BI1_RAT
ID BI1_RAT Reviewed; 237 AA.
AC P55062; Q64712; Q6PDV4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 130.
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=Bi1, Tegt;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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).
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 -!- TISSUE SPECIFICITY: Highly abundant in adult testis.
CC {ECO:0000269|PubMed:8012111}.
CC -!- DEVELOPMENTAL STAGE: During spermatogenesis, it is mainly expressed
CC postmeiotically. {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; X75855; CAA53470.1; -; mRNA.
DR EMBL; X75856; CAA53471.1; -; mRNA.
DR EMBL; BC058478; AAH58478.1; -; mRNA.
DR PIR; S42069; S42069.
DR RefSeq; NP_062254.2; NM_019381.2.
DR RefSeq; XP_006257385.1; XM_006257323.3.
DR AlphaFoldDB; P55062; -.
DR SMR; P55062; -.
DR STRING; 10116.ENSRNOP00000048834; -.
DR PaxDb; P55062; -.
DR GeneID; 24822; -.
DR KEGG; rno:24822; -.
DR UCSC; RGD:3842; rat.
DR CTD; 7009; -.
DR RGD; 3842; Tmbim6.
DR VEuPathDB; HostDB:ENSRNOG00000055579; -.
DR eggNOG; KOG1629; Eukaryota.
DR HOGENOM; CLU_061277_0_1_1; -.
DR InParanoid; P55062; -.
DR PhylomeDB; P55062; -.
DR PRO; PR:P55062; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000055579; Expressed in adult mammalian kidney and 19 other tissues.
DR ExpressionAtlas; P55062; baseline and differential.
DR Genevisible; P55062; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
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:RGD.
DR GO; GO:0060698; F:endoribonuclease inhibitor activity; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0034620; P:cellular response to unfolded protein; ISO:RGD.
DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; ISO:RGD.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0030324; P:lung development; IEP:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0010523; P:negative regulation of calcium ion transport into cytosol; ISO:RGD.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0060702; P:negative regulation of endoribonuclease activity; ISO:RGD.
DR GO; GO:1903298; P:negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0002638; P:negative regulation of immunoglobulin production; ISO:RGD.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:RGD.
DR GO; GO:0033119; P:negative regulation of RNA splicing; ISO:RGD.
DR GO; GO:1990441; P:negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:1902065; P:response to L-glutamate; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
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_0000179082"
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 90..91
FT /note="GF -> V (in Ref. 1; CAA53470/CAA53471)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 237 AA; 26464 MW; F04FCDD8877B758B CRC64;
MNIFDRKINF DALLKFSHIT PSTQQHLKKV YASFALCMFV AAAGAYVHVV TRFIQAGLLS
ALGALALMIC LMATPHSHET EQKRLGLLAG FAFLTGVGLG PALELCIAIN PSILPTAFMG
TAMIFTCFSL SALYARRRSY LFLGGILMSA MSLMFVSSLG NLFFGSIWLF QANLYMGLLV
MCGFVLFDTQ LIIEKAEHGD KDYIWHCIDL FLDFVTLFRK LMLILAFNEK DKKKEKK
