LTG13_ARATH
ID LTG13_ARATH Reviewed; 205 AA.
AC O64864; Q9CAZ6;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Non-specific lipid transfer protein GPI-anchored 13 {ECO:0000303|PubMed:23893219};
DE Short=AtLTPG-13 {ECO:0000303|PubMed:23893219};
DE Short=Protein LTP-GPI-ANCHORED 13 {ECO:0000303|PubMed:23893219};
DE AltName: Full=Protein YELLOW-LEAF-SPECIFIC GENE 3 {ECO:0000303|PubMed:11230571};
DE AltName: Full=Xylogen-like protein 9 {ECO:0000303|PubMed:21558309};
DE Short=AtXYLP9 {ECO:0000303|PubMed:21558309};
DE Short=AtXYP9 {ECO:0000303|PubMed:21558309};
DE Flags: Precursor;
GN Name=LTPG13 {ECO:0000303|PubMed:23893219};
GN Synonyms=XYLP9 {ECO:0000303|PubMed:21558309},
GN XYP9 {ECO:0000303|PubMed:21558309}, YLS3 {ECO:0000303|PubMed:11230571};
GN OrderedLocusNames=At2g44290 {ECO:0000312|Araport:AT2G44290};
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,
RP INDUCTION, GENE 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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 112-205.
RX PubMed=11230571; DOI=10.1093/pcp/pce021;
RA Yoshida S., Ito M., Nishida I., Watanabe A.;
RT "Isolation and RNA gel blot analysis of genes that could serve as potential
RT molecular markers for leaf senescence in Arabidopsis thaliana.";
RL Plant Cell Physiol. 42:170-178(2001).
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.
CC {ECO:0000250|UniProtKB:Q9C7F7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-
CC anchor {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed preferentially in expanding leaves and
CC sepals, restricted to the distal side (PubMed:21558309). Expressed at
CC low levels in roots and stems (PubMed:21558309).
CC {ECO:0000269|PubMed:21558309}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated in leaves during natural senescence.
CC {ECO:0000269|PubMed:21558309}.
CC -!- INDUCTION: By abscisic acid (ABA). {ECO:0000269|PubMed:21558309}.
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; AB246328; BAE73265.1; -; mRNA.
DR EMBL; AC004521; AAC16079.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10404.1; -; Genomic_DNA.
DR EMBL; AK118152; BAC42777.1; -; mRNA.
DR EMBL; BT005512; AAO63932.1; -; mRNA.
DR EMBL; AB047806; BAB32883.1; -; mRNA.
DR PIR; T02385; T02385.
DR RefSeq; NP_181958.1; NM_129993.5.
DR AlphaFoldDB; O64864; -.
DR STRING; 3702.AT2G44290.1; -.
DR PaxDb; O64864; -.
DR PRIDE; O64864; -.
DR ProteomicsDB; 242337; -.
DR EnsemblPlants; AT2G44290.1; AT2G44290.1; AT2G44290.
DR GeneID; 819037; -.
DR Gramene; AT2G44290.1; AT2G44290.1; AT2G44290.
DR KEGG; ath:AT2G44290; -.
DR Araport; AT2G44290; -.
DR TAIR; locus:2050482; AT2G44290.
DR eggNOG; ENOG502S0FC; Eukaryota.
DR HOGENOM; CLU_089796_1_1_1; -.
DR InParanoid; O64864; -.
DR OMA; EADQKEC; -.
DR OrthoDB; 1546514at2759; -.
DR PhylomeDB; O64864; -.
DR PRO; PR:O64864; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64864; baseline and differential.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:InterPro.
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..177
FT /note="Non-specific lipid transfer protein GPI-anchored 13"
FT /id="PRO_0000424703"
FT PROPEP 178..205
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451635"
FT REGION 141..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 177
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 36..77
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 46..61
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 62..104
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 75..113
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
SQ SEQUENCE 205 AA; 21579 MW; 4175748F4C37A007 CRC64;
MESRKIKVMA TAIALIMVAM VVDAAGADKG KDKEECTAQL VGMATCLPYV QGKAKSPTPD
CCSGLKQVIN SDMKCLCMII QERNDPDLGL QVNVSLALAL PSVCHATADI TKCPALLHLD
PNSPDAQVFY QLAKGLNETV SASAPTGSAS EPTSMSSTPG SSAGNNSGRT TSVPGTNHAQ
SFSKQWLGLE VVAHFFVIFY IFILV