BI1_BOVIN
ID BI1_BOVIN Reviewed; 236 AA.
AC Q0V882;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Suppressor of apoptosis. Modulates unfolded protein response
CC signaling. Modulates ER calcium homeostasis by acting as a calcium-leak
CC channel. Negatively regulates autophagy and autophagosome formation,
CC especially during periods of nutrient deprivation, and reduces cell
CC survival during starvation. {ECO:0000250|UniProtKB:P55061,
CC ECO:0000250|UniProtKB:Q9D2C7}.
CC -!- SUBUNIT: Interacts with BCL2. Interacts with BCL2L1.
CC {ECO:0000250|UniProtKB:P55061, ECO:0000250|UniProtKB:Q9D2C7}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P55061}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P55061}.
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; BT026337; ABG81493.1; -; mRNA.
DR EMBL; BC149995; AAI49996.1; -; mRNA.
DR RefSeq; NP_001069882.1; NM_001076414.1.
DR AlphaFoldDB; Q0V882; -.
DR SMR; Q0V882; -.
DR STRING; 9913.ENSBTAP00000043666; -.
DR PaxDb; Q0V882; -.
DR PRIDE; Q0V882; -.
DR Ensembl; ENSBTAT00000046359; ENSBTAP00000043666; ENSBTAG00000018588.
DR GeneID; 616210; -.
DR KEGG; bta:616210; -.
DR CTD; 7009; -.
DR VEuPathDB; HostDB:ENSBTAG00000018588; -.
DR VGNC; VGNC:35916; TMBIM6.
DR eggNOG; KOG1629; Eukaryota.
DR GeneTree; ENSGT01050000244940; -.
DR HOGENOM; CLU_061277_0_1_1; -.
DR InParanoid; Q0V882; -.
DR OMA; MGDVIGM; -.
DR OrthoDB; 1275249at2759; -.
DR TreeFam; TF323395; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000018588; Expressed in thyroid gland and 104 other tissues.
DR ExpressionAtlas; Q0V882; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0060698; F:endoribonuclease inhibitor activity; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IEA:Ensembl.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0010523; P:negative regulation of calcium ion transport into cytosol; IEA:Ensembl.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0060702; P:negative regulation of endoribonuclease activity; IBA:GO_Central.
DR GO; GO:1903298; P:negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0002638; P:negative regulation of immunoglobulin production; IEA:Ensembl.
DR GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
DR GO; GO:0033119; P:negative regulation of RNA splicing; IBA:GO_Central.
DR GO; GO:1990441; P:negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IEA:Ensembl.
DR GO; GO:1902065; P:response to L-glutamate; IEA:Ensembl.
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; Calcium; Endoplasmic reticulum; Isopeptide bond;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Ubl conjugation; Unfolded protein response.
FT CHAIN 1..236
FT /note="Bax inhibitor 1"
FT /id="PRO_0000327214"
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..236
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"
SQ SEQUENCE 236 AA; 26366 MW; FD84289821CCC22A CRC64;
MNIFDRKINF DALFKFSHIT PSTQQHLKKV YASFALCMFV AAAGAYIHVV THFIQAGLLS
ALGSLGLMIW LMATPHSHET EQKRLGLLAG FAFLTGVGLG PALDLCIAIN PSILPTAFMG
TAMIFTCFTL SALYARRRSY LFLGGILMSA MSLMLLSSLG NLFFGSVWLF QANLYMGLVV
MCGFVLFDTQ LIIEKAENGD KDYIWHCVDL FLDFVTLFRK LMMILAMNEK DKKKKK
