| IED ID | IndEnz0002006225 |
| Enzyme Type ID | protease006225 |
| Protein Name |
NACHT, LRR and PYD domains-containing protein 1 homolog EC 3.4.-.- Cleaved into: NACHT, LRR and PYD domains-containing protein 1, C-terminus NLRP1-CT ; NACHT, LRR and PYD domains-containing protein 1, N-terminus NLRP1-NT |
| Gene Name | nlrp1 si:ch211-66k16.28 |
| Organism | Danio rerio (Zebrafish) (Brachydanio rerio) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Actinopterygii Actinopteri Neopterygii Teleostei Osteoglossocephalai Clupeocephala Otomorpha Ostariophysi Otophysi Cypriniphysae Cypriniformes (carps and others) Cyprinoidei Danionidae Danioninae Danio Danio rerio (Zebrafish) (Brachydanio rerio) |
| Enzyme Sequence | MSSDYTDRNNLASAIKTLGDMLEKDEAFQRLMYNASTKGEINRGRVNKVFLKALLSAGDKVGEFLNELIDHLNLFKVLGDFSWNPPVLKEAELNERTSQLRTQQHKYVERVSGFSHYGFGETGTPARGDITSPRGPQVASIEEDLATSKLAELLLAVGDHLEKIEKKGQFLPENVERFSLDCFITSESVKLSSEAVELAPCYTEPVIIQRSKEQTEKYCQEYVRSPHTSSHLLSNDKTQSIRIGQLFSPDSDGNTPKTVILCGDSGRGKSFVLEKIILDWVHLEHHFENFDAVFLLKYEELKCLSEEMSLTELLSRSCSLTSDQISQILQLTPEKVLFLIDGIDDFSFNAHIQISSPTDPSQKAPVISIIHCLMRDLLLVESSVIVTTRYTAAAELSSLCKRPQRFTEIEGFSERRVQEYFQKFFQDEQLFKKAYESMKTNETLLTFCSVPLLCWMVCFCLKKDADQVMTELKTTTSIYVHFVSTLLEDHHQSQSFLRSLGQLAEEGMKNRQNLFDEKSVTRTGLDPATRVFMNKIYLKRKKKHELLFKFKHLSFQEFFAALYYIMLDEEESWCKVSELFNMMESEALIHRSPPIFRGRLSNPIPSVMMFLCGLFNKKVSSSLFEKMKSTFSHNVKLKKKELKKKLMKMIPAMIRQYGFELFALHCLYELQDERFVTKVLETHKFIDLSNVSLRSTDCLVLCYCLRLCPNIRELNFMNCDLTAAKLKILQPALGLCETLRFSVEHLSEIGDLIQILSESKILRELKVREDEYGVESPRWSFNLSVTRGDVLLTLSSSEKNPSFSSVLNIRLTCAQSQISRTDWTLFLQRLRKTGTLTEDSSADDDHVSLQLSSLHSVGLKSLDLTLVSLNESWASGIISLIQNCTSLQQLKVSVTGLLLEEGLKLLKKSLTDPHCTVIIEGRRNCSEPSEEHLRQSYEKVEIHFKPKLLEELAELSICNPGSSALNIHCQSCVDVADSDQWVQVEPSVCRGEGGTEFRITTPAGRFQCSRTRMRWVCDGDVTLHYRAVDGHFLNAELERLQCERVAPVLDVNVISGKLEEAHLPHYMCLAESDPALTNAVKLLSVEDEGISLESVELTRFHAKILQPMFSPKTVLVKLGIPVKVHCDLLIFMTHTCPIILNVYFFPSDSLVEENIKTEEKSSHQIKCSRPEAPLQMKKQHSLEVPDAVVQPEAIKLRGNMKPNFFQVKQPVVNDITMILSRVDDQKSVWTGTIWKKLIDIKLNKTESDLFQSGQKHKTSQPAHSFDKAQFFDTHWCNLIKSVENVDTVADKLLQKQIIHEQFYSEIIHHKSTSEESMRKICVIVRKGSAAVKEIFISILLQENPNLLNHLPSSDS |
| Enzyme Length | 1355 |
| Uniprot Accession Number | A0A386CAB9 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: nlrp1 inflammasome is activated by pathogens and other damage-associated signals: activation promotes ubiquitination and degradation of the N-terminal part, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1, C-terminus), which polymerizes and forms the nlrp1 inflammasome. {ECO:0000250|UniProtKB:Q9C000}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.-.- |
| Enzyme Function | FUNCTION: Acts as the sensor component of the nlrp1 inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (PubMed:30150286). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (PubMed:30150286). Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, and mediates the formation of the inflammasome polymeric complex (By similarity). In response to pathogen-associated signals, the N-terminal part of nlrp1 is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the inflammasome recruits and activate proinflammatory caspases (caspa and/or caspb), leading to pyroptosis (By similarity). {ECO:0000250|UniProtKB:Q9C000, ECO:0000269|PubMed:30150286}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1 homolog]: Constitutes the precursor of the nlrp1 inflammasome, which mediates