NLRP9_BOVIN
ID NLRP9_BOVIN Reviewed; 996 AA.
AC Q288C4; Q4U4S5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=NACHT, LRR and PYD domains-containing protein 9;
GN Name=NLRP9; Synonyms=NALP9;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15892040; DOI=10.1002/mrd.20298;
RA Dalbies-Tran R., Papillier P., Pennetier S., Uzbekova S., Monget P.;
RT "Bovine mater-like NALP9 is an oocyte marker gene.";
RL Mol. Reprod. Dev. 71:414-421(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Oocyte;
RX PubMed=16339045; DOI=10.1095/biolreprod.105.045096;
RA Ponsuksili S., Brunner R.M., Goldammer T., Kuhn C., Walz C., Chomdej S.,
RA Tesfaye D., Schellander K., Wimmers K., Schwerin M.;
RT "Bovine NALP5, NALP8, and NALP9 genes: assignment to a QTL region and the
RT expression in adult tissues, oocytes, and preimplantation embryos.";
RL Biol. Reprod. 74:577-584(2006).
CC -!- FUNCTION: As the sensor component of the NLRP9 inflammasome, plays a
CC crucial role in innate immunity and inflammation. In response to
CC pathogens, including rotavirus, initiates the formation of the
CC inflammasome polymeric complex, made of NLRP9, PYCARD and CASP1.
CC Recruitment of proCASP1 to the inflammasome promotes its activation and
CC CASP1-catalyzed IL1B and IL18 maturation and release in the
CC extracellular milieu. The active cytokines stimulate inflammatory
CC responses. Inflammasomes can also induce pyroptosis, an inflammatory
CC form of programmed cell death. NLRP9 inflammasome activation may be
CC initiated by DHX9 interaction with viral double-stranded RNA (dsRNA),
CC preferentially to short dsRNA segments. {ECO:0000250|UniProtKB:Q7RTR0}.
CC -!- SUBUNIT: Sensor component of NLRP9 inflammasomes. Inflammasomes are
CC supramolecular complexes that assemble in the cytosol in response to
CC pathogens, such as rotavirus, and play critical roles in innate
CC immunity and inflammation. The core of NLRP9 inflammasomes consists of
CC a signal sensor component (NLRP9), an adapter (ASC/PYCARD), which
CC recruits an effector pro-inflammatory caspase (CASP1). Within the
CC complex, NLRP9 and PYCARD interact via their respective DAPIN/pyrin
CC domains. This interaction initiates speck formation (nucleation) which
CC greatly enhances further addition of soluble PYCARD molecules to the
CC speck in a prion-like polymerization process. Clustered PYCARD
CC nucleates the formation of CASP1 filaments through the interaction of
CC their respective CARD domains, acting as a platform for CASP1
CC polymerization. CASP1 filament formation increases local enzyme
CC concentration, resulting in trans-autocleavage and activation. Active
CC CASP1 then processes IL1B and IL18 precursors, leading to the release
CC of mature cytokines in the extracellular milieu and inflammatory
CC response. Interacts with DHX9 upon rotavirus infection; this
CC interaction may trigger inflammasome activation and inflammatory
CC response. {ECO:0000250|UniProtKB:Q7RTR0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q66X22}.
CC Inflammasome {ECO:0000250|UniProtKB:Q7RTR0}.
CC -!- TISSUE SPECIFICITY: Detected exclusively in testis and ovary, and at
CC high level in the oocyte from antral follicles.
CC {ECO:0000269|PubMed:15892040, ECO:0000269|PubMed:16339045}.
CC -!- SIMILARITY: Belongs to the NLRP family. {ECO:0000305}.
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DR EMBL; DQ011673; AAY33775.1; -; mRNA.
DR EMBL; DQ092866; AAY90149.1; -; mRNA.
DR RefSeq; NP_001019835.1; NM_001024664.1.
DR PDB; 7WBT; X-ray; 2.75 A; A/B=89-996.
DR PDB; 7WBU; EM; 3.42 A; A=89-996.
DR PDBsum; 7WBT; -.
DR PDBsum; 7WBU; -.
DR AlphaFoldDB; Q288C4; -.
DR SMR; Q288C4; -.
DR STRING; 9913.ENSBTAP00000006201; -.
DR PaxDb; Q288C4; -.
DR PRIDE; Q288C4; -.
DR GeneID; 520716; -.
