BON3_ARATH
ID BON3_ARATH Reviewed; 584 AA.
AC Q5XQC7; O04042; Q1KS96;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein BONZAI 3;
GN Name=BON3; OrderedLocusNames=At1g08860; ORFNames=F7G19.25;
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], FUNCTION, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, GENE FAMILY, AND 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
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 [6]
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).
CC -!- FUNCTION: Negative regulator of cell death and defense responses.
CC Repress a number of R genes and may have effects in promoting growth
CC and development. May function in membrane trafficking and in fusion of
CC vesicles with plasma membrane (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:16367962, ECO:0000269|PubMed:19522566}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBUNIT: Interacts with BAP1 and BAP2. {ECO:0000269|PubMed:17631528}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed at an extremely low level.
CC {ECO:0000269|PubMed:16367962}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due to partial redundancy
CC with BON1 and BON2. Bon2 and bon3 double mutant has no visible
CC phenotype. bon1 and bon3 double mutant is seedling-lethal when grown at
CC 22 degrees Celsius. Bon1, bon2 and bon3 triple mutant is seedling-
CC lethal at any temperature. {ECO:0000269|PubMed:16367962}.
CC -!- SIMILARITY: Belongs to the copine family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB70417.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABE97164.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY741136; AAU89273.1; -; mRNA.
DR EMBL; AC000106; AAB70417.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28360.1; -; Genomic_DNA.
DR EMBL; DQ459165; ABE97164.1; ALT_FRAME; mRNA.
DR PIR; D86220; D86220.
DR RefSeq; NP_172362.3; NM_100759.4.
DR AlphaFoldDB; Q5XQC7; -.
DR SMR; Q5XQC7; -.
DR BioGRID; 22649; 1.
DR IntAct; Q5XQC7; 2.
DR STRING; 3702.AT1G08860.1; -.
DR PaxDb; Q5XQC7; -.
DR PRIDE; Q5XQC7; -.
DR ProteomicsDB; 240408; -.
DR EnsemblPlants; AT1G08860.1; AT1G08860.1; AT1G08860.
DR GeneID; 837408; -.
DR Gramene; AT1G08860.1; AT1G08860.1; AT1G08860.
DR KEGG; ath:AT1G08860; -.
DR Araport; AT1G08860; -.
DR TAIR; locus:2036074; AT1G08860.
DR eggNOG; KOG1327; Eukaryota.
DR HOGENOM; CLU_020452_3_1_1; -.
DR InParanoid; Q5XQC7; -.
DR OMA; EMAAQCV; -.
DR OrthoDB; 1067545at2759; -.
DR PhylomeDB; Q5XQC7; -.
DR PRO; PR:Q5XQC7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q5XQC7; baseline and differential.
DR Genevisible; Q5XQC7; AT.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
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:0090332; P:stomatal closure; IMP: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:SF120; PTHR10857:SF120; 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 Calcium; Cell membrane; Lipoprotein; Membrane; Metal-binding; Myristate;
KW Plant defense; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..584
FT /note="Protein BONZAI 3"
FT /id="PRO_0000399470"
FT DOMAIN 34..167
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 178..305
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 344..563
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 584 AA; 64202 MW; C0FFBD7A478352DD CRC64;
MGGCLSGDVK GGKQAIGGVQ QRPTSSTIAN NAAHNDAVDF FFRSRGQYPL FSQIELTLSA
SNLLDCDITS KSDPMAVMYL RKKDGRLEEI GRTEVILNNL NPKWIEKITV SFQFEAVQTL
VFHVYDVDTR YHNVPVKTLK LKDQDFLGEG TCVLSEIMTR QNRTLTLTLT GNVRAGVNRN
LGTLSIQAEE TVASKTVAEI NFRCVNLDNK DLFSKSDPFL RISRVVETSA AVPICRTEVV
DNNLNPMWRP VCLTMQQFGS KDTPLVIECL DFNTSGNHEL IGKTEKSVAE LERLCLQKEA
ANFVYPSLSH GRNKVLKGQL IVDRYVEKVQ YSFLDYISSG FELNFMVAVD FTASNGDPRT
PSSLHYIDPS GRLNSYQQAI MEVGEVIQFY DSDKRFPAWG FGGRTSDGSV SHAFNLNGAS
YGDEVVGVEG IMVAYASALR NVSLAGPTLF SNVVDKAAHT ASQSLSQNSP KYFVLLIITD
GVLTDMAGTV DALVRASDLP LSVLIVGVGN TDFKQMEMLD ADNGRRLESS TGRIATRDIV
QFVPMKDIHS GLVSVVQALL EELPGQFLTY VRSRKINPIG APAI
