NLTPC_ARATH
ID NLTPC_ARATH Reviewed; 119 AA.
AC Q9SCZ0; A0MF21; Q8LBC1;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Non-specific lipid-transfer protein 12;
DE Short=LTP 12;
DE Flags: Precursor;
GN Name=LTP12; OrderedLocusNames=At3g51590; ORFNames=F26O13.230, T18N14.1;
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=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 [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].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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=ABK28596.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL133452; CAB63023.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78810.1; -; Genomic_DNA.
DR EMBL; DQ446756; ABE66008.1; -; mRNA.
DR EMBL; DQ653145; ABK28596.1; ALT_SEQ; mRNA.
DR EMBL; BT026083; ABG48439.1; -; mRNA.
DR EMBL; AY087300; AAM64852.1; -; mRNA.
DR PIR; T45790; T45790.
DR RefSeq; NP_190727.1; NM_115018.3.
DR AlphaFoldDB; Q9SCZ0; -.
DR SMR; Q9SCZ0; -.
DR STRING; 3702.AT3G51590.1; -.
DR PaxDb; Q9SCZ0; -.
DR ProteomicsDB; 251182; -.
DR EnsemblPlants; AT3G51590.1; AT3G51590.1; AT3G51590.
DR GeneID; 824322; -.
DR Gramene; AT3G51590.1; AT3G51590.1; AT3G51590.
DR KEGG; ath:AT3G51590; -.
DR Araport; AT3G51590; -.
DR TAIR; locus:2081840; AT3G51590.
DR HOGENOM; CLU_128423_0_0_1; -.
DR InParanoid; Q9SCZ0; -.
DR OMA; ESTIQCG; -.
DR OrthoDB; 1546493at2759; -.
DR PhylomeDB; Q9SCZ0; -.
DR PRO; PR:Q9SCZ0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SCZ0; baseline and differential.
DR Genevisible; Q9SCZ0; AT.
DR GO; GO:0009505; C:plant-type cell wall; ISS: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 3: Inferred from homology;
KW Disulfide bond; Lipid-binding; Reference proteome; Signal; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..119
FT /note="Non-specific lipid-transfer protein 12"
FT /id="PRO_0000355621"
FT DISULFID 28..75
FT /evidence="ECO:0000255"
FT DISULFID 38..52
FT /evidence="ECO:0000255"
FT DISULFID 53..98
FT /evidence="ECO:0000255"
FT DISULFID 73..112
FT /evidence="ECO:0000255"
FT CONFLICT 19
FT /note="A -> T (in Ref. 5; AAM64852)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="L -> V (in Ref. 5; AAM64852)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 119 AA; 12572 MW; 4E4874C95B6BF8D9 CRC64;
MAFTPKIITC LIVLTIYMAS PTESTIQCGT VTSTLAQCLT YLTNSGPLPS QCCVGVKSLY
QLAQTTPDRK QVCECLKLAG KEIKGLNTDL VAALPTTCGV SIPYPISFST NCDSISTAV
