BI1_ARATH
ID BI1_ARATH Reviewed; 247 AA.
AC Q9LD45;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Bax inhibitor 1;
DE Short=AtBI-1;
DE Short=BI-1;
GN Name=BI-1; OrderedLocusNames=At5g47120; ORFNames=K14A3.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=10618494; DOI=10.1016/s0014-5793(99)01695-6;
RA Kawai M., Pan L., Reed J.C., Uchimiya H.;
RT "Evolutionally conserved plant homologue of the Bax inhibitor-1 (BI-1) gene
RT capable of suppressing Bax-induced cell death in yeast.";
RL FEBS Lett. 464:143-147(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=10758491; DOI=10.1046/j.1365-313x.2000.00690.x;
RA Sanchez P., de Torres-Zabala M., Grant M.;
RT "AtBI-1, a plant homologue of Bax inhibitor-1, suppresses Bax-induced cell
RT death in yeast and is rapidly upregulated during wounding and pathogen
RT challenge.";
RL Plant J. 21:393-399(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY HEAT-SHOCK AND MYCOTOXIN.
RX PubMed=16507080; DOI=10.1111/j.1365-313x.2006.02654.x;
RA Watanabe N., Lam E.;
RT "Arabidopsis Bax inhibitor-1 functions as an attenuator of biotic and
RT abiotic types of cell death.";
RL Plant J. 45:884-894(2006).
RN [7]
RP INTERACTION WITH CALMODULIN.
RX PubMed=17142482; DOI=10.1104/pp.106.090878;
RA Ihara-Ohori Y., Nagano M., Muto S., Uchimiya H., Kawai-Yamada M.;
RT "Cell death suppressor Arabidopsis bax inhibitor-1 is associated with
RT calmodulin binding and ion homeostasis.";
RL Plant Physiol. 143:650-660(2007).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18039663; DOI=10.1074/jbc.m706659200;
RA Watanabe N., Lam E.;
RT "BAX inhibitor-1 modulates endoplasmic reticulum stress-mediated programmed
RT cell death in Arabidopsis.";
RL J. Biol. Chem. 283:3200-3210(2008).
RN [9]
RP INTERACTION WITH CALMODULIN, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND
RP INDUCTION BY PATHOGEN.
RX PubMed=19674971; DOI=10.1074/jbc.m109.037234;
RA Kawai-Yamada M., Hori Z., Ogawa T., Ihara-Ohori Y., Tamura K., Nagano M.,
RA Ishikawa T., Uchimiya H.;
RT "Loss of calmodulin binding to Bax inhibitor-1 affects Pseudomonas-mediated
RT hypersensitive response-associated cell death in Arabidopsis thaliana.";
RL J. Biol. Chem. 284:27998-28003(2009).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CYTB5-B.
RX PubMed=19054355; DOI=10.1111/j.1365-313x.2008.03765.x;
RA Nagano M., Ihara-Ohori Y., Imai H., Inada N., Fujimoto M., Tsutsumi N.,
RA Uchimiya H., Kawai-Yamada M.;
RT "Functional association of cell death suppressor, Arabidopsis Bax
RT inhibitor-1, with fatty acid 2-hydroxylation through cytochrome b(5).";
RL Plant J. 58:122-134(2009).
RN [11]
RP INDUCTION BY WATER STRESS, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=20298483; DOI=10.1111/j.1469-8137.2010.03207.x;
RA Duan Y., Zhang W., Li B., Wang Y., Li K., Sodmergen X., Han C., Zhang Y.,
RA Li X.;
RT "An endoplasmic reticulum response pathway mediates programmed cell death
RT of root tip induced by water stress in Arabidopsis.";
RL New Phytol. 186:681-695(2010).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=22563118; DOI=10.1093/jxb/ers122;
RA Yue H., Nie S., Xing D.;
RT "Over-expression of Arabidopsis Bax inhibitor-1 delays methyl jasmonate-
RT induced leaf senescence by suppressing the activation of MAP kinase 6.";
RL J. Exp. Bot. 63:4463-4474(2012).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP INTERACTION WITH CYTB5-D.
RC STRAIN=cv. Columbia;
RX PubMed=22635113; DOI=10.1104/pp.112.199547;
RA Nagano M., Takahara K., Fujimoto M., Tsutsumi N., Uchimiya H.,
RA Kawai-Yamada M.;
RT "Arabidopsis sphingolipid fatty acid 2-hydroxylases (AtFAH1 and AtFAH2) are
RT functionally differentiated in fatty acid 2-hydroxylation and stress
RT responses.";
RL Plant Physiol. 159:1138-1148(2012).
