LTPG3_ARATH
ID LTPG3_ARATH Reviewed; 180 AA.
AC Q9LE56; A0ME74;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Non-specific lipid transfer protein GPI-anchored 3 {ECO:0000303|PubMed:23893219};
DE Short=AtLTPG-3 {ECO:0000303|PubMed:23893219};
DE Short=Protein LTP-GPI-ANCHORED 3 {ECO:0000303|PubMed:23893219};
DE Flags: Precursor;
GN Name=LTPG3 {ECO:0000303|PubMed:23893219};
GN OrderedLocusNames=At1g18280 {ECO:0000312|Araport:AT1G18280};
GN ORFNames=F15H18.20 {ECO:0000312|EMBL:AAF25992.1},
GN T10O22.25 {ECO:0000312|EMBL:AAF78376.1};
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=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 [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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=14671020; DOI=10.1105/tpc.014407;
RA Lalanne E., Honys D., Johnson A., Borner G.H.H., Lilley K.S., Dupree P.,
RA Grossniklaus U., Twell D.;
RT "SETH1 and SETH2, two components of the glycosylphosphatidylinositol anchor
RT biosynthetic pathway, are required for pollen germination and tube growth
RT in Arabidopsis.";
RL Plant Cell 16:229-240(2004).
RN [7]
RP REVIEW.
RX PubMed=23505340; DOI=10.1199/tab.0161;
RA Li-Beisson Y., Shorrosh B., Beisson F., Andersson M.X., Arondel V.,
RA Bates P.D., Baud S., Bird D., Debono A., Durrett T.P., Franke R.B.,
RA Graham I.A., Katayama K., Kelly A.A., Larson T., Markham J.E., Miquel M.,
RA Molina I., Nishida I., Rowland O., Samuels L., Schmid K.M., Wada H.,
RA Welti R., Xu C., Zallot R., Ohlrogge J.;
RT "Acyl-lipid metabolism.";
RL Arabidopsis Book 11:E0161-E0161(2013).
RN [8]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=23893219; DOI=10.1007/s11103-013-0113-5;
RA Edstam M.M., Blomqvist K., Ekloef A., Wennergren U., Edqvist J.;
RT "Coexpression patterns indicate that GPI-anchored non-specific lipid
RT transfer proteins are involved in accumulation of cuticular wax, suberin
RT and sporopollenin.";
RL Plant Mol. Biol. 83:625-649(2013).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=24460633; DOI=10.1111/ppl.12156;
RA Edstam M.M., Edqvist J.;
RT "Involvement of GPI-anchored lipid transfer proteins in the development of
RT seed coats and pollen in Arabidopsis thaliana.";
RL Physiol. Plantarum 152:32-42(2014).
RN [10]
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=30102837; DOI=10.1111/mpp.12740;
RA Fahlberg P., Buhot N., Johansson O.N., Andersson M.X.;
RT "Involvement of lipid transfer proteins in resistance against a non-host
RT powdery mildew in Arabidopsis thaliana.";
RL Mol. Plant Pathol. 20:69-77(2019).
CC -!- FUNCTION: Lipid transfer protein involved in seed and ovule maturation
CC and development, probably by regulating the fatty acids homeostasis
CC during suberin and sporopollenin biosynthesis or deposition.
CC {ECO:0000269|PubMed:24460633}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-
CC anchor {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Restricted to stamen, pollen and sporophytic
CC tissues (PubMed:14671020, PubMed:24460633). Also detected, at low
CC levels, in stems and leaves (PubMed:14671020).
CC {ECO:0000269|PubMed:14671020, ECO:0000269|PubMed:24460633}.
CC -!- DISRUPTION PHENOTYPE: Inability to limit tetrazolium salt uptake in
CC seeds, development of hair-like structures on seeds, altered pollen
CC morphologies, deformed or collapsed, and decreased levels of omega-
CC hydroxy fatty acids in seed coats. {ECO:0000269|PubMed:24460633}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28401.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC013354; AAF25992.1; -; Genomic_DNA.
DR EMBL; AC069551; AAF78376.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29697.1; -; Genomic_DNA.
DR EMBL; DQ446260; ABE65630.1; -; mRNA.
DR EMBL; DQ652842; ABK28401.1; ALT_SEQ; mRNA.
DR EMBL; BT025741; ABF83631.1; -; mRNA.
DR EMBL; AY086971; AAM64534.1; -; mRNA.
DR RefSeq; NP_173264.1; NM_101686.5.
DR AlphaFoldDB; Q9LE56; -.
DR STRING; 3702.AT1G18280.1; -.
DR PaxDb; Q9LE56; -.
DR PRIDE; Q9LE56; -.
DR ProteomicsDB; 190011; -.
DR EnsemblPlants; AT1G18280.1; AT1G18280.1; AT1G18280.
DR GeneID; 838408; -.
DR Gramene; AT1G18280.1; AT1G18280.1; AT1G18280.
DR KEGG; ath:AT1G18280; -.
DR Araport; AT1G18280; -.
DR TAIR; locus:2014074; AT1G18280.
DR eggNOG; ENOG502S5G2; Eukaryota.
DR HOGENOM; CLU_116928_3_1_1; -.
DR InParanoid; Q9LE56; -.
DR OMA; VAKDATC; -.
DR OrthoDB; 1442303at2759; -.
DR PhylomeDB; Q9LE56; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LE56; baseline and differential.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.110.10; -; 1.
DR InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR InterPro; IPR043325; LTSS.
DR PANTHER; PTHR33044; PTHR33044; 1.
DR Pfam; PF14368; LTP_2; 1.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; Protease; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..158
FT /note="Non-specific lipid transfer protein GPI-anchored 3"
FT /id="PRO_5014312954"
FT PROPEP 159..180
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451636"
FT REGION 116..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 158
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 41..78
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 48..62
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 63..104
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 76..113
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
SQ SEQUENCE 180 AA; 18073 MW; 191F591D76103C6D CRC64;
MEAVRFAVAV VLVFCYVTSS NAQMTSPPSG GAGGDAHSLP CIQKLMPCQP YLHLATPPPA
TCCMPLNEIV AKDATCLCAV FNNVDMLKSL NLTKENALDL PKACGAKADV SLCKTSAGTN
SSSTPPATPK TPPASSTSTG TGSGSTGNAA PSTAKPTSSA PAINFGGLSF ASAVVATLFF
