BI1_MOUSE
ID BI1_MOUSE Reviewed; 237 AA.
AC Q9D2C7; Q3TX81; Q8BFY4;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Bax inhibitor 1;
DE Short=BI-1;
DE AltName: Full=Testis-enhanced gene transcript protein;
DE AltName: Full=Transmembrane BAX inhibitor motif-containing protein 6;
GN Name=Tmbim6; Synonyms=Tegt;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Egg, Liver, Ovary, Spinal cord, Thymus, and Uterus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 TISSUE SPECIFICITY.
RX PubMed=8012111; DOI=10.1007/bf00360548;
RA Walter L., Dirks B., Rothermel E., Heyens M., Szpirer C., Levan G.,
RA Guenther E.;
RT "A novel, conserved gene of the rat that is developmentally regulated in
RT the testis.";
RL Mamm. Genome 5:216-221(1994).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 [5]
RP FUNCTION, AND INTERACTION WITH BCL2L1.
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 (By similarity). Modulates ER calcium
CC homeostasis by acting as a calcium-leak channel (By similarity).
CC Negatively regulates autophagy and autophagosome formation, especially
CC during periods of nutrient deprivation, and reduces cell survival
CC during starvation (PubMed:21926971). {ECO:0000250|UniProtKB:P55061,
CC ECO:0000269|PubMed:21926971}.
CC -!- SUBUNIT: Interacts with BCL2 (By similarity). Interacts with BCL2L1
CC (PubMed:21926971). {ECO:0000250|UniProtKB:P55061,
CC 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 -!- TISSUE SPECIFICITY: Highly abundant in adult testis.
CC {ECO:0000269|PubMed:8012111}.
CC -!- DOMAIN: The intra-membrane loop at the C-terminus acts as a calcium
CC pore, mediating calcium leak from the ER into the cytosol.
CC {ECO:0000250|UniProtKB:P55061}.
CC -!- SIMILARITY: Belongs to the BI1 family. {ECO:0000305}.
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DR EMBL; AK019865; BAB31892.1; -; mRNA.
DR EMBL; AK036782; BAC29575.1; -; mRNA.
DR EMBL; AK036994; BAC29662.1; -; mRNA.
DR EMBL; AK049604; BAC33837.1; -; mRNA.
DR EMBL; AK050299; BAC34174.1; -; mRNA.
DR EMBL; AK050323; BAC34188.1; -; mRNA.
DR EMBL; AK088030; BAC40107.1; -; mRNA.
DR EMBL; AK088683; BAC40503.1; -; mRNA.
DR EMBL; AK139901; BAE24176.1; -; mRNA.
DR EMBL; AK159380; BAE35035.1; -; mRNA.
DR EMBL; AK166935; BAE39128.1; -; mRNA.
DR EMBL; BC005588; AAH05588.1; -; mRNA.
DR CCDS; CCDS37201.1; -.
DR RefSeq; NP_001164505.1; NM_001171034.1.
DR RefSeq; NP_001164506.1; NM_001171035.1.
DR RefSeq; NP_001164507.1; NM_001171036.1.
DR RefSeq; NP_080945.1; NM_026669.4.
DR AlphaFoldDB; Q9D2C7; -.
DR SMR; Q9D2C7; -.
DR BioGRID; 225393; 3.
DR IntAct; Q9D2C7; 1.
DR STRING; 10090.ENSMUSP00000023749; -.
DR iPTMnet; Q9D2C7; -.
DR PhosphoSitePlus; Q9D2C7; -.
DR jPOST; Q9D2C7; -.
DR MaxQB; Q9D2C7; -.
DR PaxDb; Q9D2C7; -.
DR PRIDE; Q9D2C7; -.
DR ProteomicsDB; 273609; -.
DR Antibodypedia; 26071; 218 antibodies from 23 providers.
DR DNASU; 110213; -.
DR Ensembl; ENSMUST00000023749; ENSMUSP00000023749; ENSMUSG00000023010.
DR Ensembl; ENSMUST00000159209; ENSMUSP00000125117; ENSMUSG00000023010.
DR Ensembl; ENSMUST00000159531; ENSMUSP00000125318; ENSMUSG00000023010.
DR Ensembl; ENSMUST00000160635; ENSMUSP00000124651; ENSMUSG00000023010.
DR Ensembl; ENSMUST00000161250; ENSMUSP00000125563; ENSMUSG00000023010.
DR GeneID; 110213; -.
DR KEGG; mmu:110213; -.
DR UCSC; uc007xpm.2; mouse.
DR CTD; 7009; -.
DR MGI; MGI:99682; Tmbim6.
DR VEuPathDB; HostDB:ENSMUSG00000023010; -.
DR eggNOG; KOG1629; Eukaryota.
DR GeneTree; ENSGT01050000244940; -.
DR HOGENOM; CLU_061277_0_1_1; -.
DR InParanoid; Q9D2C7; -.
DR OMA; MGDVIGM; -.
DR OrthoDB; 1275249at2759; -.
DR PhylomeDB; Q9D2C7; -.
DR TreeFam; TF323395; -.
DR BioGRID-ORCS; 110213; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Tmbim6; mouse.
DR PRO; PR:Q9D2C7; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9D2C7; protein.
DR Bgee; ENSMUSG00000023010; Expressed in lacrimal gland and 248 other tissues.
DR ExpressionAtlas; Q9D2C7; baseline and differential.
DR Genevisible; Q9D2C7; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0060698; F:endoribonuclease inhibitor activity; IMP:ParkinsonsUK-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0034620; P:cellular response to unfolded protein; IMP:ParkinsonsUK-UCL.
DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IDA:MGI.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IDA:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0010523; P:negative regulation of calcium ion transport into cytosol; ISO:MGI.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IGI:MGI.
DR GO; GO:0060702; P:negative regulation of endoribonuclease activity; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903298; P:negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0002638; P:negative regulation of immunoglobulin production; IMP:ParkinsonsUK-UCL.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0033119; P:negative regulation of RNA splicing; IMP:ParkinsonsUK-UCL.
DR GO; GO:1990441; P:negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL.
DR GO; GO:0036483; P:neuron intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:MGI.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL.
DR GO; GO:1902065; P:response to L-glutamate; ISO:MGI.
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 1: Evidence at protein level;
KW Apoptosis; Autophagy; Calcium; Endoplasmic reticulum; Isopeptide bond;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Ubl conjugation; Unfolded protein response.
FT CHAIN 1..237
FT /note="Bax inhibitor 1"
FT /id="PRO_0000179079"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..52
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..112
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..166
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P55061"
FT CONFLICT 93
FT /note="F -> Y (in Ref. 1; BAC29575/BAC29662)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 237 AA; 26478 MW; 788E6EE7EB34AFFC CRC64;
MNIFDRKINF DALLKFSHIT PSTQQHLKKV YASFALCMFV AAAGAYVHVV THFIQAGLLS
ALGSLALMIW LMATPHSHET EQKRLGLLAG FAFLTGVGLG PALELCIAVN PSILPTAFMG
TAMIFTCFSL SALYARRRSY LFLGGILMSA MSLMLLSSLG NLFFGSIWLF QANLYLGLLV
MCGFVLFDTQ LIIEKAEHGD KDYIWHCVDL FLDFVTLFRK LMLILAFNEK DKKKEKK
