BNIP3_MOUSE
ID BNIP3_MOUSE Reviewed; 187 AA.
AC O55003; Q544Y4;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=BCL2/adenovirus E1B 19 kDa protein-interacting protein 3 {ECO:0000305};
GN Name=Bnip3 {ECO:0000312|MGI:MGI:109326}; Synonyms=Nip3;
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=9867803; DOI=10.1074/jbc.274.1.7;
RA Chen G., Cizeau J., Vande Velde C., Park J.H., Bozek G., Bolton J., Shi L.,
RA Dubik D., Greenberg A.;
RT "Nix and Nip3 form a subfamily of pro-apoptotic mitochondrial proteins.";
RL J. Biol. Chem. 274:7-10(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-85 AND SER-88, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-79; SER-85 AND
RP SER-88, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Apoptosis-inducing protein that can overcome BCL2
CC suppression. May play a role in repartitioning calcium between the two
CC major intracellular calcium stores in association with BCL2 (By
CC similarity). Involved in mitochondrial quality control via its
CC interaction with SPATA18/MIEAP: in response to mitochondrial damage,
CC participates in mitochondrial protein catabolic process (also named
CC MALM) leading to the degradation of damaged proteins inside
CC mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and
CC BNIP3L/NIX at the mitochondrial outer membrane may play a critical role
CC in the translocation of lysosomal proteins from the cytoplasm to the
CC mitochondrial matrix (By similarity). The physical interaction of
CC SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane
CC regulates the opening of a pore in the mitochondrial double membrane in
CC order to mediate the translocation of lysosomal proteins from the
CC cytoplasm to the mitochondrial matrix (By similarity). Plays an
CC important role in the calprotectin (S100A8/A9)-induced cell death
CC pathway (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Binds to BCL2. Interacts with BNIP3L and ACAA2.
CC Interacts (via BH3 domain) with SPATA18 (via coiled-coil domains).
CC Interacts with BOK; promotes BOK oligomerization.
CC {ECO:0000250|UniProtKB:Q12983}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion outer membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC Note=Coexpression with the EIB 19-kDa protein results in a shift in
CC NIP3 localization pattern to the nuclear envelope. Colocalizes with
CC ACAA2 in the mitochondria. Colocalizes with SPATA18 at the
CC mitochondrion outer membrane (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NIP3 family. {ECO:0000305}.
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DR EMBL; AF041054; AAD02922.1; -; mRNA.
DR EMBL; AK014223; BAB29214.1; -; mRNA.
DR EMBL; AK075943; BAC36072.1; -; mRNA.
DR EMBL; AK152610; BAE31356.1; -; mRNA.
DR EMBL; BC046603; AAH46603.1; -; mRNA.
DR CCDS; CCDS40168.1; -.
DR RefSeq; NP_033890.1; NM_009760.4.
DR AlphaFoldDB; O55003; -.
DR BMRB; O55003; -.
DR BioGRID; 198377; 3.
DR STRING; 10090.ENSMUSP00000101718; -.
DR iPTMnet; O55003; -.
DR PhosphoSitePlus; O55003; -.
DR EPD; O55003; -.
DR jPOST; O55003; -.
DR MaxQB; O55003; -.
DR PaxDb; O55003; -.
DR PeptideAtlas; O55003; -.
DR PRIDE; O55003; -.
DR ProteomicsDB; 273752; -.
DR Antibodypedia; 31; 602 antibodies from 36 providers.
DR DNASU; 12176; -.
DR Ensembl; ENSMUST00000106112; ENSMUSP00000101718; ENSMUSG00000078566.
DR GeneID; 12176; -.
DR KEGG; mmu:12176; -.
DR UCSC; uc009kfg.1; mouse.
DR CTD; 664; -.
DR MGI; MGI:109326; Bnip3.
DR VEuPathDB; HostDB:ENSMUSG00000078566; -.
DR eggNOG; ENOG502QQ4B; Eukaryota.
