ID M3YAL7_MUSPF Unreviewed; 948 AA.
AC M3YAL7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=NLR family pyrin domain containing 6 {ECO:0000313|Ensembl:ENSMPUP00000008374.1};
GN Name=NLRP6 {ECO:0000313|Ensembl:ENSMPUP00000008374.1};
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:ENSMPUP00000008374.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000008374.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
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DR EMBL; AEYP01101490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3YAL7; -.
DR STRING; 9669.ENSMPUP00000008374; -.
DR Ensembl; ENSMPUT00000008509.1; ENSMPUP00000008374.1; ENSMPUG00000008438.1.
DR eggNOG; ENOG502SANB; Eukaryota.
DR GeneTree; ENSGT00940000162758; -.
DR HOGENOM; CLU_002274_2_2_1; -.
DR InParanoid; M3YAL7; -.
DR OMA; FMDQSFQ; -.
DR GO; GO:0140738; C:NLRP6 inflammasome complex; IEA:Ensembl.
DR GO; GO:0043228; C:non-membrane-bounded organelle; IEA:Ensembl.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
DR GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
DR GO; GO:0070891; F:lipoteichoic acid 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:0035591; F:signaling adaptor activity; IEA:Ensembl.
DR GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; IEA:Ensembl.
DR GO; GO:0140374; P:antiviral innate immune response; IEA:Ensembl.
DR GO; GO:0048874; P:host-mediated regulation of intestinal microbiota composition; IEA:Ensembl.
DR GO; GO:0070266; P:necroptotic process; IEA:Ensembl.
DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IEA:Ensembl.
DR GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0032689; P:negative regulation of type II interferon production; IEA:Ensembl.
DR GO; GO:0070946; P:neutrophil-mediated killing of gram-positive bacterium; IEA:Ensembl.
DR GO; GO:0140739; P:NLRP6 inflammasome complex assembly; IEA:Ensembl.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:2000494; P:positive regulation of interleukin-18-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
DR GO; GO:0070269; P:pyroptosis; IEA:Ensembl.
DR GO; GO:0010506; P:regulation of autophagy; IEA:Ensembl.
DR GO; GO:0070255; P:regulation of mucus secretion; IEA:Ensembl.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR CDD; cd08321; Pyrin_ASC-like; 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; IPR004020; DAPIN.
DR InterPro; IPR011029; DEATH-like_dom_sf.
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; PTHR45690; NACHT, LRR AND PYD DOMAINS-CONTAINING PROTEIN 12; 1.
DR PANTHER; PTHR45690:SF1; NACHT, LRR AND PYD DOMAINS-CONTAINING PROTEIN 6; 1.
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; 3.
DR SMART; SM01289; PYRIN; 1.
DR SUPFAM; SSF47986; DEATH domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS50824; DAPIN; 1.
DR PROSITE; PS50837; NACHT; 1.
PE 4: Predicted;
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614}.
FT DOMAIN 70..159
FT /note="Pyrin"
FT /evidence="ECO:0000259|PROSITE:PS50824"
FT DOMAIN 253..569
FT /note="NACHT"
FT /evidence="ECO:0000259|PROSITE:PS50837"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 948 AA; 106404 MW; FA55C959453B109E CRC64;
RRQSLGAKPR SPLHASPPRE CSLEQRGLVG AADRRAPRGR VGWEAGQGRG PRNHMRVDRH
RPPAPSTEAR AAKARDLLQA ALEDLSQEQL KRFRHKLRDA ALDGRSIPWG RLERADAVDL
AEQMIQFYGP EPALDVARKT LKRADVRDVA ARLKEQGLQW FSPGSSALLS VSEYKKKYRE
HVLQQHAKVK ERNARSVKIN KRFTKLLIAR ESAALVDEAP GLAEEPEPER ARRSDTHTFN
RLFGRDEEGQ RPLTVVLQGP AGIGKTMAAK KILYDWAVGK LYHDQVDFAF FLPCRELLER
PGPCSLARLV LDQCPHRSAP VRQMLARSER LLFILDGADE LPPGPADAAP CTDPFEEADG
ARVLDGLMSK TLLPGARLLV TARATAPGRL QGRLCSPQCA EVRGFSDKDK KKYFHKFFRD
ERMAERAYRF VKENETLFAL CFVPFVCWIV CTVLRQQLQL HQDLSRTSKT TTSVYLLFIT
SVLSSAPATD GPQMQEELRK LGRLAREGTL RHRAQFPEKD LERLELRGSK VQTLFLSKKE
LPGVLETEVT YQFMDQSFQE FFAALSYLLE QEKALEAPAD SVGALLQGGT ELRGHLTLTT
RFLFGLLNGE RLRDIERHFG CGGVVSKRVK QDVLRWVQEQ GQGHPRAAPE GTEETEAPEG
SQEPEEEEEG ELSYPLELLY CLYETQESTF VHQALRGWPE LLLERVHFSR LDLLVLSYCV
RSCPAGQALR LVSCVLVPPQ EKKKKSLIKR LHGSLSGSSS QATARKSQAS PLRTLFEAMT
DQHCGLHSLT LCRCRLPDSI CRDLSEALRE APALRELGLL HNRLSEAGLR VLSEGLAWPQ
CRVQKLRVWQ PRLQEAFQYL TSVLRQSPAL TILELGDCQL SEPTVTDLCA VLQHPGCRLQ
TLRLTSVQLS EQSLKELQVV KTAKPDLVIT HPALDGHPRP PAGHSSAL
//
