LTPG1_ARATH
ID LTPG1_ARATH Reviewed; 193 AA.
AC Q9C7F7; Q570M7; Q8LEI0;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Non-specific lipid transfer protein GPI-anchored 1 {ECO:0000303|PubMed:19321705, ECO:0000303|PubMed:19366900, ECO:0000303|PubMed:23893219};
DE Short=AtLTPG-1 {ECO:0000303|PubMed:19321705, ECO:0000303|PubMed:19366900, ECO:0000303|PubMed:23893219};
DE Short=Protein LTP-GPI-ANCHORED 1 {ECO:0000303|PubMed:19321705, ECO:0000303|PubMed:19366900, ECO:0000303|PubMed:23893219};
DE Flags: Precursor;
GN Name=LTPG1 {ECO:0000303|PubMed:19321705, ECO:0000303|PubMed:22891199,
GN ECO:0000303|PubMed:23893219}; Synonyms=LTPG {ECO:0000303|PubMed:19366900};
GN OrderedLocusNames=At1g27950 {ECO:0000312|Araport:AT1G27950};
GN ORFNames=F13K9.6 {ECO:0000312|EMBL:AAG51485.1};
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=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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-193.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=19366900; DOI=10.1105/tpc.108.064451;
RA Debono A., Yeats T.H., Rose J.K., Bird D., Jetter R., Kunst L., Samuels L.;
RT "Arabidopsis LTPG is a glycosylphosphatidylinositol-anchored lipid transfer
RT protein required for export of lipids to the plant surface.";
RL Plant Cell 21:1230-1238(2009).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=19321705; DOI=10.1104/pp.109.137745;
RA Lee S.B., Go Y.S., Bae H.J., Park J.H., Cho S.H., Cho H.J., Lee D.S.,
RA Park O.K., Hwang I., Suh M.C.;
RT "Disruption of glycosylphosphatidylinositol-anchored lipid transfer protein
RT gene altered cuticular lipid composition, increased plastoglobules, and
RT enhanced susceptibility to infection by the fungal pathogen Alternaria
RT brassicicola.";
RL Plant Physiol. 150:42-54(2009).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
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 [10]
RP SUBCELLULAR LOCATION, AND 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 [11]
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 [12]
RP 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 [13]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, GENE FAMILY, AND
RP 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 LTPG2, 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. Involved in the establishment of
CC resistance to the necrotrophic fungal pathogen Alternaria brassicicola.
CC Contributes to pre-invasive defense against some non-host powdery
CC mildew pathogens by preventing the penetration of the epidermal cell
CC wall by the fungal agents (e.g. Blumeria graminis f. sp. hordei (Bgh))
CC (PubMed:30102837). Maybe involved in seed and ovule maturation and
CC development, probably by regulating the fatty acids homeostasis during
CC suberin and sporopollenin biosynthesis or deposition (By similarity).
CC {ECO:0000250|UniProtKB:Q9LZH5, ECO:0000269|PubMed:19321705,
CC ECO:0000269|PubMed:19366900, ECO:0000269|PubMed:22891199,
CC ECO:0000269|PubMed:30102837}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19321705,
CC ECO:0000269|PubMed:22891199, ECO:0000269|PubMed:23505340}; Lipid-
CC anchor, GPI-anchor {ECO:0000255}. Secreted, cell wall
CC {ECO:0000269|PubMed:19366900}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:19366900}. Golgi apparatus
CC {ECO:0000269|PubMed:19366900}. Note=Targeted to the plasma membrane via
CC the vesicular trafficking system (PubMed:19321705, PubMed:22891199).
CC Localized to the plasma membrane on all faces of epidermal cells
CC (PubMed:19366900). Also detected in the periclinal cell wall
CC (PubMed:19366900). In young meristematic cells, observed in plasma
CC membrane and in puncta resembling the Golgi (PubMed:19366900).
CC Localized to papillae at the sites of Blumeria graminis f. sp. hordei
CC (Bgh) penetration (Bgh) (PubMed:30102837).
