RMR41_ARATH
ID RMR41_ARATH Reviewed; 296 AA.
AC Q93YN8; Q9SCL9;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Remorin 4.1 {ECO:0000305};
DE Short=AtREM4.1 {ECO:0000303|PubMed:17984200};
DE AltName: Full=Remorin group 4 member 1 {ECO:0000305};
GN Name=REM4.1 {ECO:0000303|PubMed:17984200};
GN OrderedLocusNames=At3g57540 {ECO:0000312|Araport:AT3G57540};
GN ORFNames=T8H10.14 {ECO:0000312|EMBL:CAB66111.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 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 REM4.2 AND KIN11, DISRUPTION PHENOTYPE, FUNCTION, AND PHOSPHORYLATION
RP BY KIN11.
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 REM4.2 to positively regulate the BCTV and
CC BSCTV susceptibility. {ECO:0000269|PubMed:25289013}.
CC -!- SUBUNIT: Forms homodimer and heterodimer with REM4.2 (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: Phosphorylated by KIN11. {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 (BCTV) and Beet Severe Curly Top Virus (BSCTV). The double mutant
CC rem4.1 rem4.2 displays resistance to BCTV and BSCTV.
CC {ECO:0000269|PubMed:25289013}.
CC -!- SIMILARITY: Belongs to the remorin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB66111.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL133248; CAB66111.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE79669.1; -; Genomic_DNA.
DR EMBL; AY059900; AAL24382.1; -; mRNA.
DR EMBL; BT001233; AAN65120.1; -; mRNA.
DR PIR; T46190; T46190.
DR RefSeq; NP_567050.1; NM_115614.3.
DR AlphaFoldDB; Q93YN8; -.
DR SMR; Q93YN8; -.
DR IntAct; Q93YN8; 2.
DR STRING; 3702.AT3G57540.1; -.
DR iPTMnet; Q93YN8; -.
DR PaxDb; Q93YN8; -.
DR PRIDE; Q93YN8; -.
DR ProteomicsDB; 228130; -.
DR EnsemblPlants; AT3G57540.1; AT3G57540.1; AT3G57540.
DR GeneID; 824921; -.
DR Gramene; AT3G57540.1; AT3G57540.1; AT3G57540.
DR KEGG; ath:AT3G57540; -.
DR Araport; AT3G57540; -.
DR TAIR; locus:2103508; AT3G57540.
DR eggNOG; ENOG502QTT4; Eukaryota.
DR HOGENOM; CLU_053612_1_0_1; -.
DR InParanoid; Q93YN8; -.
DR OMA; FKRQDAV; -.
DR OrthoDB; 1474163at2759; -.
DR PhylomeDB; Q93YN8; -.
DR PRO; PR:Q93YN8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q93YN8; 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; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..296
FT /note="Remorin 4.1"
FT /id="PRO_0000445510"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 226..261
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 296 AA; 32867 MW; D0F4B76E2DEE7E5C CRC64;
MLTLYGQERS PENSTTSTTD ASDRRDETPS SEIVVRDIHA MTTTTELTRP QQRGSGGGYL
SPSRSIAFSD GTTSSGENFT TVSREFNALV IAGSSMDNNS NGTNQSGGHR DVIRDERNEL
TRIGENDDVG DHGQVPEEDS NPWAIVPDDY NNRDGSENNI VLASSGGQNR MVTTASVQRV
KREEVEAKIT AWQTAKVAKI NNRFKRQDAV INGWLNEQVH RANSWMKKIE RKLEDRRAKA
MEKTQNKVAK AQRKAEERRA TAEGKRGTEV ARVLEVANLM RAVGRPPAKR SFFSLS
