LTPG5_ARATH
ID LTPG5_ARATH Reviewed; 170 AA.
AC Q9LJ86; A0A178VB68; Q8H784; Q8LDP1;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 154.
DE RecName: Full=Non-specific lipid transfer protein GPI-anchored 5 {ECO:0000303|PubMed:23893219};
DE Short=AtLTPG-5 {ECO:0000303|PubMed:23893219};
DE Short=Protein LTP-GPI-ANCHORED 5 {ECO:0000303|PubMed:23893219};
DE AltName: Full=Xylogen like protein 12 {ECO:0000303|PubMed:21558309};
DE Short=AtXYLP12 {ECO:0000303|PubMed:21558309};
DE Short=AtXYP8 {ECO:0000303|PubMed:21558309};
DE Flags: Precursor;
GN Name=LTPG5 {ECO:0000303|PubMed:23893219};
GN Synonyms=XYLP12 {ECO:0000303|PubMed:21558309},
GN XYP8 {ECO:0000303|PubMed:21558309};
GN OrderedLocusNames=At3g22600 {ECO:0000312|Araport:AT3G22600};
GN ORFNames=F16J14.17 {ECO:0000312|EMBL:BAB01475.1};
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].
RA Stracke R., Palme K.;
RT "Signal Peptide Selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [4]
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 [5]
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 [6]
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 [7]
RP INDUCTION BY NLPPP AND FLG22.
RX PubMed=17194768; DOI=10.1105/tpc.106.044180;
RA Qutob D., Kemmerling B., Brunner F., Kuefner I., Engelhardt S., Gust A.A.,
RA Luberacki B., Seitz H.U., Stahl D., Rauhut T., Glawischnig E., Schween G.,
RA Lacombe B., Watanabe N., Lam E., Schlichting R., Scheel D., Nau K.,
RA Dodt G., Hubert D., Gijzen M., Nuernberger T.;
RT "Phytotoxicity and innate immune responses induced by Nep1-like proteins.";
RL Plant Cell 18:3721-3744(2006).
RN [8]
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 [9]
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 [10]
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 [11]
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: Expressed in seedlings, preferentially in the
CC endodermis of hypocotyls and roots, as well as in anthers, sepals and
CC flower tori. {ECO:0000269|PubMed:21558309,
CC ECO:0000269|PubMed:23893219}.
CC -!- DEVELOPMENTAL STAGE: In roots, restricted to the endodermis/pericycle
CC above the middle of the differentiation zone and the regions where new
CC lateral roots are emerging (PubMed:21558309). Accumulates in the
CC abscission zone of young siliques (PubMed:21558309, PubMed:23893219).
CC Expressed in senescing leaves (PubMed:23893219).
CC {ECO:0000269|PubMed:21558309, ECO:0000269|PubMed:23893219}.
CC -!- INDUCTION: Induced by Phytophthora parasitica-derived necrosis and
CC ethylene-inducing peptide (NLPPp) and microbe-associated molecular
CC patterns (e.g. flg22). {ECO:0000269|PubMed:17194768}.
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). Increased salt
CC permeability in shrunken and deformed seeds, with abnormal hair-like
CC outgrowths (PubMed:24460633). {ECO:0000269|PubMed:24460633,
CC ECO:0000269|PubMed:30102837}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM63095.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAN60349.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF083791; AAN60349.1; ALT_INIT; mRNA.
DR EMBL; AB246327; BAE73264.1; -; mRNA.
DR EMBL; AP000731; BAB01475.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76657.1; -; Genomic_DNA.
DR EMBL; AY045650; AAK74008.1; -; mRNA.
DR EMBL; AY079122; AAL79604.1; -; mRNA.
DR EMBL; AY085883; AAM63095.1; ALT_INIT; mRNA.
DR RefSeq; NP_566712.1; NM_113159.4.
DR AlphaFoldDB; Q9LJ86; -.
DR SMR; Q9LJ86; -.
DR STRING; 3702.AT3G22600.1; -.
DR PaxDb; Q9LJ86; -.
DR PRIDE; Q9LJ86; -.
DR ProteomicsDB; 174818; -.
DR EnsemblPlants; AT3G22600.1; AT3G22600.1; AT3G22600.
DR GeneID; 821832; -.
DR Gramene; AT3G22600.1; AT3G22600.1; AT3G22600.
DR KEGG; ath:AT3G22600; -.
DR Araport; AT3G22600; -.
DR TAIR; locus:2077001; AT3G22600.
DR eggNOG; ENOG502S0AW; Eukaryota.
DR HOGENOM; CLU_089796_3_0_1; -.
DR InParanoid; Q9LJ86; -.
DR OMA; PDCLCQV; -.
DR OrthoDB; 1574629at2759; -.
DR PhylomeDB; Q9LJ86; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJ86; baseline and differential.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IEA:InterPro.
DR GO; GO:0140426; P:PAMP-triggered immunity signalling pathway; IEP:UniProtKB.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IEP:UniProtKB.
DR GO; GO:0002240; P:response to molecule of oomycetes origin; IEP:UniProtKB.
DR GO; GO:0009624; P:response to nematode; IDA:TAIR.
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 InterPro; IPR000528; Plant_nsLTP.
DR PANTHER; PTHR33044; PTHR33044; 1.
DR Pfam; PF14368; LTP_2; 1.
DR PRINTS; PR00382; LIPIDTRNSFER.
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..146
FT /note="Non-specific lipid transfer protein GPI-anchored 5"
FT /id="PRO_5015099827"
FT PROPEP 147..170
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451638"
FT REGION 105..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 146
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 28..69
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 38..53
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 54..95
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 67..105
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
SQ SEQUENCE 170 AA; 17306 MW; F356528BD4E1BCDA CRC64;
MKMEMGLVFL TVFMAVMSST MVSAQSSCTN ALISMSPCLN YITGNSTSPN QQCCNQLSRV
VQSSPDCLCQ VLNGGGSQLG INVNQTQALG LPRACNVQTP PVSRCNTGGG GGGSTSDSPA
ESPNSSGPGN GSKTVPVGEG DGPPSSDGSS IKFSFPLIAF FSAVSYMAIF