CC {ECO:0000269|PubMed:19321705, ECO:0000269|PubMed:19366900,
CC ECO:0000269|PubMed:22891199, ECO:0000269|PubMed:30102837}.
CC -!- TISSUE SPECIFICITY: Up-regulated in the epidermis of stems and leaves.
CC Expressed in the epidermis, stem cortex, vascular bundles and mesophyll
CC cells in root tips, cotyledons, seedlings, leaves, caulines, flowers,
CC siliques, pollen, and early-developing seeds.
CC {ECO:0000269|PubMed:16299169, ECO:0000269|PubMed:19321705,
CC ECO:0000269|PubMed:23893219}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in seeds after imbibition
CC (PubMed:23893219). High levels in the aerial portion of 10 days old
CC seedlings. Accumulates in the epidermis during cuticle biosynthesis
CC (e.g. in inflorescence stems). Also detected in flowers, in upper
CC portion of the styles, pollen, veins of the sepals and petals, silique
CC walls and seeds in the early stages of development (PubMed:23893219).
CC In epidermis, present in trichomes, leaf mesophyll cells, and stem
CC cortex and xylem. {ECO:0000269|PubMed:19321705,
CC ECO:0000269|PubMed:19366900, 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. Increased number of plastoglobules in the stem cortex and
CC leaf mesophyll cells, protrusions of the cytoplasm into the vacuole in
CC the epidermis, and enhanced susceptibility to infection by the
CC necrotrophic fungal pathogen Alternaria brassicicola. Increased
CC susceptibility to penetration of the epidermal cell wall by the non-
CC host mildew fungal agent Blumeria graminis f. sp. hordei (Bgh)
CC (PubMed:30102837). {ECO:0000269|PubMed:19321705,
CC ECO:0000269|PubMed:19366900, ECO:0000269|PubMed:22891199,
CC ECO:0000269|PubMed:30102837}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR EMBL; AC069471; AAG51485.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30894.1; -; Genomic_DNA.
DR EMBL; AY092956; AAM12955.1; -; mRNA.
DR EMBL; AY128712; AAM91112.1; -; mRNA.
DR EMBL; AY085407; AAM62634.1; -; mRNA.
DR EMBL; AK220681; BAD93740.1; -; mRNA.
DR PIR; H86404; H86404.
DR RefSeq; NP_174116.1; NM_102560.3.
DR AlphaFoldDB; Q9C7F7; -.
DR STRING; 3702.AT1G27950.1; -.
DR SwissPalm; Q9C7F7; -.
DR PaxDb; Q9C7F7; -.
DR PRIDE; Q9C7F7; -.
DR ProteomicsDB; 238639; -.
DR EnsemblPlants; AT1G27950.1; AT1G27950.1; AT1G27950.
DR GeneID; 839688; -.
DR Gramene; AT1G27950.1; AT1G27950.1; AT1G27950.
DR KEGG; ath:AT1G27950; -.
DR Araport; AT1G27950; -.
DR TAIR; locus:2010479; AT1G27950.
DR eggNOG; ENOG502S13V; Eukaryota.
DR HOGENOM; CLU_089796_2_0_1; -.
DR InParanoid; Q9C7F7; -.
DR OMA; IVHIMIM; -.
DR OrthoDB; 1497278at2759; -.
DR PhylomeDB; Q9C7F7; -.
DR PRO; PR:Q9C7F7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C7F7; baseline and differential.
DR Genevisible; Q9C7F7; 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:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0008289; F:lipid binding; IDA: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; IMP: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 Cell membrane; Cell wall; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Golgi apparatus; GPI-anchor; Lipid-binding; Lipoprotein;
KW Membrane; Plant defense; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..165
FT /note="Non-specific lipid transfer protein GPI-anchored 1"
FT /id="PRO_0000022623"
FT PROPEP 166..193
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000022624"
FT REGION 138..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 165
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 35..76
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 45..60
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 61..106
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 74..116
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT CONFLICT 55
FT /note="I -> T (in Ref. 4; AAM62634)"
FT /evidence="ECO:0000305"
SQ 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
