LTPG2_ARATH
ID LTPG2_ARATH Reviewed; 193 AA.
AC Q9LZH5; C0Z2K5; F4J0G3; Q8L962;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Non-specific lipid transfer protein GPI-anchored 2 {ECO:0000303|PubMed:22891199, ECO:0000303|PubMed:23893219};
DE Short=AtLTPG-2 {ECO:0000303|PubMed:22891199, ECO:0000303|PubMed:23893219};
DE Short=Protein LTP-GPI-ANCHORED 2 {ECO:0000303|PubMed:22891199, ECO:0000303|PubMed:23893219};
DE AltName: Full=Xylogen-like protein 10 {ECO:0000303|PubMed:21558309};
DE Short=AtXYLP10 {ECO:0000303|PubMed:21558309};
DE Short=AtXYP5 {ECO:0000303|PubMed:21558309};
DE Flags: Precursor;
GN Name=LTPG2 {ECO:0000303|PubMed:22891199, ECO:0000303|PubMed:23893219};
GN Synonyms=XYLP10 {ECO:0000303|PubMed:21558309},
GN XYP5 {ECO:0000303|PubMed:21558309};
GN OrderedLocusNames=At3g43720 {ECO:0000312|Araport:AT3G43720};
GN ORFNames=T28A8.10 {ECO:0000312|EMBL:CAB83144.1};
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=21558309; DOI=10.1093/pcp/pcr060;
RA Kobayashi Y., Motose H., Iwamoto K., Fukuda H.;
RT "Expression and genome-wide analysis of the xylogen-type gene family.";
RL Plant Cell Physiol. 52:1095-1106(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP TISSUE SPECIFICITY.
RX PubMed=16299169; DOI=10.1104/pp.105.070805;
RA Suh M.C., Samuels A.L., Jetter R., Kunst L., Pollard M., Ohlrogge J.,
RA Beisson F.;
RT "Cuticular lipid composition, surface structure, and gene expression in
RT Arabidopsis stem epidermis.";
RL Plant Physiol. 139:1649-1665(2005).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=22891199; DOI=10.1093/pcp/pcs083;
RA Kim H., Lee S.B., Kim H.J., Min M.K., Hwang I., Suh M.C.;
RT "Characterization of glycosylphosphatidylinositol-anchored lipid transfer
RT protein 2 (LTPG2) and overlapping function between LTPG/LTPG1 and LTPG2 in
RT cuticular wax export or accumulation in Arabidopsis thaliana.";
RL Plant Cell Physiol. 53:1391-1403(2012).
RN [9]
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 [10]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, 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 [11]
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 [12]
RP FUNCTION, DISRUPTION PHENOTYPE, 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 that, together with LTPG1, binds to
CC lipids and functions as a component of the cuticular lipid export
CC machinery that performs extensive export of intracellular lipids (e.g.
CC C29 alkane) from epidermal cells to the surface to build the cuticular
CC wax layer and silique walls (PubMed:22891199). Contributes to pre-
CC invasive defense against some non-host powdery mildew pathogens by
CC preventing the penetration of the epidermal cell wall by the fungal
CC agents (e.g. Blumeria graminis f. sp. hordei (Bgh)) (PubMed:30102837).
CC Involved in seed and ovule maturation and development, probably by
CC regulating the fatty acids homeostasis during suberin and sporopollenin
CC biosynthesis or deposition (PubMed:24460633).
CC {ECO:0000269|PubMed:22891199, ECO:0000269|PubMed:24460633,
CC ECO:0000269|PubMed:30102837}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22891199};
CC Lipid-anchor, GPI-anchor {ECO:0000255}. Note=Targeted to the plasma
CC membrane via the vesicular trafficking system.
CC {ECO:0000269|PubMed:22891199}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9LZH5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LZH5-2; Sequence=VSP_053833;
CC Name=3;
CC IsoId=Q9LZH5-3; Sequence=VSP_053832;
CC -!- TISSUE SPECIFICITY: Up-regulated in the epidermis of top stems.
CC Expressed in roots, cotyledons, seedlings, leaves, stems, buds, flower
CC and silique walls (PubMed:23893219). Preferentially expressed in the
CC shoot apical meristem and the root meristem (PubMed:21558309). Also
CC detected in expanding leaves and petals, developing flowers, and
CC elongating pistils, stamens and siliques (PubMed:21558309).
