BXI1_YEAST
ID BXI1_YEAST Reviewed; 297 AA.
AC P48558; D6W0P0; Q6B2Q1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Bax inhibitor 1;
DE AltName: Full=BH3 domain-containing protein BXI1;
GN Name=BXI1; Synonyms=YBH3; OrderedLocusNames=YNL305C; ORFNames=N0405;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8553702; DOI=10.1002/yea.320111311;
RA Maurer K.C.T., Urbanus J.H.M., Planta R.J.;
RT "Sequence analysis of a 30 kb DNA segment from yeast chromosome XIV
RT carrying a ribosomal protein gene cluster, the genes encoding a plasma
RT membrane protein and a subunit of replication factor C, and a novel
RT putative serine/threonine protein kinase gene.";
RL Yeast 11:1303-1310(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21673659; DOI=10.1038/emboj.2011.197;
RA Buttner S., Ruli D., Vogtle F.N., Galluzzi L., Moitzi B., Eisenberg T.,
RA Kepp O., Habernig L., Carmona-Gutierrez D., Rockenfeller P., Laun P.,
RA Breitenbach M., Khoury C., Frohlich K.U., Rechberger G., Meisinger C.,
RA Kroemer G., Madeo F.;
RT "A yeast BH3-only protein mediates the mitochondrial pathway of
RT apoptosis.";
RL EMBO J. 30:2779-2792(2011).
RN [8]
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).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21673967; DOI=10.1371/journal.pone.0020882;
RA Cebulski J., Malouin J., Pinches N., Cascio V., Austriaco N.;
RT "Yeast Bax inhibitor, Bxi1p, is an ER-localized protein that links the
RT unfolded protein response and programmed cell death in Saccharomyces
RT cerevisiae.";
RL PLoS ONE 6:E20882-E20882(2011).
CC -!- FUNCTION: Links the unfolded protein response and programmed cell death
CC and mediates mitochondrial-dependent apoptosis (PubMed:21673659,
CC PubMed:21673967). Induces cell death and disruption of the
CC mitochondrial transmembrane potential via the mitochondrial phosphate
CC carrier MIR1 (PubMed:21673659). Dispensible for starvation-induced
CC autophagy (PubMed:21926971). {ECO:0000269|PubMed:21673659,
CC ECO:0000269|PubMed:21673967, ECO:0000269|PubMed:21926971}.
CC -!- INTERACTION:
CC P48558; Q08234: YOL075C; NbExp=2; IntAct=EBI-28349, EBI-29278;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21673967}; Multi-pass membrane protein
CC {ECO:0000255}. Vacuole membrane {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:21673659, ECO:0000269|PubMed:21673967}; Multi-pass
CC membrane protein {ECO:0000255}. Mitochondrion membrane
CC {ECO:0000269|PubMed:21673659}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Translocated from predominantly vacuolar sites in
CC healthy cells to mitochondria upon apoptosis induction.
CC {ECO:0000269|PubMed:21673659}.
CC -!- DISRUPTION PHENOTYPE: No effect on autophagy during nitrogen
CC starvation. {ECO:0000269|PubMed:21926971}.
CC -!- SIMILARITY: Belongs to the BI1 family. LFG subfamily. {ECO:0000305}.
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DR EMBL; U23084; AAC49093.1; -; Genomic_DNA.
DR EMBL; Z71581; CAA96233.1; -; Genomic_DNA.
DR EMBL; AY692679; AAT92698.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10256.1; -; Genomic_DNA.
DR PIR; S63281; S63281.
DR RefSeq; NP_014094.1; NM_001183143.1.
DR AlphaFoldDB; P48558; -.
DR BioGRID; 35534; 40.
DR DIP; DIP-7944N; -.
DR IntAct; P48558; 16.
DR MINT; P48558; -.
DR STRING; 4932.YNL305C; -.
DR TCDB; 1.A.14.3.5; the calcium transporter a (cata) (formerly the testis-enhanced gene transfer (tegt) family.
DR PaxDb; P48558; -.
DR PRIDE; P48558; -.
DR EnsemblFungi; YNL305C_mRNA; YNL305C; YNL305C.
DR GeneID; 855411; -.
DR KEGG; sce:YNL305C; -.
DR SGD; S000005249; BXI1.
DR VEuPathDB; FungiDB:YNL305C; -.
DR eggNOG; KOG2322; Eukaryota.
DR GeneTree; ENSGT01050000244940; -.
DR HOGENOM; CLU_058671_0_0_1; -.
DR InParanoid; P48558; -.
DR OMA; SHNAYAE; -.
DR BioCyc; YEAST:G3O-33292-MON; -.
DR PRO; PR:P48558; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P48558; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006915; P:apoptotic process; IMP:SGD.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:SGD.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:SGD.
DR InterPro; IPR006214; Bax_inhibitor_1-related.
DR PANTHER; PTHR23291; PTHR23291; 1.
DR Pfam; PF01027; Bax1-I; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Endoplasmic reticulum; Membrane; Mitochondrion;
KW Reference proteome; Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..297
FT /note="Bax inhibitor 1"
FT /id="PRO_0000203369"
FT TOPO_DOM 1..53
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..146
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..208
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..270
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 84
FT /note="S -> A (in Ref. 4; AAT92698)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 297 AA; 33645 MW; 330784DA17152BB0 CRC64;
MSGPPPPYEE QSSHLYGQPA SSQDGNAFIP EDFKYSTVVI SCEPIIRQRF MHKVYSLLSC
QLLASLSFCY WASVSTSLQN FIMSHIALFY ICMVVSLVSC IWLAVSPRPE DYEASVPEPL
LTGSSEEPAQ EQRRLPWYVL SSYKQKLTLL SIFTLSEAYC LSLVTLAYDK DTVLSALLIT
TIVVVGVSLT ALSERFENVL NSATSIYYWL NWGLWIMIGM GLTALLFGWN THSSKFNLLY
GWLGAILFTA YLFIDTQLIF RKVYPDEEVR CAMMLYLDIV NLFLSILRIL ANSNDDN
