LTG14_ARATH
ID LTG14_ARATH Reviewed; 204 AA.
AC O64865;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Non-specific lipid transfer protein GPI-anchored 14 {ECO:0000303|PubMed:23893219};
DE Short=AtLTPG-14 {ECO:0000303|PubMed:23893219};
DE Short=Protein LTP-GPI-ANCHORED 14 {ECO:0000303|PubMed:23893219};
DE AltName: Full=Protein SENESCENCE ASSOCIATED GENES 27 {ECO:0000303|PubMed:16299172};
DE AltName: Full=Xylogen like protein 7 {ECO:0000303|PubMed:21558309};
DE Short=AtXYLP7 {ECO:0000303|PubMed:21558309};
DE Short=AtXYP10 {ECO:0000303|PubMed:21558309};
DE Flags: Precursor;
GN Name=LTPG14 {ECO:0000303|PubMed:23893219};
GN Synonyms=SAG27 {ECO:0000303|PubMed:16299172},
GN XYLP7 {ECO:0000303|PubMed:21558309}, XYP10 {ECO:0000303|PubMed:21558309};
GN OrderedLocusNames=At2g44300 {ECO:0000312|Araport:AT2G44300};
GN ORFNames=F4I1.11 {ECO:0000312|EMBL:AAC16080.1};
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 INDUCTION BY SENESCENCE.
RX PubMed=16299172; DOI=10.1104/pp.105.070433;
RA Pegadaraju V., Knepper C., Reese J., Shah J.;
RT "Premature leaf senescence modulated by the Arabidopsis PHYTOALEXIN
RT DEFICIENT4 gene is associated with defense against the phloem-feeding green
RT peach aphid.";
RL Plant Physiol. 139:1927-1934(2005).
RN [6]
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: Vascular-specific expression in leaves, roots,
CC stems and inflorescences. {ECO:0000269|PubMed:21558309}.
CC -!- DEVELOPMENTAL STAGE: Mainly expressed in vascular tissues during the
CC mature stage. {ECO:0000269|PubMed:21558309}.
CC -!- INDUCTION: Accumulates in leaves during senescence mediated by the
CC phloem-feeding green peach aphid (GPA). {ECO:0000269|PubMed:16299172}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR EMBL; AB246329; BAE73266.1; -; mRNA.
DR EMBL; AC004521; AAC16080.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10405.1; -; Genomic_DNA.
DR EMBL; BT006196; AAP12845.1; -; mRNA.
DR PIR; T02386; T02386.
DR RefSeq; NP_181959.1; NM_129994.3.
DR AlphaFoldDB; O64865; -.
DR STRING; 3702.AT2G44300.1; -.
DR PaxDb; O64865; -.
DR PRIDE; O64865; -.
DR ProteomicsDB; 185881; -.
DR EnsemblPlants; AT2G44300.1; AT2G44300.1; AT2G44300.
DR GeneID; 819038; -.
DR Gramene; AT2G44300.1; AT2G44300.1; AT2G44300.
DR KEGG; ath:AT2G44300; -.
DR Araport; AT2G44300; -.
DR TAIR; locus:2050492; AT2G44300.
DR eggNOG; ENOG502S0FC; Eukaryota.
DR HOGENOM; CLU_089796_1_1_1; -.
DR InParanoid; O64865; -.
DR OMA; PKILGMS; -.
DR OrthoDB; 1546514at2759; -.
DR PhylomeDB; O64865; -.
DR Proteomes; UP000006548; Chromosome 2.
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:0010150; P:leaf senescence; IEP:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IEA:InterPro.
DR GO; GO:0080027; P:response to herbivore; IEP:UniProtKB.
DR GO; GO:0009625; P:response to insect; IEP: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 Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..176
FT /note="Non-specific lipid transfer protein GPI-anchored 14"
FT /id="PRO_5014306577"
FT PROPEP 177..204
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451645"
FT REGION 139..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 176
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 35..76
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 45..60
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 61..103
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 74..112
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
SQ SEQUENCE 204 AA; 21706 MW; 670CFE15C734184F CRC64;
MESRKINLMA TAIALIVVAM VVAAADDKTK DKEECTEQLV GMATCLPYVQ GQAKSPTPDC
CSGLKQVLNS NKKCLCVIIQ DRNDPDLGLQ INVSLALALP SVCHAAADVT KCPALLHLDP
NSPDAQVFYQ LAKGLNKTGP ASAPTGSSPG PISISPTSGS DDGNNSGRTT SVPGRNHAQS
FYKQWLGLEV VFHFFVIFYI FILV
