RTM2_ARATH
ID RTM2_ARATH Reviewed; 366 AA.
AC Q9M670; Q8H7A1;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Protein RESTRICTED TEV MOVEMENT 2;
DE AltName: Full=Alpha-crystallin domains containing protein 41.3;
DE Short=AtAcd41.3;
DE AltName: Full=Restricted tobacco etch virus movement protein 2;
GN Name=RTM2; OrderedLocusNames=At5g04890; ORFNames=MUK11.22;
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], IDENTIFICATION, FUNCTION, TISSUE SPECIFICITY,
RP AND REPEATS.
RC STRAIN=cv. Columbia;
RX PubMed=10760245; DOI=10.2307/3871070;
RA Whitham S.A., Anderberg R.J., Chisholm S.T., Carrington J.C.;
RT "Arabidopsis RTM2 gene is necessary for specific restriction of tobacco
RT etch virus and encodes an unusual small heat shock-like protein.";
RL Plant Cell 12:569-582(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=cv. Bla-1, cv. Ei-2, cv. Gy-0, cv. REN-1, and cv. St-0;
RX PubMed=20478894; DOI=10.1098/rstb.2010.0044;
RA Lalic J., Agudelo-Romero P., Carrasco P., Elena S.F.;
RT "Adaptation of tobacco etch potyvirus to a susceptible ecotype of
RT Arabidopsis thaliana capacitates it for systemic infection of resistant
RT ecotypes.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 365:1997-2007(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=cv. Bur-0, cv. Can-0, cv. Edi-0, cv. Ge-0, cv. Jea, cv. Ll-0,
RC cv. Mh-1, cv. Mt-0, cv. N13, cv. Nd-1, cv. Oy-0, and cv. St-0; TISSUE=Leaf;
RX PubMed=22723957; DOI=10.1371/journal.pone.0039169;
RA Cosson P., Schurdi-Levraud V., Le Q.H., Sicard O., Caballero M., Roux F.,
RA Le Gall O., Candresse T., Revers F.;
RT "The RTM resistance to potyviruses in Arabidopsis thaliana: natural
RT variation of the RTM genes and evidence for the implication of additional
RT genes.";
RL PLoS ONE 7:E39169-E39169(2012).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-157.
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9892709; DOI=10.1073/pnas.96.2.772;
RA Whitham S.A., Yamamoto M.L., Carrington J.C.;
RT "Selectable viruses and altered susceptibility mutants in Arabidopsis
RT thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:772-777(1999).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=11743111; DOI=10.1104/pp.010479;
RA Chisholm S.T., Parra M.A., Anderberg R.J., Carrington J.C.;
RT "Arabidopsis RTM1 and RTM2 genes function in phloem to restrict long-
RT distance movement of tobacco etch virus.";
RL Plant Physiol. 127:1667-1675(2001).
RN [9]
RP GENE FAMILY.
RX PubMed=16531488; DOI=10.1104/pp.105.073841;
RA Ma C., Haslbeck M., Babujee L., Jahn O., Reumann S.;
RT "Identification and characterization of a stress-inducible and a
RT constitutive small heat-shock protein targeted to the matrix of plant
RT peroxisomes.";
RL Plant Physiol. 141:47-60(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [11]
RP INDUCTION BY NAC045 AND NAC086, AND TISSUE SPECIFICITY.
RX PubMed=25081480; DOI=10.1126/science.1253736;
RA Furuta K.M., Yadav S.R., Lehesranta S., Belevich I., Miyashima S.,
RA Heo J.O., Vaten A., Lindgren O., De Rybel B., Van Isterdael G.,
RA Somervuo P., Lichtenberger R., Rocha R., Thitamadee S., Taehtiharju S.,
RA Auvinen P., Beeckman T., Jokitalo E., Helariutta Y.;
RT "Plant development. Arabidopsis NAC45/86 direct sieve element morphogenesis
RT culminating in enucleation.";
RL Science 345:933-937(2014).
CC -!- FUNCTION: Required for the restriction of long-distance movement of the
CC pathogenic tobacco etch virus (TEV) without causing a hypersensitive
CC response or inducing systemic acquired resistance. Seems to not be
CC involved in heat resistance. {ECO:0000269|PubMed:10760245,
CC ECO:0000269|PubMed:20478894, ECO:0000269|PubMed:22723957,
CC ECO:0000269|PubMed:9892709}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11743111};
CC Single-pass membrane protein {ECO:0000269|PubMed:11743111}.
CC Note=Present in sieve elements.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, and inflorescence,
CC exclusively in phloem-associated cells (e.g. sieve elements).
CC {ECO:0000269|PubMed:10760245, ECO:0000269|PubMed:11743111,
CC ECO:0000269|PubMed:25081480}.
CC -!- INDUCTION: Regulated by the transcription factors NAC045 and NAC086.
CC {ECO:0000269|PubMed:25081480}.
CC -!- DISRUPTION PHENOTYPE: Susceptible to systemic infection by tobacco etch
CC virus (TEV). {ECO:0000269|PubMed:9892709}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
CC -!- CAUTION: Has been shown to be inactive in cv. Ct-1 and cv. Ga-0 (AC
CC D5K211), cv. Bl-1 and cv. Sakata (AC D9UBX6), cv. Blh-1, cv. Pyl-1 and
CC cv. Sha (AC D9UBX4), and cv. Ge-1 (AC D9UC01) due to naturally
CC occurring sequence variation in these strains. The sequence shown is
CC from strain cv. Columbia. {ECO:0000305}.
