BIR1A_MOUSE
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 03-AUG-2022, entry version 163.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; Q9QWK5; -.
DR PeptideAtlas; Q9QWK5; -.
DR PRIDE; Q9QWK5; -.
DR ProteomicsDB; 273783; -.
DR DNASU; 17940; -.
DR Ensembl; ENSMUST00000022142; ENSMUSP00000022142; ENSMUSG00000021640.
DR Ensembl; ENSMUST00000222155; ENSMUSP00000152583; ENSMUSG00000021640.
DR GeneID; 17940; -.
DR KEGG; mmu:17940; -.
DR UCSC; uc007rqr.1; mouse.
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; 268914at2759; -.
DR PhylomeDB; Q9QWK5; -.
DR TreeFam; TF105356; -.
DR BioGRID-ORCS; 17940; 0 hits in 71 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 tissues.
DR ExpressionAtlas; Q9QWK5; baseline and differential.
DR Genevisible; Q9QWK5; MM.
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:0005524; F:ATP binding; ISS:UniProtKB.
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; -; 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; 1.
DR PROSITE; PS50143; BIR_REPEAT_2; 3.
DR PROSITE; PS50837; NACHT; 1.
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
