LTG25_ARATH
ID LTG25_ARATH Reviewed; 219 AA.
AC F4JIG1;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Non-specific lipid transfer protein GPI-anchored 25 {ECO:0000303|PubMed:23893219};
DE Short=AtLTPG-25 {ECO:0000303|PubMed:23893219};
DE Short=Protein LTP-GPI-ANCHORED 25 {ECO:0000303|PubMed:23893219};
DE Flags: Precursor;
GN Name=LTPG25 {ECO:0000303|PubMed:23893219};
GN OrderedLocusNames=At4g14805 {ECO:0000312|Araport:AT4G14805};
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
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 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).
CC -!- FUNCTION: Probable lipid transfer protein.
CC {ECO:0000250|UniProtKB:Q9C7F7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-
CC anchor {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR EMBL; Z97337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002687; AEE83502.1; -; Genomic_DNA.
DR RefSeq; NP_680688.1; NM_148322.2.
DR AlphaFoldDB; F4JIG1; -.
DR PaxDb; F4JIG1; -.
DR EnsemblPlants; AT4G14805.1; AT4G14805.1; AT4G14805.
DR GeneID; 827136; -.
DR Gramene; AT4G14805.1; AT4G14805.1; AT4G14805.
DR KEGG; ath:AT4G14805; -.
DR Araport; AT4G14805; -.
DR TAIR; locus:504955426; AT4G14805.
DR eggNOG; ENOG502SA2F; Eukaryota.
DR HOGENOM; CLU_1284867_0_0_1; -.
DR InParanoid; F4JIG1; -.
DR OMA; SRNFLVV; -.
DR OrthoDB; 1554633at2759; -.
DR PhylomeDB; F4JIG1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JIG1; baseline and differential.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 1.10.110.10; -; 1.
DR InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR Pfam; PF14368; LTP_2; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..192
FT /note="Non-specific lipid transfer protein GPI-anchored 25"
FT /id="PRO_5003311527"
FT PROPEP 193..219
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451656"
FT REGION 152..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 192
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 39..85
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 49..68
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 69..110
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 83..123
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
SQ SEQUENCE 219 AA; 23547 MW; C5A3572C39E672DF CRC64;
MATKITGVFI LILTITFSSS SAVTATQQAP SSSPPVLTCT EELVMFSPCL PYVSSPPNNM
SETPDPICCS VFTSSVHSST GNCLCYLLRQ PMILGFPLDR SRLISLSQIC TDQNSEESFE
SLCSVSESPE LPPLQSIQFT NPFVSGNNVS ASPQSVDLAP EVSPSSDLFS PETATLAPPP
PPPPLPVLQY FSSDSLKIRN FWFPSTIIMT FATSILARI
