LTPG6_ARATH
ID LTPG6_ARATH Reviewed; 184 AA.
AC F4I082; Q8LEX2; Q9C896;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 2.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Non-specific lipid transfer protein GPI-anchored 6 {ECO:0000303|PubMed:23893219};
DE Short=AtLTPG-6 {ECO:0000303|PubMed:23893219};
DE Short=Protein LTP-GPI-ANCHORED 6 {ECO:0000303|PubMed:23893219};
DE AltName: Full=Xylogen like protein 6 {ECO:0000303|PubMed:21558309};
DE Short=AtXYLP6 {ECO:0000303|PubMed:21558309};
DE Short=AtXYP12 {ECO:0000303|PubMed:21558309};
DE Flags: Precursor;
GN Name=LTPG6 {ECO:0000303|PubMed:23893219};
GN Synonyms=XYLP6 {ECO:0000303|PubMed:21558309},
GN XYP12 {ECO:0000303|PubMed:21558309};
GN OrderedLocusNames=At1g55260 {ECO:0000312|Araport:AT1G55260};
GN ORFNames=F7A10.16 {ECO:0000312|EMBL:AAG51569.1};
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], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GENE
RP 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=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 [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].
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].
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.
RC STRAIN=cv. Columbia;
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 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, 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 [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 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 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 (PubMed:24460633). Contributes to pre-invasive defense against some
CC non-host powdery mildew pathogens by preventing the penetration of the
CC epidermal cell wall by the fungal agents (e.g. Blumeria graminis f. sp.
CC hordei (Bgh)) (PubMed:30102837). {ECO:0000269|PubMed:24460633,
CC ECO:0000269|PubMed:30102837}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-
CC anchor {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in the shoot apical
CC meristem and the root meristem (PubMed:21558309). Also present in the
CC ovules and developing embryos (PubMed:21558309). Observed in
CC cotyledons, hypocotyls, flowers, leaves and siliques (PubMed:23893219).
CC Up-regulated in the epidermis of stems (PubMed:16299169).
CC {ECO:0000269|PubMed:16299169, ECO:0000269|PubMed:21558309,
CC ECO:0000269|PubMed:23893219}.
CC -!- DEVELOPMENTAL STAGE: Mainly present in proliferating tissues
CC (PubMed:21558309). In flowers, expressed in stamens, carpels, petals,
CC sepals and pedicels (PubMed:23893219). Accumulates progressively in
CC leaves during aging (PubMed:23893219). {ECO:0000269|PubMed:21558309,
CC ECO:0000269|PubMed:23893219}.
CC -!- DISRUPTION PHENOTYPE: Increased susceptibility to penetration of the
CC 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 associated with an increase in unsubstituted fatty acids but a decrease
CC in omega-hydroxy fatty acids in seed coats (PubMed:24460633).
CC {ECO:0000269|PubMed:24460633, ECO:0000269|PubMed:30102837}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM61728.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AEE33214.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB246331; BAE73268.1; -; mRNA.
DR EMBL; AC027034; AAG51569.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33214.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF412076; AAL06529.1; -; mRNA.
DR EMBL; AY090262; AAL90923.1; -; mRNA.
DR EMBL; AY085177; AAM61728.1; ALT_INIT; mRNA.
DR PIR; E96594; E96594.
DR RefSeq; NP_564682.2; NM_104400.5.
DR AlphaFoldDB; F4I082; -.
DR STRING; 3702.AT1G55260.1; -.
DR PaxDb; F4I082; -.
DR PRIDE; F4I082; -.
DR ProteomicsDB; 210142; -.
DR EnsemblPlants; AT1G55260.1; AT1G55260.1; AT1G55260.
DR GeneID; 841970; -.
DR Gramene; AT1G55260.1; AT1G55260.1; AT1G55260.
DR KEGG; ath:AT1G55260; -.
DR Araport; AT1G55260; -.
DR TAIR; locus:2035711; AT1G55260.
DR eggNOG; ENOG502RZD2; Eukaryota.
DR InParanoid; F4I082; -.
DR OrthoDB; 1546514at2759; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I082; baseline and differential.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050832; P:defense response to fungus; 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; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Plant defense; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..160
FT /note="Non-specific lipid transfer protein GPI-anchored 6"
FT /id="PRO_0000451639"
FT PROPEP 161..184
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451640"
FT REGION 138..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 160
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT DISULFID 33..74
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 43..58
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 59..101
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 72..111
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
SQ SEQUENCE 184 AA; 20126 MW; 2F597010574B004B CRC64;
MEKSTRTLFI TIVITSMLLG FGNSDLAQDR EECTNQLIEL STCIPYVGGD AKAPTKDCCA
GFGQVIRKSE KCVCILVRDK DDPQLGIKIN ATLAAHLPSA CHITAPNITD CISILHLPRN
STLAKEFENL GRIEDNYNST SPTQIHKDGT GGGKAEPVKS NGWKEKSWLG VELLIYLLVS
LIFF
