LTG28_ARATH
ID LTG28_ARATH Reviewed; 160 AA.
AC Q1G3I0;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Non-specific lipid transfer protein GPI-anchored 28 {ECO:0000303|PubMed:23893219};
DE Short=AtLTPG-28 {ECO:0000303|PubMed:23893219};
DE Short=Protein LTP-GPI-ANCHORED 28 {ECO:0000303|PubMed:23893219};
DE Flags: Precursor;
GN Name=LTPG28 {ECO:0000303|PubMed:23893219};
GN OrderedLocusNames=At4g22666 {ECO:0000312|Araport:AT4G22666};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 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; LR782545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002687; AEE84636.1; -; Genomic_DNA.
DR EMBL; DQ487604; ABF59247.1; -; mRNA.
DR RefSeq; NP_001031699.1; NM_001036622.4.
DR AlphaFoldDB; Q1G3I0; -.
DR STRING; 3702.AT4G22666.1; -.
DR PaxDb; Q1G3I0; -.
DR PRIDE; Q1G3I0; -.
DR ProteomicsDB; 178932; -.
DR EnsemblPlants; AT4G22666.1; AT4G22666.1; AT4G22666.
DR GeneID; 3770028; -.
DR Gramene; AT4G22666.1; AT4G22666.1; AT4G22666.
DR KEGG; ath:AT4G22666; -.
DR Araport; AT4G22666; -.
DR TAIR; locus:1009023377; AT4G22666.
DR eggNOG; ENOG502R3GN; Eukaryota.
DR HOGENOM; CLU_138794_0_0_1; -.
DR InParanoid; Q1G3I0; -.
DR OrthoDB; 1520535at2759; -.
DR PhylomeDB; Q1G3I0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q1G3I0; 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 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..135
FT /note="Non-specific lipid transfer protein GPI-anchored 28"
FT /id="PRO_5014308309"
FT PROPEP 136..160
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451660"
FT REGION 111..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 135
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 36..75
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 47..59
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 60..99
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 73..107
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
SQ SEQUENCE 160 AA; 16587 MW; C60DDF9CFECB35B7 CRC64;
MAYTNQISAV VFLAVAIAPL LAEPQSTMFP EMTPECATVM PDLLEKCFAT GSVTPTEDCC
TDLKSATSTQ VTCLCDNYIA NPAVSNITGP YSKAITTKCG VFDKYSCDGT SKGGEEKKGG
SSSSNGKDNG KSEGNGGRAN SVAASMAMFG LLASLVFVMF
