ID M3YIL7_MUSPF Unreviewed; 1436 AA.
AC M3YIL7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE SubName: Full=NACHT, LRR and PYD domains-containing protein 1 isoform X2 {ECO:0000313|RefSeq:XP_004760529.1};
DE SubName: Full=NLR family pyrin domain containing 1 {ECO:0000313|Ensembl:ENSMPUP00000011174.1};
GN Name=NLRP1 {ECO:0000313|Ensembl:ENSMPUP00000011174.1,
GN ECO:0000313|RefSeq:XP_004760529.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000011174.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000011174.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004760529.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004760529.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Inflammasome
CC {ECO:0000256|ARBA:ARBA00004110}.
CC -!- SIMILARITY: Belongs to the NLRP family.
CC {ECO:0000256|ARBA:ARBA00008665}.
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DR EMBL; AEYP01050968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004760529.1; XM_004760472.3.
DR STRING; 9669.ENSMPUP00000011174; -.
DR Ensembl; ENSMPUT00000011362.1; ENSMPUP00000011174.1; ENSMPUG00000011266.1.
DR GeneID; 101679990; -.
DR CTD; 22861; -.
DR eggNOG; ENOG502S4A4; Eukaryota.
DR GeneTree; ENSGT00940000162176; -.
DR HOGENOM; CLU_002274_2_4_1; -.
DR OMA; VELWEKW; -.
DR OrthoDB; 338452at2759; -.
DR Proteomes; UP000000715; Unplaced.
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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0043621; F:protein self-association; 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:pyroptosis; IEA:Ensembl.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0097264; P:self proteolysis; IEA:Ensembl.
DR GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IEA:Ensembl.
DR CDD; cd08330; CARD_ASC_NALP1; 1.
DR CDD; cd08320; Pyrin_NALPs; 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; IPR041075; NOD2_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 SMART; SM00368; LRR_RI; 6.
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 Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 1..92
FT /note="Pyrin"
FT /evidence="ECO:0000259|PROSITE:PS50824"
FT DOMAIN 293..601
FT /note="NACHT"
FT /evidence="ECO:0000259|PROSITE:PS50837"
FT DOMAIN 1039..1321
FT /note="FIIND"
FT /evidence="ECO:0000259|PROSITE:PS51830"
FT DOMAIN 1331..1420
FT /note="CARD"
FT /evidence="ECO:0000259|PROSITE:PS50209"
FT REGION 95..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..232
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1436 AA; 160706 MW; EAAE05ED1FA12FB6 CRC64;
MASGVQWRLA RYLDMLGKEE LKEFQLRLPE KPLGGPRPHL TSACGQQPGA LEAASQLVAQ
HGEQQAWDLA LHTWEQMGLS QLCAQARAEA ALMSGEGSSL PCSPGAPSMQ SPSGPTSTVV
LSFVQDPPTT SSKQPPGTSR CFLQNRYPSF SFNRVLPCSS NQKSLLQESP SAPTSTTVLE
DWVPPPQFSR KPRKQEAPRA EWLLVEMSGE HSKGIRERRQ HQKRKRPRPT KSRGKEGLHE
EFIELLLLHQ PRGGLLESQS KGSWHHSGAE EQGRLIEVKD LFGPGLGAQE EGRAVVLHGV
AGVGKSVMAR QVRRAWEEGR LYRDRFQHVF YFSCRQLAQS KTMSLKELIT KDWAAPTAPS
EQILSQPGQL LLILDGLDEL KWVFVKEKSE VCPYWDQPQP VKTLLLGLLR KTILPGASLL
ITARTTALHL FILSVEQPRW VKVLGFSESS RKEYFYKYFK SKNKANRAFH SVELNQPLLT
MCLVPLVSWL VCTCMKKQME RGESLGLPSQ TATALCLHYL AQALPAQPLG TQLRGLCSLA
AKGIRQRETL LIWEDLRKHE LEDTVSALLE MGILRKHPSS PDYDFAHQYL QEFFAAVSCV
LGSEDKECHP PDSIQGLEDL LKAYGGLDPF GVPPTCFVLG LLSEPVQREM EAVFQGKVPA
ERKRKLLCWA KEAVRNQLPV LQQSSLPMLH CLYEIQDKDF LTHAMAPFHG ARVRVHTSLE
LLVFMFCIKF CTVKELRLNE RGQHGHTGSP LHVALLRGFP VTDAWWEVLF FTLRTTGKLK
ELDLSGNCLS NTVVQSLCKA LRFPSCCLET LRLTHCSLTA EGCIGLAWVL DTPETLTELE
LSFNLLLDLG VERLCNGLKE PGCRLHRLRL VGCGLTSRCC RALASALSAS PRLTELDLQQ
NELEDAGVRL LCEGLRRPTC QLRLLWLDQT GLSEEVTRML RALEDEKPPL LIPSRWKPSE
TMPNEGPRET VPNEDPRETM PNEGPHEGET SGTSSLQQDR RESEGLSPPV VQEGLVGLLS
PAPPEDLQHK GPLGTEDDFW GPLGPVTIEM VDKDRSLHRV HLPMAGSYRW PSTGLRFVVR
EPATIDIEFC ASDKFLHQMA WEQSWMVVGP LFDIKVKPGA VATVYLPHFV DLRGGCVDTS
LFQVAHFKEP GMLLEKPTRV ELYHVVLEDP SFSPLGVFLR TIHAALRFLP ITSMVLLYHH
TRPDETVFHL YLIPSDCCVR KAIDDEEKAF QFVQIRKPPP LGSLYLGSRY TVSSSETLEA
IPKELELCYR SPGQPQLYSE FYVGDLGSGL RLQLKDGSGA VVWEALVKPG DLQLTSSLVP
PAPAASPAPP GAPASLHFLD RHREQLVARV TTVDPVLDKL LGQVLSEEQY ERVRAKATAA
NQMRELFRFS RSWDPACKDQ VYQALKETHP YLIMELWETW GGDRERGTSP PTQPLP
//