BI1_DROME
ID BI1_DROME Reviewed; 245 AA.
AC Q9VSH3;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Bax inhibitor 1 {ECO:0000312|FlyBase:FBgn0035871};
GN Name=BI-1 {ECO:0000312|FlyBase:FBgn0035871};
GN ORFNames=CG7188 {ECO:0000312|FlyBase:FBgn0035871};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP FUNCTION.
RX PubMed=19328063; DOI=10.1016/j.molcel.2009.02.017;
RA Lisbona F., Rojas-Rivera D., Thielen P., Zamorano S., Todd D., Martinon F.,
RA Glavic A., Kress C., Lin J.H., Walter P., Reed J.C., Glimcher L.H.,
RA Hetz C.;
RT "BAX inhibitor-1 is a negative regulator of the ER stress sensor
RT IRE1alpha.";
RL Mol. Cell 33:679-691(2009).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21926971; DOI=10.1038/emboj.2011.318;
RA Castillo K., Rojas-Rivera D., Lisbona F., Caballero B., Nassif M.,
RA Court F.A., Schuck S., Ibar C., Walter P., Sierralta J., Glavic A.,
RA Hetz C.;
RT "BAX inhibitor-1 regulates autophagy by controlling the IRE1alpha branch of
RT the unfolded protein response.";
RL EMBO J. 30:4465-4478(2011).
CC -!- FUNCTION: Suppressor of apoptosis (By similarity). Modulates unfolded
CC protein response signaling (PubMed:19328063). Negatively regulates
CC autophagy and autophagosome formation, especially during periods of
CC nutrient deprivation, and reduces cell survival during starvation
CC (PubMed:21926971). {ECO:0000250|UniProtKB:P55061,
CC ECO:0000269|PubMed:19328063, ECO:0000269|PubMed:21926971}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P55061}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P55061}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown induces autophagy in
CC larvae under basal and fasting conditions with larvae showing an
CC increased number of autophagosomes. Decreased larval survival following
CC treatment with tunicamycin. Impaired pupal salivary gland degradation
CC with pupae undergoing autophagy prematurely by six hours after puparium
CC formation. Increased adult survival during nutrient starvation.
CC {ECO:0000269|PubMed:21926971}.
CC -!- SIMILARITY: Belongs to the BI1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014296; AAF50446.1; -; Genomic_DNA.
DR EMBL; AY058377; AAL13606.1; -; mRNA.
DR RefSeq; NP_648205.1; NM_139948.4.
DR AlphaFoldDB; Q9VSH3; -.
DR SMR; Q9VSH3; -.
DR BioGRID; 64354; 9.
DR DIP; DIP-18925N; -.
DR IntAct; Q9VSH3; 2.
DR STRING; 7227.FBpp0076434; -.
DR PaxDb; Q9VSH3; -.
DR PRIDE; Q9VSH3; -.
DR DNASU; 38936; -.
DR EnsemblMetazoa; FBtr0076711; FBpp0076434; FBgn0035871.
DR GeneID; 38936; -.
DR KEGG; dme:Dmel_CG7188; -.
DR UCSC; CG7188-RA; d. melanogaster.
DR CTD; 38936; -.
DR FlyBase; FBgn0035871; BI-1.
DR VEuPathDB; VectorBase:FBgn0035871; -.
DR eggNOG; KOG1629; Eukaryota.
DR GeneTree; ENSGT01050000244940; -.
DR HOGENOM; CLU_061277_0_0_1; -.
DR InParanoid; Q9VSH3; -.
DR OMA; MGDVIGM; -.
DR PhylomeDB; Q9VSH3; -.
DR BioGRID-ORCS; 38936; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 38936; -.
DR PRO; PR:Q9VSH3; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035871; Expressed in antenna and 41 other tissues.
DR ExpressionAtlas; Q9VSH3; baseline and differential.
DR Genevisible; Q9VSH3; DM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISM:FlyBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISS:FlyBase.
DR GO; GO:0060698; F:endoribonuclease inhibitor activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:0019899; F:enzyme binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0009267; P:cellular response to starvation; IMP:FlyBase.
DR GO; GO:0034620; P:cellular response to unfolded protein; IDA:ParkinsonsUK-UCL.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:FlyBase.
DR GO; GO:0060548; P:negative regulation of cell death; IDA:FlyBase.
DR GO; GO:1900102; P:negative regulation of endoplasmic reticulum unfolded protein response; ISS:FlyBase.
DR GO; GO:0060702; P:negative regulation of endoribonuclease activity; IDA:FlyBase.
DR GO; GO:0033119; P:negative regulation of RNA splicing; IDA:ParkinsonsUK-UCL.
DR GO; GO:0035071; P:salivary gland cell autophagic cell death; IMP:FlyBase.
DR InterPro; IPR006213; Bax_inhbtr1_CS.
DR InterPro; IPR006214; Bax_inhibitor_1-related.
DR PANTHER; PTHR23291; PTHR23291; 1.
DR Pfam; PF01027; Bax1-I; 1.
DR PROSITE; PS01243; BI1; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Autophagy; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Unfolded protein response.
FT CHAIN 1..245
FT /note="Bax inhibitor 1"
FT /id="PRO_0000179084"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..55
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..115
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..169
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 245 AA; 27574 MW; 57ACD341C5C94720 CRC64;
MADTANYIND RFQTFMNGLG DRYEPYVREH LSKVYMVLGS TAAATAMGAM LQMRDFLDLG
VLAAVATLVL VLGLHFYKDD GKNYYTRLGM LYAFGFCSGQ TLGPLLGYIC SINPAIILSA
LTGTFVTFIS LSLSALLAEQ GKYLYLGGML VSVINTMALL SLFNMVFKSY FVQVTQLYVG
VFVMAAFIVY DTQNIVEKCR NGNRDVVQHA LDLFFDVLSM FRRLLIILTQ KEERKQNERR
QNKTK
