BON1_ARATH
ID BON1_ARATH Reviewed; 578 AA.
AC Q941L3; Q9FH53;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein BONZAI 1;
DE AltName: Full=COPINE 1;
GN Name=BON1; Synonyms=CPN1; OrderedLocusNames=At5g61900; ORFNames=K22G18.2;
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INDUCTION BY HEAT, INTERACTION WITH BAP1, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=11544183; DOI=10.1101/gad.918101;
RA Hua J., Grisafi P., Cheng S.H., Fink G.R.;
RT "Plant growth homeostasis is controlled by the Arabidopsis BON1 and BAP1
RT genes.";
RL Genes Dev. 15:2263-2272(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DISRUPTION PHENOTYPE.
RX PubMed=11595798; DOI=10.2307/3871504;
RA Jambunathan N., Siani J.M., McNellis T.W.;
RT "A humidity-sensitive Arabidopsis copine mutant exhibits precocious cell
RT death and increased disease resistance.";
RL Plant Cell 13:2225-2240(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INDUCTION BY PATHOGEN; LOW HUMIDITY; AVIRULENCE GENE PRODUCT AND SALICYLIC
RP ACID, AND DISRUPTION PHENOTYPE.
RX PubMed=12857819; DOI=10.1104/pp.103.022970;
RA Jambunathan N., McNellis T.W.;
RT "Regulation of Arabidopsis COPINE 1 gene expression in response to
RT pathogens and abiotic stimuli.";
RL Plant Physiol. 132:1370-1381(2003).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15031411; DOI=10.1105/tpc.020479;
RA Yang S., Hua J.;
RT "A haplotype-specific Resistance gene regulated by BONZAI1 mediates
RT temperature-dependent growth control in Arabidopsis.";
RL Plant Cell 16:1060-1071(2004).
RN [9]
RP DOMAIN.
RX PubMed=15843967; DOI=10.1007/s00425-004-1413-4;
RA Liu J., Jambunathan N., McNellis T.W.;
RT "Transgenic expression of the von Willebrand A domain of the BONZAI
RT 1/COPINE 1 protein triggers a lesion-mimic phenotype in Arabidopsis.";
RL Planta 221:85-94(2005).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, GENE FAMILY, AND
RP NOMENCLATURE.
RX PubMed=16367962; DOI=10.1111/j.1365-313x.2005.02585.x;
RA Yang S., Yang H., Grisafi P., Sanchatjate S., Fink G.R., Sun Q., Hua J.;
RT "The BON/CPN gene family represses cell death and promotes cell growth in
RT Arabidopsis.";
RL Plant J. 45:166-179(2006).
RN [11]
RP INTERACTION WITH BAP1 AND BAP2.
RX PubMed=17631528; DOI=10.1104/pp.107.100800;
RA Yang H., Yang S., Li Y., Hua J.;
RT "The Arabidopsis BAP1 and BAP2 genes are general inhibitors of programmed
RT cell death.";
RL Plant Physiol. 145:135-146(2007).
RN [12]
RP FUNCTION.
RX PubMed=19522566; DOI=10.1094/mpmi-22-7-0840;
RA Li Y., Pennington B.O., Hua J.;
RT "Multiple R-like genes are negatively regulated by BON1 and BON3 in
RT arabidopsis.";
RL Mol. Plant Microbe Interact. 22:840-848(2009).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY PATHOGEN AND CALCIUM.
RX PubMed=18855102; DOI=10.1007/s11103-008-9413-6;
RA Lee T.F., McNellis T.W.;
RT "Evidence that the BONZAI1/COPINE1 protein is a calcium- and pathogen-
RT responsive defense suppressor.";
RL Plant Mol. Biol. 69:155-166(2009).
RN [14]
RP FUNCTION, MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2; ASP-63; ASP-69;
RP ASP-122; ASP-124; ASP-209; ASP-215; ASP-269; ALA-350; GLY-353 AND LYS-391,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20634289; DOI=10.1074/jbc.m109.066100;
RA Li Y., Gou M., Sun Q., Hua J.;
RT "Requirement of calcium binding, myristoylation, and protein-protein
RT interaction for the copine BON1 function in Arabidopsis.";
RL J. Biol. Chem. 285:29884-29891(2010).
