BAX_MOUSE
ID BAX_MOUSE Reviewed; 192 AA.
AC Q07813;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Apoptosis regulator BAX;
GN Name=Bax;
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 BCL2, AND FUNCTION.
RC STRAIN=C57BL/6 X DBA/2;
RX PubMed=8358790; DOI=10.1016/0092-8674(93)90509-o;
RA Oltvai Z.N., Milliman C.L., Korsmeyer S.J.;
RT "Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that
RT accelerates programmed cell death.";
RL Cell 74:609-619(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 [3]
RP INTERACTION WITH NOL3.
RX PubMed=15383280; DOI=10.1016/j.molcel.2004.08.020;
RA Nam Y.J., Mani K., Ashton A.W., Peng C.F., Krishnamurthy B., Hayakawa Y.,
RA Lee P., Korsmeyer S.J., Kitsis R.N.;
RT "Inhibition of both the extrinsic and intrinsic death pathways through
RT nonhomotypic death-fold interactions.";
RL Mol. Cell 15:901-912(2004).
RN [4]
RP INTERACTION WITH GIMAP3 AND GIMAP5.
RX PubMed=16509771; DOI=10.1371/journal.pbio.0040103;
RA Nitta T., Nasreen M., Seike T., Goji A., Ohigashi I., Miyazaki T., Ohta T.,
RA Kanno M., Takahama Y.;
RT "IAN family critically regulates survival and development of T
RT lymphocytes.";
RL PLoS Biol. 4:593-605(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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).
RN [6]
RP INTERACTION WITH MURINE GAMMAHERPESVIRUS 68 PROTEIN VBCL2.
RX PubMed=18248095; DOI=10.1371/journal.ppat.0040025;
RA Ku B., Woo J.S., Liang C., Lee K.H., Hong H.S., E X., Kim K.S., Jung J.U.,
RA Oh B.H.;
RT "Structural and biochemical bases for the inhibition of autophagy and
RT apoptosis by viral BCL-2 of murine gamma-herpesvirus 68.";
RL PLoS Pathog. 4:E25-E25(2008).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 52-82 IN COMPLEX WITH BCL2,
RP FUNCTION, AND INTERACTION WITH BCL2 AND BCL2L2.
RX PubMed=21060336; DOI=10.1038/cr.2010.149;
RA Ku B., Liang C., Jung J.U., Oh B.H.;
RT "Evidence that inhibition of BAX activation by BCL-2 involves its tight and
RT preferential interaction with the BH3 domain of BAX.";
RL Cell Res. 21:627-641(2011).
CC -!- FUNCTION: Accelerates programmed cell death by binding to, and
CC antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B
CC 19k protein. Under stress conditions, undergoes a conformation change
CC that causes translocation to the mitochondrion membrane, leading to the
CC release of cytochrome c that then triggers apoptosis. Promotes
CC activation of CASP3, and thereby apoptosis. BAX deficiency leads to
CC lymphoid hyperplasia and male sterility, because of the cessation of
CC sperm production. {ECO:0000269|PubMed:21060336,
CC ECO:0000269|PubMed:8358790}.
CC -!- SUBUNIT: Homodimer. Forms higher oligomers under stress conditions.
CC Forms heterooligomers with BAK (By similarity). Interacts with BCL2L11.
CC Interaction with BCL2L11 promotes BAX oligomerization and association
CC with mitochondrial membranes, with subsequent release of cytochrome c
CC (PubMed:21060336). Forms heterodimers with BCL2 (PubMed:8358790,
CC PubMed:21060336). Forms heterodimers with BCL2L1 isoform Bcl-X(L),
CC BCL2L2, MCL1 and A1. Interacts with SH3GLB1. Interacts with SFN and
CC YWHAZ; the interaction occurs in the cytoplasm. Under stress
CC conditions, JNK-mediated phosphorylation of SFN and YWHAZ, releases BAX
CC to mitochondria. Interacts with RNF144B, which regulates the ubiquitin-
CC dependent stability of BAX. Interacts with CLU under stress conditions
CC that cause a conformation change leading to BAX oligomerization and
CC association with mitochondria. Does not interact with CLU in unstressed
CC cells (By similarity). Interacts with FAIM2/LFG2 (By similarity).
