RLP48_ARATH
ID RLP48_ARATH Reviewed; 813 AA.
AC F4JTU7; Q9SVM5;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2018, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Receptor-like protein 48 {ECO:0000303|PubMed:18434605};
DE Short=AtRLP48 {ECO:0000303|PubMed:18434605};
DE Flags: Precursor;
GN Name=RLP48 {ECO:0000303|PubMed:18434605};
GN OrderedLocusNames=At4g13880 {ECO:0000312|Araport:AT4G13880};
GN ORFNames=F18A5.270 {ECO:0000312|EMBL:CAB36852.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 GENE FAMILY.
RX PubMed=15955925; DOI=10.1104/pp.104.054452;
RA Fritz-Laylin L.K., Krishnamurthy N., Toer M., Sjoelander K.V., Jones J.D.;
RT "Phylogenomic analysis of the receptor-like proteins of rice and
RT Arabidopsis.";
RL Plant Physiol. 138:611-623(2005).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=18434605; DOI=10.1104/pp.108.119487;
RA Wang G., Ellendorff U., Kemp B., Mansfield J.W., Forsyth A., Mitchell K.,
RA Bastas K., Liu C.-M., Woods-Toer A., Zipfel C., de Wit P.J.G.M.,
RA Jones J.D.G., Toer M., Thomma B.P.H.J.;
RT "A genome-wide functional investigation into the roles of receptor-like
RT proteins in Arabidopsis.";
RL Plant Physiol. 147:503-517(2008).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25781967; DOI=10.1371/journal.pone.0120604;
RA Stetter M.G., Schmid K., Ludewig U.;
RT "Uncovering genes and ploidy involved in the high diversity in root hair
RT density, length and response to local scarce phosphate in Arabidopsis
RT thaliana.";
RL PLoS ONE 10:E0120604-E0120604(2015).
CC -!- FUNCTION: Plays a role in root hair development.
CC {ECO:0000269|PubMed:25781967}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Higher root hair density.
CC {ECO:0000269|PubMed:25781967}.
CC -!- SIMILARITY: Belongs to the RLP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEE83340.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB36852.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78430.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035528; CAB36852.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161537; CAB78430.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83340.1; ALT_SEQ; Genomic_DNA.
DR PIR; T05257; T05257.
DR RefSeq; NP_193124.2; NM_117462.2.
DR AlphaFoldDB; F4JTU7; -.
DR SMR; F4JTU7; -.
DR PaxDb; F4JTU7; -.
DR PRIDE; F4JTU7; -.
DR GeneID; 827022; -.
DR KEGG; ath:AT4G13880; -.
DR Araport; AT4G13880; -.
DR TAIR; locus:2119535; AT4G13880.
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_000288_18_3_1; -.
DR InParanoid; F4JTU7; -.
DR OrthoDB; 1085197at2759; -.
DR PRO; PR:F4JTU7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JTU7; 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:0048767; P:root hair elongation; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR045273; RLP23-like.
DR PANTHER; PTHR27004; PTHR27004; 2.
DR Pfam; PF00560; LRR_1; 2.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR PROSITE; PS51450; LRR; 11.
PE 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Leucine-rich repeat; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..813
FT /note="Receptor-like protein 48"
FT /id="PRO_5003315520"
FT TOPO_DOM 31..786
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 787..807
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 808..813
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 111..134
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 136..159
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 160..182
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 196..219
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 220..244
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 245..260
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 261..285
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 288..310
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 311..335
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 336..359
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 361..381
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 382..405
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 406..432
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 434..450
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 451..473
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 475..498
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 500..521
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 523..544
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 545..571
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 572..595
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 642..666
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 667..690
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 691..714
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 716..739
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REGION 756..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..782
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 673
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 721
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 813 AA; 90390 MW; 1AB353EC670ED749 CRC64;
MHSCSERRMM TVIWSLCLIF CLSNSILAIA KDLCLPDQRD ALLEFKNEFY VQEFDPHMKC
EKATETWRNK TDCCSWNRVS CDPKTGKVVE LDLMSSCLNG PLRSNSSLFR LQHLQSLELS
SNNISGILPD SIGNLKYLRS LSFRTCHLFG KIPSSLGSLS YLTHLDLSYN DFTSEGPDSG
GNLNRLTDLQ LVLLNLSSVT WIDLGSNQLK GMLPSNMSSL SKLVSFDISE NSFSGSIPSS
LFMIPSLNFS GPLEIGNISS HSELGYLYMG ENNFNGPIPG SLSKLVGLRD LSLSFWNTGR
GIVDFSIFLH LKSLCSLDLS YLNTRSMVDL SFFSHLMSLD ELDLSGINLK ISSTLSFPSA
TGTLILASCN IVEFPKFLEN QTSLFYLDIS ANHIEGQVPE WLWRLPTLSF VNIAQNSFSG
ELPMLPNSIY SFIASDNQFS GEIPRTVCEL VSLNTLVLSN NKFSGSIPRC FENFKTISIL
HLRNNSLSGV FPKEIISETL TSLDVGHNWL SGQLPKSLIK CTDLEFLNVE DNRINDKFPF
WLRSLSNLQI LVLRSNEFYG PIFSLEDSLS FPKLRIFDIS ENHFTGVLPS DYFAGWSAMS
SVVDIFDTTP QVHILGVFQG YYHNSVVLTN KGLNMELVGS GFTIYKTIDV SGNRLEGDIP
ESIGILKELI VLNMSNNAFT GHIPPSLSNL SNLQSLDLSQ NRLSGSIPPE LGKLTFLEWM
NFSYNRLEGP IPQATQIQSQ NSSSFAENPG LCGAPFLNKC GGEEEEEEEA TKQEEDEDEE
KEEKNQVFSW IAAAIGYVPG VFCGLTIAHI LTS