DR GeneTree; ENSGT00390000013415; -.
DR HOGENOM; CLU_091463_1_0_1; -.
DR InParanoid; O55003; -.
DR OMA; KDWKFKH; -.
DR OrthoDB; 1250566at2759; -.
DR PhylomeDB; O55003; -.
DR TreeFam; TF315424; -.
DR BioGRID-ORCS; 12176; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Bnip3; mouse.
DR PRO; PR:O55003; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O55003; protein.
DR Bgee; ENSMUSG00000078566; Expressed in hindlimb stylopod muscle and 152 other tissues.
DR ExpressionAtlas; O55003; baseline and differential.
DR Genevisible; O55003; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0051020; F:GTPase binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0048102; P:autophagic cell death; ISO:MGI.
DR GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
DR GO; GO:0010659; P:cardiac muscle cell apoptotic process; ISO:MGI.
DR GO; GO:0008219; P:cell death; ISS:UniProtKB.
DR GO; GO:0071279; P:cellular response to cobalt ion; ISO:MGI.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0140507; P:granzyme-mediated programmed cell death signaling pathway; ISO:MGI.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:1990144; P:intrinsic apoptotic signaling pathway in response to hypoxia; ISO:MGI.
DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; ISO:MGI.
DR GO; GO:0097345; P:mitochondrial outer membrane permeabilization; ISS:UniProtKB.
DR GO; GO:0035694; P:mitochondrial protein catabolic process; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IGI:ParkinsonsUK-UCL.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0045837; P:negative regulation of membrane potential; ISS:UniProtKB.
DR GO; GO:0010637; P:negative regulation of mitochondrial fusion; ISO:MGI.
DR GO; GO:1902109; P:negative regulation of mitochondrial membrane permeability involved in apoptotic process; ISO:MGI.
DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; ISO:MGI.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IGI:ParkinsonsUK-UCL.
DR GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:1903599; P:positive regulation of autophagy of mitochondrion; ISO:MGI.
DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; ISO:MGI.
DR GO; GO:0016239; P:positive regulation of macroautophagy; ISO:MGI.
DR GO; GO:0051561; P:positive regulation of mitochondrial calcium ion concentration; ISO:MGI.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; ISO:MGI.
DR GO; GO:0010940; P:positive regulation of necrotic cell death; ISO:MGI.
DR GO; GO:0043068; P:positive regulation of programmed cell death; ISO:MGI.
DR GO; GO:0043243; P:positive regulation of protein-containing complex disassembly; ISO:MGI.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:MGI.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
DR GO; GO:1903715; P:regulation of aerobic respiration; IMP:ParkinsonsUK-UCL.
DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; ISS:UniProtKB.
DR GO; GO:0010821; P:regulation of mitochondrion organization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0043067; P:regulation of programmed cell death; IBA:GO_Central.
DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0090649; P:response to oxygen-glucose deprivation; IEA:Ensembl.
DR GO; GO:1901998; P:toxin transport; IMP:MGI.
DR InterPro; IPR010548; BNIP3.
DR PANTHER; PTHR15186; PTHR15186; 1.
DR Pfam; PF06553; BNIP3; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..187
FT /note="BCL2/adenovirus E1B 19 kDa protein-interacting
FT protein 3"
FT /id="PRO_0000064965"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 42..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 93..118
FT /note="BH3"
FT COMPBIAS 54..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12983"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12983"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
SQ SEQUENCE 187 AA; 20978 MW; 901BCFACF43EE989 CRC64;
MSQSGEENLQ GSWVELHFSN GNGSSVPASV SIYNGDMEKI LLDAQHESGR SSSKSSHCDS
PPRSQTPQDT NRAEIDSHSF GEKNSTLSEE DYIERRREVE SILKKNSDWI WDWSSRPENI
PPKEFLFKHP KRTATLSMRN TSVMKKGGIF SADFLKVFLP SLLLSHLLAI GLGIYIGRRL
TTSTSTF
