LTG31_ARATH
ID LTG31_ARATH Reviewed; 182 AA.
AC Q8VYI9; Q8L8Q1; Q9FMI9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Non-specific lipid transfer protein GPI-anchored 31 {ECO:0000303|PubMed:23893219};
DE Short=AtLTPG-31 {ECO:0000303|PubMed:23893219};
DE Short=Protein LTP-GPI-ANCHORED 31 {ECO:0000303|PubMed:23893219};
DE AltName: Full=Xylogen protein 1 {ECO:0000303|PubMed:15215864, ECO:0000303|PubMed:21558309};
DE Short=AtXYP1 {ECO:0000303|PubMed:15215864, ECO:0000303|PubMed:21558309};
DE Flags: Precursor;
GN Name=LTPG31 {ECO:0000303|PubMed:23893219};
GN Synonyms=XYP1 {ECO:0000303|PubMed:15215864, ECO:0000303|PubMed:21558309};
GN OrderedLocusNames=At5g64080 {ECO:0000312|Araport:AT5G64080};
GN ORFNames=MHJ24.6 {ECO:0000312|EMBL:BAB10276.1};
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15215864; DOI=10.1038/nature02613;
RA Motose H., Sugiyama M., Fukuda H.;
RT "A proteoglycan mediates inductive interaction during plant vascular
RT development.";
RL Nature 429:873-878(2004).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GENE FAMILY, AND
RP 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 [7]
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 (By similarity).
CC Proteoglycan-like factor that exhibits xylogen activity consisting in
CC mediating local and inductive cell-cell interactions required for xylem
CC differentiation (PubMed:15215864, PubMed:21558309).
CC {ECO:0000250|UniProtKB:Q9C7F7, ECO:0000269|PubMed:15215864,
CC ECO:0000269|PubMed:21558309}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-
CC anchor {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VYI9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VYI9-2; Sequence=VSP_021391;
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, roots, stems, seedlings
CC and inflorescences, but not in mature leaves.
CC {ECO:0000269|PubMed:21558309}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in the cotyledons of embryos
CC and of young seedlings (PubMed:21558309). In adult plants, present in
CC anthers of flowers, in funicles of developing siliques and at the base
CC of roots (PubMed:21558309). {ECO:0000269|PubMed:21558309}.
CC -!- DISRUPTION PHENOTYPE: No obvious defects in morphology
CC (PubMed:15215864). Plants lacking both XYP1 and XYP2 have morphological
CC defects in vascular development; e.g. discontinuous and thicker veins
CC with the improper interconnection of tracheary elements (TEs)
CC (PubMed:15215864). {ECO:0000269|PubMed:15215864}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10276.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB008266; BAB10276.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97837.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97838.1; -; Genomic_DNA.
DR EMBL; AY070743; AAL50083.1; -; mRNA.
DR EMBL; AY093740; AAM10364.1; -; mRNA.
DR EMBL; AY088880; AAM67186.1; -; mRNA.
DR RefSeq; NP_568984.1; NM_125804.4. [Q8VYI9-1]
DR RefSeq; NP_974989.1; NM_203260.2. [Q8VYI9-2]
DR AlphaFoldDB; Q8VYI9; -.
DR SMR; Q8VYI9; -.
DR STRING; 3702.AT5G64080.1; -.
DR PaxDb; Q8VYI9; -.
DR PRIDE; Q8VYI9; -.
DR ProteomicsDB; 249124; -. [Q8VYI9-1]
DR EnsemblPlants; AT5G64080.1; AT5G64080.1; AT5G64080. [Q8VYI9-1]
DR EnsemblPlants; AT5G64080.2; AT5G64080.2; AT5G64080. [Q8VYI9-2]
DR GeneID; 836529; -.
DR Gramene; AT5G64080.1; AT5G64080.1; AT5G64080. [Q8VYI9-1]
DR Gramene; AT5G64080.2; AT5G64080.2; AT5G64080. [Q8VYI9-2]
DR KEGG; ath:AT5G64080; -.
DR Araport; AT5G64080; -.
DR TAIR; locus:2164411; AT5G64080.
DR eggNOG; ENOG502S1ZN; Eukaryota.
DR InParanoid; Q8VYI9; -.
DR OMA; TIMKYVI; -.
DR PhylomeDB; Q8VYI9; -.
DR PRO; PR:Q8VYI9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VYI9; baseline and differential.
DR Genevisible; Q8VYI9; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0046658; C:anchored component of plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:InterPro.
DR GO; GO:0010089; P:xylem development; IMP:UniProtKB.
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 Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Reference proteome; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..157
FT /note="Non-specific lipid transfer protein GPI-anchored 31"
FT /id="PRO_0000259452"
FT PROPEP 158..182
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000259453"
FT LIPID 157
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 43..86
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 53..70
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 71..111
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 84..121
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT VAR_SEQ 130..133
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_021391"
FT CONFLICT 45
FT /note="T -> I (in Ref. 4; AAM67186)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="A -> V (in Ref. 4; AAM67186)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 182 AA; 17972 MW; 64929467BA74A730 CRC64;
MATHSSFTAT TPLFLIVLLS LSSVSVLGAS HHHATAPAPS VDCSTLILNM ADCLSFVSSG
GTVAKPEGTC CSGLKTVLKA DSQCLCEAFK SSASLGVTLN ITKASTLPAA CKLHAPSIAT
CGLSVAPSTA PGLAPGVAAA GPETAGFLAP NPSSGNDGSS LIPTSFTTVL SAVLFVLFFS
SA
