LTG19_ARATH
ID LTG19_ARATH Reviewed; 171 AA.
AC F4HZB9; Q9SA59;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Non-specific lipid transfer protein GPI-anchored 19 {ECO:0000303|PubMed:23893219};
DE Short=AtLTPG-19 {ECO:0000303|PubMed:23893219};
DE Short=Protein LTP-GPI-ANCHORED 19 {ECO:0000303|PubMed:23893219};
DE Flags: Precursor;
GN Name=LTPG19 {ECO:0000303|PubMed:23893219};
GN OrderedLocusNames=At1g03103 {ECO:0000312|Araport:AT1G03103};
GN ORFNames=F10O3.7 {ECO:0000312|EMBL:AAD25798.1};
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 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 -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD25798.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006550; AAD25798.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27530.1; -; Genomic_DNA.
DR PIR; A86162; A86162.
DR RefSeq; NP_973749.1; NM_202020.1.
DR AlphaFoldDB; F4HZB9; -.
DR STRING; 3702.AT1G03103.1; -.
DR PaxDb; F4HZB9; -.
DR PRIDE; F4HZB9; -.
DR EnsemblPlants; AT1G03103.1; AT1G03103.1; AT1G03103.
DR GeneID; 2745739; -.
DR Gramene; AT1G03103.1; AT1G03103.1; AT1G03103.
DR KEGG; ath:AT1G03103; -.
DR Araport; AT1G03103; -.
DR TAIR; locus:1006230669; AT1G03103.
DR eggNOG; ENOG502S0AW; Eukaryota.
DR HOGENOM; CLU_089796_3_0_1; -.
DR InParanoid; F4HZB9; -.
DR OMA; GCNDALT; -.
DR OrthoDB; 1574629at2759; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HZB9; 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 SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..147
FT /note="Non-specific lipid transfer protein GPI-anchored 19"
FT /id="PRO_0000451649"
FT PROPEP 148..171
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451650"
FT REGION 113..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 147
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 25..66
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 35..50
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 51..93
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 64..103
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
SQ SEQUENCE 171 AA; 17664 MW; A4A33744EBC015D4 CRC64;
MILAILALVI ATFLYGGATT VQAGCRDTLT SLSPCLYYLN GGSSSPSWSC CRQFSTVVQS
SPECLCSVVN SNESSFYGFK FNRTLALNLP TACNVQTPSP SLCNTGGNVP TTLPANTPVG
SPRSAPSPSG TTSPANTPSG SKKFPLSNES SSKSNVIILS FVSIALVLAI I
