RBA1_ARATH
ID RBA1_ARATH Reviewed; 363 AA.
AC F4HT77; Q9FX07;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Disease resistance protein RBA1 {ECO:0000305};
DE AltName: Full=NAD(+) hydrolase RBA1;
DE EC=3.2.2.6 {ECO:0000269|PubMed:31439793};
DE AltName: Full=NADP(+) hydrolase RBA1 {ECO:0000305};
DE EC=3.2.2.- {ECO:0000269|PubMed:31439793};
DE AltName: Full=Response to HopBA1 protein {ECO:0000303|PubMed:28137883};
DE Short=RBA1 {ECO:0000303|PubMed:28137883};
GN Name=RBA1 {ECO:0000303|PubMed:28137883};
GN OrderedLocusNames=At1g47370 {ECO:0000312|EMBL:AEE32160.1};
GN ORFNames=T3F24.3 {ECO:0000312|EMBL:AAG11420.1};
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=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 [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 FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INDUCTION, ACTIVE SITE, AND
RP MUTAGENESIS OF 31-SER-HIS-32; SER-31; HIS-32; LYS-149 AND GLY-151.
RX PubMed=28137883; DOI=10.1073/pnas.1620973114;
RA Nishimura M.T., Anderson R.G., Cherkis K.A., Law T.F., Liu Q.L.,
RA Machius M., Nimchuk Z.L., Yang L., Chung E.H., El Kasmi F., Hyunh M.,
RA Osborne Nishimura E., Sondek J.E., Dangl J.L.;
RT "TIR-only protein RBA1 recognizes a pathogen effector to regulate cell
RT death in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E2053-E2062(2017).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF GLU-86.
RX PubMed=31439793; DOI=10.1126/science.aax1771;
RA Wan L., Essuman K., Anderson R.G., Sasaki Y., Monteiro F., Chung E.H.,
RA Osborne Nishimura E., DiAntonio A., Milbrandt J., Dangl J.L.,
RA Nishimura M.T.;
RT "TIR domains of plant immune receptors are NAD+-cleaving enzymes that
RT promote cell death.";
RL Science 365:799-803(2019).
CC -!- FUNCTION: Disease resistance (R) protein that specifically recognizes
CC the HopBA1 type III effector protein from P.syringae, and triggers cell
CC death (PubMed:28137883). Acts as a NAD(+) hydrolase (NADase): in
CC response to pathogen-recognition, catalyzes cleavage of NAD(+) into
CC ADP-D-ribose (ADPR) and nicotinamide; NAD(+) cleavage triggering a
CC defense system that promotes cell death (PubMed:31439793). In addition
CC to ADPR, also generates a cyclization variant of cyclic ADPR (cADPR),
CC termed v-cADPR, for which the cyclizing bond is unknown
CC (PubMed:31439793). Also able to hydrolyze NADP(+), but not other
CC NAD(+)-related molecules (PubMed:31439793).
CC {ECO:0000269|PubMed:28137883, ECO:0000269|PubMed:31439793}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC Evidence={ECO:0000269|PubMed:31439793};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000269|PubMed:31439793};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) = ADP-D-ribose 2'-phosphate + H(+) +
CC nicotinamide; Xref=Rhea:RHEA:19849, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58673; Evidence={ECO:0000269|PubMed:31439793};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19850;
CC Evidence={ECO:0000269|PubMed:31439793};
CC -!- SUBUNIT: Homooligomer; homooligomerization is required for activity.
CC {ECO:0000269|PubMed:28137883, ECO:0000269|PubMed:31439793}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28137883}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:28137883}. Note=Forms aggregate-like
CC cyto-nucleoplasmic puncta. {ECO:0000269|PubMed:28137883}.
CC -!- INDUCTION: Accumulates during immune responses activated by a variety
CC of NLR proteins. {ECO:0000269|PubMed:28137883}.
CC -!- DOMAIN: The TIR domain catalyzes the NAD(+) cleavage (NADase) activity
CC (PubMed:31439793). In contrast to classical TIR-NB-LRR receptor-like
CC proteins, only contains a TIR domain (Probable).
