LLG1_ARATH
ID LLG1_ARATH Reviewed; 168 AA.
AC Q9FKT1;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=GPI-anchored protein LLG1 {ECO:0000305};
DE AltName: Full=LORELEI-like-GPI-anchored protein 1 {ECO:0000303|PubMed:20163554};
DE Flags: Precursor;
GN Name=LLG1 {ECO:0000303|PubMed:20163554};
GN OrderedLocusNames=At5g56170 {ECO:0000312|Araport:AT5G56170};
GN ORFNames=MDA7.23 {ECO:0000312|EMBL:BAB09299.1};
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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 [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20163554; DOI=10.1111/j.1365-313x.2010.04177.x;
RA Tsukamoto T., Qin Y., Huang Y., Dunatunga D., Palanivelu R.;
RT "A role for LORELEI, a putative glycosylphosphatidylinositol-anchored
RT protein, in Arabidopsis thaliana double fertilization and early seed
RT development.";
RL Plant J. 62:571-588(2010).
RN [5]
RP FUNCTION, INTERACTION WITH FER, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=26052747; DOI=10.7554/elife.06587;
RA Li C., Yeh F.L., Cheung A.Y., Duan Q., Kita D., Liu M.C., Maman J.,
RA Luu E.J., Wu B.W., Gates L., Jalal M., Kwong A., Carpenter H., Wu H.M.;
RT "Glycosylphosphatidylinositol-anchored proteins as chaperones and co-
RT receptors for FERONIA receptor kinase signaling in Arabidopsis.";
RL Elife 4:0-0(2015).
CC -!- FUNCTION: Component of the FER-regulated Rho GTPase signaling complex.
CC Acts as a chaperone and coreceptor for FER. Required for localization
CC of FER to the plasma membrane. {ECO:0000269|PubMed:26052747}.
CC -!- SUBUNIT: Interacts with FER. {ECO:0000269|PubMed:26052747}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26052747};
CC Lipid-anchor, GPI-anchor {ECO:0000255, ECO:0000269|PubMed:26052747}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen, pollen tubes, sporophytic
CC pistil tissues, in the early stages of female gametophyte development,
CC and in unfertilized, mature ovules (PubMed:20163554). Expressed in
CC roots, lateral roots, shoots, cotyledons, petioles, developing leaves
CC and anther filaments. {ECO:0000269|PubMed:20163554}.
CC -!- DISRUPTION PHENOTYPE: Retarded growth, collapsed root hairs, defective
CC trichomes, abnormal accumulation of high levels of anthocyanin and
CC overall reduced plant size (PubMed:26052747). No aborted seed phenotype
CC and normal production of seed sets (PubMed:20163554, PubMed:26052747).
CC {ECO:0000269|PubMed:20163554, ECO:0000269|PubMed:26052747}.
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DR EMBL; AB011476; BAB09299.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96729.1; -; Genomic_DNA.
DR EMBL; BT000437; AAN17414.1; -; mRNA.
DR EMBL; BT001157; AAN65044.1; -; mRNA.
DR RefSeq; NP_200428.1; NM_124999.5.
DR PDB; 6A5D; X-ray; 1.40 A; A/B=24-159.
DR PDBsum; 6A5D; -.
DR AlphaFoldDB; Q9FKT1; -.
DR SMR; Q9FKT1; -.
DR STRING; 3702.AT5G56170.1; -.
DR PaxDb; Q9FKT1; -.
DR PRIDE; Q9FKT1; -.
DR ProteomicsDB; 238460; -.
DR EnsemblPlants; AT5G56170.1; AT5G56170.1; AT5G56170.
DR GeneID; 835716; -.
DR Gramene; AT5G56170.1; AT5G56170.1; AT5G56170.
DR KEGG; ath:AT5G56170; -.
DR Araport; AT5G56170; -.
DR TAIR; locus:2161780; AT5G56170.
DR eggNOG; ENOG502S17V; Eukaryota.
DR HOGENOM; CLU_119747_0_0_1; -.
DR InParanoid; Q9FKT1; -.
DR OMA; CDAFKEL; -.
DR OrthoDB; 1487552at2759; -.
DR PhylomeDB; Q9FKT1; -.
DR PRO; PR:Q9FKT1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKT1; baseline and differential.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0090406; C:pollen tube; IDA:TAIR.
DR GO; GO:0045927; P:positive regulation of growth; IMP:UniProtKB.
DR InterPro; IPR039307; LORELEI-like.
DR PANTHER; PTHR31533; PTHR31533; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..144
FT /note="GPI-anchored protein LLG1"
FT /id="PRO_5008179976"
FT PROPEP 145..168
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000438100"
FT LIPID 144
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:6A5D"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:6A5D"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:6A5D"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:6A5D"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:6A5D"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:6A5D"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:6A5D"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:6A5D"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:6A5D"
SQ SEQUENCE 168 AA; 18460 MW; 309BBA71972C0374 CRC64;
MELLSRALFF FLLLSVLSSF SSSSFISDGV FESQSLVLGR NLLQTKKTCP VNFEFMNYTI
ITSKCKGPKY PPKECCGAFK DFACPYTDQL NDLSSDCATT MFSYINLYGK YPPGLFANQC
KEGKEGLECP AGSQLPPETS AEVNAATTSS SRLWLTVSAA LLVFVKLF
