ID   BIR1A_MOUSE             Reviewed;        1403 AA.
AC   Q9QWK5; A2RT89; Q9JIB5; Q9R017;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   24-JAN-2024, entry version 170.
DE   RecName: Full=Baculoviral IAP repeat-containing protein 1a;
DE   AltName: Full=Neuronal apoptosis inhibitory protein 1;
GN   Name=Naip1; Synonyms=Birc1a, Naip;
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 [MRNA].
RX   PubMed=9693038; DOI=10.1006/geno.1998.5378;
RA   Yaraghi Z., Korneluk R.G., MacKenzie A.E.;
RT   "Cloning and characterization of the multiple murine homologues of NAIP
RT   (neuronal apoptosis inhibitory protein).";
RL   Genomics 51:107-113(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10501978; DOI=10.1007/s003359901155;
RA   Huang S., Scharf J.M., Growney J.D., Endrizzi M.G., Dietrich W.F.;
RT   "The mouse Naip gene cluster on chromosome 13 encodes several distinct
RT   functional transcripts.";
RL   Mamm. Genome 10:1032-1035(1999).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Anti-apoptotic protein which acts by inhibiting the
CC       activities of CASP3, CASP7 and CASP9. Can inhibit the autocleavage of
CC       pro-CASP9 and cleavage of pro-CASP3 by CASP9. Capable of inhibiting
CC       CASP9 autoproteolysis at 'Asp-315' and decreasing the rate of auto
CC       proteolysis at 'Asp-330'. Acts as a mediator of neuronal survival in
CC       pathological conditions. Prevents motor-neuron apoptosis induced by a
CC       variety of signals (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via NACHT domain) with APAF1 (via CARD and NACHT
CC       domains). {ECO:0000250}.
CC   -!- DOMAIN: Both the BIR and NACHT domains are essential for effective
CC       inhibition of pro-CASP9 cleavage. BIR3 domain binds to procaspase-9 and
CC       the NACHT domain interacts with the NACHT domain of APAF1 forming a
CC       bridge between pro-CASP9 and APAF1 (By similarity). {ECO:0000250}.
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DR   EMBL; AF007769; AAB69223.1; -; mRNA.
DR   EMBL; AF135491; AAD56763.1; -; mRNA.
DR   EMBL; AF242432; AAF82752.1; -; Genomic_DNA.
DR   EMBL; BC132413; AAI32414.1; -; mRNA.
DR   CCDS; CCDS26729.1; -.
DR   RefSeq; NP_032696.2; NM_008670.2.
DR   AlphaFoldDB; Q9QWK5; -.
DR   SMR; Q9QWK5; -.
DR   BioGRID; 201684; 1.
DR   STRING; 10090.ENSMUSP00000022142; -.
DR   MEROPS; I32.001; -.
DR   iPTMnet; Q9QWK5; -.
DR   PhosphoSitePlus; Q9QWK5; -.
DR   MaxQB; Q9QWK5; -.
DR   PaxDb; 10090-ENSMUSP00000022142; -.
DR   PeptideAtlas; Q9QWK5; -.
DR   ProteomicsDB; 273783; -.
DR   DNASU; 17940; -.
DR   Ensembl; ENSMUST00000022142.7; ENSMUSP00000022142.6; ENSMUSG00000021640.7.
DR   Ensembl; ENSMUST00000222155.2; ENSMUSP00000152583.2; ENSMUSG00000021640.7.
DR   GeneID; 17940; -.
DR   KEGG; mmu:17940; -.
DR   UCSC; uc007rqr.1; mouse.
DR   AGR; MGI:1298223; -.
DR   CTD; 17940; -.
DR   MGI; MGI:1298223; Naip1.
DR   VEuPathDB; HostDB:ENSMUSG00000021640; -.
DR   eggNOG; KOG1101; Eukaryota.
DR   GeneTree; ENSGT00940000163369; -.
DR   HOGENOM; CLU_005648_0_0_1; -.
DR   InParanoid; Q9QWK5; -.
DR   OrthoDB; 5404838at2759; -.
DR   PhylomeDB; Q9QWK5; -.
DR   TreeFam; TF105356; -.
DR   BioGRID-ORCS; 17940; 0 hits in 76 CRISPR screens.
DR   ChiTaRS; Naip1; mouse.
DR   PRO; PR:Q9QWK5; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q9QWK5; Protein.
DR   Bgee; ENSMUSG00000021640; Expressed in left colon and 67 other cell types or tissues.
DR   ExpressionAtlas; Q9QWK5; baseline and differential.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0072557; C:IPAF inflammasome complex; IBA:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0043204; C:perikaryon; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IMP:UniProtKB.
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:0006915; P:apoptotic process; IMP:MGI.
DR   GO; GO:0071391; P:cellular response to estrogen stimulus; IMP:MGI.
DR   GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR   GO; GO:0016045; P:detection of bacterium; IBA:GO_Central.
DR   GO; GO:1904019; P:epithelial cell apoptotic process; IMP:MGI.
DR   GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR   GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR   GO; GO:1904036; P:negative regulation of epithelial cell apoptotic process; IMP: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; IBA:GO_Central.
