RTM2D_ARATH
ID RTM2D_ARATH Reviewed; 366 AA.
AC D9UC01;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Inactive protein RESTRICTED TEV MOVEMENT 2;
DE AltName: Full=Inactive restricted tobacco etch virus movement protein 2;
GN Name=RTM2;
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=cv. Ge-1; 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).
CC -!- FUNCTION: Seems to not be involved in heat resistance (By similarity).
CC Unable to mediate restriction of long-distance movement of the
CC pathogenic tobacco etch virus (TEV) without causing a hypersensitive
CC response or inducing systemic acquired resistance. {ECO:0000250,
CC ECO:0000269|PubMed:22723957}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}. Note=Present in sieve elements. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
CC -!- CAUTION: Has been shown to be active in cv. Columbia (AC Q9M670) due to
CC naturally occurring sequence variation in this strain. The sequence
CC shown is from strains cv. Ge-1. {ECO:0000305}.
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DR EMBL; FR682072; CBW45883.1; -; Genomic_DNA.
DR AlphaFoldDB; D9UC01; -.
DR SMR; D9UC01; -.
DR ExpressionAtlas; D9UC01; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Cell membrane; Membrane; Plant defense; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..366
FT /note="Inactive protein RESTRICTED TEV MOVEMENT 2"
FT /id="PRO_0000429169"
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 REPEAT 135..139
FT /note="A-2"
FT REPEAT 156..160
FT /note="A-3"
FT REPEAT 163..176
FT /note="B-1"
FT REPEAT 178..191
FT /note="B-2"
FT REPEAT 193..205
FT /note="B-3"
FT REPEAT 206..210
FT /note="A-4"
FT REPEAT 211..215
FT /note="A-5"
FT REPEAT 216..220
FT /note="A-6"
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"
SQ SEQUENCE 366 AA; 41367 MW; FC70CB5A376E3E16 CRC64;
MAARQQQKGT GFGVQYEDFV PKSEWKDQPE ATILNIDLTG FAKEQMKVTY VHSSKMIRVT
GERPLANRKW NRFNEVFTVP QNCLVDKIHG SFKKNVLTIT MPKETITKVA YLPETSRTEA
AALEKAAKLE EKRLLEESRR KEKEEEEAKQ MKKQLLEEKE ALIRKLQEEA KAKEEAEMRK
LQEEAKANEE AAAKKLQEEI EAKEKLEERK LEERRLEERK LEDMKLAEEA KLKKIQERKS
VDESGEKEKI LKPEVVYTKS GHVATPKPES GSGLKSGFGG VGEVVKSAEE KLGNLVEKEK
KMGKGIMEKI RRKEITSEEK KLMMNVGVAA LVIFALGAYV SYTFCSSSSS SSSSSPSSSS
SSTKPE