CC Interacts with BOP (By similarity). Interacts (via a C-terminal 33
CC residues) with NOL3 (via CARD domain); inhibits BAX activation and
CC translocationand consequently cytochrome c release from mitochondria
CC (PubMed:15383280). Interacts with GIMAP3/IAN4 and GIMAP5/IAN5; this
CC interaction is increased, when cells initiate apoptosis upon IL2
CC withdrawal (PubMed:16509771). Interacts with IRF3; the interaction is
CC direct and, upon virus infection, mediates the formation of the
CC apoptosis complex TOMM70:HSP90AA1:IRF3:BAX (By similarity). Interacts
CC with MOAP1, facilitating BAX-dependent mitochondrial outer membrane
CC permeabilization and apoptosis (By similarity). Interacts with
CC BCL2L10/BCL-B (By similarity). {ECO:0000250|UniProtKB:Q07812,
CC ECO:0000269|PubMed:15383280, ECO:0000269|PubMed:16509771,
CC ECO:0000269|PubMed:21060336, ECO:0000269|PubMed:8358790}.
CC -!- SUBUNIT: (Microbial infection) Interacts with gamma-herpesvirus 68
CC protein vBCL2. {ECO:0000269|PubMed:18248095}.
CC -!- INTERACTION:
CC Q07813; P10417: Bcl2; NbExp=2; IntAct=EBI-700711, EBI-526314;
CC Q07813; O75460: ERN1; Xeno; NbExp=2; IntAct=EBI-700711, EBI-371750;
CC Q07813-1; Q07813-1: Bax; NbExp=2; IntAct=EBI-15666406, EBI-15666406;
CC Q07813-1; O43521: BCL2L11; Xeno; NbExp=7; IntAct=EBI-15666406, EBI-526406;
CC -!- SUBCELLULAR LOCATION: [Isoform Alpha]: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q07812}; Single-pass membrane protein
CC {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q07812}.
CC Note=Colocalizes with 14-3-3 proteins in the cytoplasm. Under stress
CC conditions, undergoes a conformation change that causes release from
CC JNK-phosphorylated 14-3-3 proteins and translocation to the
CC mitochondrion membrane (By similarity). {ECO:0000250|UniProtKB:Q07812}.
CC -!- SUBCELLULAR LOCATION: [Isoform Beta]: Cytoplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform Gamma]: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Alpha;
CC IsoId=Q07813-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q07813-2; Sequence=Not described;
CC Name=Gamma;
CC IsoId=Q07813-3; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues.
CC -!- DOMAIN: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for
CC their pro-apoptotic activity and for their interaction with anti-
CC apoptotic members of the Bcl-2 family. {ECO:0000250|UniProtKB:Q07812}.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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DR EMBL; L22472; AAA03622.1; -; mRNA.
DR EMBL; BC018228; AAH18228.1; -; mRNA.
DR EMBL; BC053380; AAH53380.1; -; mRNA.
DR CCDS; CCDS21246.1; -. [Q07813-1]
DR PIR; D47538; D47538.
DR RefSeq; NP_031553.1; NM_007527.3. [Q07813-1]
DR PDB; 2XA0; X-ray; 2.70 A; C/D=52-82.
DR PDB; 5W62; X-ray; 2.20 A; A=1-192.
DR PDBsum; 2XA0; -.
DR PDBsum; 5W62; -.
DR AlphaFoldDB; Q07813; -.
DR SMR; Q07813; -.
DR BioGRID; 198304; 23.
DR ComplexPortal; CPX-2031; BAX oligomer.
