BMF_MOUSE
ID BMF_MOUSE Reviewed; 185 AA.
AC Q91ZE9; Q8BUK0;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Bcl-2-modifying factor;
GN Name=Bmf;
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], INTERACTION WITH MCL1; BCL2; BCL2L1; BCL2L2 AND
RP DLC2, AND MUTAGENESIS OF ASP-67; LYS-68 AND ALA-69.
RC STRAIN=C57BL/6J;
RX PubMed=11546872; DOI=10.1126/science.1062257;
RA Puthalakath H., Villunger A., O'Reilly L.A., Beaumont J.G., Coultas L.,
RA Cheney R.E., Huang D.C.S., Strasser A.;
RT "Bmf: a proapoptotic BH3-only protein regulated by interaction with the
RT myosin V actin motor complex, activated by anoikis.";
RL Science 293:1829-1832(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, and Thymus;
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 STRAIN=C57BL/6J; 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).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=14574334; DOI=10.1038/sj.leu.2403183;
RA Morales A.A., Olsson A., Celsing F., Oesterborg A., Jondal M., Osorio L.M.;
RT "Expression and transcriptional regulation of functionally distinct Bmf
RT isoforms in B-chronic lymphocytic leukemia cells.";
RL Leukemia 18:41-47(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 126-152 IN COMPLEX WITH BCL2A1.
RX PubMed=18462686; DOI=10.1016/j.str.2008.02.009;
RA Smits C., Czabotar P.E., Hinds M.G., Day C.L.;
RT "Structural plasticity underpins promiscuous binding of the prosurvival
RT protein A1.";
RL Structure 16:818-829(2008).
CC -!- FUNCTION: May play a role in apoptosis.
CC -!- SUBUNIT: Interacts with MCL1, BCL2, BCL2L1/BCL-Xl, BCL2A1 and
CC BCL2L2/BCL-w. Interacts with the myosin V actin motor complex through
CC its binding to DLC2. {ECO:0000269|PubMed:11546872,
CC ECO:0000269|PubMed:18462686}.
CC -!- INTERACTION:
CC Q91ZE9; Q07440: Bcl2a1; NbExp=2; IntAct=EBI-708032, EBI-707754;
CC Q91ZE9; P10415: BCL2; Xeno; NbExp=2; IntAct=EBI-708032, EBI-77694;
CC Q91ZE9; Q92843: BCL2L2; Xeno; NbExp=2; IntAct=EBI-708032, EBI-707714;
CC -!- TISSUE SPECIFICITY: Widely expressed with an abundant expression in
CC pancreas, liver kidney and hematopoietic tissues.
CC {ECO:0000269|PubMed:14574334}.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39243.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY029253; AAK38747.1; -; mRNA.
DR EMBL; AK084658; BAC39243.1; ALT_INIT; mRNA.
DR EMBL; AK040622; BAC30649.1; -; mRNA.
DR EMBL; BC079650; AAH79650.1; -; mRNA.
DR CCDS; CCDS89538.1; -.
DR RefSeq; NP_001318150.1; NM_001331221.1.
DR RefSeq; NP_612186.2; NM_138313.4.
DR RefSeq; XP_006498918.1; XM_006498855.2.
DR PDB; 2VOG; X-ray; 1.90 A; B=126-152.
DR PDBsum; 2VOG; -.
DR AlphaFoldDB; Q91ZE9; -.
DR SMR; Q91ZE9; -.
DR DIP; DIP-29806N; -.
DR ELM; Q91ZE9; -.
DR IntAct; Q91ZE9; 7.
DR MINT; Q91ZE9; -.
DR STRING; 10090.ENSMUSP00000087686; -.
DR iPTMnet; Q91ZE9; -.
DR PhosphoSitePlus; Q91ZE9; -.
DR PaxDb; Q91ZE9; -.
DR PRIDE; Q91ZE9; -.
DR ProteomicsDB; 273746; -.
DR Antibodypedia; 1506; 477 antibodies from 39 providers.
DR DNASU; 171543; -.
DR Ensembl; ENSMUST00000125860; ENSMUSP00000159051; ENSMUSG00000040093.
DR GeneID; 171543; -.
DR KEGG; mmu:171543; -.
DR UCSC; uc008lsb.1; mouse.
DR CTD; 90427; -.
DR MGI; MGI:2176433; Bmf.
DR VEuPathDB; HostDB:ENSMUSG00000040093; -.
DR eggNOG; ENOG502S0P3; Eukaryota.
DR GeneTree; ENSGT00390000017896; -.
DR InParanoid; Q91ZE9; -.
DR OrthoDB; 1454053at2759; -.
DR Reactome; R-MMU-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
DR Reactome; R-MMU-139910; Activation of BMF and translocation to mitochondria.
DR BioGRID-ORCS; 171543; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Bmf; mouse.
DR EvolutionaryTrace; Q91ZE9; -.
DR PRO; PR:Q91ZE9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q91ZE9; protein.
DR Bgee; ENSMUSG00000040093; Expressed in external carotid artery and 176 other tissues.
DR ExpressionAtlas; Q91ZE9; baseline and differential.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0016459; C:myosin complex; IDA:UniProtKB.
DR GO; GO:0043276; P:anoikis; ISO:MGI.
DR GO; GO:0009267; P:cellular response to starvation; IMP:CAFA.
DR GO; GO:0034644; P:cellular response to UV; IDA:CAFA.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:MGI.
DR GO; GO:1904093; P:negative regulation of autophagic cell death; IMP:CAFA.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:CAFA.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IDA:MGI.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:BHF-UCL.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IGI:BHF-UCL.
DR DisProt; DP00645; -.
DR InterPro; IPR028192; BMF.
DR PANTHER; PTHR32014; PTHR32014; 1.
DR Pfam; PF15185; BMF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Reference proteome.
FT CHAIN 1..185
FT /note="Bcl-2-modifying factor"
FT /id="PRO_0000143112"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..75
FT /note="Interaction with DLC2"
FT /evidence="ECO:0000269|PubMed:11546872"
FT MOTIF 134..148
FT /note="BH3"
FT COMPBIAS 1..18
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 67
FT /note="D->A: Loss of interaction with DLC2."
FT /evidence="ECO:0000269|PubMed:11546872"
FT MUTAGEN 68
FT /note="K->A: Loss of interaction with DLC2."
FT /evidence="ECO:0000269|PubMed:11546872"
FT MUTAGEN 69
FT /note="A->P: Loss of interaction with DLC2."
FT /evidence="ECO:0000269|PubMed:11546872"
FT MUTAGEN 138
FT /note="L->A: Decrease in the interaction with BCL2 and
FT BCL2L2."
FT HELIX 130..149
FT /evidence="ECO:0007829|PDB:2VOG"
SQ SEQUENCE 185 AA; 20682 MW; DAE6EA080F3EA06B CRC64;
MEPPQCVEEL EDDVFQSEDG EPGTQPGGLL SADLFAQSQL DCPLSRLQLF PLTHCCGPGL
RPISQEDKAT QTLSPASPSQ GVMLPCGVTE EPQRLFYGNA GYRLPLPASF PAGSPLGEQP
PEGQFLQHRA EVQIARKLQC IADQFHRLHT QQHQQNRDRA WWQVFLFLQN LALNRQENRE
GVGPW
