Baculoviral IAP repeat-containing protein 3

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O08863 (BIRC3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 112. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Baculoviral IAP repeat-containing protein 3
EC=6.3.2.-

Alternative name(s):
Inhibitor of apoptosis protein 1
Short name=IAP-1
Short name=mIAP-1
Short name=mIAP1

Gene names

Name:	Birc3
Synonyms:	Birc2, Iap1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	600 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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, 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 By similarity. Ref.3
Enzyme regulation	USP19 regulates the stability of BIRC3/c-IAP2 by preventing its ubiquitination By similarity.
Subunit structure	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). Interacts with RIP1, RIP2, RIP3, RIP4 and USP19 By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Post-translational modification	Auto-ubiquitinated and degraded by the proteasome in apoptotic cells By similarity.
Sequence similarities	Belongs to the IAP family. Contains 3 BIR repeats. Contains 1 CARD domain. Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Apoptosis Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW necroptosis Inferred from direct assay PubMed 21052097. Source: UniProtKB negative regulation of necroptosis Inferred from mutant phenotype PubMed 21052097. Source: UniProtKB negative regulation of phosphorylation Inferred from mutant phenotype PubMed 21052097. Source: UniProtKB negative regulation of reactive oxygen species metabolic process Inferred from mutant phenotype PubMed 21052097. Source: UniProtKB protein ubiquitination Inferred from electronic annotation. Source: GOC regulation of apoptotic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ubiquitin-protein ligase activity Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Traf2	P39429	7	EBI-642236,EBI-520016

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 600

600

Baculoviral IAP repeat-containing protein 3

PRO_0000122350

Regions

Repeat

27 – 94

BIR 1

Repeat

167 – 233

BIR 2

Repeat

253 – 320

BIR 3

Domain

436 – 525

CARD

Zinc finger

553 – 588

RING-type

Sites

Metal binding

290

Zinc By similarity

Metal binding

293

Zinc By similarity

Metal binding

310

Zinc By similarity

Metal binding

317

Zinc By similarity

Experimental info

Sequence conflict

398

W → R in AAC53531. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O08863 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 2EC9C7B567721382
Show »

FASTA

600

67,228

        10         20         30         40         50         60 
MVQDSAFLAK LMKSADTFEL KYDFSCELYR LSTYSAFPRG VPVSERSLAR AGFYYTGAND 

        70         80         90        100        110        120 
KVKCFCCGLM LDNWKQGDSP MEKHRKLYPS CNFVQTLNPA NSLEASPRPS LPSTAMSTMP 

       130        140        150        160        170        180 
LSFASSENTG YFSGSYSSFP SDPVNFRANQ DCPALSTSPY HFAMNTEKAR LLTYETWPLS 

       190        200        210        220        230        240 
FLSPAKLAKA GFYYIGPGDR VACFACDGKL SNWERKDDAM SEHQRHFPSC PFLKDLGQSA 

       250        260        270        280        290        300 
SRYTVSNLSM QTHAARIRTF SNWPSSALVH SQELASAGFY YTGHSDDVKC FCCDGGLRCW 

       310        320        330        340        350        360 
ESGDDPWVEH AKWFPRCEYL LRIKGQEFVS QVQAGYPHLL EQLLSTSDSP EDENADAAIV 

       370        380        390        400        410        420 
HFGPGESSED VVMMSTPVVK AALEMGFSRS LVRQTVQWQI LATGENYRTV SDLVIGLLDA 

       430        440        450        460        470        480 
EDEMREEQME QAAEEEESDD LALIRKNKMV LFQHLTCVTP MLYCLLSARA ITEQECNAVK 

       490        500        510        520        530        540 
QKPHTLQAST LIDTVLAKGN TAATSFRNSL REIDPALYRD IFVQQDIRSL PTDDIAALPM 

       550        560        570        580        590        600 
EEQLRKLQEE RMCKVCMDRE VSIVFIPCGH LVVCKDCAPS LRKCPICRGT IKGTVRTFLS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic characterization of the mouse inhibitor of apoptosis protein 1 and 2 genes." Liston P., Lefebvre C., Fong W.G., Xuan J.Y., Korneluk R.G. Genomics 46:495-503(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Skeletal muscle.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." 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. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"c-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor alpha (TNFalpha)-induced NF-kappaB activation." Varfolomeev E., Goncharov T., Fedorova A.V., Dynek J.N., Zobel K., Deshayes K., Fairbrother W.J., Vucic D. J. Biol. Chem. 283:24295-24299(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U88908 mRNA. Translation: AAC53531.1. CT030639 Genomic DNA. No translation available.
IPI	IPI00830777.
RefSeq	NP_031490.2. NM_007464.3.
UniGene	Mm.2026.
3D structure databases
ProteinModelPortal	O08863.
SMR	O08863. Positions 24-96, 159-600.
ModBase	Search...
Protein-protein interaction databases
IntAct	O08863. 2 interactions.
MINT	MINT-1581324.
PTM databases
PhosphoSite	O08863.
Proteomic databases
PaxDb	O08863.
PRIDE	O08863.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	11796.
KEGG	mmu:11796.
Organism-specific databases
CTD	330.
MGI	MGI:1197007. Birc3.
Phylogenomic databases
eggNOG	NOG243347.
HOGENOM	HOG000232059.
HOVERGEN	HBG004848.
InParanoid	O08863.
KO	K16060.
OrthoDB	EOG4K3KVW.
Gene expression databases
ArrayExpress	O08863.
Bgee	O08863.
CleanEx	MM_BIRC2. MM_BIRC3.
Genevestigator	O08863.
GermOnline	ENSMUSG00000032000. Mus musculus.
Family and domain databases
Gene3D	1.10.1170.10. 4 hits. 1.10.533.10. 1 hit.
InterPro	IPR001370. BIR. IPR001315. CARD. IPR011029. DEATH-like_dom. IPR001841. Znf_RING. [Graphical view]
Pfam	PF00653. BIR. 3 hits. PF00619. CARD. 1 hit. [Graphical view]
SMART	SM00238. BIR. 3 hits. SM00114. CARD. 1 hit. SM00184. RING. 1 hit. [Graphical view]
SUPFAM	SSF47986. DEATH_like. 1 hit.
PROSITE	PS01282. BIR_REPEAT_1. 3 hits. PS50143. BIR_REPEAT_2. 3 hits. PS50209. CARD. 1 hit. PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	279629.
SOURCE	Search...

Entry information

Entry name

BIRC3_MOUSE

Accession

Primary (citable) accession number: O08863
Secondary accession number(s): E9QLX3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents