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BCL2/adenovirus E1B 19 kDa protein-interacting protein 3

 BNIP3_MOUSE             Reviewed;         187 AA.
O55003; Q544Y4;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
07-JUN-2017, entry version 139.
RecName: Full=BCL2/adenovirus E1B 19 kDa protein-interacting protein 3;
Name=Bnip3; Synonyms=Nip3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9867803; DOI=10.1074/jbc.274.1.7;
Chen G., Cizeau J., Vande Velde C., Park J.H., Bozek G., Bolton J.,
Shi L., Dubik D., Greenberg A.;
"Nix and Nip3 form a subfamily of pro-apoptotic mitochondrial
proteins.";
J. Biol. Chem. 274:7-10(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone marrow;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Olfactory epithelium;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
"Mitochondrial phosphoproteome revealed by an improved IMAC method and
MS/MS/MS.";
Mol. Cell. Proteomics 6:669-676(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-85 AND SER-88,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion
affinity chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-79; SER-85 AND
SER-88, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Apoptosis-inducing protein that can overcome BCL2
suppression. May play a role in repartitioning calcium between the
two major intracellular calcium stores in association with BCL2
(By similarity). Involved in mitochondrial quality control via its
interaction with SPATA18/MIEAP: in response to mitochondrial
damage, participates in mitochondrial protein catabolic process
(also named MALM) leading to the degradation of damaged proteins
inside mitochondria. The physical interaction of SPATA18/MIEAP,
BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane may play
a critical role in the translocation of lysosomal proteins from
the cytoplasm to the mitochondrial matrix (By similarity). The
physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the
mitochondrial outer membrane regulates the opening of a pore in
the mitochondrial double membrane in order to mediate the
translocation of lysosomal proteins from the cytoplasm to the
mitochondrial matrix (By similarity). Plays an important role in
the calprotectin (S100A8/A9)-induced cell death pathway (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer. Binds to BCL2. Interacts with BNIP3L and
ACAA2. Interacts (via BH3 domain) with SPATA18 (via coiled-coil
domains). Interacts with BOK; promotes BOK oligomerization.
{ECO:0000250|UniProtKB:Q12983}.
-!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion outer membrane
{ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Note=Coexpression with the EIB 19-kDa protein results in a shift
in NIP3 localization pattern to the nuclear envelope. Colocalizes
with ACAA2 in the mitochondria. Colocalizes with SPATA18 at the
mitochondrion outer membrane (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the NIP3 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF041054; AAD02922.1; -; mRNA.
EMBL; AK014223; BAB29214.1; -; mRNA.
EMBL; AK075943; BAC36072.1; -; mRNA.
EMBL; AK152610; BAE31356.1; -; mRNA.
EMBL; BC046603; AAH46603.1; -; mRNA.
CCDS; CCDS40168.1; -.
RefSeq; NP_033890.1; NM_009760.4.
UniGene; Mm.378890; -.
ProteinModelPortal; O55003; -.
SMR; O55003; -.
BioGrid; 198377; 2.
STRING; 10090.ENSMUSP00000101718; -.
iPTMnet; O55003; -.
PhosphoSitePlus; O55003; -.
MaxQB; O55003; -.
PaxDb; O55003; -.
PeptideAtlas; O55003; -.
PRIDE; O55003; -.
Ensembl; ENSMUST00000106112; ENSMUSP00000101718; ENSMUSG00000078566.
GeneID; 12176; -.
KEGG; mmu:12176; -.
UCSC; uc009kfg.1; mouse.
CTD; 664; -.
MGI; MGI:109326; Bnip3.
eggNOG; ENOG410IHYW; Eukaryota.
eggNOG; ENOG4111KXP; LUCA.
GeneTree; ENSGT00390000013415; -.
HOGENOM; HOG000232139; -.
HOVERGEN; HBG050707; -.
InParanoid; O55003; -.
KO; K15464; -.
OMA; MKKNADW; -.
OrthoDB; EOG091G0REJ; -.
PhylomeDB; O55003; -.
TreeFam; TF315424; -.
PRO; PR:O55003; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000078566; -.
CleanEx; MM_BNIP3; -.
ExpressionAtlas; O55003; baseline and differential.
Genevisible; O55003; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISS:UniProtKB.
GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IDA:MGI.
GO; GO:0051020; F:GTPase binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
GO; GO:0006915; P:apoptotic process; ISO:MGI.
GO; GO:0048102; P:autophagic cell death; IEA:Ensembl.
GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
GO; GO:0010659; P:cardiac muscle cell apoptotic process; IEA:Ensembl.
GO; GO:0008219; P:cell death; ISS:UniProtKB.
GO; GO:0071279; P:cellular response to cobalt ion; ISO:MGI.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
GO; GO:0008626; P:granzyme-mediated apoptotic signaling pathway; ISO:MGI.
GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IMP:MGI.
GO; GO:1990144; P:intrinsic apoptotic signaling pathway in response to hypoxia; ISO:MGI.
GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; ISO:MGI.
GO; GO:0097345; P:mitochondrial outer membrane permeabilization; ISS:UniProtKB.
GO; GO:0035694; P:mitochondrial protein catabolic process; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IGI:ParkinsonsUK-UCL.
GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
GO; GO:0045837; P:negative regulation of membrane potential; ISS:UniProtKB.
GO; GO:0010637; P:negative regulation of mitochondrial fusion; ISO:MGI.
GO; GO:1902109; P:negative regulation of mitochondrial membrane permeability involved in apoptotic process; IEA:Ensembl.
GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; IEA:Ensembl.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IGI:ParkinsonsUK-UCL.
GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB.
GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
GO; GO:0016239; P:positive regulation of macroautophagy; ISO:MGI.
GO; GO:0051561; P:positive regulation of mitochondrial calcium ion concentration; IEA:Ensembl.
GO; GO:0090141; P:positive regulation of mitochondrial fission; ISO:MGI.
GO; GO:1903599; P:positive regulation of mitophagy; IEA:Ensembl.
GO; GO:0010940; P:positive regulation of necrotic cell death; IEA:Ensembl.
GO; GO:0043068; P:positive regulation of programmed cell death; ISO:MGI.
GO; GO:0043243; P:positive regulation of protein complex disassembly; ISO:MGI.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:MGI.
GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
GO; GO:1903715; P:regulation of aerobic respiration; IMP:ParkinsonsUK-UCL.
GO; GO:0046902; P:regulation of mitochondrial membrane permeability; ISS:UniProtKB.
GO; GO:0010821; P:regulation of mitochondrion organization; IMP:ParkinsonsUK-UCL.
GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
GO; GO:1901998; P:toxin transport; IMP:MGI.
InterPro; IPR010548; BNIP3.
PANTHER; PTHR15186; PTHR15186; 1.
Pfam; PF06553; BNIP3; 1.
1: Evidence at protein level;
Apoptosis; Complete proteome; Membrane; Mitochondrion;
Mitochondrion outer membrane; Phosphoprotein; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 187 BCL2/adenovirus E1B 19 kDa protein-
interacting protein 3.
/FTId=PRO_0000064965.
TRANSMEM 157 177 Helical. {ECO:0000255}.
MOTIF 93 118 BH3.
MOD_RES 48 48 Phosphoserine.
{ECO:0000250|UniProtKB:Q12983}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000250|UniProtKB:Q12983}.
MOD_RES 77 77 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 79 79 Phosphoserine.
{ECO:0000244|PubMed:17208939,
ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 85 85 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 88 88 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:18630941,
ECO:0000244|PubMed:21183079}.
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


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