BBC3_RAT
ID BBC3_RAT Reviewed; 193 AA.
AC Q80ZG6;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Bcl-2-binding component 3;
DE AltName: Full=p53 up-regulated modulator of apoptosis;
GN Name=Bbc3; Synonyms=Puma;
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).
RN [2]
RP INTERACTION WITH NOL3.
RX PubMed=17998337; DOI=10.1128/mcb.00738-07;
RA Li Y.Z., Lu D.Y., Tan W.Q., Wang J.X., Li P.F.;
RT "p53 initiates apoptosis by transcriptionally targeting the antiapoptotic
RT protein ARC.";
RL Mol. Cell. Biol. 28:564-574(2008).
CC -!- FUNCTION: Essential mediator of p53/TP53-dependent and p53/TP53-
CC independent apoptosis. Promotes partial unfolding of BCL2L1 and
CC dissociation of BCL2L1 from p53/TP53, releasing the bound p53/TP53 to
CC induce apoptosis. Regulates ER stress-induced neuronal apoptosis.
CC {ECO:0000250|UniProtKB:Q99ML1, ECO:0000250|UniProtKB:Q9BXH1}.
CC -!- SUBUNIT: Interacts with MCL1 and BCL2A1 (By similarity). Interacts (via
CC BH3 domain) with BCL2 and BCL2L1/BCL-XL (By similarity). Interacts (via
CC BH3 domain) with NOL3/ARC (via CARD domain); this interaction prevents
CC BBC3 association with BCL2 and results in CASP8 activation
CC (PubMed:17998337). {ECO:0000250|UniProtKB:Q99ML1,
CC ECO:0000250|UniProtKB:Q9BXH1, ECO:0000269|PubMed:17998337}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Note=Localized to the mitochondria
CC in order to induce cytochrome c release. {ECO:0000250}.
CC -!- INDUCTION: By DNA damage, glucocorticoid treatment, growth factor
CC deprivation and p53. {ECO:0000250}.
CC -!- DOMAIN: The BH3 motif is intrinsically disordered in the absence of a
CC binding partner but folds upon binding (By similarity). Folds when
CC bound to BCL2L1 (By similarity). Also folds when bound to MCL1 (By
CC similarity). {ECO:0000250|UniProtKB:Q99ML1,
CC ECO:0000250|UniProtKB:Q9BXH1}.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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DR EMBL; AY157758; AAO16862.1; -; mRNA.
DR RefSeq; NP_776209.1; NM_173837.2.
DR AlphaFoldDB; Q80ZG6; -.
DR ComplexPortal; CPX-2028; PUMA:BCL-2 complex.
DR ComplexPortal; CPX-2030; PUMA:BCL-XL complex.
DR STRING; 10116.ENSRNOP00000064216; -.
DR PhosphoSitePlus; Q80ZG6; -.
DR PaxDb; Q80ZG6; -.
DR Ensembl; ENSRNOT00000101734; ENSRNOP00000076660; ENSRNOG00000062473.
DR GeneID; 317673; -.
DR KEGG; rno:317673; -.
DR CTD; 27113; -.
DR RGD; 631434; Bbc3.
DR GeneTree; ENSGT00390000002767; -.
DR InParanoid; Q80ZG6; -.
DR OrthoDB; 1534857at2759; -.
DR PhylomeDB; Q80ZG6; -.
DR PRO; PR:Q80ZG6; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:GOC.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0097143; C:PUMA-BCL-xl complex; ISO:RGD.
DR GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR GO; GO:0097190; P:apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:RGD.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISO:RGD.
DR GO; GO:0008340; P:determination of adult lifespan; ISO:RGD.
DR GO; GO:0097194; P:execution phase of apoptosis; ISO:RGD.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:RGD.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0032471; P:negative regulation of endoplasmic reticulum calcium ion concentration; ISO:RGD.
DR GO; GO:0045926; P:negative regulation of growth; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:2001056; P:positive regulation of cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0032464; P:positive regulation of protein homooligomerization; ISO:RGD.
DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in 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 GO; GO:0070245; P:positive regulation of thymocyte apoptotic process; ISO:RGD.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; ISO:RGD.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISO:RGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:1901998; P:toxin transport; ISO:RGD.
DR InterPro; IPR031661; Bbc3.
DR PANTHER; PTHR28639; PTHR28639; 1.
DR Pfam; PF15826; PUMA; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Mitochondrion; Phosphoprotein; Reference proteome.
FT CHAIN 1..193
FT /note="Bcl-2-binding component 3"
FT /id="PRO_0000143085"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 137..151
FT /note="BH3"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXH1"
SQ SEQUENCE 193 AA; 20718 MW; 39B5994F66065372 CRC64;
MARARQEGSS PEPVEGLARD SPRPFPLGRL MPSAVSCGLC EPGLPAAPAA PALLPAAYLC
APTAPPAVTA ALGGPRWPGG HRSRPRGPRP DGPQPSLSPA QQHLESPVPS APEALAGGPT
QAAPGVRVEE EEWAREIGAQ LRRMADDLNA QYERRRQEEQ HRHRPSPWRV MYNLFMGLLP
LPRDPGAPEM EPN
