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Database: UniProt
Entry: O65375
LinkDB: O65375
Original site: O65375 
ID   LRX1_ARATH              Reviewed;         744 AA.
AC   O65375;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 149.
DE   RecName: Full=Leucine-rich repeat extensin-like protein 1;
DE            Short=AtLRX1;
DE            Short=LRR/EXTENSIN1;
DE   AltName: Full=Cell wall hydroxyproline-rich glycoprotein;
DE   Flags: Precursor;
GN   Name=LRX1; OrderedLocusNames=At1g12040; ORFNames=F12F1.9;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=11331608; DOI=10.1101/gad.200201;
RA   Baumberger N., Ringli C., Keller B.;
RT   "The chimeric leucine-rich repeat/extensin cell wall protein LRX1 is
RT   required for root hair morphogenesis in Arabidopsis thaliana.";
RL   Genes Dev. 15:1128-1139(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12834403; DOI=10.1046/j.1365-313x.2003.01784.x;
RA   Baumberger N., Steiner M., Ryser U., Keller B., Ringli C.;
RT   "Synergistic interaction of the two paralogous Arabidopsis genes LRX1 and
RT   LRX2 in cell wall formation during root hair development.";
RL   Plant J. 35:71-81(2003).
RN   [5]
RP   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. Together with LRX2,
CC       component of the extracellular mechanism regulating root hair
CC       morphogenesis and elongation. {ECO:0000269|PubMed:11331608,
CC       ECO:0000269|PubMed:12834403}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000269|PubMed:11331608}. Note=Specifically localized in the wall
CC       of the root hair proper.
CC   -!- TISSUE SPECIFICITY: Expressed in root hair cells (at protein level).
CC       {ECO:0000269|PubMed:11331608}.
CC   -!- DEVELOPMENTAL STAGE: First observed in differentiating trichoblast and
CC       later confined to root hair proper. Soluble in the early stages of root
CC       hair development and becomes insolubilized in later stages.
CC       {ECO:0000269|PubMed:11331608}.
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}.
CC   -!- DISRUPTION PHENOTYPE: Irregular root hair development that frequently
CC       abort, swell, or branch. Stronger phenotype when associated with LRX2
CC       disruption; frequent rupture of root hairs soon after their initiation.
CC       {ECO:0000269|PubMed:11331608, ECO:0000269|PubMed:12834403}.
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DR   EMBL; AY026364; AAK07681.1; -; mRNA.
DR   EMBL; AC002131; AAC17609.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE28829.1; -; Genomic_DNA.
DR   PIR; E86255; E86255.
DR   RefSeq; NP_172668.1; NM_101076.2.
DR   AlphaFoldDB; O65375; -.
DR   SMR; O65375; -.
DR   STRING; 3702.O65375; -.
DR   GlyCosmos; O65375; 5 sites, No reported glycans.
DR   PaxDb; 3702-AT1G12040-1; -.
DR   ProteomicsDB; 238635; -.
DR   EnsemblPlants; AT1G12040.1; AT1G12040.1; AT1G12040.
DR   GeneID; 837756; -.
DR   Gramene; AT1G12040.1; AT1G12040.1; AT1G12040.
DR   KEGG; ath:AT1G12040; -.
DR   Araport; AT1G12040; -.
DR   TAIR; AT1G12040; LRX1.
DR   eggNOG; ENOG502QQD2; Eukaryota.
DR   HOGENOM; CLU_000288_23_3_1; -.
DR   InParanoid; O65375; -.
DR   OMA; TYADNFI; -.
DR   OrthoDB; 691476at2759; -.
DR   PRO; PR:O65375; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; O65375; baseline and differential.
DR   Genevisible; O65375; AT.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA: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   GO; GO:0010054; P:trichoblast differentiation; IMP:TAIR.
DR   GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR013210; LRR_N_plant-typ.
DR   PANTHER; PTHR32093:SF116; LEUCINE-RICH REPEAT EXTENSIN-LIKE PROTEIN 1; 1.
DR   PANTHER; PTHR32093; LEUCINE-RICH REPEAT EXTENSIN-LIKE PROTEIN 3-RELATED; 1.
DR   Pfam; PF00560; LRR_1; 3.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
DR   SUPFAM; SSF52058; L domain-like; 1.
PE   1: Evidence at protein level;
KW   Cell wall; Cell wall biogenesis/degradation; Developmental protein;
KW   Glycoprotein; Hydroxylation; Leucine-rich repeat; Reference proteome;
KW   Repeat; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..744
FT                   /note="Leucine-rich repeat extensin-like protein 1"
FT                   /id="PRO_0000395461"
FT   REPEAT          122..145
FT                   /note="LRR 1"
FT   REPEAT          147..170
FT                   /note="LRR 2"
FT   REPEAT          171..194
FT                   /note="LRR 3"
FT   REPEAT          196..217
FT                   /note="LRR 4"
FT   REPEAT          219..240
FT                   /note="LRR 5"
FT   REPEAT          241..265
FT                   /note="LRR 6"
FT   REPEAT          266..289
FT                   /note="LRR 7"
FT   REPEAT          290..313
FT                   /note="LRR 8"
FT   REPEAT          315..336
FT                   /note="LRR 9"
FT   REPEAT          381..404
FT                   /note="LRR 10"
FT   REGION          382..744
FT                   /note="Contains the Ser-Pro(4) repeats"
FT   REGION          408..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          518..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          555..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          658..744
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        658..682
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        700..744
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        71
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        253
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        344
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   744 AA;  80994 MW;  3C75174DBBB91F6F CRC64;
     MLFPPLRSLF LFTLLLSSVC FLQIKADHDD ESDLGSDIKV DKRLKFENPK LRQAYIALQS
     WKKAIFSDPF NFTANWNGSD VCSYNGIYCA PSPSYPKTRV VAGIDLNHAD MAGYLASELG
     LLSDLALFHI NSNRFCGEVP LTFNRMKLLY ELDLSNNRFV GKFPKVVLSL PSLKFLDLRY
     NEFEGKIPSK LFDRELDAIF LNHNRFRFGI PKNMGNSPVS ALVLADNNLG GCIPGSIGQM
     GKTLNELILS NDNLTGCLPP QIGNLKKVTV FDITSNRLQG PLPSSVGNMK SLEELHVANN
     AFTGVIPPSI CQLSNLENFT YSSNYFSGRP PICAASLLAD IVVNGTMNCI TGLARQRSDK
     QCSSLLARPV DCSKFGCYNI FSPPPPTFKM SPEVRTLPPP IYVYSSPPPP PSSKMSPTVR
     AYSPPPPPSS KMSPSVRAYS PPPPPYSKMS PSVRAYPPPP PPSPSPPPPY VYSSPPPPYV
     YSSPPPPPYV YSSPPPPPYV YSSPPPPYVY SSPPPPYVYS SPPPPPPSPP PPCPESSPPP
     PVVYYAPVTQ SPPPPSPVYY PPVTQSPPPP SPVYYPPVTN SPPPPSPVYY PPVTYSPPPP
     SPVYYPQVTP SPPPPSPLYY PPVTPSPPPP SPVYYPPVTP SPPPPSPVYY PPVTPSPPPP
     SPVYYPSETQ SPPPPTEYYY SPSQSPPPTK ACKEGHPPQA TPSYEPPPEY SYSSSPPPPS
     PTSYFPPMPS VSYDASPPPP PSYY
//
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