LTG23_ARATH
ID LTG23_ARATH Reviewed; 256 AA.
AC Q2PE60;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Non-specific lipid transfer protein GPI-anchored 23 {ECO:0000303|PubMed:23893219};
DE Short=AtLTPG-23 {ECO:0000303|PubMed:23893219};
DE Short=Protein LTP-GPI-ANCHORED 23 {ECO:0000303|PubMed:23893219};
DE AltName: Full=Xylogen-like protein 5 {ECO:0000303|PubMed:21558309};
DE Short=AtXYLP5 {ECO:0000303|PubMed:21558309};
DE Short=AtXYP13 {ECO:0000303|PubMed:21558309};
DE Flags: Precursor;
GN Name=LTPG23 {ECO:0000303|PubMed:23893219};
GN Synonyms=XYLP5 {ECO:0000303|PubMed:21558309},
GN XYP13 {ECO:0000303|PubMed:21558309};
GN OrderedLocusNames=At1g36150 {ECO:0000312|Araport:AT1G36150};
GN ORFNames=F5J5.27 {ECO:0000312|EMBL:AEE31848.1};
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 [MRNA], TISSUE SPECIFICITY, GENE FAMILY, AND
RP NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=21558309; DOI=10.1093/pcp/pcr060;
RA Kobayashi Y., Motose H., Iwamoto K., Fukuda H.;
RT "Expression and genome-wide analysis of the xylogen-type gene family.";
RL Plant Cell Physiol. 52:1095-1106(2011).
RN [2]
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 [3]
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 [4]
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: Confined to the anthers of the inflorescence.
CC {ECO:0000269|PubMed:21558309, ECO:0000269|PubMed:23893219}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR EMBL; AB246332; BAE73269.1; -; mRNA.
DR EMBL; AC006228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE31848.1; -; Genomic_DNA.
DR RefSeq; NP_174848.1; NM_103312.1.
DR AlphaFoldDB; Q2PE60; -.
DR SMR; Q2PE60; -.
DR STRING; 3702.AT1G36150.1; -.
DR PaxDb; Q2PE60; -.
DR PRIDE; Q2PE60; -.
DR ProteomicsDB; 185081; -.
DR EnsemblPlants; AT1G36150.1; AT1G36150.1; AT1G36150.
DR GeneID; 840520; -.
DR Gramene; AT1G36150.1; AT1G36150.1; AT1G36150.
DR KEGG; ath:AT1G36150; -.
DR Araport; AT1G36150; -.
DR TAIR; locus:2034325; AT1G36150.
DR eggNOG; ENOG502S0AW; Eukaryota.
DR HOGENOM; CLU_095117_0_0_1; -.
DR InParanoid; Q2PE60; -.
DR OMA; LAMPKIC; -.
DR OrthoDB; 1547699at2759; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q2PE60; baseline and differential.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:InterPro.
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 InterPro; IPR000528; Plant_nsLTP.
DR PANTHER; PTHR33044; PTHR33044; 1.
DR Pfam; PF14368; LTP_2; 1.
DR PRINTS; PR00382; LIPIDTRNSFER.
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; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..225
FT /note="Non-specific lipid transfer protein GPI-anchored 23"
FT /id="PRO_5014308748"
FT PROPEP 226..256
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451654"
FT REGION 125..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..171
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 225
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 45..88
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 55..72
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 73..113
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 86..121
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
SQ SEQUENCE 256 AA; 25907 MW; AD4D8E1E788A5413 CRC64;
MKPSFVLLSI VLLLSSSLSD AADFGSPSQP PSMAPTPQPS NSTDCSSVIY SMVDCLSFLT
VGSTDPSPTK TCCVGVKTVL NYSPKCLCSA LESSREMGFV LDDTKALAMP KICNVPIDPN
CDVSTPAAST PVSPPVESPT TSPSSAKSPA ITPSSPAVSH SPPPVRHSSP PVSHSSPPVS
HSSPPTSRSS PAVSHSSPVV AASSPVKAVS SSTASSPRAA SPSPSPSPSI SSSGILLVSK
LFIAVVMVSS FLYILA