CC {ECO:0000269|PubMed:16299169, ECO:0000269|PubMed:21558309,
CC ECO:0000269|PubMed:22891199, ECO:0000269|PubMed:23893219}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in seeds after imbibition
CC (PubMed:23893219). Mainly present in elongating or expanding tissues
CC (PubMed:21558309). Strongly expressed in the aerial portions and root
CC tips of seedlings. Present in stem and leaf epidermis, including the
CC trichomes, leaf mesophyll cells, and stem cortex and xylem. In flowers,
CC observed in the upper portion of the styles, anther filament, and veins
CC of the sepals and petals, silique walls and developing seeds
CC (PubMed:23893219). {ECO:0000269|PubMed:21558309,
CC ECO:0000269|PubMed:22891199, ECO:0000269|PubMed:23893219}.
CC -!- PTM: O-glycosylated on hydroxyprolines; noncontiguous hydroxylproline
CC residues are glycosylated with arabinogalactan. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Reduced cuticular wax load on the stem surface
CC and in silique walls, with altered cuticular lipid composition
CC (especially C29 alkane) associated with diffuse cuticular layer
CC structure (PubMed:22891199). Increased susceptibility to penetration of
CC the epidermal cell wall by the non-host mildew fungal agent Blumeria
CC graminis f. sp. hordei (Bgh) (PubMed:30102837). Some early aborted
CC seeds and infertile ovules, and increased salt permeability in seeds
CC (PubMed:24460633). {ECO:0000269|PubMed:22891199,
CC ECO:0000269|PubMed:24460633, ECO:0000269|PubMed:30102837}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR EMBL; AB246324; BAE73261.1; -; mRNA.
DR EMBL; AL162691; CAB83144.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77821.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77822.1; -; Genomic_DNA.
DR EMBL; AY045908; AAK76582.1; -; mRNA.
DR EMBL; AY079420; AAL85151.1; -; mRNA.
DR EMBL; AK318819; BAH56934.1; -; mRNA.
DR EMBL; AY088620; AAM66942.1; -; mRNA.
DR PIR; T47408; T47408.
DR RefSeq; NP_001030803.1; NM_001035726.2. [Q9LZH5-2]
DR RefSeq; NP_189958.1; NM_114240.4. [Q9LZH5-1]
DR AlphaFoldDB; Q9LZH5; -.
DR STRING; 3702.AT3G43720.1; -.
DR PaxDb; Q9LZH5; -.
DR ProteomicsDB; 238640; -. [Q9LZH5-1]
DR EnsemblPlants; AT3G43720.1; AT3G43720.1; AT3G43720. [Q9LZH5-1]
DR EnsemblPlants; AT3G43720.2; AT3G43720.2; AT3G43720. [Q9LZH5-2]
DR GeneID; 823481; -.
DR Gramene; AT3G43720.1; AT3G43720.1; AT3G43720. [Q9LZH5-1]
DR Gramene; AT3G43720.2; AT3G43720.2; AT3G43720. [Q9LZH5-2]
DR KEGG; ath:AT3G43720; -.
DR Araport; AT3G43720; -.
DR TAIR; locus:2101044; AT3G43720.
DR eggNOG; ENOG502S59X; Eukaryota.
DR InParanoid; Q9LZH5; -.
DR OMA; FSKMNIV; -.
DR OrthoDB; 1573659at2759; -.
DR PhylomeDB; Q9LZH5; -.
DR PRO; PR:Q9LZH5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LZH5; baseline and differential.
DR Genevisible; Q9LZH5; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008289; F:lipid binding; ISS:UniProtKB.
DR GO; GO:0042335; P:cuticle development; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0006869; P:lipid transport; ISS:UniProtKB.
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 Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW GPI-anchor; Lipid-binding; Lipoprotein; Membrane; Plant defense;
KW Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..165
FT /note="Non-specific lipid transfer protein GPI-anchored 2"
FT /id="PRO_0000425708"
FT PROPEP 166..193
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000425709"
FT REGION 143..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 165
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 38..83
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 48..67
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 68..110
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 81..120
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT VAR_SEQ 145..150
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_053832"
FT VAR_SEQ 149..150
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053833"
FT CONFLICT 176
FT /note="L -> R (in Ref. 6; AAM66942)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 193 AA; 19175 MW; 349983C874CE54E3 CRC64;
MSNVVVIAVV LIVASLTGHV SAQMDMSPSS GPSGAPDCMA NLMNMTGCLS YVTVGEGGGA
AKPDKTCCPA LAGLVESSPQ CLCYLLSGDM AAQLGIKIDK AKALKLPGVC GVITPDPSLC
SLFGIPVGAP VAMGDEGASP AYAPGSMSGA ESPGGFGSGP SASRGSDAPS SAPYSLFLNL
IIFPLAFAFY IFC
