LRX3_ARATH
ID LRX3_ARATH Reviewed; 760 AA.
AC Q9T0K5;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Leucine-rich repeat extensin-like protein 3;
DE Short=AtLRX3;
DE Short=LRR/EXTENSIN3;
DE AltName: Full=Cell wall hydroxyproline-rich glycoprotein;
DE Flags: Precursor;
GN Name=LRX3; OrderedLocusNames=At4g13340; ORFNames=T9E8.80;
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 INTERACTION WITH SH3P1.
RX PubMed=11701884; DOI=10.2307/3871590;
RA Lam B.C.-H., Sage T.L., Bianchi F., Blumwald E.;
RT "Role of SH3 domain-containing proteins in clathrin-mediated vesicle
RT trafficking in Arabidopsis.";
RL Plant Cell 13:2499-2512(2001).
RN [4]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12644681; DOI=10.1104/pp.102.014928;
RA Baumberger N., Doesseger B., Guyot R., Diet A., Parsons R.L., Clark M.A.,
RA Simmons M.P., Bedinger P., Goff S.A., Ringli C., Keller B.;
RT "Whole-genome comparison of leucine-rich repeat extensins in Arabidopsis
RT and rice. A conserved family of cell wall proteins form a vegetative and a
RT reproductive clade.";
RL Plant Physiol. 131:1313-1326(2003).
CC -!- FUNCTION: Modulates cell morphogenesis by regulating cell wall
CC formation and assembly, and/or growth polarization. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SH3P1. {ECO:0000269|PubMed:11701884}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000250|UniProtKB:O48809}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves and flowers,
CC mostly in vascular tissues. {ECO:0000269|PubMed:12644681}.
CC -!- PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat.
CC {ECO:0000250}.
CC -!- PTM: O-glycosylated on hydroxyprolines. {ECO:0000250}.
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DR EMBL; AL049608; CAB40769.1; -; Genomic_DNA.
DR EMBL; AL161536; CAB78376.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83265.1; -; Genomic_DNA.
DR PIR; T06291; T06291.
DR RefSeq; NP_193070.1; NM_117407.3.
DR AlphaFoldDB; Q9T0K5; -.
DR BioGRID; 12261; 1.
DR STRING; 3702.AT4G13340.1; -.
DR PaxDb; Q9T0K5; -.
DR PRIDE; Q9T0K5; -.
DR ProteomicsDB; 238739; -.
DR EnsemblPlants; AT4G13340.1; AT4G13340.1; AT4G13340.
DR GeneID; 826964; -.
DR Gramene; AT4G13340.1; AT4G13340.1; AT4G13340.
DR KEGG; ath:AT4G13340; -.
DR Araport; AT4G13340; -.
DR TAIR; locus:2142105; AT4G13340.
DR eggNOG; ENOG502QQ2D; Eukaryota.
DR HOGENOM; CLU_000288_23_3_1; -.
DR InParanoid; Q9T0K5; -.
DR OMA; NCRCEGK; -.
DR OrthoDB; 670436at2759; -.
DR PhylomeDB; Q9T0K5; -.
DR PRO; PR:Q9T0K5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9T0K5; baseline and differential.
DR Genevisible; Q9T0K5; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0042277; F:peptide binding; IPI:TAIR.
DR GO; GO:0005199; F:structural constituent of cell wall; ISS:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR Pfam; PF08263; LRRNT_2; 1.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation; Glycoprotein; Hydroxylation;
KW Leucine-rich repeat; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..760
FT /note="Leucine-rich repeat extensin-like protein 3"
FT /id="PRO_0000395463"
FT REPEAT 21..45
FT /note="LRR 1"
FT REPEAT 113..137
FT /note="LRR 2"
FT REPEAT 138..160
FT /note="LRR 3"
FT REPEAT 161..185
FT /note="LRR 4"
FT REPEAT 186..209
FT /note="LRR 5"
FT REPEAT 211..232
FT /note="LRR 6"
FT REPEAT 234..255
FT /note="LRR 7"
FT REPEAT 256..279
FT /note="LRR 8"
FT REPEAT 281..303
FT /note="LRR 9"
FT REPEAT 304..327
FT /note="LRR 10"
FT REGION 389..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..758
FT /note="Contains the Ser-Pro(4) repeats"
FT REGION 515..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..502
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 760 AA; 82246 MW; 20CDE1C8E6CEECFC CRC64;
MKKTIQILLF FFFLINLTNA LSISSDGGVL SDNEVRHIQR RQLLEFAERS VKITVDPSLN
FENPRLRNAY IALQAWKQAI LSDPNNFTSN WIGSNVCNYT GVFCSPALDN RKIRTVAGID
LNHADIAGYL PEELGLLSDL ALFHVNSNRF CGTVPHRFNR LKLLFELDLS NNRFAGKFPT
VVLQLPSLKF LDLRFNEFEG TVPKELFSKD LDAIFINHNR FRFELPENFG DSPVSVIVLA
NNRFHGCVPS SLVEMKNLNE IIFMNNGLNS CLPSDIGRLK NVTVFDVSFN ELVGPLPESV
GEMVSVEQLN VAHNMLSGKI PASICQLPKL ENFTYSYNFF TGEAPVCLRL PEFDDRRNCL
PGRPAQRSPG QCKAFLSRPP VNCGSFSCGR SVSPRPPVVT PLPPPSLPSP PPPAPIFSTP
PTLTSPPPPS PPPPVYSPPP PPPPPPPVYS PPPPPPPPPP PPVYSPPPPP PPPPPPPPVY
SPPPPSPPPP PPPVYSPPPP PPPPPPPPVY SPPPPPVYSS PPPPPSPAPT PVYCTRPPPP
PPHSPPPPQF SPPPPEPYYY SSPPPPHSSP PPHSPPPPHS PPPPIYPYLS PPPPPTPVSS
PPPTPVYSPP PPPPCIEPPP PPPCIEYSPP PPPPVVHYSS PPPPPVYYSS PPPPPVYYSS
PPPPPPVHYS SPPPPEVHYH SPPPSPVHYS SPPPPPSAPC EESPPPAPVV HHSPPPPMVH
HSPPPPVIHQ SPPPPSPEYE GPLPPVIGVS YASPPPPPFY