DR CORUM; Q07813; -.
DR DIP; DIP-29541N; -.
DR ELM; Q07813; -.
DR IntAct; Q07813; 12.
DR MINT; Q07813; -.
DR STRING; 10090.ENSMUSP00000033093; -.
DR ChEMBL; CHEMBL3414407; -.
DR iPTMnet; Q07813; -.
DR PhosphoSitePlus; Q07813; -.
DR SwissPalm; Q07813; -.
DR EPD; Q07813; -.
DR jPOST; Q07813; -.
DR PaxDb; Q07813; -.
DR PeptideAtlas; Q07813; -.
DR PRIDE; Q07813; -.
DR ProteomicsDB; 273541; -. [Q07813-1]
DR TopDownProteomics; Q07813-1; -. [Q07813-1]
DR ABCD; Q07813; 1 sequenced antibody.
DR Antibodypedia; 3777; 2081 antibodies from 51 providers.
DR DNASU; 12028; -.
DR Ensembl; ENSMUST00000033093; ENSMUSP00000033093; ENSMUSG00000003873. [Q07813-1]
DR GeneID; 12028; -.
DR KEGG; mmu:12028; -.
DR UCSC; uc009gvh.1; mouse. [Q07813-1]
DR CTD; 581; -.
DR MGI; MGI:99702; Bax.
DR VEuPathDB; HostDB:ENSMUSG00000003873; -.
DR eggNOG; KOG4728; Eukaryota.
DR GeneTree; ENSGT01050000244872; -.
DR HOGENOM; CLU_085401_2_2_1; -.
DR InParanoid; Q07813; -.
DR OMA; HFGTPTW; -.
DR OrthoDB; 1218929at2759; -.
DR PhylomeDB; Q07813; -.
DR TreeFam; TF315834; -.
DR Reactome; R-MMU-111457; Release of apoptotic factors from the mitochondria.
DR Reactome; R-MMU-114294; Activation, translocation and oligomerization of BAX.
DR Reactome; R-MMU-5620971; Pyroptosis.
DR Reactome; R-MMU-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR BioGRID-ORCS; 12028; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Bax; mouse.
DR PRO; PR:Q07813; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q07813; protein.
DR Bgee; ENSMUSG00000003873; Expressed in cortical plate and 259 other tissues.
DR ExpressionAtlas; Q07813; baseline and differential.
DR Genevisible; Q07813; MM.
DR GO; GO:0097145; C:BAK complex; ISO:MGI.
DR GO; GO:0097144; C:BAX complex; IPI:BHF-UCL.
DR GO; GO:0097136; C:Bcl-2 family protein complex; ISS:UniProtKB.
DR GO; GO:0071944; C:cell periphery; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:MGI.
DR GO; GO:0005757; C:mitochondrial permeability transition pore complex; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0046930; C:pore complex; ISS:UniProtKB.
DR GO; GO:0051400; F:BH domain binding; ISO:MGI.
DR GO; GO:0051434; F:BH3 domain binding; ISO:MGI.
DR GO; GO:0015267; F:channel activity; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0030544; F:Hsp70 protein binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008289; F:lipid binding; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; IDA:MGI.
DR GO; GO:0097296; P:activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IDA:MGI.
DR GO; GO:0006915; P:apoptotic process; IDA:MGI.
DR GO; GO:1902262; P:apoptotic process involved in blood vessel morphogenesis; IGI:MGI.
DR GO; GO:1902263; P:apoptotic process involved in embryonic digit morphogenesis; IGI:MGI.
DR GO; GO:0060057; P:apoptotic process involved in mammary gland involution; IMP:MGI.
DR GO; GO:0097190; P:apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0001783; P:B cell apoptotic process; IGI:MGI.
DR GO; GO:0001782; P:B cell homeostasis; IMP:MGI.
DR GO; GO:0002358; P:B cell homeostatic proliferation; IMP:MGI.
