IRM1_ARATH
ID IRM1_ARATH Reviewed; 113 AA.
AC Q9LV75;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein INCREASED RESISTANCE TO MYZUS PERSICAE 1 {ECO:0000303|PubMed:23951039};
DE AltName: Full=FCS-Like Zinc finger 4 {ECO:0000303|PubMed:24901469};
GN Name=IRM1 {ECO:0000303|PubMed:23951039};
GN Synonyms=DUF581-18 {ECO:0000303|PubMed:24600465},
GN FLZ4 {ECO:0000303|PubMed:24901469};
GN OrderedLocusNames=At5g65040 {ECO:0000312|Araport:AT5G65040};
GN ORFNames=MXK3.29 {ECO:0000312|EMBL:BAA97316.1};
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=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;
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 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 [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=23951039; DOI=10.1371/journal.pone.0070914;
RA Chen X., Zhang Z., Visser R.G., Broekgaarden C., Vosman B.;
RT "Overexpression of IRM1 enhances resistance to aphids in Arabidopsis
RT thaliana.";
RL PLoS ONE 8:E70914-E70914(2013).
RN [6]
RP GENE FAMILY, INTERACTION WITH KIN10; KIN11 AND GEBP, SUBCELLULAR LOCATION,
RP AND FUNCTION.
RX PubMed=24600465; DOI=10.3389/fpls.2014.00054;
RA Nietzsche M., Schiessl I., Boernke F.;
RT "The complex becomes more complex: protein-protein interactions of SnRK1
RT with DUF581 family proteins provide a framework for cell- and stimulus
RT type-specific SnRK1 signaling in plants.";
RL Front. Plant Sci. 5:54-54(2014).
RN [7]
RP ERRATUM OF PUBMED:24600465.
RX PubMed=25544057; DOI=10.3389/fpls.2014.00693;
RA Boernke F.;
RT "Corrigendum: The complex becomes more complex: protein-protein
RT interactions of SnRK1 with DUF581 family proteins provide a framework for
RT cell- and stimulus type-specific SnRK1 signaling in plants.";
RL Front. Plant Sci. 5:693-693(2014).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=24901469; DOI=10.1371/journal.pone.0099074;
RA Jamsheer K M., Laxmi A.;
RT "DUF581 is plant specific FCS-like zinc finger involved in protein-protein
RT interaction.";
RL PLoS ONE 9:E99074-E99074(2014).
RN [9]
RP INDUCTION.
RX PubMed=26442059; DOI=10.3389/fpls.2015.00746;
RA Jamsheer K M., Laxmi A.;
RT "Expression of Arabidopsis FCS-Like Zinc finger genes is differentially
RT regulated by sugars, cellular energy level, and abiotic stress.";
RL Front. Plant Sci. 6:746-746(2015).
RN [10]
RP INTERACTION WITH KIN10; KIN11 AND KINB3, AND SUBCELLULAR LOCATION.
RX PubMed=29945970; DOI=10.1074/jbc.ra118.002073;
RA Jamsheer K M., Shukla B.N., Jindal S., Gopan N., Mannully C.T., Laxmi A.;
RT "The FCS-like zinc finger scaffold of the kinase SnRK1 is formed by the
RT coordinated actions of the FLZ domain and intrinsically disordered
RT regions.";
RL J. Biol. Chem. 293:13134-13150(2018).
CC -!- FUNCTION: May act as an adapter to facilitate the interaction of SnRK1
CC complex with effector proteins, conferring tissue- and stimulus-type
CC specific differences in the SnRK1 regulation pathway.
CC {ECO:0000269|PubMed:24600465}.
CC -!- SUBUNIT: Interacts with KIN10 and KIN11 via its FLZ-type zinc finger
CC domain (PubMed:24600465, PubMed:29945970). Interacts with KINB3 via its
CC N-terminal part (PubMed:29945970). Interacts with GEBP
CC (PubMed:24600465). {ECO:0000269|PubMed:24600465,
CC ECO:0000269|PubMed:29945970}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24600465,
CC ECO:0000269|PubMed:29945970}. Cytoplasm {ECO:0000269|PubMed:24600465,
CC ECO:0000269|PubMed:29945970}. Note=Shuttles from the cytoplasm to the
CC nucleus when associated with KIN10. {ECO:0000269|PubMed:24600465}.
CC -!- INDUCTION: Up-regulated in response to mild as well as prolonged energy
CC depletion. {ECO:0000269|PubMed:26442059}.
CC -!- DISRUPTION PHENOTYPE: Promoted M.persicae aphid population development.
CC {ECO:0000269|PubMed:23951039}.
CC -!- MISCELLANEOUS: Overexpression of FLZ4/IRM1 rendered plants shorter
CC which creates mechanical resistance to M.persicae aphid attack.
CC {ECO:0000269|PubMed:23951039}.
CC -!- SIMILARITY: Belongs to the FLZ family. {ECO:0000305}.
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DR EMBL; AB019236; BAA97316.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97989.1; -; Genomic_DNA.
DR EMBL; BT002778; AAO22606.1; -; mRNA.
DR EMBL; BT004359; AAO42353.1; -; mRNA.
DR EMBL; AY086426; AAM63428.1; -; mRNA.
DR RefSeq; NP_201309.1; NM_125903.3.
DR AlphaFoldDB; Q9LV75; -.
DR IntAct; Q9LV75; 1.
DR STRING; 3702.AT5G65040.1; -.
DR PaxDb; Q9LV75; -.
DR PRIDE; Q9LV75; -.
DR EnsemblPlants; AT5G65040.1; AT5G65040.1; AT5G65040.
DR GeneID; 836628; -.
DR Gramene; AT5G65040.1; AT5G65040.1; AT5G65040.
DR KEGG; ath:AT5G65040; -.
DR Araport; AT5G65040; -.
DR TAIR; locus:2177739; AT5G65040.
DR eggNOG; ENOG502R1MD; Eukaryota.
DR HOGENOM; CLU_085535_1_0_1; -.
DR InParanoid; Q9LV75; -.
DR OMA; MLMITDD; -.
DR OrthoDB; 1567352at2759; -.
DR PhylomeDB; Q9LV75; -.
DR PRO; PR:Q9LV75; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LV75; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002213; P:defense response to insect; IMP:UniProtKB.
DR GO; GO:0009625; P:response to insect; IEP:UniProtKB.
DR GO; GO:0042594; P:response to starvation; IEP:UniProtKB.
DR InterPro; IPR007650; Zf-FLZ_dom.
DR Pfam; PF04570; zf-FLZ; 1.
DR PROSITE; PS51795; ZF_FLZ; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Nucleus; Plant defense; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..113
FT /note="Protein INCREASED RESISTANCE TO MYZUS PERSICAE 1"
FT /id="PRO_0000445495"
FT ZN_FING 56..100
FT /note="FLZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01131"
SQ SEQUENCE 113 AA; 13072 MW; 7C1FAFA6AFDEBB11 CRC64;
MVLGKRHGSL IKRTTSMKMI TLDTPTIYDA SQPSDHLTFH QHPHNPMVVM ASNYDDFLKT
CSLCNRSLCH HRDIYMYRGN NAFCSLECRE KQIKLDEKKA KTGFVTSKKP IRI
