LUR12_ARATH
ID LUR12_ARATH Reviewed; 90 AA.
AC Q4VP08; Q9LSW1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Protein LURE 1.2 {ECO:0000303|PubMed:23271953};
DE Short=AtLURE1.2 {ECO:0000303|PubMed:23271953};
DE AltName: Full=Cysteine-Rich Peptide 810_1.2 {ECO:0000303|PubMed:23271953};
DE Short=CRP810_1.2 {ECO:0000303|PubMed:23271953};
DE AltName: Full=Defensin-like protein 213 {ECO:0000303|PubMed:15955924};
DE Flags: Precursor;
GN Name=LURE1.2 {ECO:0000303|PubMed:23271953};
GN Synonyms=CRP810_1.2 {ECO:0000303|PubMed:23271953};
GN OrderedLocusNames=At5g43510 {ECO:0000312|Araport:AT5G43510};
GN ORFNames=MWF20.23 {ECO:0000312|EMBL:BAA97430.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 14-75, AND GENE FAMILY.
RX PubMed=15955924; DOI=10.1104/pp.105.060079;
RA Silverstein K.A.T., Graham M.A., Paape T.D., VandenBosch K.A.;
RT "Genome organization of more than 300 defensin-like genes in Arabidopsis.";
RL Plant Physiol. 138:600-610(2005).
RN [4]
RP FUNCTION, GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=23271953; DOI=10.1371/journal.pbio.1001449;
RA Takeuchi H., Higashiyama T.;
RT "A species-specific cluster of defensin-like genes encodes diffusible
RT pollen tube attractants in Arabidopsis.";
RL PLoS Biol. 10:E1001449-E1001449(2012).
RN [5]
RP FUNCTION, AND INTERACTION WITH MDIS1; MIK1; MIK2 AND TDR/PXY.
RX PubMed=26863186; DOI=10.1038/nature16975;
RA Wang T., Liang L., Xue Y., Jia P.F., Chen W., Zhang M.X., Wang Y.C.,
RA Li H.J., Yang W.C.;
RT "A receptor heteromer mediates the male perception of female attractants in
RT plants.";
RL Nature 531:241-244(2016).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 20-90, FUNCTION, DISULFIDE BONDS,
RP INTERACTION WITH PRK6, AND MUTAGENESIS OF ARG-67; ARG-68; LYS-70; ARG-73;
RP ARG-79 AND ARG-83.
RX PubMed=29109411; DOI=10.1038/s41467-017-01323-8;
RA Zhang X., Liu W., Nagae T.T., Takeuchi H., Zhang H., Han Z.,
RA Higashiyama T., Chai J.;
RT "Structural basis for receptor recognition of pollen tube attraction
RT peptides.";
RL Nat. Commun. 8:1331-1331(2017).
CC -!- FUNCTION: Pollen tube attractants guiding pollen tubes to the ovular
CC micropyle (PubMed:23271953, PubMed:29109411). Attracts specifically
CC pollen tubes from A.thaliana, but not those from A.lyrata
CC (PubMed:23271953). Triggers endocytosis of MDIS1 in the pollen tube tip
CC (PubMed:26863186). {ECO:0000269|PubMed:23271953,
CC ECO:0000269|PubMed:26863186, ECO:0000269|PubMed:29109411}.
CC -!- SUBUNIT: Interacts with MDIS1, MIK1, MIK2 and TDR/PXY, but not with
CC MDIS2 (PubMed:26863186). Binds to PRK6 LRRs (PubMed:29109411).
CC {ECO:0000269|PubMed:26863186, ECO:0000269|PubMed:29109411}.
CC -!- INTERACTION:
CC Q4VP08; C0LGU7: MDIS1; NbExp=5; IntAct=EBI-16196186, EBI-16196163;
CC Q4VP08; Q9M0G7: MIK1; NbExp=4; IntAct=EBI-16196186, EBI-16196224;
CC Q4VP08; Q8VZG8: MIK2; NbExp=4; IntAct=EBI-16196186, EBI-2270407;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23271953}.
CC Note=found at the micropylar end of the female gametophyte, possibly at
CC the filiform apparatus of the synergid cell. Difuses to the surface of
CC the funiculus of the ovule through the micropyle.
CC {ECO:0000269|PubMed:23271953}.
CC -!- TISSUE SPECIFICITY: Expressed in the pistil. Detected exclusively in
CC the synergid cells. {ECO:0000269|PubMed:23271953}.
