BI1_PIG
ID BI1_PIG Reviewed; 237 AA.
AC Q66RM2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 64.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kim J.-Y., Kim J.-H., Jeong M.-Y., Cho S.-G.;
RT "Eukaryotic homologs of Bax inhibitor-1 (BI-1) suppresses Bax- and hydrogen
RT peroxide-induced cell death in endothelial cell lines.";
RL Submitted (AUG-2004) 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; AY713975; AAU05320.1; -; mRNA.
DR RefSeq; NP_001005348.1; NM_001005348.1.
DR AlphaFoldDB; Q66RM2; -.
DR SMR; Q66RM2; -.
DR STRING; 9823.ENSSSCP00000026427; -.
DR PaxDb; Q66RM2; -.
DR PeptideAtlas; Q66RM2; -.
DR GeneID; 396907; -.
DR KEGG; ssc:396907; -.
DR CTD; 7009; -.
DR eggNOG; KOG1629; Eukaryota.
DR InParanoid; Q66RM2; -.
DR OrthoDB; 1275249at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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: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:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0060702; P:negative regulation of endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0033119; P:negative regulation of RNA splicing; IBA:GO_Central.
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..237
FT /note="Bax inhibitor 1"
FT /id="PRO_0000179080"
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"
SQ SEQUENCE 237 AA; 26408 MW; A303792CAF79E49F CRC64;
MNIFDRKINF DALLKFSHIT PSTQQHLKKV YASFALCMFV AAAGAYVHVV TRFIQAGLLS
ALGSLGLMIW LMATPHSHET EQKRLGLLAG FAFLTGVGLG PALDLCIAIN PSILPTAFMG
TAMIFTCFTL SALYARRRSY LFLGGILMSA MSLMVLSSLG NLFFGSIWLF QANLYVGLVV
MCGFVLFDTQ LIIEKAENGD KDYIWHCVDL FSDFVTLFRK LMMILAMNEK DKKKEKK
