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Baculoviral IAP repeat-containing protein 3 (EC 2.3.2.27) (Cellular inhibitor of apoptosis 2) (C-IAP2) (Inhibitor of apoptosis protein 1) (mIAP1) (RING-type E3 ubiquitin transferase BIRC3)

 BIRC3_MOUSE             Reviewed;         600 AA.
O08863; E9QLX3;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
20-JUN-2018, entry version 156.
RecName: Full=Baculoviral IAP repeat-containing protein 3;
EC=2.3.2.27 {ECO:0000269|PubMed:18621737};
AltName: Full=Cellular inhibitor of apoptosis 2;
Short=C-IAP2 {ECO:0000303|PubMed:18621737};
AltName: Full=Inhibitor of apoptosis protein 1 {ECO:0000303|PubMed:9441758};
Short=mIAP1 {ECO:0000303|PubMed:9441758};
AltName: Full=RING-type E3 ubiquitin transferase BIRC3 {ECO:0000305};
Name=Birc3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skeletal muscle;
PubMed=9441758; DOI=10.1006/geno.1997.5059;
Liston P., Lefebvre C., Fong W.G., Xuan J.Y., Korneluk R.G.;
"Genomic characterization of the mouse inhibitor of apoptosis protein
1 and 2 genes.";
Genomics 46:495-503(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, AND CATALYTIC ACTIVITY.
PubMed=18621737; DOI=10.1074/jbc.C800128200;
Varfolomeev E., Goncharov T., Fedorova A.V., Dynek J.N., Zobel K.,
Deshayes K., Fairbrother W.J., Vucic D.;
"c-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor
alpha (TNFalpha)-induced NF-kappaB activation.";
J. Biol. Chem. 283:24295-24299(2008).
-!- FUNCTION: Multi-functional protein which regulates not only
caspases and apoptosis, but also modulates inflammatory signaling
and immunity, mitogenic kinase signaling and cell proliferation,
as well as cell invasion and metastasis. Acts as an E3 ubiquitin-
protein ligase regulating NF-kappa-B signaling and regulates both
canonical and non-canonical NF-kappa-B signaling by acting in
opposite directions: acts as a positive regulator of the canonical
pathway and suppresses constitutive activation of non-canonical
NF-kappa-B signaling. The target proteins for its E3 ubiquitin-
protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4,
CASP3, CASP7, CASP8, IKBKE, TRAF1, and BCL10. Acts as an important
regulator of innate immune signaling via regulation of Toll-like
receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like
receptors (RLRs), collectively referred to as pattern recognition
receptors (PRRs). Protects cells from spontaneous formation of the
ripoptosome, a large multi-protein complex that has the capability
to kill cancer cells in a caspase-dependent and caspase-
independent manner. Suppresses ripoptosome formation by
ubiquitinating RIPK1 and CASP8. {ECO:0000269|PubMed:18621737}.
-!- 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:18621737}.
-!- ENZYME REGULATION: USP19 regulates the stability of BIRC3/c-IAP2
by preventing its ubiquitination. {ECO:0000250}.
-!- SUBUNIT: Interacts with DIABLO/SMAC and with PRSS25; these
interactions inhibit apoptotic suppressor activity. The BIR motifs
region interacts with TNF receptor associated factors 1 and 2
(TRAF1 and TRAF2) to form a heteromeric complex, which is then
recruited to the tumor necrosis factor receptor 2 (TNFR2).
Interaction with TRAF2 is required for ubiquitination of IKBKE,
degradation of NFKBIA and activation of NF-kappa-B. Interacts with
RIP1, RIP2, RIP3, RIP4 and USP19 (By similarity). {ECO:0000250}.
-!- INTERACTION:
P39429:Traf2; NbExp=7; IntAct=EBI-642236, EBI-520016;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- PTM: Auto-ubiquitinated and degraded by the proteasome in
apoptotic cells. {ECO:0000250}.
-!- SIMILARITY: Belongs to the IAP family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U88908; AAC53531.1; -; mRNA.
EMBL; CT030639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_031490.2; NM_007464.3.
UniGene; Mm.2026; -.
ProteinModelPortal; O08863; -.
SMR; O08863; -.
BioGrid; 198147; 15.
CORUM; O08863; -.
DIP; DIP-43742N; -.
IntAct; O08863; 6.
MINT; O08863; -.
STRING; 10090.ENSMUSP00000013949; -.
