CIAP2 (Mus musculus)
Description [+]
- Synonyms: CIAP2, BIRC3, API2, CIAP-2, CIAP2, HIAP2, IAP2, MIAP2, MIHC, RNF49
- Species: Metazoa;Bilateria;Deuterostoma;Chordata;Vertebrata;Mammalia;Rodentia; Mus musculus
- Short gene description: baculoviral IAP repeat-containing 3 Gene
- Family: BIR-containing protein : IAP
- Process: immunity,
- Pathways: TNF/NF-kappaB signaling,
- Criteria: manually curated
- Curator comment:
- WIKI: CIAP2-M_musculus
References [+]
- Cellular inhibitors of apoptosis cIAP1 and cIAP2 are required for innate immunity signaling by the pattern recognition receptors NOD1 and NOD2.
- Bertrand MJ, Doiron K, Labbe K, Korneluk RG, Barker PA, Saleh M
- Cellular inhibitor of apoptosis proteins (cIAPs) block apoptosis, but their physiological functions are still under investigation. Here, we report that cIAP1 and cIAP2 are E3 ubiquitin ligases that are required for receptor-interacting protein 2 (RIP2) ubiquitination and for nucleotide-binding and oligomerization (NOD) signaling. Macrophages derived from Birc2(-/-) or Birc3(-/-) mice, or colonocytes depleted of cIAP1 or cIAP2 by RNAi, were defective in NOD signaling and displayed sharp attenuation of cytokine and chemokine production. This blunted response was observed in vivo when Birc2(-/-) and Birc3(-/-) mice were challenged with NOD agonists. Defects in NOD2 signaling are associated with Crohn's disease, and muramyl dipeptide (MDP) activation of NOD2 signaling protects mice from experimental colitis. Here, we show that administration of MDP protected wild-type but not Ripk2(-/-) or Birc3(-/-) mice from colitis, confirming the role of the cIAPs in NOD2 signaling in vivo. This discovery provides therapeutic opportunities in the treatment of NOD-dependent immunologic and inflammatory diseases. Immunity. 2009 Jun 19;30(6):789-801. Epub 2009 May 21.
- The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins.
- Rothe M, Pan MG, Henzel WJ, Ayres TM, Goeddel DV
- The 75 kDa tumor necrosis factor receptor (TNFR2) transduces extracellular signals via receptor-associated cytoplasmic proteins. Two of these signal transducers, TRAF1 and TRAF2, were isolated and characterized previously. We report here the biochemical purification and subsequent molecular cloning of two novel TNFR2-associated proteins, designated c-IAP1 and c-IAP2, that are closely related mammalian members of the inhibitor of apoptosis protein (IAP) family originally identified in baculoviruses. The viral and cellular IAPs contain N-terminal baculovirus IAP repeat (BIR) motifs and a C-terminal RING finger. The c-IAPs do not directly contact TNFR2, but rather associate with TRAF1 and TRAF2 through their N-terminal BIR motif-comprising domain. The recruitment of c-IAP1 or c-IAP2 to the TNFR2 signaling complex requires a TRAF2-TRAF1 heterocomplex. Cell. 1995 Dec 29;83(7):1243-52.
Structure & Sequence [+]
Pfam domains:
(Pfam is a large collection of protein families.)
