BIRC3_CANLF
ID BIRC3_CANLF Reviewed; 604 AA.
AC A1E2V0;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Baculoviral IAP repeat-containing protein 3;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q13489};
DE AltName: Full=RING-type E3 ubiquitin transferase BIRC3 {ECO:0000305};
GN Name=BIRC3;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wimmershoff J., Schade B., Rickenbacher A.B., Keller S.M., Guscetti F.;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Multi-functional protein which regulates not only caspases
CC and apoptosis, but also modulates inflammatory signaling and immunity,
CC mitogenic kinase signaling and cell proliferation, as well as cell
CC invasion and metastasis. Acts as an E3 ubiquitin-protein ligase
CC regulating NF-kappa-B signaling and regulates both canonical and non-
CC canonical NF-kappa-B signaling by acting in opposite directions: acts
CC as a positive regulator of the canonical pathway and suppresses
CC constitutive activation of non-canonical NF-kappa-B signaling. The
CC target proteins for its E3 ubiquitin-protein ligase activity include:
CC RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, IKBKE, TRAF1, and
CC BCL10. Acts as an important regulator of innate immune signaling via
CC regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and
CC RIG-I like receptors (RLRs), collectively referred to as pattern
CC recognition receptors (PRRs). Protects cells from spontaneous formation
CC of the ripoptosome, a large multi-protein complex that has the
CC capability to kill cancer cells in a caspase-dependent and caspase-
CC independent manner. Suppresses ripoptosome formation by ubiquitinating
CC RIPK1 and CASP8. {ECO:0000250|UniProtKB:Q13489}.
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:Q13489};
CC -!- ACTIVITY REGULATION: USP19 regulates the stability of BIRC3/c-IAP2 by
CC preventing its ubiquitination. {ECO:0000250|UniProtKB:Q13489}.
CC -!- SUBUNIT: Interacts with PRSS25; the interaction inhibits apoptotic
CC suppressor activity. The BIR motifs region interacts with TNF receptor
CC associated factors 1 and 2 (TRAF1 and TRAF2) to form a heteromeric
CC complex, which is then recruited to the tumor necrosis factor receptor
CC 2 (TNFR2). Interaction with TRAF2 is required for ubiquitination of
CC IKBKE, degradation of NFKBIA and activation of NF-kappa-B. Interacts
CC with RIP1, RIP2, RIP3, RIP4 and USP19. {ECO:0000250|UniProtKB:Q13489}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13489}. Nucleus
CC {ECO:0000250|UniProtKB:Q13489}.
CC -!- PTM: Auto-ubiquitinated and degraded by the proteasome in apoptotic
CC cells. {ECO:0000250|UniProtKB:Q13489}.
CC -!- SIMILARITY: Belongs to the IAP family. {ECO:0000305}.
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DR EMBL; EF102104; ABL09004.1; -; mRNA.
DR RefSeq; NP_001074194.1; NM_001080725.1.
DR RefSeq; XP_005619570.1; XM_005619513.2.
DR RefSeq; XP_005619571.1; XM_005619514.2.
DR RefSeq; XP_005619572.1; XM_005619515.2.
DR AlphaFoldDB; A1E2V0; -.
DR SMR; A1E2V0; -.
DR STRING; 9615.ENSCAFP00000050122; -.
DR PaxDb; A1E2V0; -.
DR Ensembl; ENSCAFT00040039339; ENSCAFP00040034318; ENSCAFG00040021208.
DR Ensembl; ENSCAFT00040039358; ENSCAFP00040034338; ENSCAFG00040021208.
DR Ensembl; ENSCAFT00040039395; ENSCAFP00040034373; ENSCAFG00040021208.
DR Ensembl; ENSCAFT00040039446; ENSCAFP00040034420; ENSCAFG00040021208.
DR Ensembl; ENSCAFT00040039491; ENSCAFP00040034458; ENSCAFG00040021208.
DR Ensembl; ENSCAFT00040039598; ENSCAFP00040034552; ENSCAFG00040021208.
DR Ensembl; ENSCAFT00845001898; ENSCAFP00845001493; ENSCAFG00845001106.
DR GeneID; 489433; -.
DR KEGG; cfa:489433; -.
DR CTD; 330; -.
DR VEuPathDB; HostDB:ENSCAFG00845001106; -.
DR eggNOG; KOG1101; Eukaryota.
DR GeneTree; ENSGT00940000154175; -.
DR HOGENOM; CLU_016347_1_1_1; -.
DR InParanoid; A1E2V0; -.
DR OMA; VQANYPH; -.
DR OrthoDB; 1340284at2759; -.
DR TreeFam; TF105356; -.
DR Reactome; R-CFA-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-CFA-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-CFA-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-CFA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-CFA-5675482; Regulation of necroptotic cell death.
DR Reactome; R-CFA-5676594; TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
DR Reactome; R-CFA-5689880; Ub-specific processing proteases.
DR Proteomes; UP000002254; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0060546; P:negative regulation of necroptotic process; IBA:GO_Central.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR CDD; cd00022; BIR; 3.
DR CDD; cd14394; UBA_BIRC2_3; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR001370; BIR_rpt.
DR InterPro; IPR041933; BIRC2/BIRC3_UBA.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR Pfam; PF00653; BIR; 3.
DR Pfam; PF00619; CARD; 1.
DR SMART; SM00238; BIR; 3.
DR SMART; SM00114; CARD; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS01282; BIR_REPEAT_1; 3.
DR PROSITE; PS50143; BIR_REPEAT_2; 3.
DR PROSITE; PS50209; CARD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Cytoplasm; Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..604
FT /note="Baculoviral IAP repeat-containing protein 3"
FT /id="PRO_0000289583"
FT REPEAT 29..96
FT /note="BIR 1"
FT REPEAT 169..235
FT /note="BIR 2"
FT REPEAT 255..322
FT /note="BIR 3"
FT DOMAIN 439..529
FT /note="CARD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT ZN_FING 557..592
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT MOD_RES 130
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q62210"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62210"
SQ SEQUENCE 604 AA; 67940 MW; 2992B20B00ED6E07 CRC64;
MNIVQNSIFL SNLLRSSPVF ELKYDHSCEL YRMSTYSTFP AGVPVSERSL ARAGFYYTGA
KDRVRCFCCG LMLDNWKAGD SPTGKHRNLY PSCSFIQNLS AVSTVGAASQ PPAPLSEARS
THAQSPGLER SSYFSASYSS FPVDPVDFRP SPAMSPWRAG PSCVTMKSEE DRLCTFQGWP
LAFPLPSALA RAGFYYVGPG DRVACFACGG KLSNWEPDDD ALSEHLRHFP DCPFVEGQLQ
ATVRYTASNL SMQTLAARSR TFCNWPPRAP VHPEQLASAG FYYMGHSDDV KCFCCDGGLR
CWESGDDPWV EHAKWFPRCE YLIRIKGQEF ISQIQASYPH LLEQLLSTSD NTEDENTESP
IVHFGPGEYH SEDAVMMNTP VVMAALEMGF SRSLVRQTVQ SKILSTGENY RTVNEIVSDL
LHVEDEIREE EKERAAENRE SDDVSLIRKN KMVLFQHLTY VLPILDSLLM AGVLNEQEHS
SIKQKARTSL QARELIDTVL VKGSSAVTIF KNSLQEIDPM LYKRFFVQQD RKYIPTEDIS
DLPVEEQLRR LQEERTCKVC MDKEVSIVFI PCGHLVVCRD CAPSLRKCPI CRGTVRGTVR
TFLS
