REMO_ARATH
ID REMO_ARATH Reviewed; 190 AA.
AC O80837; Q39087;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Remorin;
DE AltName: Full=DNA-binding protein;
GN Name=DBP; OrderedLocusNames=At2g45820; ORFNames=F4I18.20;
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], TISSUE SPECIFICITY, INDUCTION, AND
RP DNA-BINDING.
RC STRAIN=cv. Columbia;
RX PubMed=16666616; DOI=10.1104/pp.89.3.743;
RA Alliotte T., Tire C., Engler G., Peleman J., Caplan A., van Montagu M.,
RA Inze D.;
RT "An auxin-regulated gene of Arabidopsis thaliana encodes a DNA-binding
RT protein.";
RL Plant Physiol. 89:743-752(1989).
RN [2]
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 [3]
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 [4]
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 [5]
RP SUBUNIT.
RX PubMed=15604702; DOI=10.1007/s11103-004-1520-4;
RA Bariola P.A., Retelska D., Stasiak A., Kammerer R.A., Fleming A., Hijri M.,
RA Frank S., Farmer E.E.;
RT "Remorins form a novel family of coiled coil-forming oligomeric and
RT filamentous proteins associated with apical, vascular and embryonic tissues
RT in plants.";
RL Plant Mol. Biol. 55:579-594(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND THR-58, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Exhibits a non sequence-specific DNA-binding activity.
CC -!- SUBUNIT: May polymerize to form filamentous structures.
CC {ECO:0000269|PubMed:15604702}.
CC -!- INTERACTION:
CC O80837; O82798: ARR4; NbExp=3; IntAct=EBI-1788073, EBI-625213;
CC O80837; F4I4I6: At1g16705; NbExp=3; IntAct=EBI-1788073, EBI-25518505;
CC O80837; F4J355: At3g44620; NbExp=3; IntAct=EBI-1788073, EBI-21138032;
CC O80837; O04294: IMPA3; NbExp=4; IntAct=EBI-1788073, EBI-1644689;
CC O80837; Q9FFA5: REM1.4; NbExp=6; IntAct=EBI-1788073, EBI-4465086;
CC O80837; Q42551: SCE1; NbExp=3; IntAct=EBI-1788073, EBI-4442034;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques, with a maximal expression in apical regions.
CC {ECO:0000269|PubMed:16666616}.
CC -!- INDUCTION: 10-fold by auxin, 2-fold by gibberellic acid and not by
CC cytokinin. {ECO:0000269|PubMed:16666616}.
CC -!- SIMILARITY: Belongs to the remorin family. {ECO:0000305}.
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DR EMBL; M25268; AAA57124.1; -; Genomic_DNA.
DR EMBL; AC004665; AAC28542.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10605.1; -; Genomic_DNA.
DR EMBL; AY045996; AAK76670.1; -; mRNA.
DR EMBL; AY079329; AAL85060.1; -; mRNA.
DR PIR; T02465; T02465.
DR RefSeq; NP_182106.1; NM_130145.6.
DR AlphaFoldDB; O80837; -.
DR SMR; O80837; -.
DR BioGRID; 4526; 14.
DR IntAct; O80837; 9.
DR STRING; 3702.AT2G45820.1; -.
DR iPTMnet; O80837; -.
DR SwissPalm; O80837; -.
DR PaxDb; O80837; -.
DR PRIDE; O80837; -.
DR ProteomicsDB; 236228; -.
DR EnsemblPlants; AT2G45820.1; AT2G45820.1; AT2G45820.
DR GeneID; 819190; -.
DR Gramene; AT2G45820.1; AT2G45820.1; AT2G45820.
DR KEGG; ath:AT2G45820; -.
DR Araport; AT2G45820; -.
DR TAIR; locus:2050704; AT2G45820.
DR eggNOG; ENOG502RXGE; Eukaryota.
DR HOGENOM; CLU_088771_1_1_1; -.
DR InParanoid; O80837; -.
DR OMA; EKIHNPP; -.
DR OrthoDB; 1592521at2759; -.
DR PhylomeDB; O80837; -.
DR PRO; PR:O80837; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80837; baseline and differential.
DR Genevisible; O80837; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; IDA:TAIR.
DR GO; GO:0051607; P:defense response to virus; IDA:TAIR.
DR GO; GO:0051665; P:membrane raft localization; IDA:TAIR.
DR GO; GO:0009751; P:response to salicylic acid; IDA:TAIR.
DR InterPro; IPR005516; Remorin_C.
DR InterPro; IPR005518; Remorin_N.
DR Pfam; PF03763; Remorin_C; 1.
DR Pfam; PF03766; Remorin_N; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Phosphoprotein; Reference proteome.
FT CHAIN 1..190
FT /note="Remorin"
FT /id="PRO_0000311119"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 92..147
FT /evidence="ECO:0000255"
FT COMPBIAS 50..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 58
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 168
FT /note="K -> E (in Ref. 1; AAA57124)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 190 AA; 20968 MW; 092A817CF7E1B476 CRC64;
MAEEQKTSKV DVESPAVLAP AKEPTPAPVE VADEKIHNPP PVESKALAVV EKPIEEHTPK
KASSGSADRD VILADLEKEK KTSFIKAWEE SEKSKAENRA QKKISDVHAW ENSKKAAVEA
QLRKIEEKLE KKKAQYGEKM KNKVAAIHKL AEEKRAMVEA KKGEELLKAE EMGAKYRATG
VVPKATCGCF