DR   GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR   CDD; cd00022; BIR; 3.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 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; BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR46914:SF1; BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 1; 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; SSF57924; Inhibitor of apoptosis (IAP) repeat; 3.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   PROSITE; PS01282; BIR_REPEAT_1; 1.
DR   PROSITE; PS50143; BIR_REPEAT_2; 3.
DR   PROSITE; PS50837; NACHT; 1.
DR   Genevisible; Q9QWK5; MM.
PE   2: Evidence at transcript level;
KW   Apoptosis; ATP-binding; Metal-binding; Nucleotide-binding;
KW   Protease inhibitor; Reference proteome; Repeat; Thiol protease inhibitor;
KW   Zinc.
FT   CHAIN           1..1403
FT                   /note="Baculoviral IAP repeat-containing protein 1a"
FT                   /id="PRO_0000122342"
FT   REPEAT          63..128
FT                   /note="BIR 1"
FT   REPEAT          162..228
FT                   /note="BIR 2"
FT   REPEAT          281..346
FT                   /note="BIR 3"
FT   DOMAIN          464..758
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         476
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        343
FT                   /note="V -> I (in Ref. 1; AAB69223 and 3; AAF82752)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        359
FT                   /note="Q -> L (in Ref. 1; AAB69223 and 3; AAF82752)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        624
FT                   /note="E -> K (in Ref. 2; AAD56763)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1092
FT                   /note="D -> E (in Ref. 3; AAF82752)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1116
FT                   /note="D -> N (in Ref. 3; AAF82752)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1123
FT                   /note="G -> R (in Ref. 3; AAF82752)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1129
FT                   /note="L -> H (in Ref. 1; AAB69223)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1140
FT                   /note="M -> T (in Ref. 1; AAB69223 and 3; AAF82752)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1269
FT                   /note="A -> V (in Ref. 3; AAF82752)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1403 AA;  158724 MW;  933E23BB1F1DA3E9 CRC64;
     MAEHGESSED RISEIDYEFL PELSALLGVD AVQLAKSQEE EEHKERMKMK KGFNSQMRSE
     AKRLKTFETY DTFRSWTPQE MAAAGFYHTG VKLGVQCFCC SLILFGNSLR KLPIERHKKL
     RPECEFLQGK DVGNIGKYDI RVKSPEKMLR GGKARYHEEE ARLESFEDWP FYAHGTSPRV
     LSAAGFVFTG KRDTVQCFSC GGSLGNWEEG DDPWKEHAKW FPKCEFLQSK KSSEEIAQYI
     QGYEGFVHVT GEHFVNSWVR RELPMVSAYC NDSVFANEEL RMDTFKDWPH ESPVAVDALV
     RAGLFYTGKK GIVQCFSCGG CMEKCTEGDD PIQEHNKFFP NCVFLQTPKS SAEVIPALQS
     HCALPEAMET TSESNHDDPA AVHSTVVGLG RSEAQWFQEA RSLSEQLRDN YTKATFRHMN
     LPEVCSSLGT DHLIGCDVSI ISKHISQPVQ GALTIPEVFS NLSSVMCVEG ETGSGKTTFL
     KRIAFLWASG CCPLLYRFQL VFYLSLSSIT PDQGLANIIC AQLLGAGGCI SEVCLSSIIQ
     QLQHQVLFLL DDYSGLASLP QALHTLITKN YLSRTCLLIA VHTNRVRGIR SYLDTSLEIK
     EFPLSNTVYI LKKFFSHNIK RLLEFMVYFG QNEDLQGIHK TPLFVAAVCT DWFENPSDQP
     FQDMALFKSY MQYLSLKHKG AAKPLQATVS SCGQLALTGL FSSCFEFNSD DLAEAGVDED
     EELTTCLMSK FTAQRLRPVY RFLGPLFQEF LAAMRLTELL SSDRQEDQDL GLYYLRQINS
     PLKALTTYNN FLKYVFSHPS SKAGPTVVSH LLHLVDETEL LENTYKNEDY VNHPPGTSRI
     MKGLKELWLL SPEYYSSFVS EHLLRIALNF AYESNTVAEC SPFILQFLRG RTLALKVLNL
     QYFRDHPESL LLVKSLEVSI NGNKVPKVVD YSVMEKSFET LQPPTIDQDY ASAFEQMKEH
     EKNLSENEET IKSIKNIFPL QPPKISSGYW KLSPKPCKIP RLEVGVTNMG PADQALLQVL
     MEVFSASQSI EFRLSDSSGF LESIRPALEL SKASVTKCSM SRLELSRAEQ ELLLTLPALQ
     SLEVSETNQL PDQLFHNLHK FLGLKELCVR LDGKPDVLSV LPGEFPNLLH MEKLSIRTSM
     ESDLSKLVKL IQNSPNLHVF HLKCDFLSNC DSLMAVLASC KKLREIEFSG RCFEAMPFVN
     ILPNFISLKI LNLISQQFPD KETSEKFAQA LGSLRNLEEL LVPTGDGIHQ VAKLIVRQCL
     QLPCLRVLAF HYILDNDSVI EIARVATSGG FQKLEKLDLS MNHKITEEGY RNFFQALDNL
     PNLQNLNICR HIPECIQVQA TTVKALGQCV SRLPSLTRLH MLSWLLDEED MKVINDVKER
     HPQSKRLIIF WKWIVPFSPV VLE
//