BI1_PONAB
ID BI1_PONAB Reviewed; 237 AA.
AC Q5R7R1; Q5R8G2; Q5R937;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RG The German cDNA consortium;
RL Submitted (NOV-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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH91723.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR859558; CAH91723.1; ALT_INIT; mRNA.
DR EMBL; CR859790; CAH91948.1; -; mRNA.
DR EMBL; CR860051; CAH92199.1; -; mRNA.
DR RefSeq; NP_001126131.1; NM_001132659.1.
DR RefSeq; NP_001128831.1; NM_001135359.1.
DR AlphaFoldDB; Q5R7R1; -.
DR SMR; Q5R7R1; -.
DR STRING; 9601.ENSPPYP00000005131; -.
DR Ensembl; ENSPPYT00000005332; ENSPPYP00000005131; ENSPPYG00000004495.
DR GeneID; 100173088; -.
DR KEGG; pon:100173088; -.
DR CTD; 7009; -.
DR eggNOG; KOG1629; Eukaryota.
DR GeneTree; ENSGT01050000244940; -.
DR HOGENOM; CLU_061277_0_1_1; -.
DR InParanoid; Q5R7R1; -.
DR OMA; MGDVIGM; -.
DR OrthoDB; 1275249at2759; -.
DR TreeFam; TF323395; -.
DR Proteomes; UP000001595; Chromosome 12.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
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_0000179081"
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 1
FT /note="M -> V (in Ref. 1; CAH91723)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="M -> T (in Ref. 1; CAH92199)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 237 AA; 26550 MW; 5A98C63225474CD6 CRC64;
MNIFDRKINF DALLKFSHIT PSTQQHLKKV YASFALCMFV AAAGAYVHVV THFIQAGLLS
ALGSLILMIW LMATPHSHET EQKRLGLLAG FAFLTGVGLG PALEFCITVN PSILPTAFMG
TAMIFTCFTL SALYARRRSY LFLGGILMSA LSLLLLSSLG NVFFGSIWLF QANLYVGLVV
MCGFVLFDTQ LIIEKAEHGD QDYIWHCIDL FLDFITLFRK LMMILAMNEK DKKKEKK
