BON2_ARATH
ID BON2_ARATH Reviewed; 586 AA.
AC Q5S1W2; Q94EW4; Q9LY30;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Protein BONZAI 2;
GN Name=BON2; OrderedLocusNames=At5g07300; ORFNames=T2I1.10;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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=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 [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).
CC -!- FUNCTION: Negative regulator of cell death and defense responses. May
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}.
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 -!- INTERACTION:
CC Q5S1W2; Q941L2: BAP1; NbExp=3; IntAct=EBI-1606334, EBI-1606302;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and stems. Expressed in
CC young growing tissues. {ECO:0000269|PubMed:16367962}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due to partial redundancy
CC with BON1 and BON3. Bon2 and bon3 double mutant has no visible
CC phenotype. Bon1 and bon2 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=CAB87919.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY788906; AAV66325.1; -; mRNA.
DR EMBL; AY741135; AAW65975.1; -; mRNA.
DR EMBL; AL163912; CAB87919.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91134.1; -; Genomic_DNA.
DR EMBL; AF389301; AAK63871.1; -; mRNA.
DR EMBL; BT010130; AAQ22599.1; -; mRNA.
DR PIR; T49869; T49869.
DR RefSeq; NP_568180.1; NM_120812.4.
DR AlphaFoldDB; Q5S1W2; -.
DR SMR; Q5S1W2; -.
DR BioGRID; 15900; 3.
DR IntAct; Q5S1W2; 4.
DR STRING; 3702.AT5G07300.1; -.
DR iPTMnet; Q5S1W2; -.
DR SwissPalm; Q5S1W2; -.
DR PaxDb; Q5S1W2; -.
DR PRIDE; Q5S1W2; -.
DR ProteomicsDB; 240735; -.
DR EnsemblPlants; AT5G07300.1; AT5G07300.1; AT5G07300.
DR GeneID; 830621; -.
DR Gramene; AT5G07300.1; AT5G07300.1; AT5G07300.
DR KEGG; ath:AT5G07300; -.
DR Araport; AT5G07300; -.
DR TAIR; locus:2183299; AT5G07300.
DR eggNOG; KOG1327; Eukaryota.
DR HOGENOM; CLU_020452_3_1_1; -.
DR InParanoid; Q5S1W2; -.
DR OMA; LMILVYF; -.
DR OrthoDB; 1067545at2759; -.
DR PhylomeDB; Q5S1W2; -.
DR PRO; PR:Q5S1W2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q5S1W2; baseline and differential.
DR Genevisible; Q5S1W2; AT.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA: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; IEA:InterPro.
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 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..586
FT /note="Protein BONZAI 2"
FT /id="PRO_0000399469"
FT DOMAIN 25..164
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 344..563
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 123
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:0000255"
FT CONFLICT 184
FT /note="V -> G (in Ref. 1; AAW65975/AAV66325)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 586 AA; 64033 MW; 0E762AA5FFB5A1FF CRC64;
MGSCWSDGSY AGGGMVGVGG GANSSAATPN DAVDYYLKSR GYNGLFSQIE LSFSASNLRD
RDVISKSDAM VVVYTKGRDG TLAELFRSEV VLNSLNPKWI KNFTIGYQFE IVQTLLFRVY
DIDTQFQNSK EELLKLDEQQ FLGEATCTLS EVVTKSNRTI ALELMRKEGV AAQTQPQHNG
KLIVHAEESL ASKTNTEIVF RGLNLESKDT FSKSDPFLVI SKIVEHGTPI PVSKTEVLKN
DPNPLWKPVS LSVQQVGSKD SPLVIECLDF NGNGNHDLIG KVQKSLSDLE KLHLAGQGIN
LALPTGVGHK HEDRVLKSQL FVDKFTETVQ HTFLEYLASG FELNFMVAID FTASNGNPRL
PDSLHYIDPT GRLNAYQRAI VEVGEVLQFY DSDKRFPAWG FGARPIDIPV SHCFNLNGSS
TYCEVDGIQG IMNAYNGALF NVSFAGPTLF GPVINAAATI ASDSLAQSAK KYYVLLIITD
GVITDLQETR DSIVSASDLP LSILIVGVGG ADYKEMEVLD GDKGEKLESS SGRIASRDIV
QFVALRDIQY GEVSVVEALL AELPTQFLTY MRNRNITPTT TTPSST
