BAX_BOVIN
ID BAX_BOVIN Reviewed; 192 AA.
AC O02703;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Apoptosis regulator BAX;
GN Name=BAX;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Holstein; TISSUE=Thymus;
RX PubMed=9501056; DOI=10.1006/viro.1998.9029;
RA Reyes R.A., Cockerell G.L.;
RT "Increased ratio of bcl-2/bax expression is associated with bovine leukemia
RT virus-induced leukemogenesis in cattle.";
RL Virology 242:184-192(1998).
CC -!- FUNCTION: Plays a role in the mitochondrial apoptotic process. Under
CC normal conditions, BAX is largely cytosolic via constant
CC retrotranslocation from mitochondria to the cytosol mediated by
CC BCL2L1/Bcl-xL, which avoids accumulation of toxic BAX levels at the
CC mitochondrial outer membrane (MOM). Under stress conditions, undergoes
CC a conformation change that causes translocation to the mitochondrion
CC membrane, leading to the release of cytochrome c that then triggers
CC apoptosis. Promotes activation of CASP3, and thereby apoptosis.
CC {ECO:0000250|UniProtKB:Q07812}.
CC -!- SUBUNIT: Homodimer. Forms higher oligomers under stress conditions.
CC Forms heterooligomers with BAK. Interacts with BCL2L11. Interaction
CC with BCL2L11 promotes BAX oligomerization and association with
CC mitochondrial membranes, with subsequent release of cytochrome c. Forms
CC heterodimers with BCL2, BCL2L1 isoform Bcl-X(L), BCL2L2, MCL1 and A1.
CC Interacts with SH3GLB1. Interacts with SFN and YWHAZ; the interaction
CC occurs in the cytoplasm. Under stress conditions, JNK-mediated
CC phosphorylation of SFN and YWHAZ, releases BAX to mitochondria.
CC Interacts with RNF144B, which regulates the ubiquitin-dependent
CC stability of BAX. Interacts with CLU under stress conditions that cause
CC a conformation change leading to BAX oligomerization and association
CC with mitochondria. Does not interact with CLU in unstressed cells.
CC Interacts with FAIM2/LFG2. Interacts with RTL10/BOP. Interacts (via a
CC C-terminal 33 residues) with NOL3 (via CARD domain); inhibits BAX
CC activation and translocation and consequently cytochrome c release from
CC mitochondria. Interacts with GIMAP3/IAN4 and GIMAP5/IAN5; this
CC interaction is increased, when cells initiate apoptosis upon IL2
CC withdrawal. Interacts with IRF3; the interaction is direct, increases
CC upon Sendai virus infection and mediates the formation of the apoptosis
CC complex TOMM70:HSP90AA1:IRF3:BAX. Interacts with MOAP1, facilitating
CC BAX-dependent mitochondrial outer membrane permeabilization and
CC apoptosis. Interacts with BCL2L10/BCL-B (By similarity).
CC {ECO:0000250|UniProtKB:Q07812}.
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=O02703-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=O02703-2; Sequence=Not described;
CC Name=Gamma;
CC IsoId=O02703-3; Sequence=Not described;
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 -!- MISCELLANEOUS: [Isoform Alpha]: 21 kDa protein.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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DR EMBL; U92569; AAC48806.1; -; mRNA.
DR RefSeq; NP_776319.1; NM_173894.1. [O02703-1]
DR AlphaFoldDB; O02703; -.
DR BMRB; O02703; -.
DR SMR; O02703; -.
DR STRING; 9913.ENSBTAP00000017739; -.
DR PaxDb; O02703; -.
DR PeptideAtlas; O02703; -.
DR PRIDE; O02703; -.
DR Ensembl; ENSBTAT00000017739; ENSBTAP00000017739; ENSBTAG00000013340. [O02703-1]
DR GeneID; 280730; -.
DR KEGG; bta:280730; -.
DR CTD; 581; -.
DR VEuPathDB; HostDB:ENSBTAG00000013340; -.
DR eggNOG; KOG4728; Eukaryota.
DR GeneTree; ENSGT01050000244872; -.
DR HOGENOM; CLU_085401_2_2_1; -.
DR InParanoid; O02703; -.
DR OMA; HFGTPTW; -.
DR OrthoDB; 1218929at2759; -.
DR TreeFam; TF315834; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000013340; Expressed in ileocecal valve and 104 other tissues.
DR ExpressionAtlas; O02703; baseline and differential.
DR GO; GO:0097144; C:BAX complex; ISS:UniProtKB.
DR GO; GO:0097136; C:Bcl-2 family protein complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005757; C:mitochondrial permeability transition pore complex; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046930; C:pore complex; ISS:UniProtKB.
DR GO; GO:0051434; F:BH3 domain binding; ISS:UniProtKB.
DR GO; GO:0015267; F:channel activity; ISS:UniProtKB.
DR GO; GO:0008289; F:lipid binding; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:HGNC.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; ISS:UniProtKB.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; ISS:UniProtKB.
DR GO; GO:0097190; P:apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0001783; P:B cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0010248; P:establishment or maintenance of transmembrane electrochemical gradient; ISS:UniProtKB.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0008053; P:mitochondrial fusion; ISS:UniProtKB.
DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; ISS:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:1900103; P:positive regulation of endoplasmic reticulum unfolded protein response; ISS:UniProtKB.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS: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:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; ISS:UniProtKB.
DR GO; GO:0032976; P:release of matrix enzymes from mitochondria; ISS:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Apoptosis; Cytoplasm; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..192
FT /note="Apoptosis regulator BAX"
FT /id="PRO_0000143052"
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"
SQ SEQUENCE 192 AA; 21259 MW; 6B4D5BABF1D5F87E CRC64;
MDGSGEQPRG GGPTSSEQIM KTGALLLQGF IQDRAGRMGG ETPELGLEQV PQDASTKKLS
ECLKRIGDEL DSNMELQRMI AAVDTDSPRE VFFRVAAEMF SDGNFNWGRV VALFYFASKL
VLKALCTKVP ELIRTIMGWT LDFLRERLLG WIQDQGGWDG LLSYFGTPTW QTVTIFVAGV
LTASLTIWKK MG