MEROPS; I32.003; -.
iPTMnet; O08863; -.
PhosphoSitePlus; O08863; -.
EPD; O08863; -.
MaxQB; O08863; -.
PaxDb; O08863; -.
PRIDE; O08863; -.
GeneID; 11796; -.
KEGG; mmu:11796; -.
CTD; 330; -.
MGI; MGI:1197007; Birc3.
eggNOG; KOG1101; Eukaryota.
eggNOG; ENOG410YPNM; LUCA.
HOGENOM; HOG000232059; -.
HOVERGEN; HBG004848; -.
InParanoid; O08863; -.
KO; K16060; -.
PRO; PR:O08863; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_BIRC2; -.
CleanEx; MM_BIRC3; -.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0045121; C:membrane raft; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016740; F:transferase activity; ISO:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IGI:MGI.
GO; GO:1990001; P:inhibition of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0070266; P:necroptotic process; IDA:UniProtKB.
GO; GO:0060546; P:negative regulation of necroptotic process; IMP:UniProtKB.
GO; GO:0042326; P:negative regulation of phosphorylation; IMP:UniProtKB.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:UniProtKB.
GO; GO:1902916; P:positive regulation of protein polyubiquitination; IGI:MGI.
GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:MGI.
GO; GO:0051291; P:protein heterooligomerization; ISO:MGI.
GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
GO; GO:0060544; P:regulation of necroptotic process; ISO:MGI.
GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; IGI:MGI.
GO; GO:0034121; P:regulation of toll-like receptor signaling pathway; IBA:GO_Central.
CDD; cd00022; BIR; 3.
InterPro; IPR001370; BIR_rpt.
InterPro; IPR001315; CARD.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR001841; Znf_RING.
Pfam; PF00653; BIR; 3.
Pfam; PF00619; CARD; 1.
SMART; SM00238; BIR; 3.
SMART; SM00114; CARD; 1.
SMART; SM00184; RING; 1.
SUPFAM; SSF47986; SSF47986; 1.
PROSITE; PS01282; BIR_REPEAT_1; 3.
PROSITE; PS50143; BIR_REPEAT_2; 3.
PROSITE; PS50209; CARD; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Apoptosis; Complete proteome; Cytoplasm; Metal-binding; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Transferase;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 600 Baculoviral IAP repeat-containing protein
3.
/FTId=PRO_0000122350.
REPEAT 27 94 BIR 1.
REPEAT 167 233 BIR 2.
REPEAT 253 320 BIR 3.
DOMAIN 436 525 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
ZN_FING 553 588 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
METAL 290 290 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
METAL 293 293 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
METAL 310 310 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
METAL 317 317 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
MOD_RES 138 138 Phosphoserine.
{ECO:0000250|UniProtKB:Q62210}.
CONFLICT 398 398 W -> R (in Ref. 1; AAC53531).
{ECO:0000305}.
SEQUENCE 600 AA; 67228 MW; 2EC9C7B567721382 CRC64;
MVQDSAFLAK LMKSADTFEL KYDFSCELYR LSTYSAFPRG VPVSERSLAR AGFYYTGAND
KVKCFCCGLM LDNWKQGDSP MEKHRKLYPS CNFVQTLNPA NSLEASPRPS LPSTAMSTMP
LSFASSENTG YFSGSYSSFP SDPVNFRANQ DCPALSTSPY HFAMNTEKAR LLTYETWPLS
FLSPAKLAKA GFYYIGPGDR VACFACDGKL SNWERKDDAM SEHQRHFPSC PFLKDLGQSA
SRYTVSNLSM QTHAARIRTF SNWPSSALVH SQELASAGFY YTGHSDDVKC FCCDGGLRCW
ESGDDPWVEH AKWFPRCEYL LRIKGQEFVS QVQAGYPHLL EQLLSTSDSP EDENADAAIV
HFGPGESSED VVMMSTPVVK AALEMGFSRS LVRQTVQWQI LATGENYRTV SDLVIGLLDA
EDEMREEQME QAAEEEESDD LALIRKNKMV LFQHLTCVTP MLYCLLSARA ITEQECNAVK
QKPHTLQAST LIDTVLAKGN TAATSFRNSL REIDPALYRD IFVQQDIRSL PTDDIAALPM
EEQLRKLQEE RMCKVCMDRE VSIVFIPCGH LVVCKDCAPS LRKCPICRGT IKGTVRTFLS


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