BNI3L_MOUSE
ID BNI3L_MOUSE Reviewed; 218 AA.
AC Q9Z2F7; Q545J6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like;
DE AltName: Full=NIP3-like protein X;
DE Short=NIP3L;
GN Name=Bnip3l; Synonyms=Nix;
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].
RC TISSUE=Embryo;
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, and NOD;
RC TISSUE=Cecum, Egg, Hippocampus, Lung, and Pancreas;
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=Eye;
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-61 AND SER-116, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-117 AND SER-119, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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: Induces apoptosis. Interacts with viral and cellular anti-
CC apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL,
CC although high levels of BCL-XL expression will inhibit apoptosis.
CC Inhibits apoptosis induced by BNIP3. Involved in mitochondrial quality
CC control via its interaction with SPATA18/MIEAP: in response to
CC mitochondrial damage, participates in mitochondrial protein catabolic
CC process (also named MALM) leading to the degradation of damaged
CC proteins inside mitochondria. 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). May function as
CC a tumor suppressor (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Self-associates. Interacts with BNIP3 and STEAP3. Interacts
CC (via BH3 domain) with SPATA18 (via coiled-coil domains) (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9Z2F7; Q69ZI1: Sh3rf1; NbExp=4; IntAct=EBI-1774669, EBI-957380;
CC Q9Z2F7; O95166: GABARAP; Xeno; NbExp=2; IntAct=EBI-1774669, EBI-712001;
CC Q9Z2F7; Q9H0R8: GABARAPL1; Xeno; NbExp=4; IntAct=EBI-1774669, EBI-746969;
CC Q9Z2F7; P60520: GABARAPL2; Xeno; NbExp=2; IntAct=EBI-1774669, EBI-720116;
CC Q9Z2F7; Q9H492: MAP1LC3A; Xeno; NbExp=7; IntAct=EBI-1774669, EBI-720768;
CC Q9Z2F7; Q9GZQ8: MAP1LC3B; Xeno; NbExp=5; IntAct=EBI-1774669, EBI-373144;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000250}. Endoplasmic
CC reticulum {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}.
CC Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC Note=Colocalizes with SPATA18 at the mitochondrion outer membrane.
CC {ECO:0000250}.
CC -!- PTM: Undergoes progressive proteolysis to an 11 kDa C-terminal
CC fragment, which is blocked by the proteasome inhibitor lactacystin.
CC -!- SIMILARITY: Belongs to the NIP3 family. {ECO:0000305}.
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DR EMBL; AF067395; AAD03588.1; -; mRNA.
DR EMBL; AK004667; BAB23456.1; -; mRNA.
DR EMBL; AK007920; BAB25351.1; -; mRNA.
DR EMBL; AK013467; BAB28869.1; -; mRNA.
DR EMBL; AK018668; BAB31334.1; -; mRNA.
DR EMBL; AK139950; BAE24194.1; -; mRNA.
DR EMBL; AK155040; BAE33007.1; -; mRNA.
DR EMBL; BC085237; AAH85237.1; -; mRNA.
DR CCDS; CCDS27227.1; -.
DR RefSeq; NP_033891.1; NM_009761.3.
DR AlphaFoldDB; Q9Z2F7; -.
DR SMR; Q9Z2F7; -.
DR BioGRID; 198378; 4.
DR IntAct; Q9Z2F7; 7.
DR MINT; Q9Z2F7; -.
DR STRING; 10090.ENSMUSP00000022634; -.
DR iPTMnet; Q9Z2F7; -.
DR PhosphoSitePlus; Q9Z2F7; -.
DR EPD; Q9Z2F7; -.
DR jPOST; Q9Z2F7; -.
DR MaxQB; Q9Z2F7; -.
DR PaxDb; Q9Z2F7; -.
DR PRIDE; Q9Z2F7; -.
DR ProteomicsDB; 273751; -.
DR Antibodypedia; 2292; 472 antibodies from 43 providers.
DR DNASU; 12177; -.
DR Ensembl; ENSMUST00000022634; ENSMUSP00000022634; ENSMUSG00000022051.
DR GeneID; 12177; -.
DR KEGG; mmu:12177; -.
DR UCSC; uc007uks.2; mouse.
DR CTD; 665; -.
DR MGI; MGI:1332659; Bnip3l.
DR VEuPathDB; HostDB:ENSMUSG00000022051; -.
DR eggNOG; ENOG502R8Q5; Eukaryota.
DR GeneTree; ENSGT00390000013415; -.
DR HOGENOM; CLU_091463_1_1_1; -.
DR InParanoid; Q9Z2F7; -.
DR OMA; LEMNRTH; -.
DR OrthoDB; 1250566at2759; -.
DR PhylomeDB; Q9Z2F7; -.
DR TreeFam; TF315424; -.
DR Reactome; R-MMU-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
DR BioGRID-ORCS; 12177; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Bnip3l; mouse.
DR PRO; PR:Q9Z2F7; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9Z2F7; protein.
DR Bgee; ENSMUSG00000022051; Expressed in blood and 283 other tissues.
DR ExpressionAtlas; Q9Z2F7; baseline and differential.
DR Genevisible; Q9Z2F7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0005521; F:lamin binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0097345; P:mitochondrial outer membrane permeabilization; IBA:GO_Central.
DR GO; GO:0035694; P:mitochondrial protein catabolic process; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
DR GO; GO:0016239; P:positive regulation of macroautophagy; ISO:MGI.
DR GO; GO:0035794; P:positive regulation of mitochondrial membrane permeability; ISO:MGI.
DR GO; GO:1903146; P:regulation of autophagy of mitochondrion; IGI:ParkinsonsUK-UCL.
DR GO; GO:0043067; P:regulation of programmed cell death; IBA:GO_Central.
DR GO; GO:1903214; P:regulation of protein targeting to mitochondrion; IGI:ParkinsonsUK-UCL.
DR InterPro; IPR010548; BNIP3.
DR PANTHER; PTHR15186; PTHR15186; 1.
DR Pfam; PF06553; BNIP3; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Endoplasmic reticulum; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..218
FT /note="BCL2/adenovirus E1B 19 kDa protein-interacting
FT protein 3-like"
FT /id="PRO_0000064958"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 125..147
FT /note="BH3"
FT COMPBIAS 35..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60238"
SQ SEQUENCE 218 AA; 23766 MW; EAA839DEFDDE50D7 CRC64;
MSHLVEPPPP LHNNNNNCEE GEQPLPPPAG LNSSWVELPM NSSNGNENGN GKNGGLEHVP
SSSSIHNGDM EKILLDAQHE SGQSSSRGSS HCDSPSPQED GQIMFDVEMH TSRDHSSQSE
EEVVEGEKEV EALKKSADWV SDWSSRPENI PPKEFHFRHP KRAASLSMRK SGAMKKGGIF
SAEFLKVFIP SLFLSHVLAL GLGIYIGKRL STPSASTY
