BOK_MOUSE
ID BOK_MOUSE Reviewed; 213 AA.
AC O35425;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Bcl-2-related ovarian killer protein {ECO:0000250|UniProtKB:Q9UMX3};
DE AltName: Full=Apoptosis activator Mtd;
DE AltName: Full=Protein matador;
GN Name=Bok {ECO:0000312|MGI:MGI:1858494};
GN Synonyms=Mtd {ECO:0000303|PubMed:9535847};
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] (ISOFORM 1), DEVELOPMENTAL STAGE, TISSUE
RP SPECIFICITY, MUTAGENESIS OF LEU-71; LEU-74 AND LEU-78, AND FUNCTION.
RX PubMed=9535847; DOI=10.1074/jbc.273.15.8705;
RA Inohara N., Ekhterae D., Garcia I., Carrio R., Merino J., Merry A.,
RA Chen S., Nunez G.;
RT "Mtd, a novel Bcl-2 family member activates apoptosis in the absence of
RT heterodimerization with Bcl-2 and Bcl-XL.";
RL J. Biol. Chem. 273:8705-8710(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Lung;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP 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 [4]
RP TISSUE SPECIFICITY, FUNCTION, SUBUNIT, MUTAGENESIS OF ASP-76, AND
RP SUBCELLULAR LOCATION.
RX PubMed=23429263; DOI=10.1038/cdd.2013.10;
RA Echeverry N., Bachmann D., Ke F., Strasser A., Simon H.U., Kaufmann T.;
RT "Intracellular localization of the BCL-2 family member BOK and functional
RT implications.";
RL Cell Death Differ. 20:785-799(2013).
RN [5]
RP INTERACTION WITH ITPR1; ITPR2 AND ITPR3, UBIQUITINATION, DOMAIN, REGION,
RP AND MUTAGENESIS OF 34-LEU--TYR-38.
RX PubMed=23884412; DOI=10.1074/jbc.m113.496570;
RA Schulman J.J., Wright F.A., Kaufmann T., Wojcikiewicz R.J.;
RT "The Bcl-2 protein family member Bok binds to the coupling domain of
RT inositol 1,4,5-trisphosphate receptors and protects them from proteolytic
RT cleavage.";
RL J. Biol. Chem. 288:25340-25349(2013).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=26015568; DOI=10.1073/pnas.1421063112;
RA Carpio M.A., Michaud M., Zhou W., Fisher J.K., Walensky L.D., Katz S.G.;
RT "BCL-2 family member BOK promotes apoptosis in response to endoplasmic
RT reticulum stress.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:7201-7206(2015).
RN [7]
RP FUNCTION, UBIQUITINATION AT LYS-25; LYS-32; LYS-160 AND LYS-177,
RP IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF LYS-25; LYS-32; LYS-160
RP AND LYS-177, SUBCELLULAR LOCATION, SUBUNIT, AND INDUCTION.
RX PubMed=26949185; DOI=10.1016/j.cell.2016.02.026;
RA Llambi F., Wang Y.M., Victor B., Yang M., Schneider D.M., Gingras S.,
RA Parsons M.J., Zheng J.H., Brown S.A., Pelletier S., Moldoveanu T., Chen T.,
RA Green D.R.;
RT "BOK Is a Non-canonical BCL-2 Family Effector of Apoptosis Regulated by ER-
RT Associated Degradation.";
RL Cell 165:421-433(2016).
RN [8]
RP INTERACTION WITH ITPR1, DOMAIN, MUTAGENESIS OF LEU-34, UBIQUITINATION, AND
RP ALTERNATIVE SPLICING (ISOFORM 1 AND 2).
RX PubMed=27053113; DOI=10.1074/jbc.m115.711242;
RA Schulman J.J., Wright F.A., Han X., Zluhan E.J., Szczesniak L.M.,
RA Wojcikiewicz R.J.;
RT "The Stability and Expression Level of Bok Are Governed by Binding to
RT Inositol 1,4,5-Trisphosphate Receptors.";
RL J. Biol. Chem. 291:11820-11828(2016).
RN [9]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=27098698; DOI=10.1523/jneurosci.3780-15.2016;
RA D'Orsi B., Engel T., Pfeiffer S., Nandi S., Kaufmann T., Henshall D.C.,
RA Prehn J.H.;
RT "Bok Is Not Pro-Apoptotic But Suppresses Poly ADP-Ribose Polymerase-
RT Dependent Cell Death Pathways and Protects against Excitotoxic and Seizure-
RT Induced Neuronal Injury.";
RL J. Neurosci. 36:4564-4578(2016).