DR GO; GO:0002352; P:B cell negative selection; IGI:MGI.
DR GO; GO:1990117; P:B cell receptor apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0001974; P:blood vessel remodeling; IGI:MGI.
DR GO; GO:0060402; P:calcium ion transport into cytosol; IGI:MGI.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:0045333; P:cellular respiration; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
DR GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
DR GO; GO:0034644; P:cellular response to UV; IGI:MGI.
DR GO; GO:0098586; P:cellular response to virus; ISO:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR GO; GO:0045136; P:development of secondary sexual characteristics; IMP:MGI.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IMP:MGI.
DR GO; GO:1904019; P:epithelial cell apoptotic process; IMP:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IDA:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0010248; P:establishment or maintenance of transmembrane electrochemical gradient; ISS:UniProtKB.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IGI:MGI.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IDA:MGI.
DR GO; GO:0009566; P:fertilization; IGI:MGI.
DR GO; GO:0007281; P:germ cell development; IGI:MGI.
DR GO; GO:0006687; P:glycosphingolipid metabolic process; IMP:MGI.
DR GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
DR GO; GO:0021854; P:hypothalamus development; IMP:MGI.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; ISO:MGI.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IMP:MGI.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IGI:MGI.
DR GO; GO:0001822; P:kidney development; IGI:MGI.
DR GO; GO:0001776; P:leukocyte homeostasis; IGI:MGI.
DR GO; GO:0035108; P:limb morphogenesis; IGI:MGI.
DR GO; GO:0008584; P:male gonad development; IMP:MGI.
DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0008053; P:mitochondrial fusion; IGI:MGI.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IGI:MGI.
DR GO; GO:0097049; P:motor neuron apoptotic process; IMP:MGI.
DR GO; GO:0002262; P:myeloid cell homeostasis; IGI:MGI.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IGI:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0032471; P:negative regulation of endoplasmic reticulum calcium ion concentration; IGI:MGI.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:MGI.
DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:MGI.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IGI:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IMP:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IDA:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IGI:MGI.
DR GO; GO:0007008; P:outer mitochondrial membrane organization; ISO:MGI.
DR GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IGI:MGI.
DR GO; GO:1902512; P:positive regulation of apoptotic DNA fragmentation; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
DR GO; GO:0060058; P:positive regulation of apoptotic process involved in mammary gland involution; IMP:MGI.
DR GO; GO:0002904; P:positive regulation of B cell apoptotic process; IGI:MGI.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IGI:MGI.
DR GO; GO:0048087; P:positive regulation of developmental pigmentation; IGI:MGI.
DR GO; GO:0051094; P:positive regulation of developmental process; IMP:MGI.
DR GO; GO:1900103; P:positive regulation of endoplasmic reticulum unfolded protein response; ISS:UniProtKB.
DR GO; GO:1904037; P:positive regulation of epithelial cell apoptotic process; IMP:MGI.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:1902110; P:positive regulation of mitochondrial membrane permeability involved in apoptotic process; IGI:MGI.
DR GO; GO:2000673; P:positive regulation of motor neuron apoptotic process; IMP:MGI.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IMP:MGI.
DR GO; GO:2000243; P:positive regulation of reproductive process; IMP:MGI.
DR GO; GO:0048597; P:post-embryonic camera-type eye morphogenesis; IGI:MGI.
DR GO; GO:0009791; P:post-embryonic development; IGI:MGI.
DR GO; GO:0001844; P:protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IGI:MGI.
DR GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:MGI.
DR GO; GO:0033599; P:regulation of mammary gland epithelial cell proliferation; IMP:MGI.
DR GO; GO:1902108; P:regulation of mitochondrial membrane permeability involved in apoptotic process; IGI:MGI.
DR GO; GO:1902445; P:regulation of mitochondrial membrane permeability involved in programmed necrotic cell death; IMP:MGI.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:MGI.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IGI:MGI.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:MGI.
