LTG17_ARATH
ID LTG17_ARATH Reviewed; 116 AA.
AC Q8GYS8; A0A1I9LT01; Q8LFZ3; Q9LJ89;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Non-specific lipid transfer protein GPI-anchored 17 {ECO:0000303|PubMed:23893219};
DE Short=AtLTPG-17 {ECO:0000303|PubMed:23893219};
DE Short=Protein LTP-GPI-ANCHORED 17 {ECO:0000303|PubMed:23893219};
DE Flags: Precursor;
GN Name=LTPG17 {ECO:0000303|PubMed:23893219};
GN OrderedLocusNames=At3g22570 {ECO:0000312|Araport:AT3G22570};
GN ORFNames=F16J14.13 {ECO:0000312|EMBL:BAB01472.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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].
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 [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 roots.
CC {ECO:0000269|PubMed:23893219}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ANM65709.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB01472.1; Type=Erroneous gene model prediction; Evidence={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; AP000731; BAB01472.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; ANM65709.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BT004995; AAO50528.1; -; mRNA.
DR EMBL; AK117414; BAC42080.1; -; mRNA.
DR EMBL; AY084552; AAM61119.1; -; mRNA.
DR RefSeq; NP_001327657.1; NM_001338593.1.
DR AlphaFoldDB; Q8GYS8; -.
DR IntAct; Q8GYS8; 5.
DR PaxDb; Q8GYS8; -.
DR PeptideAtlas; Q8GYS8; -.
DR ProteomicsDB; 195447; -.
DR EnsemblPlants; AT3G22570.2; AT3G22570.2; AT3G22570.
DR GeneID; 821829; -.
DR Gramene; AT3G22570.2; AT3G22570.2; AT3G22570.
DR KEGG; ath:AT3G22570; -.
DR Araport; AT3G22570; -.
DR TAIR; locus:2077056; AT3G22570.
DR HOGENOM; CLU_2100246_0_0_1; -.
DR PhylomeDB; Q8GYS8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8GYS8; baseline and differential.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; Lipoprotein;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..107
FT /note="Non-specific lipid transfer protein GPI-anchored 17"
FT /id="PRO_5010847050"
FT PROPEP 108..116
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451648"
FT LIPID 107
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 31..74
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 42..58
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 59..99
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT CONFLICT 15
FT /note="V -> A (in Ref. 5; AAM61119)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 116 AA; 12580 MW; C7AC4CE694D205C1 CRC64;
MKIGVVLVLL TVFVVVMSST SVSAQSDEDE CLKETGQMQL NCFPYLTDNR IHTPSFACCS
EVYTVGKTYV DCFCQFINNG GPSFGIVVSQ KLLDLPELCG VYGACGNGKN FKNTSL