LTG20_ARATH
ID LTG20_ARATH Reviewed; 203 AA.
AC Q9LJ85; A0A178VCH3;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Non-specific lipid transfer protein GPI-anchored 20 {ECO:0000303|PubMed:23893219};
DE Short=AtLTPG-20 {ECO:0000303|PubMed:23893219};
DE Short=Protein LTP-GPI-ANCHORED 20 {ECO:0000303|PubMed:23893219};
DE Flags: Precursor;
GN Name=LTPG20 {ECO:0000303|PubMed:23893219};
GN OrderedLocusNames=At3g22620 {ECO:0000312|Araport:AT3G22620};
GN ORFNames=F16J14.17 {ECO:0000312|EMBL:BAB01476.1};
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=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 [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 TISSUE SPECIFICITY, 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 -!- TISSUE SPECIFICITY: Expressed in seedlings, preferentially in
CC hypocotyls and roots (PubMed:23893219). Also observed in siliques and
CC sepals (PubMed:23893219). {ECO:0000269|PubMed:23893219}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP000731; BAB01476.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76658.1; -; Genomic_DNA.
DR EMBL; AY035005; AAK59510.1; -; mRNA.
DR EMBL; AY113897; AAM44945.1; -; mRNA.
DR RefSeq; NP_566713.1; NM_113160.3.
DR AlphaFoldDB; Q9LJ85; -.
DR STRING; 3702.AT3G22620.1; -.
DR PaxDb; Q9LJ85; -.
DR PRIDE; Q9LJ85; -.
DR ProteomicsDB; 185499; -.
DR EnsemblPlants; AT3G22620.1; AT3G22620.1; AT3G22620.
DR GeneID; 821833; -.
DR Gramene; AT3G22620.1; AT3G22620.1; AT3G22620.
DR KEGG; ath:AT3G22620; -.
DR Araport; AT3G22620; -.
DR TAIR; locus:2828523; AT3G22620.
DR eggNOG; ENOG502RZXE; Eukaryota.
DR HOGENOM; CLU_085549_2_0_1; -.
DR InParanoid; Q9LJ85; -.
DR OMA; CKANIAP; -.
DR OrthoDB; 1573578at2759; -.
DR PhylomeDB; Q9LJ85; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJ85; baseline and differential.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009941; C:chloroplast envelope; HDA: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 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; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..172
FT /note="Non-specific lipid transfer protein GPI-anchored 20"
FT /id="PRO_5015099825"
FT PROPEP 173..203
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451651"
FT REGION 119..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 172
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 29..74
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 40..58
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 59..99
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 72..108
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
SQ SEQUENCE 203 AA; 20779 MW; 597EE6B57B1CE4EC CRC64;
MSKIISLVVA MIAVLALPIR GQQQPLSQCT PSMMTTVSPC MGFITNSSSN GTSPSSDCCN
SLRSLTTGGM GCLCLIVTGT VPFNIPINRT TAVSLPRACN MPRVPLQCQA NIAPAAAPGP
AATFGPSMSP GPETDPIVPE PTPAAQTPQS DTTRPFTPSV DGGAPTSDDG GSTSRPSETP
SSAYALSPSL LFFSIALVAL KFY