CC -!- FUNCTION: Suppressor of apoptosis. Modulator of endoplasmic reticulum
CC stress-mediated programmed cell death. Involved in methyl jasmonate-
CC induced leaf senescence through regulating cytoplasmic calcium level.
CC {ECO:0000269|PubMed:16507080, ECO:0000269|PubMed:18039663,
CC ECO:0000269|PubMed:22563118}.
CC -!- SUBUNIT: Interacts (via C-terminus) with calmodulin, CYTB5-B and CYTB5-
CC D. Interacts indirectly with FAH1 via CYTB5-D.
CC {ECO:0000269|PubMed:17142482, ECO:0000269|PubMed:19054355,
CC ECO:0000269|PubMed:19674971, ECO:0000269|PubMed:22635113}.
CC -!- INTERACTION:
CC Q9LD45; P59220: CAM7; NbExp=2; IntAct=EBI-1644586, EBI-1236031;
CC Q9LD45; O48845: CYTB5-B; NbExp=5; IntAct=EBI-1644586, EBI-2295402;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19054355}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19054355}.
CC -!- TISSUE SPECIFICITY: Expressed in root tips, root vasculature, flower
CC tissues, including stamens and sepals, and in the base of siliques. Not
CC detected in mature leaves. {ECO:0000269|PubMed:19674971}.
CC -!- INDUCTION: Up-regulated by water stress, heat-shock, mycotoxin and
CC pathogens. {ECO:0000269|PubMed:16507080, ECO:0000269|PubMed:19674971,
CC ECO:0000269|PubMed:20298483}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. Accelerated methyl jasmonate-induced leaf senescence.
CC Enhanced sensitivity to water stress, heat shock, toxin, tunicamycin
CC and pathogens. {ECO:0000269|PubMed:16507080,
CC ECO:0000269|PubMed:18039663, ECO:0000269|PubMed:19674971,
CC ECO:0000269|PubMed:20298483, ECO:0000269|PubMed:22563118}.
CC -!- SIMILARITY: Belongs to the BI1 family. {ECO:0000305}.
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DR EMBL; AB025927; BAA89541.2; -; mRNA.
DR EMBL; AF208124; AAG35727.1; -; mRNA.
DR EMBL; AB025609; BAA98107.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95473.1; -; Genomic_DNA.
DR EMBL; AY091134; AAM14083.1; -; mRNA.
DR EMBL; AY114059; AAM45107.1; -; mRNA.
DR PIR; T52449; T52449.
DR RefSeq; NP_199523.1; NM_124083.3.
DR AlphaFoldDB; Q9LD45; -.
DR SMR; Q9LD45; -.
DR BioGRID; 20006; 9.
DR IntAct; Q9LD45; 8.
DR STRING; 3702.AT5G47120.1; -.
DR iPTMnet; Q9LD45; -.
DR PaxDb; Q9LD45; -.
DR PRIDE; Q9LD45; -.
DR ProteomicsDB; 240372; -.
DR EnsemblPlants; AT5G47120.1; AT5G47120.1; AT5G47120.
DR GeneID; 834758; -.
DR Gramene; AT5G47120.1; AT5G47120.1; AT5G47120.
DR KEGG; ath:AT5G47120; -.
DR Araport; AT5G47120; -.
DR TAIR; locus:2151977; AT5G47120.
DR eggNOG; KOG1629; Eukaryota.
DR HOGENOM; CLU_061277_1_0_1; -.
DR InParanoid; Q9LD45; -.
DR OMA; MDYVISI; -.
DR OrthoDB; 1275249at2759; -.
DR PhylomeDB; Q9LD45; -.
DR PRO; PR:Q9LD45; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LD45; baseline and differential.
DR Genevisible; Q9LD45; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
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:0005635; C:nuclear envelope; IDA:TAIR.
DR GO; GO:0006983; P:ER overload response; IMP:TAIR.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0043069; P:negative regulation of programmed cell death; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IDA:TAIR.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IMP:TAIR.
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 Acetylation; Apoptosis; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..247
FT /note="Bax inhibitor 1"
FT /id="PRO_0000179085"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 247 AA; 27483 MW; FD3AAEA713363945 CRC64;
MDAFSSFFDS QPGSRSWSYD SLKNFRQISP AVQNHLKRVY LTLCCALVAS AFGAYLHVLW
NIGGILTTIG CIGTMIWLLS CPPYEHQKRL SLLFVSAVLE GASVGPLIKV AIDVDPSILI
TAFVGTAIAF VCFSAAAMLA RRREYLYLGG LLSSGLSMLM WLQFASSIFG GSASIFKFEL
YFGLLIFVGY MVVDTQEIIE KAHLGDMDYV KHSLTLFTDF VAVFVRILII MLKNSADKEE
KKKKRRN
