VICTR_ARATH
ID VICTR_ARATH Reviewed; 1168 AA.
AC F4KHI3; Q0WVG8; Q9FHF3;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Protein VARIATION IN COMPOUND TRIGGERED ROOT growth response;
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
GN Name=VICTR; OrderedLocusNames=At5g46520; ORFNames=K11I1.11;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP REVIEW.
RX PubMed=12671079; DOI=10.1105/tpc.009308;
RA Meyers B.C., Kozik A., Griego A., Kuang H., Michelmore R.W.;
RT "Genome-wide analysis of NBS-LRR-encoding genes in Arabidopsis.";
RL Plant Cell 15:809-834(2003).
RN [5]
RP INDUCTION BY SALICYLIC ACID.
RC STRAIN=cv. Columbia;
RX PubMed=17956627; DOI=10.1186/1471-2229-7-56;
RA Tan X., Meyers B.C., Kozik A., West M.A., Morgante M., St Clair D.A.,
RA Bent A.F., Michelmore R.W.;
RT "Global expression analysis of nucleotide binding site-leucine rich repeat-
RT encoding and related genes in Arabidopsis.";
RL BMC Plant Biol. 7:56-56(2007).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH PAD4
RP AND EDS1, SUBUNIT, AND INDUCTION BY DFPM.
RC STRAIN=cv. Columbia;
RX PubMed=23275581; DOI=10.1105/tpc.112.107235;
RA Kim T.H., Kunz H.H., Bhattacharjee S., Hauser F., Park J., Engineer C.,
RA Liu A., Ha T., Parker J.E., Gassmann W., Schroeder J.I.;
RT "Natural variation in small molecule-induced TIR-NB-LRR signaling induces
RT root growth arrest via EDS1- and PAD4-complexed R protein VICTR in
RT Arabidopsis.";
RL Plant Cell 24:5177-5192(2012).
CC -!- FUNCTION: Disease resistance protein of the TIR-NB-LRR-type. Part of
CC the RPS6 locus that contains a cluster of several paralogous disease
CC resistance (R) genes. Resistance proteins guard the plant against
CC pathogens that contain an appropriate avirulence protein via an
CC indirect interaction with this avirulence protein. That triggers a
CC defense system including the hypersensitive response, which restricts
CC the pathogen growth (By similarity). Required for [5-(3,4-
CC dichlorophenyl)furan-2-yl]-piperidine-1-ylmethanethione-(DFPM-) induced
CC root growth arrest due to reduced number of meristem cells in the
CC division zone of the primary root and inhibition of abscisic
CC acid- (ABA-) induced stomatal closing. {ECO:0000250,
CC ECO:0000269|PubMed:23275581}.
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:0000255|PROSITE-ProRule:PRU00204};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
CC -!- SUBUNIT: Part of a nuclear protein complex made of VICTR, PAD4 and
CC EDS1. Interacts (via TIR domain) with PAD4 and EDS1.
CC {ECO:0000269|PubMed:23275581}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23275581}. Nucleus
CC {ECO:0000269|PubMed:23275581}.
CC -!- INDUCTION: By DFPM in the root meristematic zone. Induced by salicylic
CC acid (SA). {ECO:0000269|PubMed:17956627, ECO:0000269|PubMed:23275581}.
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 -!- DISRUPTION PHENOTYPE: Loss of [5-(3,4-dichlorophenyl)furan-2-yl]-
CC piperidine-1-ylmethanethione- (DFPM-) induced root growth arrest and
CC inhibition of stomatal closing mediated by abscisic acid (ABA).
CC {ECO:0000269|PubMed:23275581}.
CC -!- SIMILARITY: Belongs to the disease resistance NB-LRR family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10820.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB019223; BAB10820.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95394.1; -; Genomic_DNA.
DR EMBL; AK226782; BAE98880.1; -; mRNA.
DR RefSeq; NP_199464.2; NM_124022.3.
DR AlphaFoldDB; F4KHI3; -.
DR SMR; F4KHI3; -.
DR STRING; 3702.AT5G46520.1; -.
DR PaxDb; F4KHI3; -.
DR ProteomicsDB; 243198; -.
DR EnsemblPlants; AT5G46520.1; AT5G46520.1; AT5G46520.
DR GeneID; 834695; -.
DR Gramene; AT5G46520.1; AT5G46520.1; AT5G46520.
DR KEGG; ath:AT5G46520; -.
DR Araport; AT5G46520; -.
DR TAIR; locus:2151476; AT5G46520.
DR HOGENOM; CLU_001561_0_1_1; -.
DR InParanoid; F4KHI3; -.