CC -!- FUNCTION: Apoptosis regulator that functions through different
CC apoptotic signaling pathways (PubMed:23429263, PubMed:26015568,
CC PubMed:26949185, PubMed:27098698, PubMed:9535847). Plays a roles as
CC pro-apoptotic protein that positively regulates intrinsic apoptotic
CC process in a BAX- and BAK1-dependent manner or in a BAX- and BAK1-
CC independent manner (PubMed:23429263, PubMed:26015568, PubMed:26949185).
CC In response to endoplasmic reticulum stress promotes mitochondrial
CC apoptosis through downstream BAX/BAK1 activation and positive
CC regulation of PERK-mediated unfolded protein response
CC (PubMed:26015568). Activates apoptosis independently of
CC heterodimerization with survival-promoting BCL2 and BCL2L1 through
CC induction of mitochondrial outer membrane permeabilization, in a
CC BAX- and BAK1-independent manner, in response to inhibition of ERAD-
CC proteasome degradation system, resulting in cytochrome c release
CC (PubMed:9535847, PubMed:26949185). In response to DNA damage, mediates
CC intrinsic apoptotic process in a TP53-dependent manner. Plays a role in
CC granulosa cell apoptosis by CASP3 activation (By similarity). Plays a
CC roles as anti-apoptotic protein during neuronal apoptotic process, by
CC negatively regulating poly ADP-ribose polymerase-dependent cell death
CC through regulation of neuronal calcium homeostasis and mitochondrial
CC bioenergetics in response to NMDA excitation (PubMed:27098698). In
CC addition to its role in apoptosis, may regulate trophoblast cell
CC proliferation during the early stages of placental development, by
CC acting on G1/S transition through regulation of CCNE1 expression.May
CC also play a role as an inducer of autophagy by disrupting interaction
CC between MCL1 and BECN1 (By similarity). {ECO:0000250|UniProtKB:Q9UMX3,
CC ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26015568,
CC ECO:0000269|PubMed:26949185, ECO:0000269|PubMed:27098698,
CC ECO:0000269|PubMed:9535847}.
CC -!- SUBUNIT: Monomer; positively regulates apoptotic process. Homodimer
CC (PubMed:23429263). Heterodimer (By similarity). Oligomer; promoted by
CC apoptotic stimuli and BH3-only proteins; mediates constitutive
CC activation (PubMed:26949185). Interacts (via BH4 domain) with ITPR1;
CC enhances BOK expression and stabilization; limits apoptosis and
CC prevents ubiquitination and then degradation; protects ITPR1 from
CC proteolysis by CASP3 during apoptosis (PubMed:27053113,
CC PubMed:23884412). Interacts with ITPR2 AND ITPR3; binds most strongly
CC to ITPR2, and barely to ITPR3; regulates their expression
CC (PubMed:23884412). Interacts with XPO1; translocates to the cytoplasm
CC (By similarity). Interacts with BNIP3; promotes oligomerization (By
CC similarity). {ECO:0000250|UniProtKB:Q792S6,
CC ECO:0000250|UniProtKB:Q9UMX3, ECO:0000269|PubMed:23429263,
CC ECO:0000269|PubMed:23884412, ECO:0000269|PubMed:26949185,
CC ECO:0000269|PubMed:27053113}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26949185}; Single-pass
CC membrane protein {ECO:0000269|PubMed:26949185}. Endoplasmic reticulum
CC membrane {ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26949185};
CC Single-pass membrane protein {ECO:0000269|PubMed:26949185}.
CC Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9UMX3}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9UMX3}. Nucleus {ECO:0000250|UniProtKB:Q9UMX3}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q9UMX3}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9UMX3}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q9UMX3}. Early endosome membrane
CC {ECO:0000269|PubMed:23429263}. Recycling endosome membrane
CC {ECO:0000269|PubMed:23429263}. Nucleus outer membrane
CC {ECO:0000269|PubMed:23429263}. Golgi apparatus, cis-Golgi network
CC membrane {ECO:0000269|PubMed:23429263}. Golgi apparatus, trans-Golgi
CC network membrane {ECO:0000269|PubMed:23429263}. Membrane
CC {ECO:0000250|UniProtKB:Q9UMX3}. Note=Nuclear and cytoplasmic
CC compartments in the early stages of apoptosis and during apoptosis
CC associates with mitochondria. In healthy cells, associates loosely with
CC the membrane in a hit-and-run mode. The insertion and accumulation on
CC membranes is enhanced through the activity of death signals, resulting
CC in the integration of the membrane-bound protein into the membrane (By
CC similarity). The transmembrane domain controls subcellular
CC localization; constitutes a tail-anchor (PubMed:23429263,
CC PubMed:26949185). Localizes in early and late endosome upon blocking of
CC apoptosis (PubMed:23429263). Must localize to the mitochondria to
CC induce mitochondrial outer membrane permeabilization and apoptosis
CC (PubMed:26949185). {ECO:0000250|UniProtKB:Q9UMX3,
CC ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:26949185}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=O35425-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O35425-2; Sequence=VSP_058600;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:9535847, PubMed:23429263).
