LTG10_ARATH
ID LTG10_ARATH Reviewed; 193 AA.
AC Q9C9B1;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Non-specific lipid transfer protein GPI-anchored 10 {ECO:0000303|PubMed:23893219};
DE Short=AtLTPG-10 {ECO:0000303|PubMed:23893219};
DE Short=Protein LTP-GPI-ANCHORED 10 {ECO:0000303|PubMed:23893219};
DE Flags: Precursor;
GN Name=LTPG10 {ECO:0000303|PubMed:23893219};
GN OrderedLocusNames=At1g73890 {ECO:0000312|Araport:AT1G73890};
GN ORFNames=F2P9.24 {ECO:0000312|EMBL:AAG52526.1};
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}.
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DR EMBL; AC016662; AAG52526.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35522.1; -; Genomic_DNA.
DR PIR; E96766; E96766.
DR RefSeq; NP_177530.1; NM_106049.1.
DR AlphaFoldDB; Q9C9B1; -.
DR STRING; 3702.AT1G73890.1; -.
DR PaxDb; Q9C9B1; -.
DR PRIDE; Q9C9B1; -.
DR EnsemblPlants; AT1G73890.1; AT1G73890.1; AT1G73890.
DR GeneID; 843727; -.
DR Gramene; AT1G73890.1; AT1G73890.1; AT1G73890.
DR KEGG; ath:AT1G73890; -.
DR Araport; AT1G73890; -.
DR TAIR; locus:2031551; AT1G73890.
DR eggNOG; ENOG502RZD2; Eukaryota.
DR HOGENOM; CLU_124101_0_0_1; -.
DR InParanoid; Q9C9B1; -.
DR OMA; ALMPCAP; -.
DR OrthoDB; 1430465at2759; -.
DR PhylomeDB; Q9C9B1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9B1; 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 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..168
FT /note="Non-specific lipid transfer protein GPI-anchored 10"
FT /id="PRO_5014312686"
FT PROPEP 169..193
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451644"
FT REGION 109..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 168
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 30..71
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 40..55
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 56..98
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 69..107
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
SQ SEQUENCE 193 AA; 19881 MW; C602806C2B9BD9FA CRC64;
MASSTLLITL LISLSAFFLR MVLAQVPATC ASRLLSLAPC GPFVQGFAQL PAQPCCDSLN
QIYSQEATCL CLFLNNTSTL SPAFPINQTL ALQLPPLCNI PANSSTCSSS FPGEAPSDSS
SVAPPPSSST GSQISQGAKN NSRVAATPVA QMAPRPTSFM GLGYGLKSSG SKSEIQLTIF
ALAAILPAAL LLI