DR KEGG; bta:520716; -.
DR CTD; 338321; -.
DR eggNOG; KOG4308; Eukaryota.
DR InParanoid; Q288C4; -.
DR OrthoDB; 114368at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0061702; C:inflammasome complex; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; 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 Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR004020; DAPIN.
DR InterPro; IPR011029; DEATH-like_dom_sf.
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 Pfam; PF13516; LRR_6; 2.
DR Pfam; PF05729; NACHT; 1.
DR Pfam; PF17776; NLRC4_HD2; 1.
DR Pfam; PF17779; NOD2_WH; 1.
DR Pfam; PF02758; PYRIN; 1.
DR SMART; SM01289; PYRIN; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50824; DAPIN; 1.
DR PROSITE; PS50837; NACHT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Immunity; Inflammasome;
KW Inflammatory response; Innate immunity; Leucine-rich repeat;
KW Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..996
FT /note="NACHT, LRR and PYD domains-containing protein 9"
FT /id="PRO_0000286333"
FT DOMAIN 1..94
FT /note="Pyrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00061"
FT DOMAIN 150..469
FT /note="NACHT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT REPEAT 748..769
FT /note="LRR 1"
FT REPEAT 777..798
FT /note="LRR 2"
FT REPEAT 805..825
FT /note="LRR 3"
FT REPEAT 834..855
FT /note="LRR 4"
FT REPEAT 862..883
FT /note="LRR 5"
FT REPEAT 891..914
FT /note="LRR 6"
FT BINDING 156..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT CONFLICT 245
FT /note="A -> T (in Ref. 1; AAY33775)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="G -> E (in Ref. 1; AAY33775)"
FT /evidence="ECO:0000305"
FT CONFLICT 631
FT /note="A -> T (in Ref. 1; AAY33775)"
FT /evidence="ECO:0000305"
FT CONFLICT 756
FT /note="E -> D (in Ref. 1; AAY33775)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 996 AA; 114162 MW; 8CBDF85F0413D7B8 CRC64;
MAESFFSDFG LLWYLEELKK EEFWKFKELL KQEPLKLKLK PIPWTELKKA SRENVSKLLS
KHYPGKLAWD VTLNLFLQIS RDDLWRKARN EIRQKINPYR SHMKQKFQVL WEKEPCLLVP
EDFYEETTKI EYELLSTVYL DAFKPGESSP TVVLHGPEGI GKTTFLRKVM LEWAKGNLWR
DRFSFVFFLT GREMNGVTDM SLVELLSRDW PESSEPIEDI FSQPERILFI LDGMEELKFD
LDCNADLCED WEQPQSMQVV LQSLLQKQML PECSLLLALS KMGMRKNYSL LKHMKCIFLL
GFSEHQRKLY FSHYFQEKDA SSRAFSFVRE KSSLFVLCQS PFLCWLVCTS LKCQLEKGED
LELDSETITG LYVSFFTKVF RSGSETCPLK QRRARLKSLC TLAAEGMWTC TFLFCPEDLR
RNGVSESDTS MWLDMKLLHR SGDCLAFIHT CIQEFCAAMF YMFTRPKDPP HSVIGNVTQL
ITRAVSGHYS RLSWTAVFLF VFSTERMTHR LETSFGFPLS KEIKQEITQS LDTLSQCDPN
NVMMSFQALF NCLFETQDPE FVAQVVNFFK DIDIYIGTKE ELIICAACLR HCHSLQKFHL
CMEHVFPDES GCISNTIEKL TLWRDVCSAF AASEDFEILN LDNCRFDEPS LAVLCRTLSQ
PVCKLRKFVC NFASNLANSL ELFKVILHNP HLKHLNFYGS SLSHMDARQL CEALKHPMCN
IEELMLGKCD ITGEACEDIA SVLVHNKKLN LLSLCENALK DDGVLVLCEA LKNPDCALEA
LLLSHCCFSS AACDHLSQVL LYNRSLTFLD LGSNVLKDEG VTTLCESLKH PSCNLQELWL
MNCYFTSVCC VDIATVLIHS EKLKTLKLGN NKIYDAGAKQ LCKALKHPKC KLENLGLEAC
ELSPASCEDL ASALTTCKSL TCVNLEWITL DYDGAAVLCE ALVSLECSLQ LLGLNKSSYD
EEIKMMLTQV EEMNPNLIIS HHLWTDDEGR RRGILV
