BOI_ARATH
ID BOI_ARATH Reviewed; 304 AA.
AC O81851; Q8W4E8;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=E3 ubiquitin-protein ligase BOI;
DE EC=2.3.2.27 {ECO:0000269|PubMed:20921156};
DE AltName: Full=Inhibitor of apoptosis (IAP)-like protein;
DE Short=AtILP;
DE AltName: Full=Protein BOTRYTIS SUSCEPTIBLE 1 INTERACTOR;
DE Short=AtBOI;
DE AltName: Full=RING-type E3 ubiquitin transferase BOI {ECO:0000305};
GN Name=BOI; Synonyms=ILP; OrderedLocusNames=At4g19700; ORFNames=T16H5.60;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH MYB108/BOS1, DOMAIN,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY PATHOGEN; METHYL
RP VIOLAGEN; SALICYLIC ACID; GIBBERELLIC ACID; ACC; METHYL JASMONATE AND SALT.
RX PubMed=20921156; DOI=10.1104/pp.110.163915;
RA Luo H., Laluk K., Lai Z., Veronese P., Song F., Mengiste T.;
RT "The Arabidopsis Botrytis Susceptible1 Interactor defines a subclass of
RT RING E3 ligases that regulate pathogen and stress responses.";
RL Plant Physiol. 154:1766-1782(2010).
RN [5]
RP FUNCTION, DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=21926169; DOI=10.1074/jbc.m111.262204;
RA Kim W.Y., Lee S.Y., Jung Y.J., Chae H.B., Nawkar G.M., Shin M.R., Kim S.Y.,
RA Park J.H., Kang C.H., Chi Y.H., Ahn I.P., Yun D.J., Lee K.O., Kim Y.M.,
RA Kim M.G., Lee S.Y.;
RT "Inhibitor of apoptosis (IAP)-like protein lacks a baculovirus IAP repeat
RT (BIR) domain and attenuates cell death in plant and animal systems.";
RL J. Biol. Chem. 286:42670-42678(2011).
RN [6]
RP FUNCTION, INTERACTION WITH GAI; RGA; RGL1; RGL2 AND RGL3, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23482857; DOI=10.1105/tpc.112.108951;
RA Park J., Nguyen K.T., Park E., Jeon J.S., Choi G.;
RT "DELLA proteins and their interacting RING Finger proteins repress
RT gibberellin responses by binding to the promoters of a subset of
RT gibberellin-responsive genes in Arabidopsis.";
RL Plant Cell 25:927-943(2013).
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in the regulation of
CC pathogen and abiotic stress responses by facilitating degradation of
CC MYB108/BOI. Attenuates cell death by preventing caspase activation. Has
CC no effect on the stability of the DELLA proteins. Not regulated by
CC MYB108/BOI. {ECO:0000269|PubMed:20921156, ECO:0000269|PubMed:21926169,
CC ECO:0000269|PubMed:23482857}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:20921156};
CC -!- PATHWAY: Protein degradation; proteasomal ubiquitin-dependent pathway.
CC -!- SUBUNIT: Interacts with MYB108/BOS1 and the DELLA proteins GAI, RGA,
CC RGL1, RGL2 and RGL3. {ECO:0000269|PubMed:20921156,
CC ECO:0000269|PubMed:23482857}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20921156,
CC ECO:0000269|PubMed:21926169}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, siliques, roots, flowering
CC tissues and stigma tips. {ECO:0000269|PubMed:20921156}.
CC -!- INDUCTION: Up-regulated by pathogen, methyl violagen, salicylic acid,
CC 1-aminocyclopropane-1-carboxylic acid (ACC) and salt. Down-regulated by
CC methyl jasmonate and gibberellic acid. {ECO:0000269|PubMed:20921156}.
CC -!- DOMAIN: The N-terminal domain (1-150) prevents cell death by
CC suppressing caspase-like protease activation.
CC {ECO:0000269|PubMed:21926169}.
CC -!- DOMAIN: The WRD domain (178-214) is necessary for interaction with
CC MYB108/BOS1. {ECO:0000269|PubMed:20921156}.