DR PRO; PR:F4KHI3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KHI3; baseline and differential.
DR Genevisible; F4KHI3; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0010082; P:regulation of root meristem growth; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.8.430; -; 1.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR045344; C-JID.
DR InterPro; IPR044974; Disease_R_plants.
DR InterPro; IPR011713; Leu-rich_rpt_3.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002182; NB-ARC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11017; PTHR11017; 1.
DR Pfam; PF20160; C-JID; 1.
DR Pfam; PF07725; LRR_3; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Hydrolase; Leucine-rich repeat; NAD;
KW Nucleotide-binding; Nucleus; Plant defense; Reference proteome; Repeat.
FT CHAIN 1..1168
FT /note="Protein VARIATION IN COMPOUND TRIGGERED ROOT growth
FT response"
FT /id="PRO_0000429489"
FT DOMAIN 10..171
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT DOMAIN 187..452
FT /note="NB-ARC"
FT REPEAT 539..562
FT /note="LRR 1"
FT REPEAT 606..629
FT /note="LRR 2"
FT REPEAT 631..653
FT /note="LRR 3"
FT REPEAT 676..699
FT /note="LRR 4"
FT REPEAT 701..720
FT /note="LRR 5"
FT REPEAT 721..744
FT /note="LRR 6"
FT REPEAT 795..820
FT /note="LRR 7"
FT REPEAT 839..865
FT /note="LRR 8"
FT REPEAT 873..896
FT /note="LRR 9"
FT REPEAT 1065..1089
FT /note="LRR 10"
FT ACT_SITE 85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CONFLICT 511
FT /note="E -> V (in Ref. 3; BAE98880)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1168 AA; 132789 MW; A71B2F2EB97AD408 CRC64;
MASSSSSRNW VYDVFLSFSG KDVRVTFRSH FLKELDRKLI SAFRDNEIER SHSLWPDLEQ
AIKDSRIAVV VFSKNYASSS WCLNELLEIV NCNDKIIIPV FYGVDPSQVR YQIGEFGSIF
EKTCKRQTEE VKNQWKKALT DVANMLGFDS AKWDDEAKMI EEIANDVLAK LLLTSSTDSA
ENSIGIEDHI ANMSVLLKLE AEEVRMVGIW GSSGIGKTTI ARALFNQLSR HFPVSKFIDR
AFVYKSRETY KGANPDDPNM KLHLQGCFLS EILGKKDIKI DHLGALGERL KHQKTLIIID
DLDDLVVLDS LVGKTNWFGC GSRIIVITNN KQFLRAHGID HIYEVSLPSK ERAQEMFCQS
AFGENSPPEG FEELVVEIAW LAGSLPLGLT VFGSALRGRK KEYWVKMLPR LQNDLDGNIE
ETLKVSYDAI GNVKDQALFR LIACLFNHVK VRDIELLLAD SGLDVNIALE NLVDKSLIHV
RNDHVEMHRL LQETGRNIVR SQSTDNPGER EFLVDSNDSR TVLSEGIGTR KVLGISLDTS
KVSEFCVHEN AFKGMGNLLF LDISSKTFIE EEVKVHLPEK INYYSVQPKQ LIWDRFPLKC
MPYTFLRNLV KLEMHDSKLE KLWEGAMSFT CLKELDMWAS KYLKEIPDLS KATNIEKLDF
GHCWSLVELP SSIRNLNKLL ELNMEYCGEL ETLPTGFNLK SLDYLNFNEC WKLRTFPEFA
TNISNLILAE TSIEEYPSNL YFKNVRELSM GKADSDENKC QGVKPFMPML SPTLTLLELW
NIPNLVELSS SFQNLNNLER LDICYCRNLE SLPTGINLES LVSLNLFGCS RLKRFPDIST
NIKYLDLDQT GIEEVPWQIE NFFNLTKLTM KGCRELKCVS LNIFKLKHLG EVSFSNCGAL
TRVDLSCYPS GVEMMKADNA DIVSEETTSS LPDSCVLNVN FMDCVNLDRE PVLHQQSIIF
NSMILPGEEV PSYFTYRTSD SQPFGTSSSL PIPLLPTQLS QPFFRFRVCA VVSASNGVYI
GVYSRFKGRI GNKFDSFGEV HNFMEIEKGI HLCIFDCRIR LYKDNVPLSQ LNYDHVDINI
HITSGDWRST VVLKEWGIRL LETGSSAENR LGNPNSTLPH VSQAEEGNMG YYTHVQGLVN
EIENSEDSGD NNVETERSKK RMRLHHFI