DR GO; GO:0032976; P:release of matrix enzymes from mitochondria; ISS:UniProtKB.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:MGI.
DR GO; GO:0048678; P:response to axon injury; IMP:MGI.
DR GO; GO:0010332; P:response to gamma radiation; IMP:MGI.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:MGI.
DR GO; GO:0009651; P:response to salt stress; IGI:MGI.
DR GO; GO:0009636; P:response to toxic substance; IMP:MGI.
DR GO; GO:0009611; P:response to wounding; IMP:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0046666; P:retinal cell programmed cell death; IMP:MGI.
DR GO; GO:0060011; P:Sertoli cell proliferation; IGI:MGI.
DR GO; GO:0007548; P:sex differentiation; IMP:MGI.
DR GO; GO:0048515; P:spermatid differentiation; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0097435; P:supramolecular fiber organization; ISO:MGI.
DR GO; GO:0001777; P:T cell homeostatic proliferation; IMP:MGI.
DR GO; GO:0070242; P:thymocyte apoptotic process; IGI:MGI.
DR GO; GO:0060068; P:vagina development; IGI:MGI.
DR CDD; cd06845; Bcl-2_like; 1.
DR Gene3D; 1.10.437.10; -; 1.
DR InterPro; IPR026304; BAX.
DR InterPro; IPR036834; Bcl-2-like_sf.
DR InterPro; IPR046371; Bcl-2_BH1-3.
DR InterPro; IPR026298; Bcl-2_fam.
DR InterPro; IPR002475; Bcl2-like.
DR InterPro; IPR020717; Bcl2_BH1_motif_CS.
DR InterPro; IPR020726; Bcl2_BH2_motif_CS.
DR InterPro; IPR020728; Bcl2_BH3_motif_CS.
DR PANTHER; PTHR11256; PTHR11256; 1.
DR PANTHER; PTHR11256:SF42; PTHR11256:SF42; 1.
DR Pfam; PF00452; Bcl-2; 1.
DR PRINTS; PR01862; BCL2FAMILY.
DR SMART; SM00337; BCL; 1.
DR SUPFAM; SSF56854; SSF56854; 1.
DR PROSITE; PS50062; BCL2_FAMILY; 1.
DR PROSITE; PS01080; BH1; 1.
DR PROSITE; PS01258; BH2; 1.
DR PROSITE; PS01259; BH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cytoplasm;
KW Host-virus interaction; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..192
FT /note="Apoptosis regulator BAX"
FT /id="PRO_0000143057"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 59..73
FT /note="BH3"
FT MOTIF 98..118
FT /note="BH1"
FT MOTIF 150..165
FT /note="BH2"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q07812"
FT HELIX 16..34
FT /evidence="ECO:0007829|PDB:5W62"
FT HELIX 54..70
FT /evidence="ECO:0007829|PDB:5W62"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:5W62"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:5W62"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:5W62"
FT HELIX 107..124
FT /evidence="ECO:0007829|PDB:5W62"
FT HELIX 131..147
FT /evidence="ECO:0007829|PDB:5W62"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:5W62"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:5W62"
FT HELIX 159..165
FT /evidence="ECO:0007829|PDB:5W62"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:5W62"
FT HELIX 173..188
FT /evidence="ECO:0007829|PDB:5W62"
SQ SEQUENCE 192 AA; 21395 MW; D2E0B3566579FAFF CRC64;
MDGSGEQLGS GGPTSSEQIM KTGAFLLQGF IQDRAGRMAG ETPELTLEQP PQDASTKKLS
ECLRRIGDEL DSNMELQRMI ADVDTDSPRE VFFRVAADMF ADGNFNWGRV VALFYFASKL
VLKALCTKVP ELIRTIMGWT LDFLRERLLV WIQDQGGWEG LLSYFGTPTW QTVTIFVAGV
LTASLTIWKK MG