CC Highly expressed in brain, kidney, and spleen (PubMed:27098698).
CC {ECO:0000269|PubMed:23429263, ECO:0000269|PubMed:27098698,
CC ECO:0000269|PubMed:9535847}.
CC -!- DEVELOPMENTAL STAGE: At 15.0 dpc, expressed in brain, liver, thymus,
CC lung, intestinal epithelium and follicles of the whiskers.
CC {ECO:0000269|PubMed:9535847}.
CC -!- INDUCTION: Induced upon proteasome inhibition.
CC {ECO:0000269|PubMed:26949185}.
CC -!- DOMAIN: BH4 domain mediates interaction with ITPR1.
CC {ECO:0000269|PubMed:23884412, ECO:0000269|PubMed:27053113}.
CC -!- PTM: Ubiquitinated by AMFR/gp78 E3 ubiquitin ligase complex; mediates
CC degradation by ubiquitin-proteasome pathway in a VCP/p97-dependent
CC manner; prevents from proapoptotic activity; promotes degradation of
CC newly synthesized proteins that are not ITPR1 associated.
CC {ECO:0000269|PubMed:23884412, ECO:0000269|PubMed:26949185,
CC ECO:0000269|PubMed:27053113}.
CC -!- DISRUPTION PHENOTYPE: Knockout Bok mice have a normal development.
CC {ECO:0000269|PubMed:26015568}.
CC -!- MISCELLANEOUS: 'Matador' means killer in Spanish.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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DR EMBL; AF027707; AAC53582.1; -; mRNA.
DR EMBL; BC030069; AAH30069.1; -; mRNA.
DR CCDS; CCDS15193.1; -. [O35425-1]
DR RefSeq; NP_058058.1; NM_016778.3. [O35425-1]
DR AlphaFoldDB; O35425; -.
DR SMR; O35425; -.
DR STRING; 10090.ENSMUSP00000027499; -.
DR iPTMnet; O35425; -.
DR PhosphoSitePlus; O35425; -.
DR PaxDb; O35425; -.
DR PeptideAtlas; O35425; -.
DR PRIDE; O35425; -.
DR ProteomicsDB; 273623; -. [O35425-1]
DR ProteomicsDB; 273624; -. [O35425-2]
DR Antibodypedia; 20324; 280 antibodies from 32 providers.
DR DNASU; 51800; -.
DR Ensembl; ENSMUST00000027499; ENSMUSP00000027499; ENSMUSG00000026278. [O35425-1]
DR Ensembl; ENSMUST00000201863; ENSMUSP00000144347; ENSMUSG00000026278. [O35425-1]
DR GeneID; 51800; -.
DR KEGG; mmu:51800; -.
DR UCSC; uc007cee.1; mouse. [O35425-1]
DR CTD; 666; -.
DR MGI; MGI:1858494; Bok.
DR VEuPathDB; HostDB:ENSMUSG00000026278; -.
DR eggNOG; KOG4728; Eukaryota.
DR GeneTree; ENSGT01050000244872; -.
DR HOGENOM; CLU_114994_0_0_1; -.
DR InParanoid; O35425; -.
DR OMA; DMTKCVV; -.
DR PhylomeDB; O35425; -.
DR TreeFam; TF315834; -.
DR BioGRID-ORCS; 51800; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Bok; mouse.
DR PRO; PR:O35425; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O35425; protein.
DR Bgee; ENSMUSG00000026278; Expressed in decidua and 245 other tissues.
DR ExpressionAtlas; O35425; baseline and differential.
DR Genevisible; O35425; MM.
DR GO; GO:0033106; C:cis-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0051400; F:BH domain binding; ISO:MGI.
DR GO; GO:0046983; F:protein dimerization activity; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; IDA:UniProtKB.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISO:MGI.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0051902; P:negative regulation of mitochondrial depolarization; IMP:UniProtKB.
DR GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0060546; P:negative regulation of necroptotic process; IMP:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:UniProtKB.
DR GO; GO:0051402; P:neuron apoptotic process; IDA:MGI.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:1902237; P:positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:1900119; P:positive regulation of execution phase of apoptosis; ISS:UniProtKB.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:1903899; P:positive regulation of PERK-mediated unfolded protein response; IMP:UniProtKB.
