ID A0A287DBR3_ICTTR Unreviewed; 1216 AA.
AC A0A287DBR3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 05-FEB-2025, entry version 34.
DE SubName: Full=NLR family pyrin domain containing 1 {ECO:0000313|Ensembl:ENSSTOP00000030969.1};
GN Name=NLRP1 {ECO:0000313|Ensembl:ENSSTOP00000030969.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000030969.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000030969.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (OCT-2024) to UniProtKB.
CC -!- FUNCTION: Constitutes the active part of the Nlrp1a inflammasome. In
CC absence of pathogens and other damage-associated signals, interacts
CC with the N-terminal part of Nlrp1a (NACHT, LRR and PYD domains-
CC containing protein 1a, N-terminus), preventing activation of the Nlrp1a
CC inflammasome. In response to pathogen-associated signals, the N-
CC terminal part of Nlrp1a is degraded by the proteasome, releasing this
CC form, which polymerizes to form the Nlrp1a inflammasome complex: the
CC Nlrp1a inflammasome complex then directly recruits pro-caspase-1
CC (proCASP1) and promotes caspase-1 (CASP1) activation, leading to
CC gasdermin-D (GSDMD) cleavage and subsequent pyroptosis.
CC {ECO:0000256|ARBA:ARBA00024315}.
CC -!- FUNCTION: Constitutes the precursor of the Nlrp1a inflammasome, which
CC mediates autoproteolytic processing within the FIIND domain to generate
CC the N-terminal and C-terminal parts, which are associated non-
CC covalently in absence of pathogens and other damage-associated signals.
CC {ECO:0000256|ARBA:ARBA00029394}.
CC -!- SUBUNIT: Interacts with the C-terminal part of Nlrp1a (NACHT, LRR and
CC PYD domains-containing protein 1a, C-terminus) in absence of pathogens
CC and other damage-associated signals. {ECO:0000256|ARBA:ARBA00024369}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the NLRP family.
CC {ECO:0000256|ARBA:ARBA00008665}.
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DR EMBL; AGTP01092386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01092387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A287DBR3; -.
DR STRING; 43179.ENSSTOP00000030969; -.
DR Ensembl; ENSSTOT00000040427.1; ENSSTOP00000030969.1; ENSSTOG00000012657.3.
DR eggNOG; ENOG502S4A4; Eukaryota.
DR GeneTree; ENSGT00940000162176; -.
DR InParanoid; A0A287DBR3; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0072558; C:NLRP1 inflammasome complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR GO; GO:0140608; F:cysteine-type endopeptidase activator activity; IEA:Ensembl.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0140693; F:molecular condensate scaffold activity; IEA:Ensembl.
DR GO; GO:0038187; F:pattern recognition receptor activity; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0035591; F:signaling adaptor activity; IEA:Ensembl.
DR GO; GO:0140374; P:antiviral innate immune response; IEA:Ensembl.
DR GO; GO:0071493; P:cellular response to UV-B; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:1904784; P:NLRP1 inflammasome complex assembly; IEA:Ensembl.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IEA:Ensembl.
DR GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
DR GO; GO:0070269; P:pyroptotic inflammatory response; IEA:Ensembl.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0097264; P:self proteolysis; IEA:Ensembl.
DR CDD; cd08330; CARD_ASC_NALP1; 1.
DR FunFam; 1.10.533.10:FF:000013; Apoptosis-associated speck-like protein containing a CARD; 1.
DR FunFam; 3.40.50.300:FF:000897; NLR family pyrin domain containing 1; 1.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR033516; CARD8/ASC/NALP1_CARD.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR025307; FIIND_dom.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR041267; NLRP_HD2.
DR InterPro; IPR051249; NLRP_Inflammasome.
DR InterPro; IPR041075; NOD1/2_WH.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR46985; NACHT, LRR AND PYD DOMAINS-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR46985:SF3; NACHT, LRR AND PYD DOMAINS-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00619; CARD; 1.
DR Pfam; PF13553; FIIND; 1.