RN [15]
RP INTERACTION WITH HSP70-1 AND HSP70-2.
RX PubMed=26408532; DOI=10.1104/pp.15.00970;
RA Gou M., Zhang Z., Zhang N., Huang Q., Monaghan J., Yang H., Shi Z.,
RA Zipfel C., Hua J.;
RT "Opposing effects on two phases of defense responses from concerted actions
RT of HEAT SHOCK COGNATE70 and BONZAI1 in Arabidopsis.";
RL Plant Physiol. 169:2304-2323(2015).
CC -!- FUNCTION: Negative regulator of cell death and defense responses.
CC Negative regulator of several R genes, including SNC1. May have effects
CC in promoting growth and development. May function in membrane
CC trafficking and in fusion of vesicles with plasma membrane at low
CC temperature. Exhibits calcium-dependent phospholipid binding
CC properties. {ECO:0000269|PubMed:15031411, ECO:0000269|PubMed:16367962,
CC ECO:0000269|PubMed:18855102, ECO:0000269|PubMed:19522566,
CC ECO:0000269|PubMed:20634289}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBUNIT: Interacts (via VWA domain) with BAP1 and BAP2
CC (PubMed:17631528). Interacts with HSP70-1 and HSP70-2
CC (PubMed:26408532). {ECO:0000269|PubMed:17631528,
CC ECO:0000269|PubMed:26408532}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}. Note=Calcium enhances the association with membranes.
CC {ECO:0000269|PubMed:11544183, ECO:0000269|PubMed:20634289}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and flowers and, at higher
CC levels, in leaves and stems. Strongly expressed in growing tissues. Not
CC detected in green siliques. {ECO:0000269|PubMed:11544183,
CC ECO:0000269|PubMed:16367962, ECO:0000269|PubMed:18855102}.
CC -!- INDUCTION: Down-regulated by high temperature. Up-regulated by
CC pathogen, calcium, low humidity, avirulence gene product avrRpt2 and
CC salicylic acid. {ECO:0000269|PubMed:11544183,
CC ECO:0000269|PubMed:12857819, ECO:0000269|PubMed:18855102}.
CC -!- DOMAIN: The N-terminus (1-116) is sufficient for plasma membrane
CC localization. VWA domain fragments interfere with the function of the
CC full-length protein, triggering a lesion-mimic phenotype.
CC {ECO:0000269|PubMed:15843967}.
CC -!- PTM: Based on mass spectrometry analysis, the N-peptide must be
CC modified and there might be additional modifications other than
CC myristoylation. {ECO:0000269|PubMed:20634289}.
CC -!- DISRUPTION PHENOTYPE: Dwarf, twisted leaves and enhanced disease
CC resistance in cv. Columbia when grown at 22 degrees Celsius. No visible
CC phenotype when grown at 28 degrees Celsius, or in cv. Landsberg erecta,
CC cv. No-0, and cv. Wassilewskija at any temperature. Humidity and
CC temperature sensitive lesion mimic phenotype, accelerated
CC hypersensitive response (HR) and increased disease resistance. Bon1 and
CC bon2 double mutants, as well as bon1 and bon3 double mutants are
CC seedling-lethal when grown at 22 degrees Celsius. bon1, bon2 and bon3
CC triple mutant is seedling-lethal at any temperature.
CC {ECO:0000269|PubMed:11544183, ECO:0000269|PubMed:11595798,
CC ECO:0000269|PubMed:12857819, ECO:0000269|PubMed:15031411,
CC ECO:0000269|PubMed:16367962}.
CC -!- MISCELLANEOUS: Overexpression of BON1 has no effects on pathogen
CC resistance.
CC -!- SIMILARITY: Belongs to the copine family. {ECO:0000305}.
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DR EMBL; AY045764; AAK98797.1; -; mRNA.
DR EMBL; AB022212; BAB08876.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97534.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97535.1; -; Genomic_DNA.
