BMF_RAT
ID BMF_RAT Reviewed; 185 AA.
AC Q8K589;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Bcl-2-modifying factor;
GN Name=Bmf;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=12787069; DOI=10.1046/j.1471-4159.2003.01795.x;
RA Itoh T., Itoh A., Pleasure D.;
RT "Bcl-2-related protein family gene expression during oligodendroglial
RT differentiation.";
RL J. Neurochem. 85:1500-1512(2003).
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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DR EMBL; AF506761; AAM28890.1; -; mRNA.
DR RefSeq; NP_640351.1; NM_139258.1.
DR AlphaFoldDB; Q8K589; -.
DR SMR; Q8K589; -.
DR STRING; 10116.ENSRNOP00000010381; -.
DR PhosphoSitePlus; Q8K589; -.
DR PaxDb; Q8K589; -.
DR GeneID; 246142; -.
DR KEGG; rno:246142; -.
DR UCSC; RGD:628658; rat.
DR CTD; 90427; -.
DR RGD; 628658; Bmf.
DR VEuPathDB; HostDB:ENSRNOG00000007529; -.
DR eggNOG; ENOG502S0P3; Eukaryota.
DR HOGENOM; CLU_090680_0_0_1; -.
DR InParanoid; Q8K589; -.
DR OMA; HRLHMQR; -.
DR OrthoDB; 1454053at2759; -.
DR PhylomeDB; Q8K589; -.
DR Reactome; R-RNO-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
DR Reactome; R-RNO-139910; Activation of BMF and translocation to mitochondria.
DR PRO; PR:Q8K589; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000007529; Expressed in thymus and 18 other tissues.
DR Genevisible; Q8K589; RN.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:RGD.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016459; C:myosin complex; ISO:RGD.
DR GO; GO:0043276; P:anoikis; ISO:RGD.
DR GO; GO:0009267; P:cellular response to starvation; ISO:RGD.
DR GO; GO:0034644; P:cellular response to UV; ISO:RGD.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:1904093; P:negative regulation of autophagic cell death; ISO:RGD.
DR GO; GO:0010507; P:negative regulation of autophagy; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:RGD.
DR InterPro; IPR028192; BMF.
DR PANTHER; PTHR32014; PTHR32014; 1.
DR Pfam; PF15185; BMF; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Reference proteome.
FT CHAIN 1..185
FT /note="Bcl-2-modifying factor"
FT /id="PRO_0000143113"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..75
FT /note="Interaction with DLC2"
FT MOTIF 134..148
FT /note="BH3"
FT COMPBIAS 1..18
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 185 AA; 20710 MW; A8F8D9FF10AD15B4 CRC64;
MEPPQCVEEL EDDVFQPEDG EPGTQPGSLL SADLFAQSQL DCPLSRLQLF PLTHCCGPGL
RPVSQEDKAT QTLSPASPSQ GVMLPCGVTE EPQRLFYGNA GYRLPLPASF PAGSALGEQP
PEGQFLQHRA EVQIARKLQC IADQFHRLHM QQHQQNRDRA WRQVFLFLQN LALNRRENRE
GVGPW