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. It is required for the ubiquitination
CC activity, but dispensable and not sufficient for interaction with
CC MYB108/BOS1 (PubMed:20921156). {ECO:0000269|PubMed:20921156}.
CC -!- DISRUPTION PHENOTYPE: No effect on germination. Boi, brg1, brg2 and
CC brg3 quadruple mutant shows a higher GA signaling resulting in a higher
CC seed germination in the presence of paclobutrazol, precocious juvenile-
CC to-adult phase transition and early flowering.
CC {ECO:0000269|PubMed:23482857}.
CC -!- MISCELLANEOUS: Shares anti-apoptotic activity with IAP family proteins.
CC However, it lacks the baculovirus IAP repeat (BIR) domain, which was
CC shown to be essential for anti-apoptotic activity in other IAP family
CC members (PubMed:21926169). {ECO:0000305|PubMed:21926169}.
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; AL024486; CAA19687.1; -; Genomic_DNA.
DR EMBL; AL161551; CAB78972.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84218.1; -; Genomic_DNA.
DR EMBL; AY062603; AAL32681.1; -; mRNA.
DR EMBL; AY114665; AAM47984.1; -; mRNA.
DR PIR; T04751; T04751.
DR RefSeq; NP_193705.1; NM_118090.4.
DR AlphaFoldDB; O81851; -.
DR SMR; O81851; -.
DR BioGRID; 13007; 43.
DR IntAct; O81851; 40.
DR STRING; 3702.AT4G19700.1; -.
DR PaxDb; O81851; -.
DR PRIDE; O81851; -.
DR ProteomicsDB; 240672; -.
DR EnsemblPlants; AT4G19700.1; AT4G19700.1; AT4G19700.
DR GeneID; 827714; -.
DR Gramene; AT4G19700.1; AT4G19700.1; AT4G19700.
DR KEGG; ath:AT4G19700; -.
DR Araport; AT4G19700; -.
DR TAIR; locus:2133990; AT4G19700.
DR eggNOG; KOG1100; Eukaryota.
DR HOGENOM; CLU_038018_3_1_1; -.
DR InParanoid; O81851; -.
DR OMA; CDSGMDA; -.
DR OrthoDB; 889964at2759; -.
DR PhylomeDB; O81851; -.
DR UniPathway; UPA00144; -.
DR PRO; PR:O81851; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O81851; baseline and differential.
DR Genevisible; O81851; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; IDA:TAIR.
DR GO; GO:0043069; P:negative regulation of programmed cell death; IMP:TAIR.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0043067; P:regulation of programmed cell death; IBA:GO_Central.
DR GO; GO:0009739; P:response to gibberellin; IEP:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR017066; E3ligase_BOI-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR42647; PTHR42647; 1.
DR PIRSF; PIRSF036836; RNase_bind_SBP1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Coiled coil; Metal-binding; Nucleus; Plant defense;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..304
FT /note="E3 ubiquitin-protein ligase BOI"
FT /id="PRO_0000424716"
FT ZN_FING 254..291
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 178..214
FT /note="WRD domain"
FT COILED 197..220
FT /evidence="ECO:0000255"
FT CONFLICT 37
FT /note="Missing (in Ref. 3; AAL32681/AAM47984)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 304 AA; 33509 MW; 132989B291ECC9DD CRC64;
MAVQAHHMNI FSQFISPNRD CVKFQENMNH GEFEFTGGEV PLITGESFAV EPLAAKANFN
KAESGLSYNF TVPPLSTKRQ RDFQFSDSNA PVKRRSVAFD SSSPSLINVE LVSQIQNQQQ
SEIDRFVAQQ TEKLRIEIEA RQQTQTRMLA SAVQNVIAKK LKEKDDEIVR IRNLNWVLQE
RVKSLYVENQ IWRDIAQTNE ANANTLRTNL DQVLAQLETF PTASAVVEDD AESSCGSCCG
DGGGEAVTAV GGGCKRCGER EASVLVLPCR HLCLCTVCGG SALLRTCPVC DMVMNASVHV
NMSS