DR Pfam; PF05729; NACHT; 1.
DR Pfam; PF17776; NLRC4_HD2; 1.
DR Pfam; PF17779; NOD2_WH; 1.
DR SMART; SM00368; LRR_RI; 2.
DR SUPFAM; SSF47986; DEATH domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS50209; CARD; 1.
DR PROSITE; PS51830; FIIND; 1.
DR PROSITE; PS50837; NACHT; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Inflammatory response {ECO:0000256|ARBA:ARBA00023198};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 110..419
FT /note="NACHT"
FT /evidence="ECO:0000259|PROSITE:PS50837"
FT DOMAIN 811..1095
FT /note="FIIND"
FT /evidence="ECO:0000259|PROSITE:PS51830"
FT DOMAIN 1126..1209
FT /note="CARD"
FT /evidence="ECO:0000259|PROSITE:PS50209"
SQ SEQUENCE 1216 AA; 138362 MW; 482424FB5D01897F CRC64;
VLEKVTSEEL SPLLASQEAQ PDSHLFLPYL GIRERYQNQR REKLRHAQSW KNDNMHQKFT
QLLLLQKPHS RGKNPLARKS WHRNAVEEQG HLIEIRELFG PGPGFQKEPH IVILHGAPGI
GKSTLARQVK GAWEEGQLYR DRFQHVFYFS CRELAQCKLV SLAELISEDG TAPTAPIRQI
LSQPEQLLFI LDGIDEPKWV LENQSPELCV HWSQSQPVHA LLGGLLGKAI LPEASLLLTS
RTTDLQKLIP SLKQPRWVEV LGFSESGRKE YFYKYFTDES QANRAFTMLK SNPELLTLCL
MPLVSWMVCT YLKENMKLGK VLPPTIQTLT SLYMHYLFQA FPAPHLGTQL KDFCSLAAEG
LWQRKTVFSA GDLRKHELNE AIITIFLKRG VLRKGPDSLT YSFIHLCFQE FFAAMSYALR
DKEERSQSPD GLGGMEELLD VYGRNNLFGA PTVRFLFGLL SDHWSRATEE PFTFQLYPER
KWELLQWVEA KSPPGKPHSL EFLHCLYETQ DEEFLMQAMD CFQRTRMYVQ TDMELLVFIF
CIKFCGHVKR LQLNESPQKG QGWRPPGVVL SRWVPITDNS WQVLFSTLRV SGGLRELDLS
GNSLSHSAVQ NLRRTLRPPL CYLETLSETD GGGDIPGRGN SIPLPPLHGT SILVSCGLTS
SCCQDLASAL SVSPRLLELD LQQNDLGDHG VRLLYKGLKH PACQLTLLWL DYIPLSDQVR
EELKALEEEI PRLLISSRWK PSVMIPTGDP DEGQMGENMS SLKQENIQLT TVLLIPEESS
PQVAQVEPFH LSSHASAEDL HMEPLGTEDN FWGPTGPVAT EMVDKEKSLY RVHFPMAGSY
CWSNTGLTFV VRRAVTIEIE FCAWDQFLGN TIPPQSWMVA GPLFDIKAEQ GAVAAVYLPH
FVALQEGPVD ISLFHVAHFK EEGMLLEKPS RVEPHYAVLE DPSFSPMGIL LRMIPTALCF
IPITSTTLLY HQLHPKEITS FHLYLIPSDC SIQKAIDDEE KKFQFVRIHK PPPVTPLYLG
SRYTVSASRK LEIIPKELEL CYRSPREPQL FSEFYIGHLG SGIRLQIKNK KGGTVVWKAQ
LKPGKTRTSL DSSEVGERRS GDLWWEPFLA HCQPHLFSPD ALGSLHFVDR HREQLVARVT
SVDPVLDKLH GQVLSEEQYE KVRAETTKPG QMRKLFSFSR SWDWACKDQL YRALKEIHPH
LIVELWEKWG GDLGSL
//