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DR EMBL; AF208051; AAF61902.1; -; mRNA.
DR EMBL; GU396190; ADE43080.1; -; Genomic_DNA.
DR EMBL; GU396196; ADE43086.1; -; Genomic_DNA.
DR EMBL; GU396199; ADE43089.1; -; Genomic_DNA.
DR EMBL; GU396202; ADE43092.1; -; Genomic_DNA.
DR EMBL; GU396206; ADE43096.1; -; Genomic_DNA.
DR EMBL; FR682046; CBW45857.1; -; Genomic_DNA.
DR EMBL; FR682048; CBW45859.1; -; Genomic_DNA.
DR EMBL; FR682050; CBW45861.1; -; Genomic_DNA.
DR EMBL; FR682053; CBW45864.1; -; Genomic_DNA.
DR EMBL; FR682054; CBW45865.1; -; Genomic_DNA.
DR EMBL; FR682057; CBW45868.1; -; Genomic_DNA.
DR EMBL; FR682059; CBW45870.1; -; Genomic_DNA.
DR EMBL; FR682063; CBW45874.1; -; Genomic_DNA.
DR EMBL; FR682064; CBW45875.1; -; Genomic_DNA.
DR EMBL; FR682068; CBW45879.1; -; Genomic_DNA.
DR EMBL; FR682073; CBW45884.1; -; Genomic_DNA.
DR EMBL; FR682075; CBW45886.1; -; Genomic_DNA.
DR EMBL; AB008271; BAB08993.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90800.1; -; Genomic_DNA.
DR EMBL; AF083773; AAN60331.1; -; mRNA.
DR RefSeq; NP_568144.1; NM_120571.3.
DR AlphaFoldDB; Q9M670; -.
DR SMR; Q9M670; -.
DR STRING; 3702.AT5G04890.1; -.
DR iPTMnet; Q9M670; -.
DR PaxDb; Q9M670; -.
DR PRIDE; Q9M670; -.
DR ProteomicsDB; 228067; -.
DR EnsemblPlants; AT5G04890.1; AT5G04890.1; AT5G04890.
DR GeneID; 830370; -.
DR Gramene; AT5G04890.1; AT5G04890.1; AT5G04890.
DR KEGG; ath:AT5G04890; -.
DR Araport; AT5G04890; -.
DR TAIR; locus:2175438; AT5G04890.
DR eggNOG; KOG0710; Eukaryota.
DR HOGENOM; CLU_063780_0_0_1; -.
DR InParanoid; Q9M670; -.
DR OMA; GFAKEQM; -.
DR OrthoDB; 1346275at2759; -.
DR PRO; PR:Q9M670; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9M670; baseline and differential.
DR Genevisible; Q9M670; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009615; P:response to virus; IMP:TAIR.
DR GO; GO:0046741; P:transport of virus in host, tissue to tissue; IDA:UniProtKB.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR045045; RTM2-like.
DR PANTHER; PTHR43670; PTHR43670; 1.
DR Pfam; PF00011; HSP20; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Plant defense; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..366
FT /note="Protein RESTRICTED TEV MOVEMENT 2"
FT /id="PRO_0000429165"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 14..121
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REPEAT 129..133
FT /note="A-1"
FT /evidence="ECO:0000269|PubMed:10760245"
FT REPEAT 135..139
FT /note="A-2"
FT /evidence="ECO:0000269|PubMed:10760245"
FT REPEAT 156..160
FT /note="A-3"
FT /evidence="ECO:0000269|PubMed:10760245"
FT REPEAT 163..176
FT /note="B-1"
FT /evidence="ECO:0000269|PubMed:10760245"
FT REPEAT 178..191
FT /note="B-2"
FT /evidence="ECO:0000269|PubMed:10760245"
FT REPEAT 193..205
FT /note="B-3"
FT /evidence="ECO:0000269|PubMed:10760245"
FT REPEAT 206..210
FT /note="A-4"
FT /evidence="ECO:0000269|PubMed:10760245"
FT REPEAT 211..215
FT /note="A-5"
FT /evidence="ECO:0000269|PubMed:10760245"
FT REPEAT 216..220
FT /note="A-6"
FT /evidence="ECO:0000269|PubMed:10760245"
FT REGION 129..220
FT /note="6 X 5 AA repeats A of L-E-E-[SKR]-[ERK]"
FT REGION 163..206
FT /note="3 X 14 AA repeats B of [IMA]-[RK]-K-L-Q-E-E-A-K-A-K-
FT E-[EK]-[LA]"
FT REGION 345..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 71
FT /note="S -> N (in Ref. 6; AAN60331)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 366 AA; 41340 MW; 5AECACE58D7E18FF CRC64;
MAARQQQKGT GFGVQYEDFV PKSEWKDQPE ATILNIDLTG FAKEQMKVTY VHSSKMIRVT
GERPLANRKW SRFNEVFTVP QNCLVDKIHG SFKNNVLTIT MPKETITKVA YLPETSRTEA
AALEKAAKLE EKRLLEESRR KEKEEEEAKQ MKKQLLEEKE ALIRKLQEEA KAKEEAEMRK
LQEEAKAKEE AAAKKLQEEI EAKEKLEERK LEERRLEERK LEDMKLAEEA KLKKIQERKS
VDESGEKEKI LKPEVVYTKS GHVATPKPES GSGLKSGFGG VGEVVKSAEE KLGNLVEKEK
KMGKGIMEKI RRKEITSEEK KLMMNVGVAA LVIFALGAYV SYTFCSSSSS SSSSSPSSSS
SSTKPE
