BIR1F_MOUSE
ID BIR1F_MOUSE Reviewed; 1403 AA.
AC Q9JIB6; O09121; O09122; P81704; Q8CH68;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Baculoviral IAP repeat-containing protein 1f;
DE AltName: Full=Neuronal apoptosis inhibitory protein 6;
GN Name=Naip6; Synonyms=Birc1f, Naip-rs4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10958627; DOI=10.1101/gr.10.8.1095;
RA Endrizzi M.G., Hadinoto V., Growney J.D., Miller W., Dietrich W.F.;
RT "Genomic sequence analysis of the mouse Naip gene array.";
RL Genome Res. 10:1095-1102(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=12526741; DOI=10.1016/s0960-9822(02)01359-3;
RA Wright E.K., Goodart S.A., Growney J.D., Hadinoto V., Endrizzi M.G.,
RA Long E.M., Sadigh K., Abney A.L., Bernstein-Hanley I., Dietrich W.F.;
RT "Naip5 affects host susceptibility to the intracellular pathogen Legionella
RT pneumophila.";
RL Curr. Biol. 13:27-36(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-168.
RC STRAIN=129/SvJ;
RX PubMed=8975718; DOI=10.1006/geno.1996.0644;
RA Scharf J.M., Damron D., Frisella A., Bruno S., Beggs A.H., Kunkel L.M.,
RA Dietrich W.F.;
RT "The mouse region syntenic for human spinal muscular atrophy lies within
RT the Lgn1 critical interval and contains multiple copies of Naip exon 5.";
RL Genomics 38:405-417(1996).
RN [5]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH S.TYPHIMURIUM FLAGELLIN.
RX PubMed=21874021; DOI=10.1038/nature10394;
RA Kofoed E.M., Vance R.E.;
RT "Innate immune recognition of bacterial ligands by NAIPs determines
RT inflammasome specificity.";
RL Nature 477:592-595(2011).
CC -!- FUNCTION: Sensor component of the NLRC4 inflammasome that specifically
CC recognizes and binds flagellin from pathogenic bacteria. Association of
CC pathogenic bacteria proteins drives in turn drive assembly and
CC activation of the NLRC4 inflammasome, promoting caspase-1 activation,
CC cytokine production and macrophage pyroptosis. The NLRC4 inflammasome
CC is activated as part of the innate immune response to a range of
CC intracellular bacteria (PubMed:21874021). The NLRC4 inflammasome senses
CC Gram-negative bacteria such as L.pneumophila and P.aeruginosa, enteric
CC pathogens S.typhimurium (Salmonella) and S.flexneri. May contribute to
CC prevent motor-neuron apoptosis induced by a variety of signals (By
CC similarity). {ECO:0000250|UniProtKB:Q13075,
CC ECO:0000269|PubMed:21874021}.
CC -!- SUBUNIT: Component of the NLRC4 inflammasome, at least composed of
CC NLRC4, caspase-1 (CASP1) and some NAIP protein.
CC {ECO:0000269|PubMed:21874021}.
CC -!- SUBUNIT: (Microbial infection) Interacts with S.typhimurium
CC (Salmonella) flagellin. {ECO:0000269|PubMed:21874021}.
CC -!- INTERACTION:
CC Q9JIB6; Q48824: flaA; Xeno; NbExp=2; IntAct=EBI-15944303, EBI-15944232;
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DR EMBL; AF242431; AAF82751.1; -; Genomic_DNA.
DR EMBL; AF367969; AAN77617.1; -; Genomic_DNA.
DR EMBL; CT009518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U66327; AAC52975.1; -; Genomic_DNA.
DR CCDS; CCDS26728.1; -.
DR RefSeq; NP_035001.2; NM_010871.2.
DR AlphaFoldDB; Q9JIB6; -.
DR SMR; Q9JIB6; -.
DR BioGRID; 201690; 1.
DR DIP; DIP-59149N; -.
DR IntAct; Q9JIB6; 4.
DR STRING; 10090.ENSMUSP00000112867; -.
DR MEROPS; I32.001; -.
DR iPTMnet; Q9JIB6; -.
DR PhosphoSitePlus; Q9JIB6; -.
DR MaxQB; Q9JIB6; -.
DR PaxDb; Q9JIB6; -.
DR PRIDE; Q9JIB6; -.
DR DNASU; 17952; -.
DR Ensembl; ENSMUST00000042220; ENSMUSP00000041766; ENSMUSG00000078942.
DR Ensembl; ENSMUST00000118574; ENSMUSP00000112867; ENSMUSG00000078942.
DR GeneID; 17952; -.
DR KEGG; mmu:17952; -.
DR UCSC; uc007rqn.1; mouse.
DR CTD; 17952; -.
DR MGI; MGI:1298222; Naip6.
DR VEuPathDB; HostDB:ENSMUSG00000078942; -.
DR eggNOG; KOG1101; Eukaryota.
DR GeneTree; ENSGT00940000163369; -.
DR HOGENOM; CLU_005648_0_0_1; -.
DR InParanoid; Q9JIB6; -.
DR OMA; ESTRESH; -.
DR OrthoDB; 268914at2759; -.
DR PhylomeDB; Q9JIB6; -.
DR TreeFam; TF105356; -.
DR BioGRID-ORCS; 17952; 2 hits in 52 CRISPR screens.
DR PRO; PR:Q9JIB6; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9JIB6; protein.
