RMR42_ARATH
ID RMR42_ARATH Reviewed; 274 AA.
AC P93758; Q8H138;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Remorin 4.2 {ECO:0000305};
DE Short=AtREM4.2 {ECO:0000303|PubMed:17984200};
DE AltName: Full=Remorin group 4 member 2 {ECO:0000305};
GN Name=REM4.2 {ECO:0000303|PubMed:17984200};
GN OrderedLocusNames=At2g41870 {ECO:0000312|Araport:AT2G41870};
GN ORFNames=T11A7.23 {ECO:0000312|EMBL:AAM14826.1},
GN T6D20.22 {ECO:0000312|EMBL:AAB63554.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 GENE FAMILY.
RX PubMed=17984200; DOI=10.1104/pp.107.108639;
RA Raffaele S., Mongrand S., Gamas P., Niebel A., Ott T.;
RT "Genome-wide annotation of remorins, a plant-specific protein family:
RT evolutionary and functional perspectives.";
RL Plant Physiol. 145:593-600(2007).
RN [5]
RP INDUCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION
RP WITH REM4.1 AND KIN11, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=25289013; DOI=10.5423/ppj.oa.06.2014.0061;
RA Son S., Oh C.J., An C.S.;
RT "Arabidopsis thaliana remorins interact with SnRK1 and play a role in
RT susceptibility to Beet Curly Top Virus and Beet Severe Curly Top Virus.";
RL Plant Pathol. J. 30:269-278(2014).
CC -!- FUNCTION: Collaborates with REM4.1 to positively regulate the BCTV and
CC BSCTV susceptibility. {ECO:0000269|PubMed:25289013}.
CC -!- SUBUNIT: Forms homodimer and heterodimer with REM4.1 (PubMed:25289013).
CC Interacts with KIN11 (PubMed:25289013). {ECO:0000269|PubMed:25289013}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25289013}.
CC -!- TISSUE SPECIFICITY: Predominantly detected in bud, stem, root, flower,
CC silique, and leaves, and enhanced dramatically in senescence leaf.
CC {ECO:0000269|PubMed:25289013}.
CC -!- INDUCTION: Induced by mannitol, NaCl, drought, as well exogenous
CC abscisic acid (ABA) application. {ECO:0000269|PubMed:25289013}.
CC -!- PTM: Probably ubiquitinated and degraded by the 26S proteasome pathway.
CC {ECO:0000269|PubMed:25289013}.
CC -!- DISRUPTION PHENOTYPE: Slightly reduced susceptibility to Beet Curly Top
CC Virus and Beet Severe Curly Top Virus. The double mutant rem4.1 rem4.2
CC displays resistance to BCTV and BSCTV. {ECO:0000269|PubMed:25289013}.
CC -!- SIMILARITY: Belongs to the remorin family. {ECO:0000305}.
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DR EMBL; AC002339; AAM14826.1; -; Genomic_DNA.
DR EMBL; U90439; AAB63554.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10043.1; -; Genomic_DNA.
DR EMBL; AF326883; AAG41465.1; -; mRNA.
DR EMBL; AF339703; AAK00385.1; -; mRNA.
DR EMBL; BT000793; AAN31932.1; -; mRNA.
DR PIR; B84847; B84847.
DR RefSeq; NP_181718.1; NM_129751.2.
DR AlphaFoldDB; P93758; -.
DR SMR; P93758; -.
DR IntAct; P93758; 2.
DR STRING; 3702.AT2G41870.1; -.
DR iPTMnet; P93758; -.
DR PaxDb; P93758; -.
DR PRIDE; P93758; -.
DR ProteomicsDB; 228141; -.
DR EnsemblPlants; AT2G41870.1; AT2G41870.1; AT2G41870.
DR GeneID; 818787; -.
DR Gramene; AT2G41870.1; AT2G41870.1; AT2G41870.
DR KEGG; ath:AT2G41870; -.
DR Araport; AT2G41870; -.
DR TAIR; locus:2054376; AT2G41870.
DR eggNOG; ENOG502QTT4; Eukaryota.
DR HOGENOM; CLU_053612_1_0_1; -.
DR InParanoid; P93758; -.
DR OMA; FKCEDAV; -.
DR OrthoDB; 1474163at2759; -.
DR PhylomeDB; P93758; -.
DR PRO; PR:P93758; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P93758; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IPI:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0010555; P:response to mannitol; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR InterPro; IPR005516; Remorin_C.
DR Pfam; PF03763; Remorin_C; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Membrane; Reference proteome; Ubl conjugation.
FT CHAIN 1..274
FT /note="Remorin 4.2"
FT /id="PRO_0000445511"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 204..239
FT /evidence="ECO:0000255"
FT COMPBIAS 11..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 274 AA; 30944 MW; 87A4DC3BBEE7E104 CRC64;
MLTLYHQERS PDATSNDRDE TPETVVREVH ALTPAPEDNS RTMTATLPPP PAFRGYFSPP
RSATTMSEGE NFTTISREFN ALVIAGSSME NNELMTRDVT QREDERQDEL MRIHEDTDHE
EETNPLAIVP DQYPGSGLDP GSDNGPGQSR VGSTVQRVKR EEVEAKITAW QTAKLAKINN
RFKREDAVIN GWFNEQVNKA NSWMKKIERK LEERKAKAME KTQNNVAKAQ RKAEERRATA
EAKRGTEVAK VVEVANLMRA LGRPPAKRSF FSFS
