LTG15_ARATH
ID LTG15_ARATH Reviewed; 183 AA.
AC Q7EB72; A0A178VVU1; Q8LBJ9;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Non-specific lipid transfer protein GPI-anchored 15 {ECO:0000303|PubMed:23893219};
DE Short=AtLTPG-15 {ECO:0000303|PubMed:23893219};
DE Short=Protein LTP-GPI-ANCHORED 15 {ECO:0000303|PubMed:23893219};
DE AltName: Full=Xylogen-like protein 10 {ECO:0000303|PubMed:21558309};
DE Short=AtXYLP11 {ECO:0000303|PubMed:21558309};
DE Short=AtXYP7 {ECO:0000303|PubMed:21558309};
DE Flags: Precursor;
GN Name=LTPG15 {ECO:0000303|PubMed:23893219};
GN Synonyms=XYLP11 {ECO:0000303|PubMed:21558309},
GN XYP7 {ECO:0000303|PubMed:21558309};
GN OrderedLocusNames=At2g48130 {ECO:0000312|Araport:AT2G48130};
GN ORFNames=F11L15.3 {ECO:0000312|EMBL:AEC10943.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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, 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 the
CC endodermis of hypocotyls and roots (PubMed:21558309, PubMed:23893219).
CC Also observed in siliques (PubMed:23893219).
CC {ECO:0000269|PubMed:21558309, 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. {ECO:0000269|PubMed:21558309}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR EMBL; AB246326; BAE73263.1; -; mRNA.
DR EMBL; LR699746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002685; AEC10943.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62793.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62794.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62795.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62796.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62797.1; -; Genomic_DNA.
DR EMBL; AY065446; AAL38887.1; -; mRNA.
DR EMBL; AY117278; AAM51353.1; -; mRNA.
DR EMBL; AY087167; AAM64723.1; -; mRNA.
DR PIR; G84923; G84923.
DR RefSeq; NP_001318446.1; NM_001337297.1.
DR RefSeq; NP_001324923.1; NM_001337301.1.
DR RefSeq; NP_001324924.1; NM_001337300.1.
DR RefSeq; NP_001324925.1; NM_001337299.1.
DR RefSeq; NP_001324926.1; NM_001337298.1.
DR RefSeq; NP_566126.1; NM_130380.3.
DR AlphaFoldDB; Q7EB72; -.
DR SMR; Q7EB72; -.
DR STRING; 3702.AT2G48130.1; -.
DR PaxDb; Q7EB72; -.
DR PRIDE; Q7EB72; -.
DR ProteomicsDB; 185651; -.
DR EnsemblPlants; AT2G48130.1; AT2G48130.1; AT2G48130.
DR EnsemblPlants; AT2G48130.2; AT2G48130.2; AT2G48130.
DR EnsemblPlants; AT2G48130.3; AT2G48130.3; AT2G48130.
DR EnsemblPlants; AT2G48130.4; AT2G48130.4; AT2G48130.
DR EnsemblPlants; AT2G48130.5; AT2G48130.5; AT2G48130.
DR EnsemblPlants; AT2G48130.6; AT2G48130.6; AT2G48130.
DR GeneID; 819425; -.
DR Gramene; AT2G48130.1; AT2G48130.1; AT2G48130.
DR Gramene; AT2G48130.2; AT2G48130.2; AT2G48130.
DR Gramene; AT2G48130.3; AT2G48130.3; AT2G48130.
DR Gramene; AT2G48130.4; AT2G48130.4; AT2G48130.
DR Gramene; AT2G48130.5; AT2G48130.5; AT2G48130.
DR Gramene; AT2G48130.6; AT2G48130.6; AT2G48130.
DR KEGG; ath:AT2G48130; -.
DR Araport; AT2G48130; -.
DR TAIR; locus:2039366; AT2G48130.
DR eggNOG; ENOG502S0AW; Eukaryota.
DR HOGENOM; CLU_089796_3_0_1; -.
DR InParanoid; Q7EB72; -.
DR OMA; NPQCLCA; -.
DR OrthoDB; 1574629at2759; -.
DR PhylomeDB; Q7EB72; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q7EB72; baseline and differential.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0005319; F:lipid transporter activity; IMP:TAIR.
DR GO; GO:0015908; P:fatty acid transport; IMP:TAIR.
DR GO; GO:0010214; P:seed coat development; IMP:TAIR.
DR GO; GO:0009845; P:seed germination; IMP: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; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..158
FT /note="Non-specific lipid transfer protein GPI-anchored 15"
FT /id="PRO_5015098699"
FT PROPEP 159..183
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451646"
FT REGION 108..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 158
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 30..71
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 40..55
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 56..97
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 69..107
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT CONFLICT 155
FT /note="T -> N (in Ref. 5; AAM64723)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 183 AA; 18853 MW; E90F40A9BD75FDA0 CRC64;
MGYRRSYAIT FVALVAALWS VTKAQPSSSC VSTLTTLSPC LSYITGNSTT PSQPCCSRLD
SVIKSSPQCI CSAVNSPIPN IGLNINRTQA LQLPNACNIQ TPPLTQCNAA TGPTAQPPAP
SPTEKTPDVT LTPTSLPGAR SGVGGGSKTV PSVGTGSSSR NVDPLPLHFL MFAVLVVCTS
SFL
