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Non-specific lipid transfer protein GPI-anchored 1 (AtLTPG-1) (Protein LTP-GPI-ANCHORED 1)

 LTPG1_ARATH             Reviewed;         193 AA.
Q9C7F7; Q570M7; Q8LEI0;
31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
25-OCT-2017, entry version 105.
RecName: Full=Non-specific lipid transfer protein GPI-anchored 1;
Short=AtLTPG-1;
Short=Protein LTP-GPI-ANCHORED 1;
Flags: Precursor;
Name=LTPG1; OrderedLocusNames=At1g27950; ORFNames=F13K9.6;
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 [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-193.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
GPI-ANCHOR [LARGE SCALE ANALYSIS] AT ALA-161, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=cv. Columbia; TISSUE=Callus;
PubMed=12805588; DOI=10.1104/pp.103.021170;
Borner G.H.H., Lilley K.S., Stevens T.J., Dupree P.;
"Identification of glycosylphosphatidylinositol-anchored proteins in
Arabidopsis. A proteomic and genomic analysis.";
Plant Physiol. 132:568-577(2003).
[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]
GPI-ANCHOR [LARGE SCALE ANALYSIS].
PubMed=16602701; DOI=10.1021/pr050419u;
Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S.,
Brodbeck U., Peck S.C., Jensen O.N.;
"Modification-specific proteomics of plasma membrane proteins:
identification and characterization of glycosylphosphatidylinositol-
anchored proteins released upon phospholipase D treatment.";
J. Proteome Res. 5:935-943(2006).
[9]
FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND SUBCELLULAR
LOCATION.
STRAIN=cv. Columbia;
PubMed=19366900; DOI=10.1105/tpc.108.064451;
Debono A., Yeats T.H., Rose J.K., Bird D., Jetter R., Kunst L.,
Samuels L.;
"Arabidopsis LTPG is a glycosylphosphatidylinositol-anchored lipid
transfer protein required for export of lipids to the plant surface.";
Plant Cell 21:1230-1238(2009).
[10]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR
LOCATION, AND DEVELOPMENTAL STAGE.
STRAIN=cv. Columbia;
PubMed=19321705; DOI=10.1104/pp.109.137745;
Lee S.B., Go Y.S., Bae H.J., Park J.H., Cho S.H., Cho H.J., Lee D.S.,
Park O.K., Hwang I., Suh M.C.;
"Disruption of glycosylphosphatidylinositol-anchored lipid transfer
protein gene altered cuticular lipid composition, increased
plastoglobules, and enhanced susceptibility to infection by the fungal
pathogen Alternaria brassicicola.";
Plant Physiol. 150:42-54(2009).
[11]
FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
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 LTPG2, 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. Involved in the
establishment of resistance to the necrotrophic fungal pathogen
Alternaria brassicicola. {ECO:0000269|PubMed:19321705,
ECO:0000269|PubMed:19366900, ECO:0000269|PubMed:22891199}.
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
Secreted, cell wall. Endoplasmic reticulum. Golgi apparatus.
Note=Targeted to the plasma membrane via the vesicular trafficking
system. Localized to the plasma membrane on all faces of epidermal
cells. Also detected in the periclinal cell wall. In young
meristematic cells, observed in plasma membrane and in puncta
resembling the Golgi.
-!- TISSUE SPECIFICITY: Up-regulated in the epidermis of stems and
leaves. Expressed in the epidermis, stem cortex, vascular bundles
and mesophyll cells in root tips, seedlings, leaves, caulines,
flowers, siliques, pollen, and early-developing seeds.
{ECO:0000269|PubMed:16299169, ECO:0000269|PubMed:19321705}.
-!- DEVELOPMENTAL STAGE: High levels in the aerial portion of 10 days
old seedlings. Accumulates in the epidermis during cuticle
biosynthesis (e.g. in inflorescence stems). Also detected in
flowers, in upper portion of the styles, pollen, veins of the
sepals and petals, silique walls and seeds in the early stages of
development. In epidermis, present in trichomes, leaf mesophyll
cells, and stem cortex and xylem. {ECO:0000269|PubMed:19321705,
ECO:0000269|PubMed:19366900}.
-!- 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. Increased number of plastoglobules in
the stem cortex and leaf mesophyll cells, protrusions of the
cytoplasm into the vacuole in the epidermis, and enhanced
susceptibility to infection by the necrotrophic fungal pathogen
Alternaria brassicicola. {ECO:0000269|PubMed:19321705,
ECO:0000269|PubMed:19366900, ECO:0000269|PubMed:22891199}.
-!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AC069471; AAG51485.1; -; Genomic_DNA.
EMBL; CP002684; AEE30894.1; -; Genomic_DNA.
EMBL; AY092956; AAM12955.1; -; mRNA.
EMBL; AY128712; AAM91112.1; -; mRNA.
EMBL; AY085407; AAM62634.1; -; mRNA.
EMBL; AK220681; BAD93740.1; -; mRNA.
PIR; H86404; H86404.
RefSeq; NP_174116.1; NM_102560.3.
UniGene; At.22627; -.
ProteinModelPortal; Q9C7F7; -.
STRING; 3702.AT1G27950.1; -.
SwissPalm; Q9C7F7; -.
PaxDb; Q9C7F7; -.
PRIDE; Q9C7F7; -.
EnsemblPlants; AT1G27950.1; AT1G27950.1; AT1G27950.
GeneID; 839688; -.
Gramene; AT1G27950.1; AT1G27950.1; AT1G27950.
KEGG; ath:AT1G27950; -.
Araport; AT1G27950; -.
TAIR; locus:2010479; AT1G27950.
eggNOG; ENOG410J072; Eukaryota.
eggNOG; ENOG410YMSF; LUCA.
HOGENOM; HOG000090402; -.
InParanoid; Q9C7F7; -.
OMA; HNASITN; -.
OrthoDB; EOG09360RMP; -.
PhylomeDB; Q9C7F7; -.
PRO; PR:Q9C7F7; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9C7F7; baseline and differential.
Genevisible; Q9C7F7; AT.
GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0009505; C:plant-type cell wall; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
GO; GO:0042335; P:cuticle development; IMP:UniProtKB.
GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
GO; GO:0006869; P:lipid transport; IMP: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.
1: Evidence at protein level;
Cell membrane; Cell wall; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Golgi apparatus; GPI-anchor;
Lipid-binding; Lipoprotein; Membrane; Plant defense;
Reference proteome; Secreted; Signal.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 161 Non-specific lipid transfer protein GPI-
anchored 1.
/FTId=PRO_0000022623.
PROPEP 162 193 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000022624.
LIPID 161 161 GPI-anchor amidated alanine.
{ECO:0000305|PubMed:12805588}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 135 135 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 45 60 {ECO:0000255}.
DISULFID 61 106 {ECO:0000255}.
CONFLICT 55 55 I -> T (in Ref. 4; AAM62634).
{ECO:0000305}.
SEQUENCE 193 AA; 19759 MW; D54B38B12FFE6610 CRC64;
MKGLHLHLVL VTMTIVASIA AAAPAAPGGA LADECNQDFQ KVTLCLDFAT GKATIPSKKC
CDAVEDIKER DPKCLCFVIQ QAKTGGQALK DLGVQEDKLI QLPTSCQLHN ASITNCPKLL
GISPSSPDAA VFTNNATTTP VAPAGKSPAT PATSTDKGGS ASAKDGHAVV ALAVALMAVS
FVLTLPRHVT LGM


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