; TF105356; -.
DR BioGRID-ORCS; 329581; 0 hits in 75 CRISPR screens.
DR PRO; PR:A2AWP0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AWP0; protein.
DR Bgee; ENSMUSG00000038840; Expressed in lens of camera-type eye and 12 other tissues.
DR Genevisible; A2AWP0; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; ISO:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0070247; P:regulation of natural killer cell apoptotic process; ISS:UniProtKB.
DR CDD; cd00022; BIR; 1.
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 InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00653; BIR; 1.
DR SMART; SM00238; BIR; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS01282; BIR_REPEAT_1; 1.
DR PROSITE; PS50143; BIR_REPEAT_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Cytoplasm; Golgi apparatus; Metal-binding; Nucleus;
KW Protease inhibitor; Reference proteome; Thiol protease inhibitor;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..285
FT /note="Baculoviral IAP repeat-containing protein 7"
FT /id="PRO_0000416248"
FT CHAIN 53..285
FT /note="Baculoviral IAP repeat-containing protein 7 30 kDa
FT subunit"
FT /id="PRO_0000416249"
FT REPEAT 96..161
FT /note="BIR"
FT ZN_FING 239..273
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 18..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT SITE 52..53
FT /note="Cleavage; by CASP3 and CASP7"
FT /evidence="ECO:0000250"
SQ SEQUENCE 285 AA; 31992 MW; 34F08B4F5C660B80 CRC64;
MFSPADLFRA AVFSMGPESR ARDSVRGPEL SHREDGSGRT QEQDKPHCPC NHVLGQDCLD
GQILGQLRPL SEEEESSGAA FLGEPAFPEM DSEDLRLASF YDWPSTAGIQ PEPLAAAGFF
HTGQQDKVRC FFCYGGLQSW ERGDDPWTEH ARWFPRCQFL LRSKGRDFVE RIQTYTPLLG
SWDQREEPED AVSATPSAPA HGSPELLRSR RETQPEDVSE PGAKDVQEQL RQLQEERRCK
VCLDRAVSIV FVPCGHFVCT ECAPNLQLCP ICRVPICSCV RTFLS