DR EMBL; AY062824; AAL32902.1; -; mRNA.
DR EMBL; BT010555; AAQ65178.1; -; mRNA.
DR EMBL; AY085339; AAM62570.1; -; mRNA.
DR RefSeq; NP_568944.1; NM_125583.4.
DR RefSeq; NP_974977.1; NM_203248.2.
DR PDB; 6KXT; X-ray; 1.25 A; A=192-326.
DR PDBsum; 6KXT; -.
DR AlphaFoldDB; Q941L3; -.
DR SMR; Q941L3; -.
DR BioGRID; 21555; 7.
DR IntAct; Q941L3; 2.
DR STRING; 3702.AT5G61900.3; -.
DR iPTMnet; Q941L3; -.
DR SwissPalm; Q941L3; -.
DR PaxDb; Q941L3; -.
DR PRIDE; Q941L3; -.
DR EnsemblPlants; AT5G61900.1; AT5G61900.1; AT5G61900.
DR EnsemblPlants; AT5G61900.3; AT5G61900.3; AT5G61900.
DR GeneID; 836311; -.
DR Gramene; AT5G61900.1; AT5G61900.1; AT5G61900.
DR Gramene; AT5G61900.3; AT5G61900.3; AT5G61900.
DR KEGG; ath:AT5G61900; -.
DR Araport; AT5G61900; -.
DR TAIR; locus:2156186; AT5G61900.
DR eggNOG; KOG1327; Eukaryota.
DR HOGENOM; CLU_020452_3_1_1; -.
DR InParanoid; Q941L3; -.
DR PhylomeDB; Q941L3; -.
DR PRO; PR:Q941L3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR Genevisible; Q941L3; AT.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071277; P:cellular response to calcium ion; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:TAIR.
DR GO; GO:0045793; P:positive regulation of cell size; IMP:TAIR.
DR GO; GO:0009270; P:response to humidity; IMP:TAIR.
DR GO; GO:0009266; P:response to temperature stimulus; IEP:TAIR.
DR CDD; cd04047; C2B_Copine; 1.
DR CDD; cd01459; vWA_copine_like; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR031116; BONZAI.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037768; C2B_Copine.
DR InterPro; IPR045052; Copine.
DR InterPro; IPR010734; Copine_C.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10857; PTHR10857; 1.
DR PANTHER; PTHR10857:SF116; PTHR10857:SF116; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF07002; Copine; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Lipoprotein; Membrane; Metal-binding;
KW Myristate; Plant defense; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:20634289"
FT CHAIN 2..578
FT /note="Protein BONZAI 1"
FT /id="PRO_0000399468"
FT DOMAIN 26..163
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 176..303
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 341..560
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000305|PubMed:20634289"
FT MUTAGEN 2
FT /note="G->A: Loss of function and altered targeting."
FT /evidence="ECO:0000269|PubMed:20634289"
FT MUTAGEN 63
FT /note="D->A: No effect. No effect; when associated with A-
FT 69. Loss of function; when associated with A-69; A-122 and
FT A-124. Loss of function, but no effect on targeting; when
FT associated with A-69; A-122; A-124; A-209; A-215 and A-
FT 269."
FT /evidence="ECO:0000269|PubMed:20634289"
FT MUTAGEN 69
FT /note="D->A: No effect; when associated with A-63. Loss of
FT function; when associated with A-63; A-122 and A-124. Loss
FT of function, but no effect on targeting; when associated
FT with A-63; A-122; A-124; A-209; A-215 and A-269."
FT /evidence="ECO:0000269|PubMed:20634289"
FT MUTAGEN 122
FT /note="D->A: No effect; when associated with A-124. No
FT effect; when associated with A-269. Loss of function; when
FT associated with A-63; A-69 and A-124. Loss of function, but
FT no effect on targeting; when associated with A-63; A-69; A-
FT 124; A-209; A-215 and A-269."
