LTPG7_ARATH
ID LTPG7_ARATH Reviewed; 150 AA.
AC Q6NLF7; Q9SI70;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Non-specific lipid transfer protein GPI-anchored 7 {ECO:0000303|PubMed:23893219};
DE Short=AtLTPG-7 {ECO:0000303|PubMed:23893219};
DE Short=Protein LTP-GPI-ANCHORED 7 {ECO:0000303|PubMed:23893219};
DE Flags: Precursor;
GN Name=LTPG7 {ECO:0000303|PubMed:23893219};
GN OrderedLocusNames=At1g62790 {ECO:0000312|Araport:AT1G62790};
GN ORFNames=F23N19.16 {ECO:0000312|EMBL:AAF19539.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=16299169; DOI=10.1104/pp.105.070805;
RA Suh M.C., Samuels A.L., Jetter R., Kunst L., Pollard M., Ohlrogge J.,
RA Beisson F.;
RT "Cuticular lipid composition, surface structure, and gene expression in
RT Arabidopsis stem epidermis.";
RL Plant Physiol. 139:1649-1665(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: Up-regulated in the epidermis of stems.
CC {ECO:0000269|PubMed:16299169}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF19539.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007190; AAF19539.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34004.1; -; Genomic_DNA.
DR EMBL; BT011764; AAS65935.1; -; mRNA.
DR EMBL; BT012377; AAS88767.1; -; mRNA.
DR EMBL; AK229732; BAF01570.1; -; mRNA.
DR RefSeq; NP_176467.1; NM_104957.5.
DR AlphaFoldDB; Q6NLF7; -.
DR SMR; Q6NLF7; -.
DR STRING; 3702.AT1G62790.1; -.
DR PaxDb; Q6NLF7; -.
DR ProteomicsDB; 183027; -.
DR EnsemblPlants; AT1G62790.1; AT1G62790.1; AT1G62790.
DR GeneID; 842578; -.
DR Gramene; AT1G62790.1; AT1G62790.1; AT1G62790.
DR KEGG; ath:AT1G62790; -.
DR Araport; AT1G62790; -.
DR TAIR; locus:2026257; AT1G62790.
DR eggNOG; ENOG502S7AI; Eukaryota.
DR InParanoid; Q6NLF7; -.
DR OrthoDB; 1459300at2759; -.
DR PhylomeDB; Q6NLF7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6NLF7; baseline and differential.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..125
FT /note="Non-specific lipid transfer protein GPI-anchored 7"
FT /id="PRO_5014310543"
FT PROPEP 126..150
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451641"
FT REGION 103..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 125
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 29..66
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 36..50
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 51..92
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 64..101
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
SQ SEQUENCE 150 AA; 15711 MW; 3BA043EEE018BABA CRC64;
MTKTMMIFAA AMTVMALLLV PTIEAQTECV SKLVPCFNDL NTTTTPVKEC CDSIKEAVEK
ELTCLCTIYT SPGLLAQFNV TTEKALGLSR RCNVTTDLSA CTAKGAPSPK ASLPPPAPAG
NTKKDAGAGN KLAGYGVTTV ILSLISSIFF
