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Non-specific lipid transfer protein GPI-anchored 2 (AtLTPG-2) (Protein LTP-GPI-ANCHORED 2) (Xylogen-like protein 5) (AtXYP5)

 LTPG2_ARATH             Reviewed;         193 AA.
Q9LZH5; C0Z2K5; F4J0G3; Q8L962;
19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-APR-2018, entry version 108.
RecName: Full=Non-specific lipid transfer protein GPI-anchored 2;
Short=AtLTPG-2;
Short=Protein LTP-GPI-ANCHORED 2;
AltName: Full=Xylogen-like protein 5;
Short=AtXYP5;
Flags: Precursor;
Name=LTPG2; Synonyms=XYP5; OrderedLocusNames=At3g43720;
ORFNames=T28A8.10;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Kobayashi Y., Sawa S., Iwamoto K., Motose H., Fukuda H.;
"Xylogen family genes, involved in cell-cell communication in
Arabidopsis.";
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
TISSUE SPECIFICITY.
PubMed=16299169; DOI=10.1104/pp.105.070805;
Suh M.C., Samuels A.L., Jetter R., Kunst L., Pollard M., Ohlrogge J.,
Beisson F.;
"Cuticular lipid composition, surface structure, and gene expression
in Arabidopsis stem epidermis.";
Plant Physiol. 139:1649-1665(2005).
[8]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=22891199; DOI=10.1093/pcp/pcs083;
Kim H., Lee S.B., Kim H.J., Min M.K., Hwang I., Suh M.C.;
"Characterization of glycosylphosphatidylinositol-anchored lipid
transfer protein 2 (LTPG2) and overlapping function between LTPG/LTPG1
and LTPG2 in cuticular wax export or accumulation in Arabidopsis
thaliana.";
Plant Cell Physiol. 53:1391-1403(2012).
-!- FUNCTION: Lipid transfer protein that, together with LTPG1, binds
to lipids and functions as a component of the cuticular lipid
export machinery that performs extensive export of intracellular
lipids (e.g. C29 alkane) from epidermal cells to the surface to
build the cuticular wax layer and silique walls.
{ECO:0000269|PubMed:22891199}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22891199};
Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:22891199}.
Note=Targeted to the plasma membrane via the vesicular trafficking
system.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9LZH5-1; Sequence=Displayed;
Name=2;
IsoId=Q9LZH5-2; Sequence=VSP_053833;
Note=Derived from EST data. No experimental confirmation
available.;
Name=3;
IsoId=Q9LZH5-3; Sequence=VSP_053832;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Up-regulated in the epidermis of top stems.
Expressed in roots, seedlings, leaves, stems, buds, flower and
silique walls. {ECO:0000269|PubMed:16299169,
ECO:0000269|PubMed:22891199}.
-!- DEVELOPMENTAL STAGE: Strongly expressed in the aerial portions and
root tips of seedlings. Present in stem and leaf epidermis,
including the trichomes, leaf mesophyll cells, and stem cortex and
xylem. In flowers, observed in the upper portion of the styles,
anther filament, and veins of the sepals and petals, silique walls
and developing seeds. {ECO:0000269|PubMed:22891199}.
-!- PTM: O-glycosylated on hydroxyprolines; noncontiguous
hydroxylproline residues are glycosylated with arabinogalactan.
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Reduced cuticular wax load on the stem
surface and in silique walls, with altered cuticular lipid
composition (especially C29 alkane) associated with diffuse
cuticular layer structure. {ECO:0000269|PubMed:22891199}.
-!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB246324; BAE73261.1; -; mRNA.
EMBL; AL162691; CAB83144.1; -; Genomic_DNA.
EMBL; CP002686; AEE77821.1; -; Genomic_DNA.
EMBL; CP002686; AEE77822.1; -; Genomic_DNA.
EMBL; AY045908; AAK76582.1; -; mRNA.
EMBL; AY079420; AAL85151.1; -; mRNA.
EMBL; AK318819; BAH56934.1; -; mRNA.
EMBL; AY088620; AAM66942.1; -; mRNA.
PIR; T47408; T47408.
RefSeq; NP_001030803.1; NM_001035726.2. [Q9LZH5-2]
RefSeq; NP_189958.1; NM_114240.4. [Q9LZH5-1]
UniGene; At.4842; -.
ProteinModelPortal; Q9LZH5; -.
SMR; Q9LZH5; -.
STRING; 3702.AT3G43720.1; -.
PaxDb; Q9LZH5; -.
EnsemblPlants; AT3G43720.1; AT3G43720.1; AT3G43720. [Q9LZH5-1]
EnsemblPlants; AT3G43720.2; AT3G43720.2; AT3G43720. [Q9LZH5-2]
GeneID; 823481; -.
Gramene; AT3G43720.1; AT3G43720.1; AT3G43720. [Q9LZH5-1]
Gramene; AT3G43720.2; AT3G43720.2; AT3G43720. [Q9LZH5-2]
KEGG; ath:AT3G43720; -.
Araport; AT3G43720; -.
TAIR; locus:2101044; AT3G43720.
eggNOG; ENOG410J3MX; Eukaryota.
eggNOG; ENOG410YY93; LUCA.
HOGENOM; HOG000130016; -.
InParanoid; Q9LZH5; -.
OMA; KSSNHAP; -.
OrthoDB; EOG09360P9P; -.
PhylomeDB; Q9LZH5; -.
PRO; PR:Q9LZH5; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9LZH5; baseline and differential.
Genevisible; Q9LZH5; AT.
GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0008289; F:lipid binding; ISS:UniProtKB.
GO; GO:0042335; P:cuticle development; IMP:UniProtKB.
GO; GO:0006869; P:lipid transport; ISS:UniProtKB.
InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
Pfam; PF14368; LTP_2; 1.
SMART; SM00499; AAI; 1.
SUPFAM; SSF47699; SSF47699; 1.
2: Evidence at transcript level;
Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; GPI-anchor; Lipid-binding; Lipoprotein;
Membrane; Reference proteome; Signal.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 162 Non-specific lipid transfer protein GPI-
anchored 2.
/FTId=PRO_0000425708.
PROPEP 163 193 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000425709.
LIPID 162 162 GPI-anchor amidated alanine.
{ECO:0000255}.
CARBOHYD 44 44 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 48 67 {ECO:0000255}.
DISULFID 68 110 {ECO:0000255}.
VAR_SEQ 145 150 Missing (in isoform 3).
{ECO:0000303|PubMed:19423640}.
/FTId=VSP_053832.
VAR_SEQ 149 150 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_053833.
CONFLICT 176 176 L -> R (in Ref. 6; AAM66942).
{ECO:0000305}.
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


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