FT /evidence="ECO:0000269|PubMed:20634289"
FT MUTAGEN 124
FT /note="D->A: No effect; when associated with A-122. Loss of
FT function; when associated with A-63; A-69 and A-122. Loss
FT of function, but no effect on targeting; when associated
FT with A-63; A-69; A-122; A-209; A-215 and A-269."
FT /evidence="ECO:0000269|PubMed:20634289"
FT MUTAGEN 209
FT /note="D->A: No effect; when associated with A-215. Loss of
FT function; when associated with A-215 and A-269. Loss of
FT function, but no effect on targeting; when associated with
FT A-63; A-69; A-122; A-124; A-215 and A-269."
FT /evidence="ECO:0000269|PubMed:20634289"
FT MUTAGEN 215
FT /note="D->A: No effect; when associated with A-209. Loss of
FT function; when associated with A-209 and A-269. Loss of
FT function, but no effect on targeting; when associated with
FT A-63; A-69; A-122; A-124; A-209 and A-269."
FT /evidence="ECO:0000269|PubMed:20634289"
FT MUTAGEN 269
FT /note="D->A: No effect. No effect; when associated with A-
FT 122. Loss of function; when associated with A-209 and A-
FT 215. Loss of function, but no effect on targeting; when
FT associated with A-63; A-69; A-122; A-124; A-209 and A-215."
FT /evidence="ECO:0000269|PubMed:20634289"
FT MUTAGEN 350
FT /note="A->V: Loss of function and reduced interaction with
FT BAP1; when associated with A-353."
FT /evidence="ECO:0000269|PubMed:20634289"
FT MUTAGEN 353
FT /note="G->A: Loss of function and reduced interaction with
FT BAP1; when associated with V-350."
FT /evidence="ECO:0000269|PubMed:20634289"
FT MUTAGEN 391
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:20634289"
FT MUTAGEN 391
FT /note="K->NAAIRS: Loss of function and loss of interaction
FT with BAP1."
FT /evidence="ECO:0000269|PubMed:20634289"
FT CONFLICT 421
FT /note="E -> Q (in Ref. 1; AAK98797)"
FT /evidence="ECO:0000305"
FT STRAND 195..203
FT /evidence="ECO:0007829|PDB:6KXT"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:6KXT"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:6KXT"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:6KXT"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:6KXT"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:6KXT"
FT STRAND 277..284
FT /evidence="ECO:0007829|PDB:6KXT"
FT HELIX 286..295
FT /evidence="ECO:0007829|PDB:6KXT"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:6KXT"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:6KXT"
FT STRAND 311..325
FT /evidence="ECO:0007829|PDB:6KXT"
SQ SEQUENCE 578 AA; 63120 MW; 61CA6FAF1DAAA30F CRC64;
MGNCCSDVAS GAGATAGVGG SGSSAALGAT NDALDYYLKS KGFNGLFSQI ELSFSASNLR
DRDVLSKSDP MVVVYQKEKD ATLSEVFRSE VVLNSLAPKW IKKFIVAYHF ETVQTLVFRV
YDVDTKFQNS REEMLKLDEQ QFLGEATCAL SEIITKSTRT STLELKRKDG FAPQAQPHHG
KLIIHAEESL ASKISTEIVF RCSNLESKDL FSKSDPFLVV SKIVEHGTPI PVSKTEVRKN
DLNPIWKPVF LSVQQVGSKD SPVIIECSDF NSNGKHSLIG KVQKSLSDLE KLHLAGQGIN
FSLPTGAGQN KVLKSQLFVD KFTETVHHTF LEYLASGFEL NFMVAIDFTA SNGNPRLPDS
LHYIDPSGRL NAYQRAIMDV GEVLQFYDSD KRFPAWGFGA RPIDAPVSHC FNLNGSSSYS
EVDGIQGIMT SYTSALFNVS LAGPTLFGPV INAAAMIASA SLAQGSRKYY VLLIITDGVI
TDLQETKDAL VSASDLPLSI LIVGVGGADF KEMEILDADK GERLESSSGR LASRDIVQFV
ALRDVQYGEI SVVQALLAEL PSQFLTYMRI RNMKPIPP