DR Bgee; ENSMUSG00000078942; Expressed in epithelium of small intestine and 72 other tissues.
DR Genevisible; Q9JIB6; MM.
DR GO; GO:0072557; C:IPAF inflammasome complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0120283; F:protein serine/threonine kinase binding; ISO:MGI.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; IDA:MGI.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0016045; P:detection of bacterium; IMP:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; ISO:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR GO; GO:0070269; P:pyroptosis; IMP:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR CDD; cd00022; BIR; 3.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001370; BIR_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR028789; Naip.
DR InterPro; IPR040535; NLRC4_HD.
DR InterPro; IPR041075; NOD2_WH.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR46914; PTHR46914; 1.
DR Pfam; PF00653; BIR; 3.
DR Pfam; PF05729; NACHT; 1.
DR Pfam; PF17889; NLRC4_HD; 1.
DR Pfam; PF17779; NOD2_WH; 1.
DR SMART; SM00238; BIR; 3.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS01282; BIR_REPEAT_1; 2.
DR PROSITE; PS50143; BIR_REPEAT_2; 3.
DR PROSITE; PS50837; NACHT; 1.
PE 1: Evidence at protein level;
KW Apoptosis; ATP-binding; Immunity; Inflammatory response; Innate immunity;
KW Metal-binding; Nucleotide-binding; Reference proteome; Repeat; Zinc.
FT CHAIN 1..1403
FT /note="Baculoviral IAP repeat-containing protein 1f"
FT /id="PRO_0000122345"
FT REPEAT 60..127
FT /note="BIR 1"
FT REPEAT 159..227
FT /note="BIR 2"
FT REPEAT 278..345
FT /note="BIR 3"
FT DOMAIN 464..759
FT /note="NACHT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 473..478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q3UP24"
FT CONFLICT 1283..1284
FT /note="AR -> GE (in Ref. 1; AAF82751)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1403 AA; 159866 MW; AEFE1450334FC2E7 CRC64;
MAEHGESSED RISEIDYEFL AELSARFGMN LVQLAKSQEE EDHKERMKMK KGFNSQMRSE
AKRLKTFESY DTFRSWTPQE MAAAGFYHTG VKLGVQCFCC SLILFGNSLR KLPIERHKKL
RPECEFLQGK DVGNIGKYDI RVKSPEKMLR GGKARYHEEE ARLESFEDWP FYAHGTSPRA
LSAAGFVFTG KRDTVQCFSC GGSLGNWEEG DDPWKEHAKW FPKCEFLQSK KSSEEIAQYI
QDYEGFVHVT GEHFVKSWVR RELPMVSAYC NDSVFTNEEL RMDMFKDWPQ ESPVGFEALV
RAGFFYTGKK DIVRCFSCGG CLEKWAEGDD PMEDHIKFFP ECVFLQTLKS SAEVIPTLQS
QYALPEATET TRESNHDDAA AVHSTVVDLG RSEAQWFQEA RSLSEQLRDT YTKTSFCHMN
LPEVCSSLGT DHLLGCDVSI ISKHVSQPVQ GALTIPEVFS NLSSVMCVEG EAGSGKTTFL
KRIAFLWASG CCPLLYRFQL VFYLSLSSIT PDQGLANIIC TQLLGAGGCI SEVCLSSSIQ
QLQHQVLFLL DDYSGLASLP QALHTLITKN YLFRTCLLIA VHTNRVRDIR PYLGTSLEIQ
EFPFYNTVFV LRKFFSHDII CVEKLIIYFS ENKDLQGVYK TPLFVAAVCN DWNQNASAQD
DFQDVTLFHS YMQYLSLKYK ATAESLQATV SSCGQLALTG LFSSCFEFNS DDLAEAGVDE
DVKLTTFLMS KFTAQRLRPV YRFLGPLFQE FLAAVRLTEL LSSDRQEDQD LGLYYLRQID
SPLKAINSFN IFLYYVSSHS SSKAAPTVVS HLLQLVDEKE SLENMSENED YMKLHPQTFL
WFQFVRGLWL VSPESFSSFV SEHLLRLALI FAYESNTVAE CSPFILQFLR GRTLALRVLN
LEYFWDHPES LLLLRSLKVS INGNKMSSYV DYSFKTYFEN LQPPAINEEY TSAFEHVSEW
RRNFAQDEEI IKNYENIWPR ALPDISEGYW NLSPKPCKIP KLEVQVNNMG PADQALLQVL
MEVFSASQSI EFHLFNSSGF LESIRPALEL SKASVTKCSM SRLELSRAEQ ELLLTLPALQ
SLEVSETNQL PDQLFHNLHK FLGLKELCVR LDGKPDVLSV LPEEFLNLHH MEKLSIRTST
ESDLSKLVKF IQNFPNLHVF HLKCDFLSNC ESLMTALASC KKLREIEFSG QCFEAMTFVN
ILPNFVSLKI LSLKGQQFAD KETSEKFAQA LGSLRNLEEL LVPTGDGIHQ VAKLIVRQCL
QLPCLRVLAF HDILDDESVI EIARAATSGS FQKLENLDIS MNHKITEEGY RNFFQALDNL
PNLQMLNICR NIPGRIQVQA TTVKALGHCV SRLPSLTRLG MLSWLLDEED MKVINDVKER
HPQSKRLTIF WKWIVPFSPV VLE