LTPG9_ARATH
ID LTPG9_ARATH Reviewed; 147 AA.
AC Q1PFD8; A0MEG2; Q8LA57; Q9FX48;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Non-specific lipid transfer protein GPI-anchored 9 {ECO:0000303|PubMed:23893219};
DE Short=AtLTPG-9 {ECO:0000303|PubMed:23893219};
DE Short=Protein LTP-GPI-ANCHORED 9 {ECO:0000303|PubMed:23893219};
DE Flags: Precursor;
GN Name=LTPG9 {ECO:0000303|PubMed:23893219};
GN OrderedLocusNames=At1g73560 {ECO:0000312|Araport:AT1G73560};
GN ORFNames=F6D5.5 {ECO:0000312|EMBL:AAG51810.1},
GN T9L24.28 {ECO:0000312|EMBL:AAG30968.1};
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;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=16299181; DOI=10.1104/pp.105.067314;
RA Yu H.-J., Hogan P., Sundaresan V.;
RT "Analysis of the female gametophyte transcriptome of Arabidopsis by
RT comparative expression profiling.";
RL Plant Physiol. 139:1853-1869(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: Expressed in ovules. {ECO:0000269|PubMed:16299181}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG30968.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG51810.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABK28466.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC012396; AAG30968.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC079676; AAG51810.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35476.1; -; Genomic_DNA.
DR EMBL; DQ446425; ABE65768.1; -; mRNA.
DR EMBL; DQ652932; ABK28466.1; ALT_SEQ; mRNA.
DR EMBL; AY088017; AAM65563.1; -; mRNA.
DR PIR; D96762; D96762.
DR RefSeq; NP_565067.1; NM_106014.2.
DR AlphaFoldDB; Q1PFD8; -.
DR SMR; Q1PFD8; -.
DR PaxDb; Q1PFD8; -.
DR ProteomicsDB; 187871; -.
DR EnsemblPlants; AT1G73560.1; AT1G73560.1; AT1G73560.
DR GeneID; 843690; -.
DR Gramene; AT1G73560.1; AT1G73560.1; AT1G73560.
DR KEGG; ath:AT1G73560; -.
DR Araport; AT1G73560; -.
DR TAIR; locus:2035052; AT1G73560.
DR HOGENOM; CLU_116928_3_1_1; -.
DR InParanoid; Q1PFD8; -.
DR OMA; QFKINIT; -.
DR OrthoDB; 1517142at2759; -.
DR PhylomeDB; Q1PFD8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q1PFD8; 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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..125
FT /note="Non-specific lipid transfer protein GPI-anchored 9"
FT /id="PRO_5014308379"
FT PROPEP 126..147
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451643"
FT LIPID 125
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 33..71
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 40..55
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 56..97
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 69..106
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT CONFLICT 12
FT /note="A -> V (in Ref. 4; AAM65563)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="N -> S (in Ref. 4; AAM65563)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="Q -> H (in Ref. 4; AAM65563)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="I -> T (in Ref. 4; AAM65563)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="K -> N (in Ref. 4; AAM65563)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 147 AA; 15512 MW; FF5C33B32D6F7224 CRC64;
MEINKFLAVV VAVVVLYSVE ATAQGGNPQL TACLQKLLPC QPYIHSLNPP PPPSCCGPMK
EIVEKDAPCL CIAFNNPEVL KALNLTKENA LLLPKACGVN PDVSLCSKIA TPSPIASPGS
TNGTSSASTI SFNRFSFLSA FVAMIFF