CC {ECO:0000269|PubMed:31439793, ECO:0000305}.
CC -!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
CC Self-association of TIR domains is required for NADase activity.
CC {ECO:0000255|PROSITE-ProRule:PRU00204}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG11420.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC015449; AAG11420.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32160.1; -; Genomic_DNA.
DR PIR; D96514; D96514.
DR RefSeq; NP_175170.1; NM_103631.1.
DR AlphaFoldDB; F4HT77; -.
DR SMR; F4HT77; -.
DR STRING; 3702.AT1G47370.1; -.
DR PaxDb; F4HT77; -.
DR PRIDE; F4HT77; -.
DR EnsemblPlants; AT1G47370.1; AT1G47370.1; AT1G47370.
DR GeneID; 841140; -.
DR Gramene; AT1G47370.1; AT1G47370.1; AT1G47370.
DR KEGG; ath:AT1G47370; -.
DR Araport; AT1G47370; -.
DR TAIR; locus:2203776; AT1G47370.
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_763668_0_0_1; -.
DR InParanoid; F4HT77; -.
DR OrthoDB; 1766717at2759; -.
DR PRO; PR:F4HT77; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HT77; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IDA:UniProtKB.
DR GO; GO:0003953; F:NAD+ nucleosidase activity; IDA:UniProtKB.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0052542; P:defense response by callose deposition; IMP:TAIR.
DR GO; GO:0019677; P:NAD catabolic process; IDA:UniProtKB.
DR GO; GO:0034052; P:positive regulation of plant-type hypersensitive response; IMP:TAIR.
DR GO; GO:0043068; P:positive regulation of programmed cell death; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 3.40.50.10140; -; 1.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; NAD; Nucleus; Plant defense; Reference proteome.
FT CHAIN 1..363
FT /note="Disease resistance protein RBA1"
FT /id="PRO_0000448795"
FT DOMAIN 12..175
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT ACT_SITE 86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204,
FT ECO:0000305|PubMed:31439793"
FT BINDING 21..26
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:V9M398"
FT BINDING 53
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:V9M398"
FT MUTAGEN 31..32
FT /note="SH->AA: Decreased ability to induce cell death due
FT to impaired homooligomerization."
FT /evidence="ECO:0000269|PubMed:28137883"
FT MUTAGEN 31
FT /note="S->A: Decreased ability to induce cell death."
FT /evidence="ECO:0000269|PubMed:28137883"
FT MUTAGEN 32
FT /note="H->A: Abolished ability to induced cell death."
FT /evidence="ECO:0000269|PubMed:28137883"
FT MUTAGEN 86
FT /note="E->A: Loss of NAD(+) hydrolase activity."
FT /evidence="ECO:0000269|PubMed:31439793"
FT MUTAGEN 149
FT /note="K->E: Decreased ability to induce cell death due to
FT impaired homooligomerization."
FT /evidence="ECO:0000269|PubMed:28137883"
FT MUTAGEN 151
FT /note="G->R: Abolished ability to induce cell death."
FT /evidence="ECO:0000269|PubMed:28137883"
SQ SEQUENCE 363 AA; 42118 MW; 850F477F21D01ACB CRC64;
MTSVSPRYRN VPVPKVFLSF RGEEIRHGFI SHLADALERY GIMFIIDKDE QRGNDLTSLL
LRIKESKVAL VIFSSRFAES RFCMDEIVKM KECVDERKLL VIPIFYKVRA RDVSGRTGDF
GKKFWALAQK SRGCQIKEWM EALECISNKM GLSLGDGRSE ADFIKEIVKE VERVLATFTS
EDTEDHHCQT VKLLKGLVVG CLAHQELPLV LVFTQVYYYV KFSIFFIEEI FSSCFRKGFV
LKPCKEDLQI NSISIPGIDL ENFKNMMQQA MYELNQMLLQ SLGNIDPHRD VAFENQPQDQ
PDSPIALPEE RRVALEATKF CGHAAYWWNQ TKTTRARIGK VLIHFWEKLK KKFKDTYDRT
VRI