CC -!- SIMILARITY: Belongs to the DEFL family. {ECO:0000305}.
CC -!- CAUTION: Lacks 1 of the 4 disulfide bonds, which are conserved features
CC of the family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97430.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB025638; BAA97430.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94973.1; -; Genomic_DNA.
DR EMBL; AY803254; AAX39295.1; -; mRNA.
DR RefSeq; NP_001078701.1; NM_001085232.2.
DR PDB; 5Y9W; X-ray; 1.85 A; C=20-90.
DR PDB; 5YAH; X-ray; 2.10 A; C=20-90.
DR PDBsum; 5Y9W; -.
DR PDBsum; 5YAH; -.
DR AlphaFoldDB; Q4VP08; -.
DR SMR; Q4VP08; -.
DR DIP; DIP-61970N; -.
DR IntAct; Q4VP08; 4.
DR STRING; 3702.AT5G43510.2; -.
DR PaxDb; Q4VP08; -.
DR PRIDE; Q4VP08; -.
DR EnsemblPlants; AT5G43510.2; AT5G43510.2; AT5G43510.
DR GeneID; 834371; -.
DR Gramene; AT5G43510.2; AT5G43510.2; AT5G43510.
DR KEGG; ath:AT5G43510; -.
DR Araport; AT5G43510; -.
DR TAIR; locus:2176521; AT5G43510.
DR HOGENOM; CLU_180309_0_0_1; -.
DR OrthoDB; 1816864at2759; -.
DR PhylomeDB; Q4VP08; -.
DR PRO; PR:Q4VP08; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q4VP08; baseline.
DR Genevisible; Q4VP08; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0010183; P:pollen tube guidance; IDA:TAIR.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..90
FT /note="Protein LURE 1.2"
FT /id="PRO_0000379705"
FT REGION 67..87
FT /note="PRK6 binding"
FT /evidence="ECO:0000269|PubMed:29109411,
FT ECO:0007744|PDB:5Y9W, ECO:0007744|PDB:5YAH"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 58..75
FT /evidence="ECO:0000269|PubMed:29109411,
FT ECO:0007744|PDB:5Y9W, ECO:0007744|PDB:5YAH"
FT DISULFID 61..82
FT /evidence="ECO:0000269|PubMed:29109411,
FT ECO:0007744|PDB:5Y9W, ECO:0007744|PDB:5YAH"
FT DISULFID 65..84
FT /evidence="ECO:0000269|PubMed:29109411,
FT ECO:0007744|PDB:5Y9W, ECO:0007744|PDB:5YAH"
FT MUTAGEN 67
FT /note="R->G: Compromised interaction with PRK6; when
FT associated with G-68 and G-70."
FT /evidence="ECO:0000269|PubMed:29109411"
FT MUTAGEN 68
FT /note="R->A: Reduced interaction with PRK6. Normal pollen
FT tube attraction."
FT /evidence="ECO:0000269|PubMed:29109411"
FT MUTAGEN 68
FT /note="R->G: Compromised interaction with PRK6; when
FT associated with G-67 and G-70."
FT /evidence="ECO:0000269|PubMed:29109411"
FT MUTAGEN 70
FT /note="K->G: Compromised interaction with PRK6; when
FT associated with G-67 and G-68."
FT /evidence="ECO:0000269|PubMed:29109411"
FT MUTAGEN 73
FT /note="R->A: Reduced interaction with PRK6. Normal pollen
FT tube attraction."
FT /evidence="ECO:0000269|PubMed:29109411"
FT MUTAGEN 79
FT /note="R->A: Reduced interaction with PRK6. Normal pollen
FT tube attraction."
FT /evidence="ECO:0000269|PubMed:29109411"
FT MUTAGEN 83
FT /note="R->A: Compromised interaction with PRK6. Reduced
FT pollen tube attraction."
FT /evidence="ECO:0000269|PubMed:29109411"
FT HELIX 54..67
FT /evidence="ECO:0007829|PDB:5Y9W"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:5Y9W"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:5Y9W"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:5Y9W"
SQ SEQUENCE 90 AA; 10289 MW; 6C48D0A4ADDAB673 CRC64;
MKLPIIFLTL LIFVSSCTST LINGSSDEER TYSFSPTTSP FDPRSLNQEL KIGRIGYCFD
CARACMRRGK YIRTCSFERK LCRCSISDIK
