LTG30_ARATH
ID LTG30_ARATH Reviewed; 151 AA.
AC Q9FFY3;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Non-specific lipid transfer protein GPI-anchored 30 {ECO:0000303|PubMed:23893219};
DE Short=AtLTPG-30 {ECO:0000303|PubMed:23893219};
DE Short=Protein LTP-GPI-ANCHORED 30 {ECO:0000303|PubMed:23893219};
DE AltName: Full=Lipid transfer-like protein VAS {ECO:0000303|PubMed:12472696};
DE Flags: Precursor;
GN Name=LTPG30 {ECO:0000303|PubMed:23893219};
GN Synonyms=VAS {ECO:0000303|PubMed:12472696};
GN OrderedLocusNames=At5g13900 {ECO:0000312|Araport:AT5G13900};
GN ORFNames=MAC12.14 {ECO:0000312|EMBL:BAB11118.1};
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 [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. C24;
RX PubMed=12472696; DOI=10.1046/j.1365-313x.2002.01470.x;
RA van der Graaff E., Hooykaas P.J.J., Keller B.;
RT "Activation tagging of the two closely linked genes LEP and VAS
RT independently affects vascular cell number.";
RL Plant J. 32:819-830(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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: Lipid transfer protein that promotes the number of phloem
CC (pro)cambial and pericycle cells. {ECO:0000269|PubMed:12472696}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-
CC anchor {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in vascular tissues of all organs
CC (PubMed:12472696). Expressed in seedlings, preferentially in hypocotyls
CC and roots (PubMed:23893219). Also observed in siliques
CC (PubMed:23893219). {ECO:0000269|PubMed:12472696,
CC ECO:0000269|PubMed:23893219}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR EMBL; AF463514; AAL68835.1; -; Genomic_DNA.
DR EMBL; AB005230; BAB11118.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91957.1; -; Genomic_DNA.
DR EMBL; BT015106; AAT71978.1; -; mRNA.
DR EMBL; AK175242; BAD43005.1; -; mRNA.
DR RefSeq; NP_196894.1; NM_121393.4.
DR AlphaFoldDB; Q9FFY3; -.
DR SMR; Q9FFY3; -.
DR STRING; 3702.AT5G13900.1; -.
DR PaxDb; Q9FFY3; -.
DR PRIDE; Q9FFY3; -.
DR ProteomicsDB; 243260; -.
DR EnsemblPlants; AT5G13900.1; AT5G13900.1; AT5G13900.
DR GeneID; 831237; -.
DR Gramene; AT5G13900.1; AT5G13900.1; AT5G13900.
DR KEGG; ath:AT5G13900; -.
DR Araport; AT5G13900; -.
DR TAIR; locus:2159053; AT5G13900.
DR eggNOG; ENOG502S410; Eukaryota.
DR HOGENOM; CLU_116928_2_0_1; -.
DR OMA; KLLPCMN; -.
DR OrthoDB; 1542931at2759; -.
DR PhylomeDB; Q9FFY3; -.
DR PRO; PR:Q9FFY3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFY3; baseline and differential.
DR Genevisible; Q9FFY3; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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 SUPFAM; SSF47699; SSF47699; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipid-binding;
KW Lipoprotein; Membrane; Reference proteome; Signal; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..151
FT /note="Non-specific lipid transfer protein GPI-anchored 30"
FT /id="PRO_0000297962"
FT PROPEP 121..151
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451634"
FT LIPID 120
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 32..69
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 39..53
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 54..97
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 67..106
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
SQ SEQUENCE 151 AA; 16532 MW; 52A590132FDDB1BC CRC64;
MMMGMKFFSF YVVLLLVAAS SGMRINGQSV SCLNQLAPCL NYLNGTKEVP QVCCNPLKSV
IRNNPECLCR MISNRWSSQA ERAGIDVNDA QMLPARCGEH VNPIACLTRS RGGSTNSDRS
SSIGNTFSQS YWMTTLAIAA TVLSYCHHII S
