ID A0A8C2W7Y3_CHILA Unreviewed; 1344 AA.
AC A0A8C2W7Y3;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 05-FEB-2025, entry version 17.
DE SubName: Full=NACHT, LRR and PYD domains-containing protein 1-like {ECO:0000313|Ensembl:ENSCLAP00000024432.1};
GN Name=LOC102013491 {ECO:0000313|Ensembl:ENSCLAP00000024432.1};
OS Chinchilla lanigera (Long-tailed chinchilla) (Chinchilla villidera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha;
OC Chinchillidae; Chinchilla.
OX NCBI_TaxID=34839 {ECO:0000313|Ensembl:ENSCLAP00000024432.1, ECO:0000313|Proteomes:UP000694398};
RN [1] {ECO:0000313|Ensembl:ENSCLAP00000024432.1}
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: Inflammasome {ECO:0000256|ARBA:ARBA00004110}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the NLRP family.
CC {ECO:0000256|ARBA:ARBA00008665}.
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DR RefSeq; XP_013377615.1; XM_013522161.1.
DR RefSeq; XP_013377616.1; XM_013522162.1.
DR Ensembl; ENSCLAT00000024667.1; ENSCLAP00000024432.1; ENSCLAG00000016776.1.
DR GeneID; 102013491; -.
DR GeneTree; ENSGT00940000162176; -.
DR OMA; ELVTHEM; -.
DR OrthoDB; 428577at2759; -.
DR Proteomes; UP000694398; Unassembled WGS sequence.
DR GO; GO:0061702; C:canonical inflammasome complex; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0012501; P:programmed cell death; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR CDD; cd08330; CARD_ASC_NALP1; 1.
DR CDD; cd08320; Pyrin_NALPs; 1.
DR FunFam; 1.10.533.10:FF:000013; Apoptosis-associated speck-like protein containing a CARD; 1.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 2.
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; IPR004020; DAPIN.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR025307; FIIND_dom.
DR InterPro; IPR001611; Leu-rich_rpt.
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; PF13516; LRR_6; 3.
DR Pfam; PF05729; NACHT; 1.
DR Pfam; PF17776; NLRC4_HD2; 1.
DR Pfam; PF17779; NOD2_WH; 1.
DR Pfam; PF02758; PYRIN; 1.
DR PRINTS; PR00364; DISEASERSIST.
DR SMART; SM00368; LRR_RI; 5.
DR SMART; SM01289; PYRIN; 1.
DR SUPFAM; SSF47986; DEATH domain; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS50209; CARD; 1.
DR PROSITE; PS50824; DAPIN; 1.
DR PROSITE; PS51830; FIIND; 1.
DR PROSITE; PS50837; NACHT; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Inflammasome {ECO:0000256|ARBA:ARBA00023233};
KW Inflammatory response {ECO:0000256|ARBA:ARBA00023198};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Necrosis {ECO:0000256|ARBA:ARBA00022590};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000694398};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 23..115
FT /note="Pyrin"
FT /evidence="ECO:0000259|PROSITE:PS50824"
FT DOMAIN 218..532
FT /note="NACHT"
FT /evidence="ECO:0000259|PROSITE:PS50837"
FT DOMAIN 925..1208
FT /note="FIIND"
FT /evidence="ECO:0000259|PROSITE:PS51830"
FT DOMAIN 1247..1337
FT /note="CARD"
FT /evidence="ECO:0000259|PROSITE:PS50209"
FT REGION 878..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1344 AA; 153550 MW; B7FE102063803E9C CRC64;
MEISEAVGIA EEEQSAHLHR AKMAGKRKYH LLVYYLDLLE KEELKEFQLL LQNKTFLRIS
PTTTAAQAKK ISGREVALWL VAEYGEQQAW DLAIKTWEQM GLTVLCDKAR REVFLTWGAR
GSEKKSLTQP SEKSVHSKGI EPINFPKISE KSCPTQSRET KYFHEKFTQL LLLRTPHFRS
KEYLAREMWI YESKVGQGHL IKIQDLFGPV PGTQEESHRV VLYGAAGIGK STLARQVRGA
WEEGWLFRDR FRYVFYFNCR DLPQCQVNSM EEVIAASWAS TAVPIMDILS SPEQVLFILD
NVDQPKLNLR FLDSKGLRLQ AQPKLSHSPQ VRLVLDHLLQ SLLFVRAFFL ITARTTSLEM
FPHSWEKPRW VEVLGFSEWG RKDYFKKYFT DESQSIIAFS AVEPNPLLLA QCLVPWVCWL
VCTCLQQQIE QGEVHPLTSQ TTTGLFLHYL SQVIPTALQE IQLRCLCSLA AEGIWRRKTL
FSTNELSKHG LEGALITTFL KIGFLQEHPD TLSYSFTHQC FQEFFAALSC VLGNSAHTDK
YNFSLRWMTQ LLKEYRWPES SRIQILCFLS SLLSDYGAKE MKKIFSCQLL PRRSWELLQI
VRPHGILLSQ YYLNFFHYLY ETQDEELVTH EMAHFQERRV CVRTDRELLL VTFCVKFCNH
VKWLQLNESD LRKQERRRPG IAVSTWARLT DASWKVLFSV LQSTGSLEEL ALSGNPLSLS
AVQSLGETLG QPRCCLQTLR LAGCGLTAKG CKHLAFGLST SQTLTELELD FNMLTDAGAQ
HLCLGLKHPS CKLQRLRLVH CGLTSTCCQD LASVLSTSPS LKELDLQQNE LGSYGVQLLF
EGLRNPTCRL TLLWLDLTLL NEEELRIGEQ EKPQLLISSG QIPDTRIPPE DPEEAEESYS
TSSFMQQRPQ LGDLHMEALD IEDDFCDPTG PLPIELVNKD GSLWRVHFPM AGYYHWPHTG
LSFVVRREVM MAIQFCAWDQ FLSIHDLQDT WMVAGPLFDI KAEQGAVAAV YLPHFVALQR
EHVDRSLFQV AHFKEEGMLL DKPDRVEPHH TILENPTFSP MGVLLKIIPG ARRFFRVTCT
TLLYHHIHAE EVKFHLYLIP SDCTIRQAID DEEKKFQFER IHKPPPTDPL YLGSRYIVSG
SGMLEIMPKE LELCYRSPRQ PQLFSEIYVG CLGSGIQLEM RYKKDETVVW EALLKPGDLR
PAASLFPPSA IGQQRLSETT GDSGIPGTFC LVLEGREETG ASASPPNVPA SLHFVDQHRE
QLVARVTSVD SVLDKLLSEQ VLSEEQYTSV RAEATKPSQM RKLFSFSPSW NSACKDKLYQ
ALREIHPHLI MDLWEAGAKH SGDL
//