Source | Domain Name | Start | End |
---|---|---|---|
PFAM A | BIR | 32 | 97 |
PFAM A | BIR | 172 | 236 |
PFAM A | BIR | 258 | 323 |
PFAM A | CARD | 443 | 526 |
Protein sequence [+]
cIAP2 | Mus musculus | 10090 | length:602
MNMVQDSAFLAKLMKSADTFELKYDFSCELYRLSTYSAFPRGVPVSERSLARAGFYYTGA
NDKVKCFCCGLMLDNWKQGDSPMEKHRKLYPSCNFVQTLNPANSLEASPRPSLPSTAMST
MPLSFASSENTGYFSGSYSSFPSDPVNFRANQDCPALSTSPYHFAMNTEKARLLTYETWP
LSFLSPAKLAKAGFYYIGPGDRVACFACDGKLSNWERKDDAMSEHQRHFPSCPFLKDLGQ
SASRYTVSNLSMQTHAARIRTFSNWPSSALVHSQELASAGFYYTGHSDDVKCFCCDGGLR
CWESGDDPWVEHAKWFPRCEYLLRIKGQEFVSQVQAGYPHLLEQLLSTSDSPEDENADAA
IVHFGPGESSEDVVMMSTPVVKAALEMGFSRSLVRQTVQWQILATGENYRTVSDLVIGLL
DAEDEMREEQMEQAAEEEESDDLALIRKNKMVLFQHLTCVTPMLYCLLSARAITEQECNA
VKQKPHTLQASTLIDTVLAKGNTAATSFRNSLREIDPALYRDIFVQQDIRSLPTDDIAAL
PMEEQLRKLQEERMCKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPICRGTIKGTVRTF
LS
NDKVKCFCCGLMLDNWKQGDSPMEKHRKLYPSCNFVQTLNPANSLEASPRPSLPSTAMST
MPLSFASSENTGYFSGSYSSFPSDPVNFRANQDCPALSTSPYHFAMNTEKARLLTYETWP
LSFLSPAKLAKAGFYYIGPGDRVACFACDGKLSNWERKDDAMSEHQRHFPSCPFLKDLGQ
SASRYTVSNLSMQTHAARIRTFSNWPSSALVHSQELASAGFYYTGHSDDVKCFCCDGGLR
CWESGDDPWVEHAKWFPRCEYLLRIKGQEFVSQVQAGYPHLLEQLLSTSDSPEDENADAA
IVHFGPGESSEDVVMMSTPVVKAALEMGFSRSLVRQTVQWQILATGENYRTVSDLVIGLL
DAEDEMREEQMEQAAEEEESDDLALIRKNKMVLFQHLTCVTPMLYCLLSARAITEQECNA
VKQKPHTLQASTLIDTVLAKGNTAATSFRNSLREIDPALYRDIFVQQDIRSLPTDDIAAL
PMEEQLRKLQEERMCKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPICRGTIKGTVRTF
LS
Structure links:
Evolution [+]
View protein alignment and tree with Jalview:  
Explore tree at phylomeDB:   Click here.
Homologs list [+]
Name | Relationship | Species |
---|
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Gene Ontology [+]
GO id | Name | Ontology type | Evidence |
---|---|---|---|
GO:0042981 | regulation of apoptosis | biological_proccess | IEA |
GO:0006915 | apoptosis | biological_proccess | IEA |
GO:0007283 | spermatogenesis | biological_proccess | IEA |
GO:0051291 | protein heterooligomerization | biological_proccess | IEA |
GO:0005515 | protein binding | mollecular_function | IPI |
GO:0008270 | zinc ion binding | mollecular_function | IEA |
GO:0046872 | metal ion binding | mollecular_function | IEA |
GO:0005515 | protein binding | mollecular_function | IEA |
GO:0004842 | ubiquitin-protein ligase activity | mollecular_function | IEA |
GO:0005622 | intracellular | cell_component | IEA |
GO:0005737 | cytoplasm | cell_component | IEA |
GO:0005634 | nucleus | cell_component | IEA |
GO:0043234 | protein complex | cell_component | IEA |
GO:0045121 | membrane raft | cell_component | IEA |
Check GO Evidence Codes here
KEGG Pathways [+]
Information from other databases [+]
- Gene info from MGI [?] MGI:1197007
- Ensembl genome browser [?] : ENSMUSG00000032000
- Expression info from Arrayexpress [?] : ENSMUSG00000032000
- Protein expression from Protein Atlas: [?] ENSMUSG00000032000
- Community gene edition from Wikigenes: [?] 11796
Click on [?] for more information.