BAP1_ARATH
ID BAP1_ARATH Reviewed; 192 AA.
AC Q941L2; Q8LBT3; Q9M2E5;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=BON1-associated protein 1;
GN Name=BAP1; OrderedLocusNames=At3g61190; ORFNames=T20K12.90;
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], INTERACTION WITH BON1, TISSUE SPECIFICITY, AND
RP INDUCTION BY HEAT.
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BON1, INDUCTION BY
RP PATHOGEN AND SALICYLIC ACID, AND DISRUPTION PHENOTYPE.
RX PubMed=17018034; DOI=10.1111/j.1365-313x.2006.02869.x;
RA Yang H., Li Y., Hua J.;
RT "The C2 domain protein BAP1 negatively regulates defense responses in
RT Arabidopsis.";
RL Plant J. 48:238-248(2006).
RN [8]
RP FUNCTION, INDUCTION BY PATHOGEN; NEMATODE; CHEMICALS AND SALT STRESS,
RP INTERACTION WITH BON1; BON2 AND BON3, AND DISRUPTION PHENOTYPE.
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 [9]
RP INTERACTION WITH BON1.
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).
CC -!- FUNCTION: Negative regulator of cell death and defense responses.
CC Exhibits calcium-dependent phospholipid binding properties.
CC {ECO:0000269|PubMed:17018034, ECO:0000269|PubMed:17631528}.
CC -!- SUBUNIT: Interacts with BON1 (via VWA domain), BON2 and BON3.
CC {ECO:0000269|PubMed:11544183, ECO:0000269|PubMed:17018034,
CC ECO:0000269|PubMed:17631528, ECO:0000269|PubMed:20634289}.
CC -!- INTERACTION:
CC Q941L2; Q5S1W2: BON2; NbExp=3; IntAct=EBI-1606302, EBI-1606334;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17018034};
CC Peripheral membrane protein {ECO:0000269|PubMed:17018034}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q941L2-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers.
CC {ECO:0000269|PubMed:11544183}.
CC -!- INDUCTION: Down-regulated by high temperature. Up-regulated by
CC salicylic acid, AgNO(3), chitin, cycloheximide, ozone, syringolin, salt
CC stress and upon pathogen or nematode infection.
CC {ECO:0000269|PubMed:11544183, ECO:0000269|PubMed:17018034,
CC ECO:0000269|PubMed:17631528}.
CC -!- DISRUPTION PHENOTYPE: Dwarf, twisted leaves and enhanced disease
CC resistance to bacterial and oomycete pathogens in cv. Columbia when
CC grown under constant loght at 22 degrees Celsius. No visible phenotype
CC when grown at 28 degrees Celsius. Accelerated hypersensitive response
CC (HR). Bap1 and bap2 double mutant is seedling lethal.
CC {ECO:0000269|PubMed:17018034, ECO:0000269|PubMed:17631528}.
CC -!- MISCELLANEOUS: Overexpression of BAP1 can suppress a defect in BON1 and
CC confers more susceptibility to virulent pathogens.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM64568.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB71049.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AY045765; AAK98798.1; -; mRNA.
DR EMBL; AL137898; CAB71049.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE80170.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80171.2; -; Genomic_DNA.
DR EMBL; AK117234; BAC41910.1; -; mRNA.
DR EMBL; BT003727; AAO39955.1; -; mRNA.
DR EMBL; AY087007; AAM64568.1; ALT_INIT; mRNA.
DR PIR; T47911; T47911.
DR RefSeq; NP_001190150.2; NM_001203221.2. [Q941L2-1]
DR RefSeq; NP_567111.1; NM_115983.3. [Q941L2-1]
DR AlphaFoldDB; Q941L2; -.
DR SMR; Q941L2; -.
DR BioGRID; 10605; 2.
DR IntAct; Q941L2; 3.
DR STRING; 3702.AT3G61190.1; -.
DR PaxDb; Q941L2; -.
DR PRIDE; Q941L2; -.
DR EnsemblPlants; AT3G61190.1; AT3G61190.1; AT3G61190. [Q941L2-1]
DR EnsemblPlants; AT3G61190.2; AT3G61190.2; AT3G61190. [Q941L2-1]
DR GeneID; 825291; -.
DR Gramene; AT3G61190.1; AT3G61190.1; AT3G61190. [Q941L2-1]
DR Gramene; AT3G61190.2; AT3G61190.2; AT3G61190. [Q941L2-1]
DR KEGG; ath:AT3G61190; -.
DR Araport; AT3G61190; -.
DR TAIR; locus:2098931; AT3G61190.
DR eggNOG; ENOG502SU1K; Eukaryota.
DR InParanoid; Q941L2; -.
DR OMA; HRTERTL; -.
DR PhylomeDB; Q941L2; -.
DR PRO; PR:Q941L2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q941L2; baseline and differential.
DR Genevisible; Q941L2; AT.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0005543; F:phospholipid binding; IDA:TAIR.
DR GO; GO:0019725; P:cellular homeostasis; IPI:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0031348; P:negative regulation of defense response; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009408; P:response to heat; IEP:TAIR.
DR GO; GO:0009751; P:response to salicylic acid; IEP:TAIR.
DR GO; GO:0009266; P:response to temperature stimulus; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR CDD; cd04051; C2_SRC2_like; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR044750; C2_SRC2/BAP.
DR Pfam; PF00168; C2; 1.
DR SMART; SM00239; C2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Plant defense; Reference proteome.
FT CHAIN 1..192
FT /note="BON1-associated protein 1"
FT /id="PRO_0000399505"
FT DOMAIN 1..119
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
SQ SEQUENCE 192 AA; 21992 MW; FB2FDB691B33975C CRC64;
MIYFGRSIDN HYTTMMTKTL EIDLRSAEGL KLNRRPIKKK TFAVVKIDEK CRKSNLDESR
RSNPTWNYKS EMPINGNEQF IFIEVFYRTG SGHDKKIGEA KIPTNDFMGR YSPEGHLNFL
SYRLRDEFGD KCGIVNLSIL VKSDPTRDYG ACSSQAAVTG LWRPRLETAS IDGYGGRTVT
GVPVWGLYQR QF
