REM41_ORYSJ
ID REM41_ORYSJ Reviewed; 316 AA.
AC Q7XII4;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Remorin 4.1 {ECO:0000305};
DE Short=OsREM4.1 {ECO:0000303|PubMed:17984200};
DE AltName: Full=Remorin group 4 member 1 {ECO:0000303|PubMed:17984200};
GN Name=REM4.1 {ECO:0000303|PubMed:17984200};
GN OrderedLocusNames=Os07g0569100 {ECO:0000312|EMBL:BAF21950.1},
GN LOC_Os07g38170 {ECO:0000305};
GN ORFNames=OJ1019_E02.9 {ECO:0000312|EMBL:BAC79688.1},
GN OsJ_24800 {ECO:0000312|EMBL:EAZ40353.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
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 [6]
RP FUNCTION, INTERACTION WITH BAK1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INDUCTION BY ABSCISIC ACID, AND PHOSPHORYLATION.
RX PubMed=27424498; DOI=10.1016/j.devcel.2016.06.011;
RA Gui J., Zheng S., Liu C., Shen J., Li J., Li L.;
RT "OsREM4.1 interacts with OsSERK1 to coordinate the interlinking between
RT abscisic acid and brassinosteroid signaling in rice.";
RL Dev. Cell 38:201-213(2016).
CC -!- FUNCTION: Functions in abscisic acid (ABA) signaling downstream of
CC BZIP23. Acts as antagonistic and negative regulator of brassinosteroid
CC (BR) signaling. Binds to BAK1 and inhibits its interaction with the BR
CC receptor BRI1. Inhibits the formation and subsequent activation of the
CC BRI1-BAK1 receptor complex. {ECO:0000269|PubMed:27424498}.
CC -!- SUBUNIT: Interacts with BAK1. {ECO:0000269|PubMed:27424498}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27424498};
CC Peripheral membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaf blades and leaf sheaths.
CC Expressed at low levels in stems and spikelets.
CC {ECO:0000269|PubMed:27424498}.
CC -!- INDUCTION: Induced by abscisic acid (ABA).
CC {ECO:0000269|PubMed:27424498}.
CC -!- PTM: Phosphorylated by BRI1. Phosphorylation reduces the binding
CC affinity to BAK1. {ECO:0000269|PubMed:27424498}.
CC -!- MISCELLANEOUS: Plants over-expressing REM4.1 are dwarf, with dark-
CC green, short and wide flat leaf blades, short panicles, spikelets and
CC grains, narrow bending angle of the lamina joint, and short leaf
CC epidermis cells. {ECO:0000269|PubMed:27424498}.
CC -!- SIMILARITY: Belongs to the remorin family. {ECO:0000305}.
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DR EMBL; AP003981; BAC79688.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF21950.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT02216.1; -; Genomic_DNA.
DR EMBL; CM000144; EAZ40353.1; -; Genomic_DNA.
DR RefSeq; XP_015646986.1; XM_015791500.1.
DR AlphaFoldDB; Q7XII4; -.
DR SMR; Q7XII4; -.
DR STRING; 4530.OS07T0569100-01; -.
DR PaxDb; Q7XII4; -.
DR PRIDE; Q7XII4; -.
DR EnsemblPlants; Os07t0569100-01; Os07t0569100-01; Os07g0569100.
DR GeneID; 4343649; -.
DR Gramene; Os07t0569100-01; Os07t0569100-01; Os07g0569100.
DR KEGG; osa:4343649; -.
DR eggNOG; ENOG502QTT4; Eukaryota.
DR HOGENOM; CLU_053612_0_0_1; -.
DR InParanoid; Q7XII4; -.
DR OMA; HEHETAN; -.
DR OrthoDB; 1474163at2759; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IDA:UniProtKB.
DR GO; GO:1900458; P:negative regulation of brassinosteroid mediated signaling pathway; IMP:UniProtKB.
DR InterPro; IPR005516; Remorin_C.
DR Pfam; PF03763; Remorin_C; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Cell membrane; Coiled coil; Membrane;
KW Reference proteome.
FT CHAIN 1..316
FT /note="Remorin 4.1"
FT /id="PRO_0000439019"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 242..288
FT /evidence="ECO:0000255"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 316 AA; 34096 MW; 48445576797C56A7 CRC64;
MLSEQTAASG SSSSSRGADD REIVISTGRE IVVRSSGGEE REEEVVVEEE LEEPEFRDIH
ALSPPPTPTP SQPSSSYHRR RRESWESAAG SRHTSIRSVG SDTAPSELFP TMSREFSAMV
AAAANANAAA AAAANGGDSS RAGVDDALGR IGEDELEETN PLAIVPDSNP IPSPRRAHLA
LPAPGDVSSA GGGHGDEVSV GQVKKEEVES KIAAWQIAEV AKVNNRFKRE EVVINGWEGD
QVEKANAWLK KYERKLEEKR AKAMEKAQNE VAKARRKAEE KRASAEAKRG TKVARVLELA
NFMRAVGRAP SKRSFF
