UniProt functional annotation for Q86UT6



	UniProt functional annotation for Q86UT6

UniProt code: Q86UT6.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Participates in antiviral signaling. Acts as a negative regulator of MAVS-mediated antiviral responses, through the inhibition of the virus-induced RLH (RIG-like helicase)-MAVS interaction (PubMed:18200010). Instead, promotes autophagy by interacting with TUFM and subsequently recruiting the autophagy-related proteins ATG5 and ATG12 (PubMed:22749352). Regulates also MAVS-dependent NLRP3 inflammasome activation to attenuate apoptosis (PubMed:27393910). Has no inhibitory function on NF-kappa-B signaling pathway, but enhances NF-kappa-B and JUN N-terminal kinase dependent signaling through the production of reactive oxygen species (PubMed:18219313). {ECO:0000269|PubMed:18200010, ECO:0000269|PubMed:18219313, ECO:0000269|PubMed:22749352, ECO:0000269|PubMed:27393910}.

Subunit: Homohexamer. Interacts with MAVS (PubMed:18200010). Interacts with TUFM (PubMed:22749352). {ECO:0000269|PubMed:18200010, ECO:0000269|PubMed:22386589, ECO:0000269|PubMed:22749352}.

Subunit: (Microbial infection) Interacts with influenza A virus protein PB1-F2. {ECO:0000269|PubMed:24799673}.

Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:18200010, ECO:0000269|PubMed:18219313, ECO:0000269|PubMed:27393910}.

Tissue specificity: Ubiquitously expressed. Strongest expression in mammary gland, heart and muscle. Detected in HeLa, HEK293T, THP-1, HL- 60, Raji and Jurkat cell lines (at protein level). {ECO:0000269|PubMed:15952891, ECO:0000269|PubMed:18200010, ECO:0000269|PubMed:18219313}.

Domain: The LRRCT domain mediates homodimerization and LRRNT mediates trimerization of the dimers.

Similarity: Belongs to the NLRP family. {ECO:0000305}.

Sequence caution: Sequence=BAB15075.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=BAG51714.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=BAG51714.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Participates in antiviral signaling. Acts as a negative regulator of MAVS-mediated antiviral responses, through the inhibition of the virus-induced RLH (RIG-like helicase)-MAVS interaction (PubMed:18200010). Instead, promotes autophagy by interacting with TUFM and subsequently recruiting the autophagy-related proteins ATG5 and ATG12 (PubMed:22749352). Regulates also MAVS-dependent NLRP3 inflammasome activation to attenuate apoptosis (PubMed:27393910). Has no inhibitory function on NF-kappa-B signaling pathway, but enhances NF-kappa-B and JUN N-terminal kinase dependent signaling through the production of reactive oxygen species (PubMed:18219313). {ECO:0000269\|PubMed:18200010, ECO:0000269\|PubMed:18219313, ECO:0000269\|PubMed:22749352, ECO:0000269\|PubMed:27393910}.


Subunit:		Homohexamer. Interacts with MAVS (PubMed:18200010). Interacts with TUFM (PubMed:22749352). {ECO:0000269\|PubMed:18200010, ECO:0000269\|PubMed:22386589, ECO:0000269\|PubMed:22749352}.
Subunit:		(Microbial infection) Interacts with influenza A virus protein PB1-F2. {ECO:0000269\|PubMed:24799673}.
Subcellular location:		Mitochondrion outer membrane {ECO:0000269\|PubMed:18200010, ECO:0000269\|PubMed:18219313, ECO:0000269\|PubMed:27393910}.
Tissue specificity:		Ubiquitously expressed. Strongest expression in mammary gland, heart and muscle. Detected in HeLa, HEK293T, THP-1, HL- 60, Raji and Jurkat cell lines (at protein level). {ECO:0000269\|PubMed:15952891, ECO:0000269\|PubMed:18200010, ECO:0000269\|PubMed:18219313}.
Domain:		The LRRCT domain mediates homodimerization and LRRNT mediates trimerization of the dimers.
Similarity:		Belongs to the NLRP family. {ECO:0000305}.
Sequence caution:		Sequence=BAB15075.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=BAG51714.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=BAG51714.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};