DR GO; GO:0051259; P:protein complex oligomerization; IDA:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; ISO:MGI.
DR GO; GO:1901382; P:regulation of chorionic trophoblast cell proliferation; ISS:UniProtKB.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IMP:UniProtKB.
DR GO; GO:1904708; P:regulation of granulosa cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; ISO:MGI.
DR CDD; cd06845; Bcl-2_like; 1.
DR Gene3D; 1.10.437.10; -; 1.
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; IPR026309; BOK.
DR PANTHER; PTHR11256; PTHR11256; 1.
DR PANTHER; PTHR11256:SF48; PTHR11256:SF48; 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.
PE 1: Evidence at protein level;
KW Alternative initiation; Apoptosis; Cytoplasm; Endoplasmic reticulum;
KW Endosome; Golgi apparatus; Isopeptide bond; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Mitochondrion outer membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT CHAIN 1..213
FT /note="Bcl-2-related ovarian killer protein"
FT /id="PRO_0000143087"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 15..45
FT /note="Interactions with ITPR1"
FT /evidence="ECO:0000269|PubMed:23884412"
FT REGION 71..79
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:Q9UMX3"
FT MOTIF 32..44
FT /note="BH4"
FT MOTIF 67..83
FT /note="BH3"
FT MOTIF 113..132
FT /note="BH1"
FT MOTIF 165..179
FT /note="BH2"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 25
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:26949185"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:26949185"
FT CROSSLNK 160
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:26949185"
FT CROSSLNK 177
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:26949185"
FT VAR_SEQ 1..14
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:27053113"
FT /id="VSP_058600"
FT MUTAGEN 25
FT /note="K->R: Increases protein expression and stability;
FT when associated with R-32, R-160 and R-177. Increases
FT apoptosis; when associated with R-32, R-160 and R-177."
FT /evidence="ECO:0000269|PubMed:26949185"
FT MUTAGEN 32
FT /note="K->R: Increases protein expression and stability;
FT when associated with R-25, R-160 and R-177. Increases
FT apoptosis; when associated with R-25, R-160 and R-177."
FT /evidence="ECO:0000269|PubMed:26949185"
FT MUTAGEN 34..38
FT /note="LGREY->AAAAA: Does not interacts with ITPR1."
FT /evidence="ECO:0000269|PubMed:23884412"
FT MUTAGEN 34
FT /note="L->G: Does not interacts with ITPR1. Triggers
FT apoptosis."
FT /evidence="ECO:0000269|PubMed:27053113"
FT MUTAGEN 71
FT /note="L->Q: No change in apoptosis induction; when
FT associated with Q-74 and Q-78."
FT /evidence="ECO:0000269|PubMed:9535847"
FT MUTAGEN 74
FT /note="L->Q: No change in apoptosis induction; when
FT associated with Q-71 and Q-78."
FT /evidence="ECO:0000269|PubMed:9535847"
FT MUTAGEN 76
FT /note="D->A: Disrupts homodimerization. Positively
FT regulates intrinsic apoptotic signaling pathway."
FT /evidence="ECO:0000269|PubMed:23429263"
FT MUTAGEN 78
FT /note="L->Q: No change in apoptosis induction; when
FT associated with Q-71 and Q-74."
FT /evidence="ECO:0000269|PubMed:9535847"
FT MUTAGEN 160
FT /note="K->R: Increases protein expression and stability;
FT when associated with R-25, R-32 and R-177. Increases
FT apoptosis; when associated with R-25, R-32 and R-177."
FT /evidence="ECO:0000269|PubMed:26949185"
FT MUTAGEN 177
FT /note="K->R: Increases protein expression and stability;
FT when associated with R-25, R-32 and R-160. Increases
FT apoptosis; when associated with R-25, R-32 and R-160."
FT /evidence="ECO:0000269|PubMed:26949185"
SQ SEQUENCE 213 AA; 23456 MW; F8755C45CB05D626 CRC64;
MEVLRRSSVF AAEIMDAFDR SPTDKELVAQ AKALGREYVH ARLLRAGLSW SAPERASPAP
GGRLAEVCTV LLRLGDELEQ IRPSVYRNVA RQLHIPLQSE PVVTDAFLAV AGHIFSAGIT
WGKVVSLYSV AAGLAVDCVR QAQPAMVHAL VDCLGEFVRK TLATWLRRRG GWTDVLKCVV
STDPGFRSHW LVATLCSFGR FLKAAFFLLL PER