autoproteolytic processing within the FIIND domain to generate the N-terminal and C-terminal parts, which are associated non-covalently in absence of pathogens and other damage-associated signals. {ECO:0000250|UniProtKB:Q9C000}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1, N-terminus]: Regulatory part that prevents formation of the nlrp1 inflammasome: in absence of pathogens and other damage-associated signals, interacts with the C-terminal part of nlrp1 (NACHT, LRR and PYD domains-containing protein 1, C-terminus), preventing activation of the nlrp1 inflammasome (By similarity). In response to pathogen-associated signals, this part is ubiquitinated and degraded by the proteasome, releasing the cleaved C-terminal part of the protein, which polymerizes and forms the nlrp1 inflammasome (By similarity). {ECO:0000250|UniProtKB:Q9C000}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1, C-terminus]: Constitutes the active part of the nlrp1 inflammasome (By similarity). In absence of pathogens and other damage-associated signals, interacts with the N-terminal part of nlrp1 (NACHT, LRR and PYD domains-containing protein 1, N-terminus), preventing activation of the nlrp1 inflammasome (By similarity). In response to pathogen-associated signals, the N-terminal part of nlrp1 is degraded by the proteasome, releasing this form, which polymerizes to form the nlrp1 inflammasome complex: the nlrp1 inflammasome complex then directly recruits and activates proinflammatory caspases (caspa and/or caspb) activation, leading to subsequent pyroptosis (By similarity). {ECO:0000250|UniProtKB:Q9C000}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 263..270; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00136 |
| Features | Chain (3); Domain (3); Nucleotide binding (1); Region (2); Site (1) |
| Keywords | ATP-binding;Cytoplasm;Hydrolase;Immunity;Inflammasome;Inflammatory response;Innate immunity;Necrosis;Nucleotide-binding;Protease;Reference proteome;Repeat;Ubl conjugation |
| Interact With | |
| Induction | INDUCTION: Up-regulated in response to infection with the bacteriim E.tarda. {ECO:0000269|PubMed:30150286}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30150286}. Note=Co-localizes with pycard, caspa and caspb in the cytoplasm. {ECO:0000269|PubMed:30150286}.; SUBCELLULAR LOCATION: [NACHT, LRR and PYD domains-containing protein 1, C-terminus]: Inflammasome {ECO:0000269|PubMed:30150286}. |
| Modified Residue | |
| Post Translational Modification | PTM: [NACHT, LRR and PYD domains-containing protein 1 homolog]: Autocatalytically cleaved. Autocatalytic cleavage in FIIND region occurs constitutively, prior to activation signals, and is required for inflammasome activity (IL1B release), possibly by facilitating proinflammatory caspases (caspa and/or caspb) binding. Both N- and C-terminal parts remain associated non-covalently. {ECO:0000250|UniProtKB:Q9C000}.; PTM: [NACHT, LRR and PYD domains-containing protein 1, N-terminus]: Ubiquitinated in response to pathogen-associated signals, leading to its degradation by the proteasome and subsequent release of the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1, C-terminus), which polymerizes and forms the nlrp1 inflammasome. {ECO:0000250|UniProtKB:Q9C000}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 154,257 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |