NLTP5_ARATH
ID NLTP5_ARATH Reviewed; 118 AA.
AC Q9XFS7; Q42005; Q8L966;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Non-specific lipid-transfer protein 5;
DE Short=LTP 5;
DE Flags: Precursor;
GN Name=LTP5; OrderedLocusNames=At3g51600; ORFNames=F26O13.240;
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].
RA Cooke R.M.;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=10940464; DOI=10.1016/s0168-9452(00)00232-6;
RA Arondel V.A., Vergnolle C., Cantrel C., Kader J.-C.;
RT "Lipid transfer proteins are encoded by a small multigene family in
RT Arabidopsis thaliana.";
RL Plant Sci. 157:1-12(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-118.
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-79.
RC STRAIN=cv. Columbia; TISSUE=Flower bud;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [8]
RP PROTEIN SEQUENCE OF 26-43.
RC STRAIN=cv. Columbia;
RX PubMed=8405465; DOI=10.1016/0014-5793(93)80641-7;
RA Segura A., Moreno M., Garcia-Olmedo F.;
RT "Purification and antipathogenic activity of lipid transfer proteins (LTPs)
RT from the leaves of Arabidopsis and spinach.";
RL FEBS Lett. 332:243-246(1993).
RN [9]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18674922; DOI=10.1016/j.plaphy.2008.06.011;
RA Sels J., Mathys J., De Coninck B.M.A., Cammue B.P.A., De Bolle M.F.C.;
RT "Plant pathogenesis-related (PR) proteins: a focus on PR peptides.";
RL Plant Physiol. Biochem. 46:941-950(2008).
CC -!- FUNCTION: Plant non-specific lipid-transfer proteins transfer
CC phospholipids as well as galactolipids across membranes. May play a
CC role in wax or cutin deposition in the cell walls of expanding
CC epidermal cells and certain secretory tissues (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM66937.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ238804; CAB43522.1; -; mRNA.
DR EMBL; AF159802; AAF76931.1; -; mRNA.
DR EMBL; AL133452; CAB63024.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78811.1; -; Genomic_DNA.
DR EMBL; AY058111; AAL25528.1; -; mRNA.
DR EMBL; AY094052; AAM16208.1; -; mRNA.
DR EMBL; AY088614; AAM66937.1; ALT_INIT; mRNA.
DR EMBL; Z18392; CAA79179.1; -; mRNA.
DR PIR; T45791; T45791.
DR RefSeq; NP_190728.1; NM_115019.3.
DR AlphaFoldDB; Q9XFS7; -.
DR SMR; Q9XFS7; -.
DR BioGRID; 9641; 1.
DR STRING; 3702.AT3G51600.1; -.
DR iPTMnet; Q9XFS7; -.
DR PaxDb; Q9XFS7; -.
DR PRIDE; Q9XFS7; -.
DR ProteomicsDB; 251063; -.
DR EnsemblPlants; AT3G51600.1; AT3G51600.1; AT3G51600.
DR GeneID; 824323; -.
DR Gramene; AT3G51600.1; AT3G51600.1; AT3G51600.
DR KEGG; ath:AT3G51600; -.
DR Araport; AT3G51600; -.
DR TAIR; locus:2081855; AT3G51600.
DR eggNOG; ENOG502S4CI; Eukaryota.
DR HOGENOM; CLU_128423_0_0_1; -.
DR InParanoid; Q9XFS7; -.
DR OMA; TAGCIRY; -.
DR OrthoDB; 1546493at2759; -.
DR PhylomeDB; Q9XFS7; -.
DR PRO; PR:Q9XFS7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9XFS7; baseline and differential.
DR Genevisible; Q9XFS7; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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; IPR000528; Plant_nsLTP.
DR PANTHER; PTHR33076; PTHR33076; 1.
DR Pfam; PF00234; Tryp_alpha_amyl; 1.
DR PRINTS; PR00382; LIPIDTRNSFER.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
DR PROSITE; PS00597; PLANT_LTP; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Lipid-binding;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:8405465"
FT CHAIN 26..118
FT /note="Non-specific lipid-transfer protein 5"
FT /id="PRO_0000018365"
FT DISULFID 29..76
FT /evidence="ECO:0000255"
FT DISULFID 39..53
FT /evidence="ECO:0000255"
FT DISULFID 54..100
FT /evidence="ECO:0000255"
FT DISULFID 74..114
FT /evidence="ECO:0000255"
FT CONFLICT 75
FT /note="R -> C (in Ref. 7; CAA79179)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="Q -> P (in Ref. 7; CAA79179)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 118 AA; 12495 MW; 6193D73DCF10E68F CRC64;
MEGLLKLSTL VIVCMLVTAP MASEAAISCG AVTGSLGQCY NYLTRGGFIP RGCCSGVQRL
NSLARTTRDR QQACRCIQGA ARALGSRLNA GRAARLPGAC RVRISYPISA RTNCNTVR
